interpro_id
string
interpro_numeric_id
int64
name
string
short_name
string
entry_type
string
protein_count
int64
is_llm
bool
is_llm_reviewed
bool
abstract
string
go_ids
list
go_terms
list
go_categories
list
go_count
int64
member_databases
list
member_accessions
list
member_names
list
member_protein_counts
list
member_count
int64
external_databases
list
external_accessions
list
external_xrefs
list
external_xref_count
int64
pdb_ids
list
structure_count
int64
publication_ids
list
pubmed_ids
list
publication_titles
list
publication_years
list
publication_count
int64
parent_ids
list
child_ids
list
parent_count
int64
child_count
int64
tree_depth
float64
taxonomy_names
list
taxonomy_protein_counts
list
taxonomy_count
int64
key_species_names
list
key_species_protein_counts
list
key_species_count
int64
in_entry_list
bool
entry_list_type
string
entry_list_name
string
names_dat_name
string
short_names_dat_name
string
split_bucket
int64
IPR002151
2,151
Kinesin light chain
Kinesin_light
Family
12,263
false
false
Kinesin is a microtubule-associated force-producing molecular motor protein that transports numerous organelles along mirotubules. Kinesin is an oligomeric complex composed of two heavy chains and two identical light chains. The light chain has been proposed to function in the coupling of cargo to the heavy chain or in...
[ "GO:0005871" ]
[ "kinesin complex" ]
[ "cellular_component" ]
1
[ "PANTHER" ]
[ "PTHR45783" ]
[ "" ]
[ 12263 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CEL-6811434", "R-CEL-983189", "R-DME-6811434", "R-DME-983189", "R-HSA-2132295", "R-HSA-5625970", "R-HSA-6811434", "R-HSA-9725370", "R-HSA-983189", "R-MMU-2132295", "R-MMU-5625970", "R-MMU-6811434", "R-MMU-983189", "R-RNO-2132295", "R-RNO-5625970", "R-RNO-6811434", "R-RNO-983189" ]
[ "REACTOME:R-CEL-6811434", "REACTOME:R-CEL-983189", "REACTOME:R-DME-6811434", "REACTOME:R-DME-983189", "REACTOME:R-HSA-2132295", "REACTOME:R-HSA-5625970", "REACTOME:R-HSA-6811434", "REACTOME:R-HSA-9725370", "REACTOME:R-HSA-983189", "REACTOME:R-MMU-2132295", "REACTOME:R-MMU-5625970", "REACTOME:R...
17
[ "3ceq", "3edt", "3nf1", "3zfw", "5fjy", "5oj8", "5ojf", "6ejn", "6f9i", "6fuz", "6fv0", "6swu", "7ai4", "7aie" ]
14
[ "PUB00002785", "PUB00015444", "PUB00094625" ]
[ "8514798", "15491159", "19605495" ]
[ "The Drosophila kinesin light chain. Primary structure and interaction with kinesin heavy chain.", "The tetrameric molecule of conventional kinesin contains identical light chains.", "UNC-83 is a nuclear-specific cargo adaptor for kinesin-1-mediated nuclear migration." ]
[ 1993, 2004, 2009 ]
3
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "Stenosarchaea group", "metagenomes" ]
[ 1996, 10191, 37, 39 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 20, 3, 45, 23, 25 ]
6
true
Family
Kinesin light chain
Kinesin light chain
Kinesin_light
6
IPR002152
2,152
Glycoside hydrolase, family 23
Glyco_hydro_23
Family
2,247
false
false
O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,...
[ "GO:0003796", "GO:0009253" ]
[ "lysozyme activity", "peptidoglycan catabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PIRSF", "PRINTS" ]
[ "PIRSF001065", "PR00749" ]
[ "Lysozyme_g", "LYSOZYMEG" ]
[ 1382, 2231 ]
2
[ "CAZY", "EC" ]
[ "GH23", "3.2.1.17" ]
[ "CAZY:GH23", "EC:3.2.1.17" ]
2
[ "153l", "154l", "1gbs", "1lsp", "3gxk", "3gxr", "3mgw", "3wyh", "4g9s" ]
9
[ "PUB00000543", "PUB00003340", "PUB00004870", "PUB00005266" ]
[ "8687420", "7823320", "7624375", "8535779" ]
[ "Updating the sequence-based classification of glycosyl hydrolases.", "The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the \"goose-type\" lysozymes lack a catalytic aspartate residue.", "Conserved catalytic machinery and the prediction of a common fold for several f...
[ 1996, 1995, 1995, 1995 ]
4
[]
[]
0
0
null
[ "Bacteria", "Eumetazoa" ]
[ 73, 2174 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 4, 4, 3 ]
4
true
Family
Glycoside hydrolase, family 23
Glycoside hydrolase, family 23
Glyco_hydro_23
6
IPR002153
2,153
Transient receptor potential channel, canonical
TRPC_channel
Family
16,059
false
false
The classical or canonical TRPC family (formerly short-TRPs, STRPs) encompasses channels presenting a large number of different activation modes. Some are store-operated, whereas others are receptor-operated channels activated by the production of diacylglicerol or redox processes. TRPC proteins also control growth con...
[ "GO:0005262", "GO:0070588", "GO:0016020" ]
[ "calcium channel activity", "calcium ion transmembrane transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS", "PANTHER" ]
[ "PR01097", "PTHR10117" ]
[ "TRNSRECEPTRP", "" ]
[ 12581, 14984 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-114508", "R-BTA-139853", "R-BTA-3295583", "R-CEL-114508", "R-CEL-139853", "R-CEL-3295583", "R-DME-3295583", "R-DME-5578775", "R-DME-983695", "R-HSA-114508", "R-HSA-139853", "R-HSA-3295583", "R-HSA-418890", "R-HSA-5578775", "R-HSA-9022699", "R-HSA-983695", "R-MMU-114508", "R-...
[ "REACTOME:R-BTA-114508", "REACTOME:R-BTA-139853", "REACTOME:R-BTA-3295583", "REACTOME:R-CEL-114508", "REACTOME:R-CEL-139853", "REACTOME:R-CEL-3295583", "REACTOME:R-DME-3295583", "REACTOME:R-DME-5578775", "REACTOME:R-DME-983695", "REACTOME:R-HSA-114508", "REACTOME:R-HSA-139853", "REACTOME:R-HSA...
26
[ "5vkq", "5yx9", "5z96", "5zbg", "6aei", "6cud", "6cv9", "6d7l", "6djs", "6g1k", "6jzo", "6pw4", "6pw5", "6uz8", "6uza", "6ysn", "7a6u", "7b05", "7b0j", "7b0s", "7b16", "7b1g", "7d4p", "7d4q", "7dxb", "7dxc", "7dxd", "7dxe", "7dxf", "7dxg", "7e4t", "7mbp"...
63
[ "PUB00054048", "PUB00054049", "PUB00054050", "PUB00054051", "PUB00054052" ]
[ "18535090", "20025796", "20861159", "15909153", "12032305" ]
[ "TRP channels entering the structural era.", "Structure-functional intimacies of transient receptor potential channels.", "The role of transient receptor potential cation channels in Ca2+ signaling.", "Functional characterization and physiological relevance of the TRPC3/6/7 subfamily of cation channels.", "...
[ 2008, 2009, 2010, 2005, 2002 ]
5
[]
[ "IPR005457", "IPR005458", "IPR005459", "IPR005460", "IPR005461", "IPR005462", "IPR005463" ]
0
7
0
[ "Eukaryota" ]
[ 16059 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 55, 17, 29, 35, 51 ]
6
true
Family
Transient receptor potential channel, canonical
Transient receptor potential channel, canonical
TRPC_channel
5
IPR002155
2,155
Thiolase
Thiolase
Family
148,684
false
false
Thiolases are ubiquitous enzymes that catalyse the reversible thiolytic cleavage of 3-ketoacyl-CoA into acyl-CoA and acetyl-CoA, a 2-step reaction involving a covalent intermediate formed with a catalytic cysteine. They are found in prokaryotes and eukaryotes. Two different types of thiolase [ , , ] are found both in e...
[ "GO:0016747" ]
[ "acyltransferase activity, transferring groups other than amino-acyl groups" ]
[ "molecular_function" ]
1
[ "PIRSF", "NCBIFAM", "CDD" ]
[ "PIRSF000429", "TIGR01930", "cd00751" ]
[ "Ac-CoA_Ac_transf", "AcCoA-C-Actrans", "thiolase" ]
[ 139647, 119690, 121924 ]
3
[ "EC", "EC", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", ...
[ "2.3.1", "2.3.1.16", "GenProp0283", "GenProp1240", "GenProp1308", "GenProp1432", "GenProp1441", "GenProp1510", "GenProp1533", "GenProp1544", "GenProp1562", "GenProp1717", "PWY-481", "PWY-5109", "PWY-5136", "PWY-6080", "PWY-6435", "PWY-6443", "PWY-6458", "PWY-6944", "PWY-6945"...
[ "EC:2.3.1", "EC:2.3.1.16", "GP:GenProp0283", "GP:GenProp1240", "GP:GenProp1308", "GP:GenProp1432", "GP:GenProp1441", "GP:GenProp1510", "GP:GenProp1533", "GP:GenProp1544", "GP:GenProp1562", "GP:GenProp1717", "METACYC:PWY-481", "METACYC:PWY-5109", "METACYC:PWY-5136", "METACYC:PWY-6080", ...
142
[ "1afw", "1dlu", "1dlv", "1dm3", "1m1o", "1m1t", "1m3k", "1m3z", "1m4s", "1m4t", "1nl7", "1ou6", "1pxt", "1qfl", "1ulq", "1wdk", "1wdl", "1wdm", "1wl4", "1wl5", "2c7y", "2c7z", "2d3t", "2f2s", "2ib7", "2ib8", "2ib9", "2ibu", "2ibw", "2iby", "2iik", "2vtz"...
185
[ "PUB00001113", "PUB00002552", "PUB00003423", "PUB00052320", "PUB00070339" ]
[ "1755959", "2191949", "1354266", "15589695", "23793631" ]
[ "Similarity between the amino-terminal portion of mammalian 58-kD sterol carrier protein (SCPx) and Escherichia coli acetyl-CoA acyltransferase: evidence for a gene fusion in SCPx.", "Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural...
[ 1991, 1990, 1992, 2004, 2013 ]
5
[]
[ "IPR012793", "IPR012806", "IPR049957", "IPR050215" ]
0
4
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 3319, 120253, 23411, 1701 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 23, 5, 10, 9, 5, 31, 19, 5, 11, 46, 2, 1, 41 ]
13
true
Family
Thiolase
Thiolase
Thiolase
4
IPR002156
2,156
Ribonuclease H domain
RNaseH_domain
Domain
192,462
false
false
This entry represents the RNase H type-I domain. Ribonuclease H (RNase H) ( ) is a member of the ribonuclease family, which recognises and cleaves the RNA strand of RNA-DNA heteroduplexes. The enzyme is widely present in all three kingdoms of living organisms, including bacteria, archaea, and eukaryotes, and their coun...
[ "GO:0003676", "GO:0004523" ]
[ "nucleic acid binding", "RNA-DNA hybrid ribonuclease activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "PFAM", "PFAM", "PROFILE" ]
[ "PF00075", "PF13456", "PS50879" ]
[ "RNase_H", "RVT_3", "RNASE_H_1" ]
[ 95458, 89466, 126631 ]
3
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.1.26.4", "PDOC50879", "R-HSA-162585", "R-HSA-162588", "R-HSA-162592", "R-HSA-162594", "R-HSA-164516", "R-HSA-164525", "R-HSA-164843", "R-HSA-173107", "R-HSA-175474", "R-HSA-175567", "R-HSA-177539", "R-HSA-180689", "R-HSA-180910", "R-HSA-9913635" ]
[ "EC:3.1.26.4", "PROSITEDOC:PDOC50879", "REACTOME:R-HSA-162585", "REACTOME:R-HSA-162588", "REACTOME:R-HSA-162592", "REACTOME:R-HSA-162594", "REACTOME:R-HSA-164516", "REACTOME:R-HSA-164525", "REACTOME:R-HSA-164843", "REACTOME:R-HSA-173107", "REACTOME:R-HSA-175474", "REACTOME:R-HSA-175567", "RE...
16
[ "1bqm", "1bqn", "1c0t", "1c0u", "1c1b", "1c1c", "1dlo", "1dtq", "1dtt", "1eet", "1ep4", "1f21", "1fk9", "1fko", "1fkp", "1g15", "1goa", "1gob", "1goc", "1hmv", "1hni", "1hnv", "1hpz", "1hqe", "1hqu", "1hrh", "1hvu", "1hys", "1ikv", "1ikw", "1ikx", "1iky"...
644
[ "PUB00006422", "PUB00006461", "PUB00015351", "PUB00015352", "PUB00015353", "PUB00025090", "PUB00040141", "PUB00042692", "PUB00079405", "PUB00081183", "PUB00096386", "PUB00100891" ]
[ "9741851", "10603172", "2169648", "8108376", "1707186", "11083878", "16343535", "17964265", "19228198", "17663799", "16093691", "31371183" ]
[ "Folding the ribonuclease H domain of Moloney murine leukemia virus reverse transcriptase requires metal binding or a short N-terminal extension.", "Sequence and comparative structural analysis of the murine leukaemia virus amphotropic strain 4070A RNase H domain.", "Structure of ribonuclease H phased at 2 A re...
[ 1998, 1999, 1990, 1993, 1991, 2001, 2006, 2007, 2009, 2007, 2005, 2019 ]
12
[]
[ "IPR044730" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 766, 30225, 121793, 38790, 888 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 393, 4, 6, 5, 1, 28, 31, 1, 1099, 8, 1, 1, 44 ]
13
true
Domain
Ribonuclease H domain
Ribonuclease H domain
RNaseH_domain
9
IPR002157
2,157
Cobalamin (vitamin B12)-binding protein
Cbl-bd_prot
Family
2,768
false
false
Cobalamin (Cbl or vitamin B12) is only accessible through diet in mammals. Absorption, plasma transport and cellular uptake of Cbl in mammals involves three Cbl-transporting proteins, which are listed below in order of increasing Cbl-specificity: Haptocorrin (cobalophilin), which binds Cbl and Cbl-derivatives such as c...
[ "GO:0031419", "GO:0015889" ]
[ "cobalamin binding", "cobalamin transport" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PROSITE" ]
[ "PF01122", "PS00468" ]
[ "Cobalamin_bind", "COBALAMIN_BINDING" ]
[ 2768, 422 ]
2
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00428", "R-BTA-9758890", "R-CFA-9758881", "R-DME-6798695", "R-DME-9758881", "R-DME-9758890", "R-HSA-3359454", "R-HSA-3359457", "R-HSA-3359462", "R-HSA-3359463", "R-HSA-3359485", "R-HSA-6798695", "R-HSA-9758881", "R-HSA-9758890", "R-MMU-9758881", "R-MMU-9758890", "R-RNO-9758881",...
[ "PROSITEDOC:PDOC00428", "REACTOME:R-BTA-9758890", "REACTOME:R-CFA-9758881", "REACTOME:R-DME-6798695", "REACTOME:R-DME-9758881", "REACTOME:R-DME-9758890", "REACTOME:R-HSA-3359454", "REACTOME:R-HSA-3359457", "REACTOME:R-HSA-3359462", "REACTOME:R-HSA-3359463", "REACTOME:R-HSA-3359485", "REACTOME:...
18
[ "2bb5", "2bb6", "2bbc", "2pmv", "2v3n", "2v3p", "3kq4", "4kki", "4kkj", "4zrp", "4zrq", "7qbd", "7qbe", "7qbf", "7qbg", "8ixt", "8ixu" ]
17
[ "PUB00035336", "PUB00035337" ]
[ "16537422", "17274763" ]
[ "Structural basis for mammalian vitamin B12 transport by transcobalamin.", "Structural study on ligand specificity of human vitamin B12 transporters." ]
[ 2006, 2007 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eumetazoa", "bird metagenome" ]
[ 5, 2762, 1 ]
3
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 2, 16, 2, 8 ]
5
true
Family
Cobalamin (vitamin B12)-binding protein
Cobalamin (vitamin B12)-binding protein
Cbl-bd_prot
9
IPR002159
2,159
CD36 family
CD36_fam
Family
13,731
false
false
This entry includes CD36 and CD36-like proteins, including SCARB1/2 from vertebrates and SNMP1/2 from flies.
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF01130", "PR01609", "PTHR11923" ]
[ "CD36", "CD36FAMILY", "" ]
[ 13712, 11939, 13325 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-114608", "R-BTA-1236973", "R-BTA-3000471", "R-BTA-434313", "R-BTA-5686938", "R-BTA-6798695", "R-BTA-8964011", "R-CEL-114608", "R-CEL-1236973", "R-CEL-434313", "R-CEL-6798695", "R-DDI-114608", "R-DDI-434313", "R-DDI-6798695", "R-DDI-8856825", "R-DDI-8856828", "R-DME-114608", ...
[ "REACTOME:R-BTA-114608", "REACTOME:R-BTA-1236973", "REACTOME:R-BTA-3000471", "REACTOME:R-BTA-434313", "REACTOME:R-BTA-5686938", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-8964011", "REACTOME:R-CEL-114608", "REACTOME:R-CEL-1236973", "REACTOME:R-CEL-434313", "REACTOME:R-CEL-6798695", "REACTOME:R-...
60
[ "4f7b", "4q4b", "4q4f", "4tvz", "4tw0", "4tw2", "5ktf", "5lgd", "5uph", "5xbm", "6i2k", "9fjf" ]
12
[ "PUB00003034" ]
[ "9478926" ]
[ "Lysosomal integral membrane protein II binds thrombospondin-1. Structure-function homology with the cell adhesion molecule CD36 defines a conserved recognition motif." ]
[ 1998 ]
1
[]
[ "IPR005428", "IPR005429" ]
0
2
0
[ "Archaea", "Eukaryota" ]
[ 2, 13729 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 10, 31, 61, 14, 30 ]
6
true
Family
CD36 family
CD36 family
CD36_fam
6
IPR002160
2,160
Proteinase inhibitor I3, Kunitz legume
Prot_inh_Kunz-lg
Family
5,991
false
false
The Kunitz-type soybean trypsin inhibitor (STI) family consists mainly of proteinase inhibitors from Leguminosae seeds [ ]. They belong to MEROPS inhibitor family I3, clan IC. They exhibit proteinase inhibitory activity against serine proteinases; trypsin (MEROPS peptidase family S1, ) and subtilisin (MEROPS peptidase ...
[ "GO:0004866" ]
[ "endopeptidase inhibitor activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS", "PROSITE", "PANTHER", "SMART" ]
[ "PF00197", "PR00291", "PS00283", "PTHR33107", "SM00452" ]
[ "Kunitz_legume", "KUNITZINHBTR", "SOYBEAN_KUNITZ", "", "STI" ]
[ 5818, 3335, 2946, 5614, 5447 ]
5
[ "PROSITEDOC" ]
[ "PDOC00255" ]
[ "PROSITEDOC:PDOC00255" ]
1
[ "1ava", "1avu", "1avw", "1avx", "1ba7", "1eyl", "1fmz", "1fn0", "1r8n", "1r8o", "1tie", "1wba", "1wbc", "1xg6", "2bea", "2beb", "2dre", "2esu", "2et2", "2go2", "2gzb", "2iwt", "2qn4", "2qyi", "2wbc", "3bx1", "3e8l", "3i29", "3i2a", "3i2x", "3iir", "3qyd"...
97
[ "PUB00003265", "PUB00003281", "PUB00014133" ]
[ "1988676", "1738162", "14705960" ]
[ "Crystal structure of a Kunitz-type trypsin inhibitor from Erythrina caffra seeds.", "beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 alpha and fibroblast growth factors.", "Evolutionary families of peptidase inhibitors." ]
[ 1991, 1992, 2004 ]
3
[]
[ "IPR016308", "IPR056368" ]
0
2
0
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 108, 5878, 5 ]
3
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 26, 3, 3 ]
3
true
Family
Proteinase inhibitor I3, Kunitz legume
Proteinase inhibitor I3, Kunitz legume
Prot_inh_Kunz-lg
4
IPR002161
2,161
Pyridoxal 5'-phosphate synthase subunit PdxT/SNO
PdxT/SNO
Family
12,116
false
false
This entry represents a family of pyridoxal 5'-phosphate synthase subunit, also known as the pdxT/SNO family. This family belongs to a superfamily containing a triad glutamine aminotransferase fold, characterised by a conserved Cys-His-Glu active site [ ]. Two regions are highly conserved across all taxa, the PGGEST mo...
[ "GO:0004359", "GO:0042819", "GO:0042823" ]
[ "glutaminase activity", "vitamin B6 biosynthetic process", "pyridoxal phosphate biosynthetic process" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "HAMAP", "PFAM", "PIRSF", "PROFILE", "PANTHER", "NCBIFAM", "CDD" ]
[ "MF_01615", "PF01174", "PIRSF005639", "PS51130", "PTHR31559", "TIGR03800", "cd01749" ]
[ "PdxT", "SNO", "Glut_amidoT_SNO", "PDXT_SNO_2", "", "PLP_synth_Pdx2", "GATase1_PB" ]
[ 10654, 11933, 10836, 11994, 11987, 11569, 10959 ]
7
[ "EC", "EC", "METACYC", "METACYC", "PROSITEDOC" ]
[ "3.5.1.2", "4.3.3.6", "PWY-5921", "PWY-6466", "PDOC00950" ]
[ "EC:3.5.1.2", "EC:4.3.3.6", "METACYC:PWY-5921", "METACYC:PWY-6466", "PROSITEDOC:PDOC00950" ]
5
[ "1q7r", "1r9g", "2abw", "2iss", "2nv0", "2nv2", "2ywd", "2ywj", "4ads", "4wxy", "8u7j" ]
11
[ "PUB00018041", "PUB00018042", "PUB00018044", "PUB00018045" ]
[ "14764090", "14762015", "14585832", "11344146" ]
[ "Characterization of the products of the genes SNO1 and SNZ1 involved in pyridoxine synthesis in Saccharomyces cerevisiae.", "Physical and enzymological interaction of Bacillus subtilis proteins required for de novo pyridoxal 5'-phosphate biosynthesis.", "Three-dimensional structure of YaaE from Bacillus subtil...
[ 2004, 2004, 2004, 2001 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctg0K17", "unclassified sequences" ]
[ 849, 8105, 2829, 1, 332 ]
5
[ "Arabidopsis thaliana", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 3, 1, 2, 3, 1, 10 ]
6
true
Family
Pyridoxal 5'-phosphate synthase subunit PdxT/SNO
Pyridoxal 5'-phosphate synthase subunit PdxT/SNO
PdxT/SNO
8
IPR002164
2,164
Nucleosome assembly protein
NAP
Family
19,258
false
false
It is thought that NAPs act as histone chaperones, shuttling both core and linker histones from their site of synthesis in the cytoplasm to the nucleus. The proteins may be involved in regulating gene expression and therefore cellular differentiation [ , ]. The centrosomal protein c-Nap1, also known as Cep250, has been...
[ "GO:0006334", "GO:0005634" ]
[ "nucleosome assembly", "nucleus" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PANTHER" ]
[ "PF00956", "PTHR11875" ]
[ "NAP", "" ]
[ 18877, 18746 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DME-450520", "R-HSA-2299718", "R-HSA-381038", "R-HSA-450520", "R-MMU-2299718", "R-MMU-450520", "R-RNO-2299718", "R-RNO-450520" ]
[ "REACTOME:R-DME-450520", "REACTOME:R-HSA-2299718", "REACTOME:R-HSA-381038", "REACTOME:R-HSA-450520", "REACTOME:R-MMU-2299718", "REACTOME:R-MMU-450520", "REACTOME:R-RNO-2299718", "REACTOME:R-RNO-450520" ]
8
[ "2ayu", "2e50", "2z2r", "2zd7", "3c9b", "3c9d", "3dm7", "3fs3", "3gyv", "3gyw", "3hfd", "3q33", "3q35", "3q66", "3q68", "5agc", "5day", "5g2e", "5gpk", "5gpl", "5x7v", "5yps", "5zb5", "6jqv", "6k00", "6k02", "6k09", "6k0c", "6n2g", "6o22", "7c7x", "7mto"...
41
[ "PUB00001982", "PUB00002002", "PUB00007177", "PUB00007178" ]
[ "9325046", "8923009", "12138188", "12140259" ]
[ "Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone.", "Testis-specific protein, Y-encoded (TSPY) expression in testicular tissues.", "Identification of a chromosome-targeting domain in the human condensin subunit CNAP1/hCAP-D2/Eg7.", "The mechan...
[ 1997, 1996, 2002, 2002 ]
4
[]
[]
0
0
null
[ "Eukaryota", "Nocardioides oceani", "bird metagenome" ]
[ 19256, 1, 1 ]
3
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 30, 3, 20, 9, 87, 30, 2, 14, 52, 2, 3, 40 ]
12
true
Family
Nucleosome assembly protein
Nucleosome assembly protein
NAP
8
IPR002165
2,165
Plexin repeat
Plexin_repeat
Repeat
43,494
false
false
This is a cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found in plexin ( ) [ ]. Two copies of the repeat are found in mahogany protein. A related Caenorhabditis elegans protein ( ) contains four copies of the repeat, while...
[]
[]
[]
0
[ "PFAM" ]
[ "PF01437" ]
[ "PSI" ]
[ 43494 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-CEL-399954", "R-CEL-399955", "R-CEL-399956", "R-CEL-416482", "R-CEL-416550", "R-CEL-416572", "R-CEL-416700", "R-CEL-9013405", "R-DME-399954", "R-DME-399955", "R-DME-399956", "R-DME-416482", "R-DME-416572", "R-DME-416700", "R-DME-5173214", "R-DME-9013405", "R-DRE-399954", "R-DRE-...
[ "REACTOME:R-CEL-399954", "REACTOME:R-CEL-399955", "REACTOME:R-CEL-399956", "REACTOME:R-CEL-416482", "REACTOME:R-CEL-416550", "REACTOME:R-CEL-416572", "REACTOME:R-CEL-416700", "REACTOME:R-CEL-9013405", "REACTOME:R-DME-399954", "REACTOME:R-DME-399955", "REACTOME:R-DME-399956", "REACTOME:R-DME-41...
114
[ "1olz", "1shy", "1ssl", "2uzx", "2uzy", "3afc", "3al8", "3al9", "3nvn", "3nvq", "3okt", "3okw", "3oky", "3ol2", "4fww", "4gza", "4k3j", "4o3t", "4o3u", "4qt8", "5b4w", "5l56", "5l59", "5l5c", "5l5g", "5l5k", "5l5l", "5l5m", "5l5n", "5lsp", "6fkk", "6fkm"...
53
[ "PUB00004313" ]
[ "7605632" ]
[ "Plexin: a novel neuronal cell surface molecule that mediates cell adhesion via a homophilic binding mechanism in the presence of calcium ions." ]
[ 1995 ]
1
[]
[]
0
0
null
[ "Eukaryota", "Phenylobacterium kunshanense", "Viruses", "organismal metagenomes" ]
[ 43466, 1, 22, 5 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 11, 194, 24, 104, 60, 93 ]
6
true
Repeat
Plexin repeat
Plexin repeat
Plexin_repeat
1
IPR002166
2,166
RNA dependent RNA polymerase, hepatitis C virus
RNA_pol_HCV
Family
48,836
false
false
The RNA dependent RNA polymerase is also known as non-structural protein NS5B. NS5B is a 65kDa protein that resembles other viral RNA polymerases. Hepatitis C virus (HCV) replication is thought to occur in membrane bound replication complexes. These complexes transcribe the positive strand and the resulting minus stran...
[ "GO:0003723", "GO:0003968", "GO:0039694" ]
[ "RNA binding", "RNA-directed RNA polymerase activity", "viral RNA genome replication" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM" ]
[ "PF00998" ]
[ "RdRP_3" ]
[ 48836 ]
1
[ "EC", "EC", "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME" ]
[ "2.7.7.48", "3.4.21", "3.4.22.-", "3.6.1.15", "3.6.4.13", "PWY-6545", "PWY-7184", "PWY-7185", "PWY-7198", "PWY-7210", "R-HSA-5621480", "R-HSA-8854214" ]
[ "EC:2.7.7.48", "EC:3.4.21", "EC:3.4.22.-", "EC:3.6.1.15", "EC:3.6.4.13", "METACYC:PWY-6545", "METACYC:PWY-7184", "METACYC:PWY-7185", "METACYC:PWY-7198", "METACYC:PWY-7210", "REACTOME:R-HSA-5621480", "REACTOME:R-HSA-8854214" ]
12
[ "1c2p", "1csj", "1gx5", "1gx6", "1nb4", "1nb6", "1nb7", "1nhu", "1nhv", "1os5", "1quv", "1s48", "1s49", "1s4f", "1yuy", "1yv2", "1yvf", "1yvx", "1yvz", "1z4u", "2awz", "2ax0", "2ax1", "2brk", "2brl", "2cjq", "2d3u", "2d3z", "2d41", "2dxs", "2fvc", "2gc8"...
231
[ "PUB00000263", "PUB00001279", "PUB00003539" ]
[ "9514871", "8598194", "9343198" ]
[ "Complex formation of NS5B with NS3 and NS4A proteins of hepatitis C virus.", "Identification and properties of the RNA-dependent RNA polymerase of hepatitis C virus.", "Biochemical properties of hepatitis C virus NS5B RNA-dependent RNA polymerase and identification of amino acid sequence motifs essential for e...
[ 1998, 1996, 1997 ]
3
[]
[]
0
0
null
[ "Neoptera", "Viruses", "organismal metagenomes" ]
[ 6, 48828, 2 ]
3
[]
[]
0
true
Family
RNA dependent RNA polymerase, hepatitis C virus
RNA dependent RNA polymerase, hepatitis C virus
RNA_pol_HCV
7
IPR002167
2,167
Solute carrier family 25 member 16-like
GDC-like
Family
7,917
false
false
This family includes a variety of substrate carrier proteins that are involved in energy transfer are found in the inner mitochondrial membrane [ , , , ]. Such proteins include: ADP, ATP carrier protein (ADP/ATP translocase); 2-oxoglutarate/malate carrier protein; phosphate carrier protein; tricarboxylate transport pro...
[ "GO:0005743" ]
[ "mitochondrial inner membrane" ]
[ "cellular_component" ]
1
[ "PRINTS" ]
[ "PR00928" ]
[ "GRAVESDC" ]
[ 7917 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DDI-199220", "R-DRE-199220", "R-HSA-199220", "R-MMU-199220", "R-RNO-199220", "R-SCE-199220", "R-SPO-199220", "R-XTR-199220" ]
[ "REACTOME:R-DDI-199220", "REACTOME:R-DRE-199220", "REACTOME:R-HSA-199220", "REACTOME:R-MMU-199220", "REACTOME:R-RNO-199220", "REACTOME:R-SCE-199220", "REACTOME:R-SPO-199220", "REACTOME:R-XTR-199220" ]
8
[]
0
[ "PUB00001005", "PUB00003301", "PUB00003712", "PUB00005084", "PUB00005351", "PUB00101072" ]
[ "8325039", "8487299", "2575220", "8140286", "2158156", "11158296" ]
[ "The mitochondrial carrier family of transport proteins: structural, functional, and evolutionary relationships.", "Site-directed mutagenesis of the yeast mitochondrial ADP/ATP translocator. Six arginines and one lysine are essential.", "Sequence and chromosomal assignment of a novel cDNA identified by immunosc...
[ 1993, 1993, 1989, 1993, 1990, 2001 ]
6
[ "IPR002067" ]
[]
1
0
1
[ "Eukaryota" ]
[ 7917 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 8, 2, 15, 4, 10, 5, 1, 2, 15, 1, 1, 3 ]
12
true
Family
Solute carrier family 25 member 16-like
Solute carrier family 25 member 16-like
GDC-like
9
IPR002168
2,168
Lipase, GDXG, putative histidine active site
Lipase_GDXG_HIS_AS
Active_site
23,697
false
false
The following lipolytic enzymes are evolutionary related: Mammalian hormone sensitive lipase (HSL). In adipose tissue and heart, HSL primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone productio...
[ "GO:0016787" ]
[ "hydrolase activity" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS01173" ]
[ "LIPASE_GDXG_HIS" ]
[ 23697 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.1.1", "PDOC00903", "R-HSA-163560", "R-HSA-9841922", "R-MMU-211945", "R-RNO-211945" ]
[ "EC:3.1.1", "PROSITEDOC:PDOC00903", "REACTOME:R-HSA-163560", "REACTOME:R-HSA-9841922", "REACTOME:R-MMU-211945", "REACTOME:R-RNO-211945" ]
6
[ "2o7r", "2o7v", "2zsh", "2zsi", "3dnm", "3ebl", "3ed1", "3fak", "3g9t", "3g9u", "3g9z", "3h17", "3h18", "3h19", "3h1a", "3h1b", "3k6k", "3l1h", "3l1i", "3l1j", "3v9a", "4krx", "4kry", "4ob6", "4ob7", "4ob8", "4ou4", "4ou5", "4wy8", "4xvc", "4ypv", "5gmr"...
55
[ "PUB00001111" ]
[ "1907455" ]
[ "Nucleotide sequence of the lipase gene lip2 from the antarctic psychrotroph Moraxella TA144 and site-specific mutagenesis of the conserved serine and histidine residues." ]
[ 1991 ]
1
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Sym plasmid", "Viruses", "unclassified sequences" ]
[ 195, 13526, 9785, 1, 9, 181 ]
6
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 18, 2, 19, 6, 1, 6, 5, 1, 23, 8, 34 ]
11
true
Active_site
Lipase, GDXG, putative histidine active site
Lipase, GDXG, putative histidine active site
Lipase_GDXG_HIS_AS
7
IPR002169
2,169
Peptidase M9A/M9B, collagenase, bacterial
Peptidase_M9A/M9B
Family
2,902
false
false
Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation, which is usually zinc but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidase...
[ "GO:0004222", "GO:0008270", "GO:0006508", "GO:0005576" ]
[ "metalloendopeptidase activity", "zinc ion binding", "proteolysis", "extracellular region" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PFAM", "PRINTS" ]
[ "PF01752", "PR00931" ]
[ "Peptidase_M9", "MICOLLPTASE" ]
[ 2902, 2765 ]
2
[ "EC" ]
[ "3.4.24.3" ]
[ "EC:3.4.24.3" ]
1
[ "2y3u", "2y50", "2y6i", "4ar1", "4ar8", "4ar9", "4are", "4arf", "5o7e", "7esi", "7vlz", "7wss", "7xeb", "7z5u", "7zbv", "7zoc", "8jt1", "9l5o" ]
18
[ "PUB00002239", "PUB00003579" ]
[ "8282691", "7674922" ]
[ "Purification and characterization of Clostridium perfringens 120-kilodalton collagenase and nucleotide sequence of the corresponding gene.", "Evolutionary families of metallopeptidases." ]
[ 1994, 1995 ]
2
[]
[]
0
0
null
[ "Bacteria", "Candidatus Naiadarchaeum limnaeum", "Eukaryota", "Euproctis pseudoconspersa nucleopolyhedrovirus", "ecological metagenomes" ]
[ 2889, 1, 9, 1, 2 ]
5
[]
[]
0
true
Family
Peptidase M9A/M9B, collagenase, bacterial
Peptidase M9A/M9B, collagenase, bacterial
Peptidase_M9A/M9B
4
IPR002172
2,172
Low-density lipoprotein (LDL) receptor class A repeat
LDrepeatLR_classA_rpt
Repeat
97,127
false
false
This entry represents the LDLR class A (cysteine-rich) repeat, which contains 6 disulphide-bound cysteines and a highly conserved cluster of negatively charged amino acids, of which many are clustered on one face of the module [ ]. In LDL receptors, the class A domains form the binding site for LDL and calcium. The aci...
[ "GO:0005515" ]
[ "protein binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS", "PROFILE", "SMART", "CDD" ]
[ "PF00057", "PR00261", "PS50068", "SM00192", "cd00112" ]
[ "Ldl_recept_a", "LDLRECEPTOR", "LDLRA_2", "LDLa", "LDLa" ]
[ 82839, 51804, 91373, 91313, 93318 ]
5
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00929", "R-BTA-166665", "R-BTA-8856825", "R-BTA-8856828", "R-BTA-8964026", "R-BTA-8964038", "R-BTA-9758890", "R-BTA-977606", "R-CFA-444821", "R-DME-9758890", "R-DRE-201556", "R-DRE-9842663", "R-DRE-9851151", "R-GGA-8866376", "R-GGA-8866427", "R-HSA-1442490", "R-HSA-1474228", "...
[ "PROSITEDOC:PDOC00929", "REACTOME:R-BTA-166665", "REACTOME:R-BTA-8856825", "REACTOME:R-BTA-8856828", "REACTOME:R-BTA-8964026", "REACTOME:R-BTA-8964038", "REACTOME:R-BTA-9758890", "REACTOME:R-BTA-977606", "REACTOME:R-CFA-444821", "REACTOME:R-DME-9758890", "REACTOME:R-DRE-201556", "REACTOME:R-DR...
119
[ "1ajj", "1cr8", "1d2j", "1d2l", "1f5y", "1f8z", "1j8e", "1jrf", "1k7b", "1ldl", "1ldr", "1n7d", "1v9u", "1xfe", "2fcw", "2fyj", "2fyl", "2gtl", "2i1p", "2jm4", "2knx", "2kny", "2kri", "2lgp", "2m0p", "2m7p", "2m96", "2xrc", "3a7q", "3dpr", "3m0c", "3ojy"...
164
[ "PUB00000798", "PUB00003391", "PUB00004868", "PUB00017008", "PUB00017009", "PUB00042617" ]
[ "6091915", "9790844", "7603991", "3513311", "3494949", "17457719" ]
[ "The human LDL receptor: a cysteine-rich protein with multiple Alu sequences in its mRNA.", "An extracellular beta-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursor, and extracellular matrix components.", "Three-dimensional structure of a cyst...
[ 1984, 1998, 1995, 1986, 1987, 2007 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 17, 125, 96963, 4, 18 ]
5
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 42, 259, 138, 235, 151, 166, 1 ]
7
true
Repeat
Low-density lipoprotein (LDL) receptor class A repeat
Low-density lipoprotein (LDL) receptor class A repeat
LDrepeatLR_classA_rpt
5
IPR002173
2,173
Carbohydrate/purine kinase, PfkB, conserved site
Carboh/pur_kinase_PfkB_CS
Conserved_site
116,726
false
false
It has been shown [ , , ] that the following carbohydrate and purine kinases are evolutionary related and can be grouped into a single family, which is known [ ] as the 'pfkB family': Fructokinase ( ) (gene scrK). 6-phosphofructokinase isozyme 2 ( ) (phosphofructokinase-2) (gene pfkB). pfkB is a minor phosphofructokina...
[ "GO:0016301" ]
[ "kinase activity" ]
[ "molecular_function" ]
1
[ "PROSITE", "PROSITE" ]
[ "PS00583", "PS00584" ]
[ "PFKB_KINASES_1", "PFKB_KINASES_2" ]
[ 43513, 96906 ]
2
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.1", "PDOC00504", "R-DDI-70350", "R-HSA-71336", "R-HSA-74217", "R-HSA-9755088", "R-MMU-71336", "R-MMU-74217", "R-MMU-9755088", "R-RNO-74217", "R-RNO-9755088", "R-SCE-71336", "R-SCE-74217", "R-SCE-9755088", "R-SPO-71336", "R-SPO-74217", "R-SPO-9755088" ]
[ "EC:2.7.1", "PROSITEDOC:PDOC00504", "REACTOME:R-DDI-70350", "REACTOME:R-HSA-71336", "REACTOME:R-HSA-74217", "REACTOME:R-HSA-9755088", "REACTOME:R-MMU-71336", "REACTOME:R-MMU-74217", "REACTOME:R-MMU-9755088", "REACTOME:R-RNO-74217", "REACTOME:R-RNO-9755088", "REACTOME:R-SCE-71336", "REACTOME:...
17
[ "1bx4", "1dgm", "1gqt", "1lii", "1lij", "1lik", "1lio", "1rk2", "1rka", "1rkd", "1rks", "1tyy", "1tz3", "1tz6", "1v19", "1v1a", "1v1b", "1v1s", "1vm7", "2a9y", "2a9z", "2aa0", "2ab8", "2abq", "2abs", "2ajr", "2awd", "2c49", "2c4e", "2f02", "2fv7", "2i6a"...
174
[ "PUB00001797", "PUB00002140", "PUB00004930" ]
[ "2174811", "1850730", "1981619" ]
[ "Nucleotide sequence and analysis of the Vibrio alginolyticus sucrose uptake-encoding region.", "Nucleotide sequence of the Rhodobacter capsulatus fruK gene, which encodes fructose-1-phosphate kinase: evidence for a kinase superfamily including both phosphofructokinases of Escherichia coli.", "Sequence similari...
[ 1990, 1991, 1990 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 1626, 95641, 13, 18161, 1285 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 72, 2, 7, 8, 18, 6, 3, 3, 28, 8, 2, 3, 71 ]
13
true
Conserved_site
Carbohydrate/purine kinase, PfkB, conserved site
Carbohydrate/purine kinase, PfkB, conserved site
Carboh/pur_kinase_PfkB_CS
8
IPR002175
2,175
Endothelin receptor A
ETA_rcpt
Family
1,127
false
false
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...
[ "GO:0004962", "GO:0007186", "GO:0008217", "GO:0042310", "GO:0016020" ]
[ "endothelin receptor activity", "G protein-coupled receptor signaling pathway", "regulation of blood pressure", "vasoconstriction", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "cellular_component" ]
5
[ "PRINTS" ]
[ "PR00570" ]
[ "ENDOTHELINAR" ]
[ 1127 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "219", "R-BTA-375276", "R-BTA-416476", "R-HSA-375276", "R-HSA-416476", "R-MMU-375276", "R-MMU-416476", "R-RNO-375276", "R-RNO-416476" ]
[ "IUPHAR:219", "REACTOME:R-BTA-375276", "REACTOME:R-BTA-416476", "REACTOME:R-HSA-375276", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-416476" ]
9
[ "8hcq", "8xvi", "8xvj", "8xvk", "8xvl" ]
5
[ "PUB00000131", "PUB00001510", "PUB00002477", "PUB00004960", "PUB00004961", "PUB00053635", "PUB00063437", "PUB00063438", "PUB00063439", "PUB00063440", "PUB00063441", "PUB00063442", "PUB00063443", "PUB00063444", "PUB00063445", "PUB00063446", "PUB00063447", "PUB00063448", "PUB000634...
[ "2111655", "1916094", "2830256", "8386361", "8170923", "12679517", "2451132", "11264479", "11984741", "16529555", "1331845", "16340664", "8480469", "8466176", "1847708", "2156267", "12037137", "11067800", "9239759", "1351106", "18758495", "1719979", "1849646", "1710450"...
[ "G proteins in signal transduction.", "Endothelins.", "G protein involvement in receptor-effector coupling.", "Design of a discriminating fingerprint for G-protein-coupled receptors.", "Fingerprinting G-protein-coupled receptors.", "The G protein-coupled receptor repertoires of human and mouse.", "A nov...
[ 1990, 1991, 1988, 1993, 1994, 2003, 1988, 2001, 2002, 2006, 1992, 2006, 1993, 1993, 1991, 1990, 2002, 2000, 1997, 1992, 2008, 1991, 1991, 1991, 1995, 1995, 1997, 1994, 2005, 2009, 2006, 2013 ]
32
[ "IPR000499" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 1127 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 1, 1, 8 ]
4
true
Family
Endothelin receptor A
Endothelin receptor A
ETA_rcpt
9
IPR002178
2,178
PTS EIIA type-2 domain
PTS_EIIA_type-2_dom
Domain
59,565
false
false
The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [ , ] is a major carbohydrate transport system in bacteria. The PTS catalyses the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is the following: a phosp...
[]
[]
[]
0
[ "PFAM", "PROSITE", "PROFILE", "CDD" ]
[ "PF00359", "PS00372", "PS51094", "cd00211" ]
[ "PTS_EIIA_2", "PTS_EIIA_TYPE_2_HIS", "PTS_EIIA_TYPE_2", "PTS_IIA_fru" ]
[ 59099, 26956, 59315, 48641 ]
4
[ "GP", "PROSITEDOC" ]
[ "GenProp0119", "PDOC00528" ]
[ "GP:GenProp0119", "PROSITEDOC:PDOC00528" ]
2
[ "1a3a", "1a6j", "1j6t", "1xiz", "2a0j", "2few", "2oq3", "2oqt", "3bjv", "3lf6", "3oxp", "3t43", "3urr", "4gqx", "4m62", "4m8q", "4odx", "5sy8", "5t29", "5t5b", "5t6l", "5t80", "5t85", "5tfw", "6mto", "6mtq", "8sx3", "8tzn", "8tzw", "8u03", "8u08", "8v2e"...
34
[ "PUB00000073", "PUB00002162", "PUB00003612", "PUB00006380", "PUB00017027", "PUB00017028", "PUB00017925", "PUB00017926", "PUB00017927" ]
[ "2197982", "1537788", "8246840", "9261069", "7815935", "11361063", "15667312", "1911744", "8676384" ]
[ "The bacterial phosphoenolpyruvate: glycose phosphotransferase system.", "Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.", "Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria.", "The structure of en...
[ 1990, 1992, 1993, 1997, 1994, 2001, 2005, 1991, 1996 ]
9
[]
[ "IPR004715" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 139, 58818, 211, 397 ]
4
[ "Escherichia coli (strain K12)" ]
[ 12 ]
1
true
Domain
PTS EIIA type-2 domain
PTS EIIA type-2 domain
PTS_EIIA_type-2_dom
2
IPR002180
2,180
Lumazine/riboflavin synthase
LS/RS
Family
27,690
false
false
6,7-dimethyl-8-ribityllumazine synthase (lumazine synthase, LS), catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate, the penultimate step in the biosynthesis of riboflavin.
[ "GO:0009231", "GO:0009349" ]
[ "riboflavin biosynthetic process", "riboflavin synthase complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM" ]
[ "PF00885" ]
[ "DMRL_synthase" ]
[ 27690 ]
1
[ "EC", "GP", "METACYC", "METACYC" ]
[ "2.5.1.78", "GenProp1734", "PWY-6167", "PWY-6168" ]
[ "EC:2.5.1.78", "GP:GenProp1734", "METACYC:PWY-6167", "METACYC:PWY-6168" ]
4
[ "1c2y", "1c41", "1di0", "1ejb", "1hqk", "1kyv", "1kyx", "1kyy", "1kz1", "1kz4", "1kz6", "1kz9", "1nqu", "1nqv", "1nqw", "1nqx", "1rvv", "1t13", "1w19", "1w29", "1xn1", "1zis", "2a57", "2a58", "2a59", "2b98", "2b99", "2c92", "2c94", "2c97", "2c9b", "2c9d"...
73
[ "PUB00043427", "PUB00043428" ]
[ "18298940", "18331058" ]
[ "Biosynthesis of vitamin B2: Structure and mechanism of riboflavin synthase.", "A new series of N-[2,4-dioxo-6-d-ribitylamino-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid derivatives as inhibitors of lumazine synthase and riboflavin synthase: design, synthesis, biochemical evaluation, crystallography, and mecha...
[ 2008, 2008 ]
2
[]
[ "IPR006399", "IPR034964" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1158, 23002, 2987, 4, 539 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 3, 1, 1, 3, 1, 1, 14 ]
7
true
Family
Lumazine/riboflavin synthase
Lumazine/riboflavin synthase
LS/RS
7
IPR002181
2,181
Fibrinogen, alpha/beta/gamma chain, C-terminal globular domain
Fibrinogen_a/b/g_C_dom
Domain
57,958
false
false
This entry represents the C-terminal globular D domain of the alpha, beta and gamma chains. These domains are related to domains in other proteins: in the Parastichopus parvimensis (Sea cucumber) fibrogen-like FreP-A and FreP-B proteins; in the C terminus of the Drosophila scabrous protein that is involved in the regul...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART", "CDD" ]
[ "PF00147", "PS51406", "SM00186", "cd00087" ]
[ "Fibrinogen_C", "FIBRINOGEN_C_2", "FBG", "FReD" ]
[ 49860, 56702, 45785, 37585 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00445", "R-BTA-166662", "R-BTA-166663", "R-BTA-210993", "R-BTA-2129379", "R-BTA-2855086", "R-BTA-5673001", "R-BTA-6798695", "R-BTA-8963889", "R-BTA-9762292", "R-CFA-210993", "R-HSA-114608", "R-HSA-1236974", "R-HSA-140875", "R-HSA-166058", "R-HSA-166662", "R-HSA-166663", "R-HSA...
[ "PROSITEDOC:PDOC00445", "REACTOME:R-BTA-166662", "REACTOME:R-BTA-166663", "REACTOME:R-BTA-210993", "REACTOME:R-BTA-2129379", "REACTOME:R-BTA-2855086", "REACTOME:R-BTA-5673001", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-8963889", "REACTOME:R-BTA-9762292", "REACTOME:R-CFA-210993", "REACTOME:R-HS...
91
[ "1deq", "1ei3", "1fib", "1fic", "1fid", "1fza", "1fzb", "1fzc", "1fzd", "1fze", "1fzf", "1fzg", "1jc9", "1lt9", "1ltj", "1lwu", "1m1j", "1n73", "1n86", "1n8e", "1re3", "1re4", "1rf0", "1rf1", "1z3s", "1z3u", "2d39", "2ffd", "2fib", "2gy7", "2h43", "2hlo"...
121
[ "PUB00016231", "PUB00016232", "PUB00016233", "PUB00016234", "PUB00017188" ]
[ "12799374", "11460466", "11593005", "12396010", "15837518" ]
[ "Identification of a novel binding site for platelet integrins alpha IIb beta 3 (GPIIbIIIa) and alpha 5 beta 1 in the gamma C-domain of fibrinogen.", "The structure and biological features of fibrinogen and fibrin.", "Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolution...
[ 2003, 2001, 2001, 2002, 2005 ]
5
[]
[]
0
0
null
[ "Bacteria", "Caudoviricetes", "Eukaryota", "Nanobdellati", "metagenomes" ]
[ 466, 4, 57484, 2, 2 ]
5
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 206, 34, 126, 82, 140 ]
6
true
Domain
Fibrinogen, alpha/beta/gamma chain, C-terminal globular domain
Fibrinogen, alpha/beta/gamma chain, C-terminal globular domain
Fibrinogen_a/b/g_C_dom
1
IPR002182
2,182
NB-ARC
NB-ARC
Domain
163,453
false
false
This is the NB-ARC domain, a novel signalling motif found in bacteria and eukaryotes, shared by plant resistance gene products and regulators of cell death in animals [ ]. This domain has been structurally characterised in the human protein apoptotic protease-activating factor 1 (Apaf-1) [ ]. It contains the three-laye...
[ "GO:0043531" ]
[ "ADP binding" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF00931" ]
[ "NB-ARC" ]
[ 163453 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-DME-111458", "R-DME-111459", "R-DME-6798695", "R-DME-9627069", "R-DRE-111458", "R-DRE-111459", "R-DRE-6798695", "R-DRE-9627069", "R-HSA-111458", "R-HSA-111459", "R-HSA-111463", "R-HSA-111464", "R-HSA-6798695", "R-HSA-6803207", "R-HSA-8953750", "R-HSA-9627069", "R-MMU-111458", "R...
[ "REACTOME:R-DME-111458", "REACTOME:R-DME-111459", "REACTOME:R-DME-6798695", "REACTOME:R-DME-9627069", "REACTOME:R-DRE-111458", "REACTOME:R-DRE-111459", "REACTOME:R-DRE-6798695", "REACTOME:R-DRE-9627069", "REACTOME:R-HSA-111458", "REACTOME:R-HSA-111459", "REACTOME:R-HSA-111463", "REACTOME:R-HSA...
24
[ "1z6t", "2a5y", "3j2t", "3j9k", "3j9l", "3jbt", "3lqq", "3lqr", "3sfz", "3shf", "4m9s", "4m9x", "4m9y", "4m9z", "4v4l", "5jul", "5juy", "5wve", "6j5t", "6j5u", "6j5v", "6j5w", "6j6i", "6mfv", "6s2p", "7crb", "7crc", "7dfv", "7jlu", "7jlv", "7jlx", "7xc2"...
61
[ "PUB00006218", "PUB00032726" ]
[ "9545207", "15829969" ]
[ "The NB-ARC domain: a novel signalling motif shared by plant resistance gene products and regulators of cell death in animals.", "Structure of the apoptotic protease-activating factor 1 bound to ADP." ]
[ 1998, 2005 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacillus phage 0105phi7-2", "Bacteria", "Eukaryota", "metagenomes" ]
[ 60, 1, 17467, 145903, 22 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 1254, 1, 7, 3, 4, 4, 1, 1441, 10, 531 ]
10
true
Domain
NB-ARC
NB-ARC
NB-ARC
6
IPR002183
2,183
Interleukin-3
IL-3
Family
117
false
false
Interleukin-3 (IL3) is a cytokine that regulates blood-cell production by controlling the production, differentiation and function of granulocytes and macrophages [ , ]. The protein, which exists in vivo as a monomer, is produced in activated T-cells and mast cells [ , ], and is activated by the cleavage of an N-termin...
[ "GO:0005135", "GO:0008083", "GO:0006955", "GO:0005576" ]
[ "interleukin-3 receptor binding", "growth factor activity", "immune response", "extracellular region" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PFAM", "PIRSF", "PRINTS", "PANTHER" ]
[ "PF02059", "PIRSF001939", "PR00430", "PTHR48489" ]
[ "IL3", "IL-3", "INTERLEUKIN3", "" ]
[ 117, 55, 100, 114 ]
4
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-512988", "R-BTA-5673001", "R-BTA-912526", "R-CFA-512988", "R-CFA-5673001", "R-CFA-912526", "R-HSA-512988", "R-HSA-5673001", "R-HSA-8939247", "R-HSA-912526", "R-MMU-512988", "R-MMU-5673001", "R-MMU-912526", "R-RNO-512988", "R-RNO-5673001", "R-RNO-912526" ]
[ "REACTOME:R-BTA-512988", "REACTOME:R-BTA-5673001", "REACTOME:R-BTA-912526", "REACTOME:R-CFA-512988", "REACTOME:R-CFA-5673001", "REACTOME:R-CFA-912526", "REACTOME:R-HSA-512988", "REACTOME:R-HSA-5673001", "REACTOME:R-HSA-8939247", "REACTOME:R-HSA-912526", "REACTOME:R-MMU-512988", "REACTOME:R-MMU...
16
[ "1jli", "2l3o", "5uv8", "5uwc", "6nmy" ]
5
[ "PUB00001758", "PUB00003991" ]
[ "3497843", "2413359" ]
[ "Characterization of a human multilineage-colony-stimulating factor cDNA clone identified by a conserved noncoding sequence in mouse interleukin-3.", "Constitutive synthesis of interleukin-3 by leukaemia cell line WEHI-3B is due to retroviral insertion near the gene." ]
[ 1987, 1985 ]
2
[]
[]
0
0
null
[ "Eutheria" ]
[ 117 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 3, 4 ]
3
true
Family
Interleukin-3
Interleukin-3
IL-3
8
IPR002185
2,185
Dopamine D4 receptor
Dopamine_D4_rcpt
Family
1,193
false
false
Dopamine receptors are members of the rhodopsin-like G-protein coupled receptor family and are prominent in the vertebrate central nervous system (CNS). Dysfunction of dopaminergic neurotransmission in the CNS has been implicated in a variety of neuropsychiatric disorders [ ], including social phobia [ ], Tourette's sy...
[ "GO:0004952", "GO:0007195", "GO:0005886" ]
[ "dopamine neurotransmitter receptor activity", "adenylate cyclase-inhibiting dopamine receptor signaling pathway", "plasma membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00569" ]
[ "DOPAMINED4R" ]
[ 1193 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "217", "R-HSA-390651", "R-HSA-418594", "R-MMU-390651", "R-MMU-418594", "R-RNO-390651", "R-RNO-418594" ]
[ "IUPHAR:217", "REACTOME:R-HSA-390651", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-390651", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-390651", "REACTOME:R-RNO-418594" ]
7
[ "5wiu", "5wiv", "6iql", "8iru" ]
4
[ "PUB00064281", "PUB00064282", "PUB00064283", "PUB00064284", "PUB00064285", "PUB00064286", "PUB00064287", "PUB00064288", "PUB00064289", "PUB00064290", "PUB00064291", "PUB00064292", "PUB00064293", "PUB00067001", "PUB00067010", "PUB00067011" ]
[ "15148138", "10698826", "16613557", "17017512", "12555236", "16961425", "11920678", "9633679", "16433053", "14060771", "1060115", "12836695", "9457173", "16458973", "8152334", "9323127" ]
[ "The neurobiology of dopamine signaling.", "Low dopamine D(2) receptor binding potential in social phobia.", "Dopamine and the diseased brain.", "The nigrostriatal DA pathway and Parkinson's disease.", "Relationship between functional dopamine D2 and D3 receptors gene polymorphisms and neuroleptic malignant...
[ 2004, 2000, 2006, 2006, 2003, 2006, 2002, 1998, 2005, 1963, 1975, 2003, 1998, 2006, 1994, 1997 ]
16
[ "IPR000929" ]
[]
1
0
1
[ "Vertebrata" ]
[ 1193 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 8, 1, 1, 3 ]
4
true
Family
Dopamine D4 receptor
Dopamine D4 receptor
Dopamine_D4_rcpt
8
IPR002186
2,186
Neocarzinostatin-like
Neocarzinostatin_fam
Family
771
false
false
This family is comprised of antitumour antibiotic chromoproteins, as represented by neocarzinostatin [ ]. These chromoproteins consist of a noncovalently bound, labile enediyne chromophore and its stabilising carrier apoprotein. The protein component of the chromophore displays an unusual bicyclic dienediyne structure....
[ "GO:0003677", "GO:0006952" ]
[ "DNA binding", "defense response" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PRINTS" ]
[ "PF00960", "PR01885" ]
[ "Neocarzinostat", "MACROMOMYCIN" ]
[ 763, 181 ]
2
[]
[]
[]
0
[ "1acx", "1akp", "1hzk", "1hzl", "1j48", "1j5h", "1j5i", "1nco", "1noa", "1o5p", "2cbm", "2cbo", "2cbq", "2cbt", "2g0k", "2g0l", "2mcm", "4jw3", "7qhm", "7qho" ]
20
[ "PUB00005172", "PUB00013962", "PUB00013963" ]
[ "8235619", "11491295", "9383447" ]
[ "Crystal structure of neocarzinostatin, an antitumor protein-chromophore complex.", "Solution structures of C-1027 apoprotein and its complex with the aromatized chromophore.", "The proteolytic specificity of the natural enediyne-containing chromoproteins is unique to each chromoprotein." ]
[ 1993, 2001, 1995 ]
3
[]
[]
0
0
null
[ "Actinomycetota", "Panicoideae", "freshwater metagenome" ]
[ 746, 8, 17 ]
3
[ "Zea mays" ]
[ 3 ]
1
true
Family
Neocarzinostatin-like
Neocarzinostatin-like
Neocarzinostatin_fam
7
IPR002187
2,187
Nitrogen regulatory protein PII
N-reg_PII
Family
33,677
false
false
In Gram-negative bacteria, the activity and concentration of glutamine synthetase (GS) is regulated in response to nitrogen source availability. PII, a tetrameric protein encoded by the glnB gene, is a component of the adenylation cascade involved in the regulation of GS activity [ ]. In nitrogen-limiting conditions, w...
[ "GO:0030234", "GO:0006808" ]
[ "enzyme regulator activity", "regulation of nitrogen utilization" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PIRSF", "PRINTS", "PROFILE", "PANTHER", "SMART" ]
[ "PF00543", "PIRSF039144", "PR00340", "PS51343", "PTHR30115", "SM00938" ]
[ "P-II", "GlnB", "PIIGLNB", "PII_GLNB_DOM", "", "P-II" ]
[ 33405, 18880, 29022, 31692, 28234, 30866 ]
6
[ "PROSITEDOC" ]
[ "PDOC00439" ]
[ "PROSITEDOC:PDOC00439" ]
1
[ "1gnk", "1hwu", "1pil", "1qy7", "1ufl", "1ul3", "1v3r", "1v3s", "1v9o", "1vfj", "2cz4", "2eg1", "2eg2", "2gnk", "2gw8", "2j9c", "2j9d", "2j9e", "2jj4", "2ns1", "2nuu", "2o66", "2o67", "2pii", "2rd5", "2v5h", "2xbp", "2xg8", "2xul", "2xzw", "2z0g", "3bzq"...
103
[ "PUB00001837", "PUB00002236", "PUB00003738", "PUB00005081", "PUB00047830", "PUB00059047" ]
[ "7904973", "8282685", "1702507", "2068380", "17203075", "22039461" ]
[ "Cloning and organization of the abc and mdl genes of Escherichia coli: relationship to eukaryotic multidrug resistance.", "The nitrogen-regulated Bacillus subtilis nrgAB operon encodes a membrane protein and a protein highly similar to the Escherichia coli glnB-encoded PII protein.", "Characterization of three...
[ 1993, 1994, 1990, 1991, 2007, 2011 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Podoviridae sp. ctxJ29", "unclassified sequences" ]
[ 1368, 30815, 632, 1, 861 ]
5
[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica" ]
[ 6, 2, 1 ]
3
true
Family
Nitrogen regulatory protein PII
Nitrogen regulatory protein PII
N-reg_PII
8
IPR002189
2,189
F-actin-capping protein subunit alpha
CapZ_alpha
Family
6,794
false
false
The F-actin capping protein binds in a calcium-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike gelsolin and severin this protein does not sever actin filaments. The F-actin capping protein is a heterodimer composed of two unrela...
[ "GO:0051016", "GO:0008290" ]
[ "barbed-end actin filament capping", "F-actin capping protein complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF01267", "PR00191", "PTHR10653" ]
[ "F-actin_cap_A", "FACTINCAPA", "" ]
[ 6791, 6027, 6579 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-2132295", "R-BTA-3371497", "R-BTA-6807878", "R-BTA-6811436", "R-BTA-879415", "R-BTA-983231", "R-CEL-6807878", "R-CEL-6811436", "R-CEL-983231", "R-DDI-6807878", "R-DDI-983231", "R-DME-3371497", "R-DME-6807878", "R-DME-6811436", "R-DME-983231", "R-GGA-3371497", "R-GGA-6807878", ...
[ "REACTOME:R-BTA-2132295", "REACTOME:R-BTA-3371497", "REACTOME:R-BTA-6807878", "REACTOME:R-BTA-6811436", "REACTOME:R-BTA-879415", "REACTOME:R-BTA-983231", "REACTOME:R-CEL-6807878", "REACTOME:R-CEL-6811436", "REACTOME:R-CEL-983231", "REACTOME:R-DDI-6807878", "REACTOME:R-DDI-983231", "REACTOME:R-...
47
[ "1izn", "2kxp", "2kz7", "3aa0", "3aa1", "3aa6", "3aa7", "3aaa", "3aae", "3lk2", "3lk3", "3lk4", "4akr", "5adx", "5afu", "5nw4", "6f1t", "6f1u", "6f38", "6f3a", "6znl", "7a0h", "7ccc", "7ds2", "7ds3", "7ds4", "7ds6", "7ds8", "7dsa", "7dsb", "7pdz", "7t5q"...
45
[ "PUB00000981", "PUB00002626", "PUB00054152", "PUB00071410" ]
[ "1711931", "2341404", "19922875", "16143599" ]
[ "Variant cDNAs encoding proteins similar to the alpha subunit of chicken CapZ.", "Beta-actinin is equivalent to Cap Z protein.", "The Arp2/3 activator WASH controls the fission of endosomes through a large multiprotein complex.", "Mutations in the Drosophila orthologs of the F-actin capping protein alpha- and...
[ 1991, 1990, 2009, 2005 ]
4
[]
[]
0
0
null
[ "Eukaryota" ]
[ 6794 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 9, 1, 2, 1, 12, 16, 1, 4, 19, 1, 1, 18 ]
12
true
Family
F-actin-capping protein subunit alpha
F-actin-capping protein subunit alpha
CapZ_alpha
3
IPR002190
2,190
MAGE homology domain
MHD_dom
Domain
10,473
false
false
The first mammalian members of the MAGE (melanoma-associated antigen) gene family were originally described as completely silent in normal adult tissues, with the exception of male germ cells and, for some of them, placenta. By contrast, these genes were expressed in various kinds of tumors. However, other members of t...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART" ]
[ "PF01454", "PS50838", "SM01373" ]
[ "MAGE", "MAGE", "MAGE" ]
[ 9952, 9045, 10116 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC50838", "R-HSA-114608", "R-HSA-193648", "R-HSA-3108214", "R-HSA-418889", "R-HSA-6785807", "R-HSA-9768919", "R-MMU-3108214", "R-MMU-9768919", "R-RNO-9768919", "R-SCE-114608", "R-SCE-3108214", "R-SPO-114608", "R-SPO-3108214", "R-SSC-9768919" ]
[ "PROSITEDOC:PDOC50838", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-193648", "REACTOME:R-HSA-3108214", "REACTOME:R-HSA-418889", "REACTOME:R-HSA-6785807", "REACTOME:R-HSA-9768919", "REACTOME:R-MMU-3108214", "REACTOME:R-MMU-9768919", "REACTOME:R-RNO-9768919", "REACTOME:R-SCE-114608", "REACTOME:R-SC...
15
[ "2wa0", "4v0p", "5hvq", "5wy5", "6r7t", "6wjh", "7dg2", "7qcd", "7tve", "7uoa", "7ymd", "7yqh", "8hqs", "8i13", "8t9a", "8wjn", "9bd2", "9bd3" ]
18
[ "PUB00007179" ]
[ "11454705" ]
[ "An overview of the MAGE gene family with the identification of all human members of the family." ]
[ 2001 ]
1
[]
[]
0
0
null
[ "Archaea", "Chryseobacterium", "Eukaryota", "bird metagenome" ]
[ 8, 3, 10461, 1 ]
4
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "...
[ 11, 1, 2, 95, 74, 1, 2, 72, 1, 1, 8 ]
11
true
Domain
MAGE homology domain
MAGE homology domain
MHD_dom
4
IPR002191
2,191
Bacterial export protein family 3
Bac_export_3
Family
15,567
false
false
The fliL operon of Escherichia coli contains seven genes (including fliO, fliP, fliQ and fliR) involved in the biosynthesis and functioning of the flagellar organelle [ ]. The fliO, fliP, fliQ and fliR genes encode highly hydrophobic polypeptides. The fliQ gene product, a small integral membrane protein that contains t...
[ "GO:0009306", "GO:0016020" ]
[ "protein secretion", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PIRSF", "PRINTS", "PANTHER" ]
[ "PF01313", "PIRSF004669", "PR00952", "PTHR34040" ]
[ "Bac_export_3", "FliQ", "TYPE3IMQPROT", "" ]
[ 15567, 13791, 15453, 15496 ]
4
[]
[]
[]
0
[ "6f2d", "6pem", "6pep", "6q14", "6q15", "6q16", "6r69", "6r6b", "6rwy", "6s3l", "6s3r", "6s3s", "7agx", "7ah9", "7ahi", "7bin", "7cgo", "7e80", "7nvg", "8axk", "8wk3", "8wkk", "8wkq", "8wl2", "8wlh", "8wln", "8wlq", "8wlt", "8wo5", "8woe", "8z5s", "8z5u"...
35
[ "PUB00001240", "PUB00002241", "PUB00002255", "PUB00002272", "PUB00004254" ]
[ "8404849", "8282695", "8300512", "7814323", "9163424" ]
[ "Cognate gene clusters govern invasion of host epithelial cells by Salmonella typhimurium and Shigella flexneri.", "Molecular characterization, nucleotide sequence, and expression of the fliO, fliP, fliQ, and fliR genes of Escherichia coli.", "A low-Ca2+ response (LCR) secretion (ysc) locus lies within the lcrB...
[ 1993, 1994, 1994, 1995, 1997 ]
5
[]
[ "IPR006305", "IPR006306" ]
0
2
0
[ "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 15392, 9, 166 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Bacterial export protein family 3
Bacterial export protein family 3
Bac_export_3
3
IPR002192
2,192
Pyruvate phosphate dikinase, AMP/ATP-binding
PPDK_AMP/ATP-bd
Domain
38,934
false
false
This enzyme catalyses the reversible conversion of ATP to AMP, pyrophosphate and phosphoenolpyruvate (PEP) [ ]. This domain is present at the N terminus of some PEP-utilizing enzymes, and has been shown to be the AMP/ATP-binding domain [ ]. This domain is also found in Rifampicin phosphotransferase that catalyses the p...
[ "GO:0005524", "GO:0016301", "GO:0016310" ]
[ "ATP binding", "kinase activity", "phosphorylation" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PFAM" ]
[ "PF01326" ]
[ "PPDK_N" ]
[ 38934 ]
1
[ "EC", "GP" ]
[ "2.7.9", "GenProp1726" ]
[ "EC:2.7.9", "GP:GenProp1726" ]
2
[ "1dik", "1ggo", "1jde", "1kbl", "1kc7", "1vbg", "1vbh", "2dik", "2ols", "2r82", "2x0s", "5fbs", "5fbt", "5fbu", "5hv1", "5hv2", "5hv3", "5hv6", "5jvj", "5jvl", "5jvn", "5lu4", "8a8e", "9dae", "9goj", "9pzl" ]
26
[ "PUB00004887", "PUB00049284", "PUB00153683", "PUB00153684" ]
[ "8610096", "18052212", "24778229", "27001859" ]
[ "Swiveling-domain mechanism for enzymatic phosphotransfer between remote reaction sites.", "Swiveling domain mechanism in pyruvate phosphate dikinase.", "A rifamycin inactivating phosphotransferase family shared by environmental and pathogenic bacteria.", "Structural basis of rifampin inactivation by rifampin...
[ 1996, 2007, 2014, 2016 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1312, 31530, 5291, 11, 790 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 21, 1, 1, 14, 79 ]
5
true
Domain
Pyruvate phosphate dikinase, AMP/ATP-binding
Pyruvate phosphate dikinase, AMP/ATP-binding
PPDK_AMP/ATP-bd
3
IPR002194
2,194
Chaperonin TCP-1, conserved site
Chaperonin_TCP-1_CS
Conserved_site
42,584
false
false
The TCP-1 protein [ , ] (Tailless Complex Polypeptide 1) was first identified in mice where it is especially abundant in testis but present in all cell types. It has since been found and characterised in many other animal species, as well as in yeast, plants and protists. TCP-1 is a highly conserved protein of about 60...
[ "GO:0005524", "GO:0016887", "GO:0051082", "GO:0006457" ]
[ "ATP binding", "ATP hydrolysis activity", "unfolded protein binding", "protein folding" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
4
[ "PROSITE", "PROSITE", "PROSITE" ]
[ "PS00750", "PS00751", "PS00995" ]
[ "TCP1_1", "TCP1_2", "TCP1_3" ]
[ 36312, 35364, 36844 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00610", "R-BTA-390471", "R-BTA-6798695", "R-BTA-6814122", "R-BTA-9013418", "R-BTA-9013422", "R-CEL-390471", "R-CEL-6798695", "R-CEL-6814122", "R-DDI-390471", "R-DDI-6798695", "R-DDI-6814122", "R-DDI-9013418", "R-DDI-9013422", "R-DME-390471", "R-DME-6814122", "R-GGA-390471", "R...
[ "PROSITEDOC:PDOC00610", "REACTOME:R-BTA-390471", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-6814122", "REACTOME:R-BTA-9013418", "REACTOME:R-BTA-9013422", "REACTOME:R-CEL-390471", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-6814122", "REACTOME:R-DDI-390471", "REACTOME:R-DDI-6798695", "REACTOME:R-D...
46
[ "1a6d", "1a6e", "1q2v", "1q3q", "1q3r", "1q3s", "3aq1", "3iyf", "3iyg", "3izh", "3izi", "3izj", "3izk", "3izl", "3izm", "3izn", "3j02", "3j03", "3j1b", "3j1c", "3j1e", "3j1f", "3j3x", "3kfb", "3kfe", "3kfk", "3ko1", "3ktt", "3los", "3ruq", "3rus", "3ruv"...
134
[ "PUB00000756", "PUB00001019", "PUB00001034", "PUB00004112", "PUB00004124", "PUB00004127", "PUB00004129", "PUB00005432" ]
[ "7794526", "15335898", "7953530", "1836250", "1352040", "1352857", "1630492", "7846767" ]
[ "Primary structure of the thermosome from Thermoplasma acidophilum.", "TCP1 - molecular chaperonin of the cytoplasm?", "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin.", "A molecular chaperone from a thermophilic archaebacterium is related to the eukar...
[ 1995, 1992, 1994, 1991, 1992, 1992, 1992, 1994 ]
8
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences", "uncultured virus" ]
[ 2517, 235, 39739, 88, 5 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 24, 10, 10, 12, 52, 55, 7, 25, 42, 8, 8, 78 ]
12
true
Conserved_site
Chaperonin TCP-1, conserved site
Chaperonin TCP-1, conserved site
Chaperonin_TCP-1_CS
1
IPR002195
2,195
Dihydroorotase, conserved site
Dihydroorotase_CS
Conserved_site
35,861
false
false
This group contains a number of protein families, example are: Archaeal and bacterial dihydroorotase ( ) (DHOase) Allantoinase ( ) Dihydroorotase belongs to MEROPS peptidase family M38 (clan MJ), where it is classified as a non-peptidase homologue. DHOase catalyses the third step in the de novo biosynthesis of pyrimidi...
[ "GO:0016812" ]
[ "hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides" ]
[ "molecular_function" ]
1
[ "PROSITE", "PROSITE" ]
[ "PS00482", "PS00483" ]
[ "DIHYDROOROTASE_1", "DIHYDROOROTASE_2" ]
[ 21566, 31731 ]
2
[ "EC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.5.2.3", "PWY-5686", "PWY-7790", "PWY-7791", "PDOC00401", "R-CEL-500753", "R-DDI-500753", "R-DME-500753", "R-HSA-202433", "R-HSA-500753", "R-MMU-500753" ]
[ "EC:3.5.2.3", "METACYC:PWY-5686", "METACYC:PWY-7790", "METACYC:PWY-7791", "PROSITEDOC:PDOC00401", "REACTOME:R-CEL-500753", "REACTOME:R-DDI-500753", "REACTOME:R-DME-500753", "REACTOME:R-HSA-202433", "REACTOME:R-HSA-500753", "REACTOME:R-MMU-500753" ]
11
[ "1j79", "1xge", "1xrf", "1xrt", "2e25", "2eg6", "2eg7", "2eg8", "2gwn", "2z00", "2z24", "2z25", "2z26", "2z27", "2z28", "2z29", "2z2a", "2z2b", "3d6n", "3gri", "3hm7", "3jze", "3mjm", "3mpg", "3pnu", "4bjh", "4by3", "4c6b", "4c6c", "4c6d", "4c6e", "4c6f"...
96
[ "PUB00000720", "PUB00001777", "PUB00002652", "PUB00002839", "PUB00003725", "PUB00004994", "PUB00005645", "PUB00070199" ]
[ "8098212", "2570735", "1671037", "8163532", "2897615", "9144792", "1803816", "15278241" ]
[ "The evolutionary history of the first three enzymes in pyrimidine biosynthesis.", "Organization of the yeast URA2 gene: identification of a defective dihydroorotase-like domain in the multifunctional carbamoylphosphate synthetase-aspartate transcarbamylase complex.", "Dihydroorotase from Escherichia coli. Subs...
[ 1993, 1989, 1991, 1994, 1988, 1997, 1991, 2004 ]
8
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Homavirus sp.", "unclassified sequences" ]
[ 895, 27396, 6887, 1, 682 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 2, 2, 6, 3, 1, 5, 5, 3, 1, 7, 2, 1, 6 ]
13
true
Conserved_site
Dihydroorotase, conserved site
Dihydroorotase, conserved site
Dihydroorotase_CS
8
IPR002196
2,196
Glycoside hydrolase, family 24
Glyco_hydro_24
Family
16,870
false
false
Glycoside hydrolase family 24 comprises enzymes with only one known activity; lysozyme ( ). This entry includes Bacteriophage lambda lysozyme and Escherichia coli endolysin [ ]. Lysozyme helps to release mature phage particles from the cell wall by breaking down the peptidoglycan. The enzyme hydrolyses the 1,4-beta lin...
[ "GO:0003796", "GO:0009253", "GO:0016998" ]
[ "lysozyme activity", "peptidoglycan catabolic process", "cell wall macromolecule catabolic process" ]
[ "molecular_function", "biological_process", "biological_process" ]
3
[ "PFAM" ]
[ "PF00959" ]
[ "Phage_lysozyme" ]
[ 16870 ]
1
[ "CAZY", "EC" ]
[ "GH24", "3.2.1.17" ]
[ "CAZY:GH24", "EC:3.2.1.17" ]
2
[ "102l", "103l", "104l", "107l", "108l", "109l", "110l", "111l", "112l", "113l", "114l", "115l", "118l", "119l", "120l", "122l", "123l", "125l", "126l", "127l", "128l", "129l", "130l", "131l", "137l", "138l", "139l", "140l", "141l", "142l", "143l", "144l"...
808
[ "PUB00003216", "PUB00004082", "PUB00004870", "PUB00005266" ]
[ "3586019", "2234094", "7624375", "8535779" ]
[ "Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution.", "A mutant T4 lysozyme displays five different crystal conformations.", "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases." ]
[ 1987, 1990, 1995, 1995 ]
4
[]
[ "IPR001165", "IPR034690" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 3, 13177, 1177, 2398, 115 ]
5
[ "Escherichia coli (strain K12)" ]
[ 2 ]
1
true
Family
Glycoside hydrolase, family 24
Glycoside hydrolase, family 24
Glyco_hydro_24
1
IPR002197
2,197
DNA binding HTH domain, Fis-type
HTH_Fis
Domain
129,572
false
false
The Factor for Inversion Stimulation (FIS) protein is a regulator of bacterial functions, and binds specifically to weakly related DNA sequences [ , ]. It activates ribosomal RNA transcription, and is involved in upstream activation of rRNA promoters. The protein has been shown to play a role in the regulation of virul...
[ "GO:0043565" ]
[ "sequence-specific DNA binding" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS" ]
[ "PF02954", "PR01590" ]
[ "HTH_8", "HTHFIS" ]
[ 128088, 98341 ]
2
[]
[]
[]
0
[ "1etk", "1eto", "1etq", "1etv", "1etw", "1etx", "1ety", "1f36", "1fia", "1fip", "1ntc", "1ojl", "2m8g", "3e7l", "3fis", "3iv5", "3jr9", "3jra", "3jrb", "3jrc", "3jrd", "3jre", "3jrf", "3jrg", "3jrh", "3jri", "3rqi", "4fis", "4fth", "4ihv", "4ihw", "4ihx"...
54
[ "PUB00005701", "PUB00007180", "PUB00007181", "PUB00007182", "PUB00007183", "PUB00007184" ]
[ "1619650", "7536730", "11123690", "11532124", "9738943", "11183780" ]
[ "Crystal structure of the factor for inversion stimulation FIS at 2.0 A resolution.", "Sequence, regulation, and functions of fis in Salmonella typhimurium.", "Fis, a DNA nucleoid-associated protein, is involved in Salmonella typhimurium SPI-1 invasion gene expression.", "Role of the nucleoid-associated prote...
[ 1992, 1995, 2001, 2001, 1998, 2000 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 4, 127545, 210, 38, 1775 ]
5
[ "Escherichia coli (strain K12)" ]
[ 9 ]
1
true
Domain
DNA binding HTH domain, Fis-type
DNA binding HTH domain, Fis-type
HTH_Fis
5
IPR002201
2,201
Glycosyl transferase, family 9
Glyco_trans_9
Family
39,862
false
false
Glycosyltransferase family 9 comprises enzymes with two known activity; lipopolysaccharide N-acetylglucosaminyltransferase ( ), heptosyltransferase ( ). Heptosyltransferase I is thought to add L-glycero-D-manno-heptose to the inner 3-deoxy-D-manno-octulosonic acid (Kdo) residue of the lipopolysaccharide core [ ]. Hepto...
[ "GO:0016757" ]
[ "glycosyltransferase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "CDD" ]
[ "PF01075", "cd03789" ]
[ "Glyco_transf_9", "GT9_LPS_heptosyltransferase" ]
[ 39787, 34263 ]
2
[ "CAZY", "EC", "GP", "GP" ]
[ "GT9", "2.4.99", "GenProp1647", "GenProp1651" ]
[ "CAZY:GT9", "EC:2.4.99", "GP:GenProp1647", "GP:GenProp1651" ]
4
[ "1psw", "2gt1", "2h1f", "2h1h", "3tov", "4rap", "4rb4", "6dfe" ]
8
[ "PUB00003027", "PUB00006687", "PUB00009409", "PUB00151498", "PUB00151499", "PUB00151500" ]
[ "9446588", "11054112", "9334165", "25211077", "25293534", "25310236" ]
[ "Enzymatic synthesis of lipopolysaccharide in Escherichia coli. Purification and properties of heptosyltransferase i.", "Comparative functional characterization in vitro of heptosyltransferase I (WaaC) and II (WaaF) from Escherichia coli.", "A classification of nucleotide-diphospho-sugar glycosyltransferases ba...
[ 1998, 2000, 1997, 2014, 2015, 2014 ]
6
[]
[ "IPR011908", "IPR011910", "IPR011916", "IPR030929" ]
0
4
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 41, 38828, 105, 14, 874 ]
5
[ "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica" ]
[ 4, 3 ]
2
true
Family
Glycosyl transferase, family 9
Glycosyl transferase, family 9
Glyco_trans_9
7
IPR002202
2,202
Hydroxymethylglutaryl-CoA reductase, class I/II
HMG_CoA_Rdtase
Family
16,178
false
false
There are two distinct classes of hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase enzymes: class I consists of eukaryotic and most archaeal enzymes ( ), while class II consists of prokaryotic enzymes ( ) [ , ]. Class I HMG-CoA reductases catalyse the NADP-dependent synthesis of mevalonate from 3-hydroxy-3-methylgl...
[ "GO:0004420", "GO:0015936" ]
[ "hydroxymethylglutaryl-CoA reductase (NADPH) activity", "coenzyme A metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PRINTS", "PROFILE", "PANTHER" ]
[ "PF00368", "PR00071", "PS50065", "PTHR10572" ]
[ "HMG-CoA_red", "HMGCOARDTASE", "HMG_COA_REDUCTASE_4", "" ]
[ 15495, 13318, 16048, 15470 ]
4
[ "EC", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.1.1.34", "GenProp1432", "PWY-6174", "PWY-7391", "PWY-7524", "PWY-8125", "PWY-922", "PDOC00064", "R-BTA-191273", "R-DDI-191273", "R-DME-191273", "R-HSA-191273", "R-HSA-1989781", "R-HSA-2426168", "R-HSA-9619665", "R-MMU-191273", "R-RNO-191273", "R-SCE-191273", "R-SPO-191273" ]
[ "EC:1.1.1.34", "GP:GenProp1432", "METACYC:PWY-6174", "METACYC:PWY-7391", "METACYC:PWY-7524", "METACYC:PWY-8125", "METACYC:PWY-922", "PROSITEDOC:PDOC00064", "REACTOME:R-BTA-191273", "REACTOME:R-DDI-191273", "REACTOME:R-DME-191273", "REACTOME:R-HSA-191273", "REACTOME:R-HSA-1989781", "REACTOM...
19
[ "1dq8", "1dq9", "1dqa", "1hw8", "1hw9", "1hwi", "1hwj", "1hwk", "1hwl", "1qax", "1qay", "1r31", "1r7i", "1t02", "2q1l", "2q6b", "2q6c", "2r4f", "3bgl", "3cct", "3ccw", "3ccz", "3cd0", "3cd5", "3cd7", "3cda", "3cdb", "3qae", "3qau", "4i4b", "4i56", "4i64"...
54
[ "PUB00019711", "PUB00036052", "PUB00036053", "PUB00036054" ]
[ "15535874", "10068515", "10600463", "15028676" ]
[ "The 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-CoA) reductases.", "Sequence comparisons reveal two classes of 3-hydroxy-3-methylglutaryl coenzyme A reductase.", "Expression and characterization of the HMG-CoA reductase of the thermophilic archaeon Sulfolobus solfataricus.", "Class II 3-hydroxy-3-methylglutar...
[ 2004, 1999, 1999, 2004 ]
4
[]
[ "IPR004553", "IPR004554" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 983, 6205, 8837, 5, 148 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 6, 1, 7, 3, 7, 6, 1, 12, 7, 2, 1, 42 ]
12
true
Family
Hydroxymethylglutaryl-CoA reductase, class I/II
Hydroxymethylglutaryl-CoA reductase, class I/II
HMG_CoA_Rdtase
9
IPR002204
2,204
3-hydroxyisobutyrate dehydrogenase-related, conserved site
3-OH-isobutyrate_DH-rel_CS
Conserved_site
37,629
false
false
This entry identifies a conserved site in reductases/dehydrogenases. 3-hydroxyisobutyrate dehydrogenase ( ) catalyses the NAD-dependent, reversible oxidation of 3-hydroxbutyrate to methylmalonate [ ]. In eukaryotes, it is a homodimeric mitochondrial protein involved in valine catabolism. In Pseudomonas aeruginosa [ ] (...
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS00895" ]
[ "3_HYDROXYISOBUT_DH" ]
[ 37629 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.1.1", "PDOC00697", "R-CEL-70895", "R-DME-70895", "R-HSA-70895", "R-MMU-70895", "R-RNO-70895" ]
[ "EC:1.1.1", "PROSITEDOC:PDOC00697", "REACTOME:R-CEL-70895", "REACTOME:R-DME-70895", "REACTOME:R-HSA-70895", "REACTOME:R-MMU-70895", "REACTOME:R-RNO-70895" ]
7
[ "1vpd", "1wp4", "1yb4", "2cvz", "2gf2", "2i9p", "3cky", "3doj", "3g0o", "3obb", "3pdu", "3pef", "3q3c", "3qha", "3w6u", "3w6z", "3ws7", "4e21", "4om8", "5je8", "5xvh", "5y8g", "5y8h", "5y8i", "5y8j", "5y8k", "5y8l", "5y8m", "5y8n", "5y8o", "5y8p", "6sm7"...
34
[ "PUB00002541", "PUB00002721" ]
[ "2647728", "1339433" ]
[ "Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate dehydrogenase. Evidence for its evolutionary relationship to other pyridine nucleotide-dependent dehydrogenases.", "Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyi...
[ 1989, 1992 ]
2
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]
[ 141, 30072, 43, 7070, 303 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 18, 1, 5, 2, 4, 2, 2, 2, 10, 4, 41 ]
11
true
Conserved_site
3-hydroxyisobutyrate dehydrogenase-related, conserved site
3-hydroxyisobutyrate dehydrogenase-related, conserved site
3-OH-isobutyrate_DH-rel_CS
2
IPR002205
2,205
DNA topoisomerase, type IIA, domain A
Topo_IIA_dom_A
Domain
66,104
false
false
Type II topoisomerases are ATP-dependent enzymes, and can be subdivided according to their structure and reaction mechanisms: type IIA (topoisomerase II or gyrase, and topoisomerase IV) and type IIB (topoisomerase VI). These enzymes are responsible for relaxing supercoiled DNA as well as for introducing both negative a...
[ "GO:0003677", "GO:0003918", "GO:0005524", "GO:0006265" ]
[ "DNA binding", "DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity", "ATP binding", "DNA topological change" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
4
[ "PFAM", "PROFILE", "SMART", "CDD" ]
[ "PF00521", "PS52040", "SM00434", "cd00187" ]
[ "DNA_topoisoIV", "TOPO_IIA", "TOP4c", "TOP4c" ]
[ 65999, 65761, 63131, 54229 ]
4
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "5.6.2.2", "R-CEL-4615885", "R-DDI-4615885", "R-DME-4615885", "R-HSA-1362277", "R-HSA-4615885", "R-HSA-9638771", "R-HSA-9913143", "R-MMU-4615885", "R-RNO-4615885", "R-SCE-4615885", "R-SPO-4615885", "R-SSC-4615885" ]
[ "EC:5.6.2.2", "REACTOME:R-CEL-4615885", "REACTOME:R-DDI-4615885", "REACTOME:R-DME-4615885", "REACTOME:R-HSA-1362277", "REACTOME:R-HSA-4615885", "REACTOME:R-HSA-9638771", "REACTOME:R-HSA-9913143", "REACTOME:R-MMU-4615885", "REACTOME:R-RNO-4615885", "REACTOME:R-SCE-4615885", "REACTOME:R-SPO-4615...
13
[ "1ab4", "1bgw", "1bjt", "1x75", "1zvu", "2inr", "2nov", "2rgr", "2xco", "2xcq", "2xcr", "2xcs", "2xct", "2xkj", "2xkk", "2y3p", "3foe", "3fof", "3ifz", "3ilw", "3k9f", "3ksa", "3ksb", "3l4j", "3l4k", "3lpx", "3ltn", "3nuh", "3qx3", "3rad", "3rae", "3raf"...
175
[ "PUB00004227", "PUB00020795", "PUB00020802", "PUB00020803", "PUB00023307", "PUB00065887", "PUB00081705", "PUB00113625", "PUB00160236" ]
[ "8538787", "7980433", "16023670", "8982450", "9278055", "23022727", "17293019", "8696977", "37610250" ]
[ "Structure and mechanism of DNA topoisomerase II.", "Structure and function of type II DNA topoisomerases.", "The structural basis for substrate specificity in DNA topoisomerase IV.", "Bacterial diversity based on type II DNA topoisomerase genes.", "Crystal structure of the breakage-reunion domain of DNA gy...
[ 1996, 1994, 2005, 1996, 1997, 2012, 2007, 1996, 2023 ]
9
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 560, 53979, 9406, 735, 1424 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 9, 3, 5, 1, 2, 11, 6, 2, 7, 8, 1, 1, 71 ]
13
true
Domain
DNA topoisomerase, type IIA, domain A
DNA topoisomerase, type IIA, domain A
Topo_IIA_dom_A
8
IPR002206
2,206
Opsin, pineal type
Opsin_pineal
Family
655
false
false
Recently, a non-visual opsin (designated P-opsin or pinopsin) has been isolated from Gallus gallus (Chicken) pineal gland [ , ]. Environmental light signals reset the phase of the endogenous circadian pacemaker that controls the rhythmic production of melatonin via this protein [ ]. Sharing ~45% identity with retinal o...
[ "GO:0007186", "GO:0007602", "GO:0016020" ]
[ "G protein-coupled receptor signaling pathway", "phototransduction", "membrane" ]
[ "biological_process", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00666" ]
[ "PINOPSIN" ]
[ 655 ]
1
[]
[]
[]
0
[]
0
[ "PUB00004197", "PUB00005197" ]
[ "7969427", "7878470" ]
[ "Pinopsin is a chicken pineal photoreceptive molecule.", "Pineal opsin: a nonvisual opsin expressed in chick pineal." ]
[ 1994, 1995 ]
2
[ "IPR001760" ]
[]
1
0
1
[ "Chordata" ]
[ 655 ]
1
[ "Danio rerio" ]
[ 1 ]
1
true
Family
Opsin, pineal type
Opsin, pineal type
Opsin_pineal
2
IPR002207
2,207
Class I peroxidase
Peroxidase_I
Family
9,922
false
false
Peroxidases are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to catalyse a number of oxidative reactions. They are found in bacteria, fungi, plants and animals. On the basis of sequence similarity, fungal, plant and bacterial peroxidases can be viewed as members of a superfamily consistin...
[ "GO:0004601", "GO:0020037", "GO:0006979" ]
[ "peroxidase activity", "heme binding", "response to oxidative stress" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PRINTS" ]
[ "PR00459" ]
[ "ASPEROXIDASE" ]
[ 9922 ]
1
[ "EC" ]
[ "1.11.1" ]
[ "EC:1.11.1" ]
1
[ "1a2f", "1a2g", "1aa4", "1ac4", "1ac8", "1aeb", "1aed", "1aee", "1aef", "1aeg", "1aeh", "1aej", "1aek", "1aem", "1aen", "1aeo", "1aeq", "1aes", "1aet", "1aeu", "1aev", "1apx", "1bej", "1bek", "1bem", "1bep", "1beq", "1bes", "1bj9", "1bva", "1cca", "1ccb"...
285
[ "PUB00000418", "PUB00053582" ]
[ "7703247", "15291807" ]
[ "Crystal structure of recombinant pea cytosolic ascorbate peroxidase.", "Phylogenetic relationships in class I of the superfamily of bacterial, fungal, and plant peroxidases." ]
[ 1995, 2004 ]
2
[ "IPR044831" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "marine metagenome" ]
[ 84, 9837, 1 ]
3
[ "Arabidopsis thaliana", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Zea mays" ]
[ 40, 1, 27, 1, 108 ]
5
true
Family
Class I peroxidase
Class I peroxidase
Peroxidase_I
3
IPR002208
2,208
SecY/SEC61-alpha family
SecY/SEC61-alpha
Family
41,412
false
false
This family consists of the protein translocase subunit SecY and protein transport protein Sec61 subunit alpha (Sec61a). Sec61a is part of the Sec61 complex, which plays a crucial role in the insertion of secretory and membrane polypeptides into the ER. It is required for assembly of membrane and secretory proteins. Se...
[ "GO:0015031", "GO:0016020" ]
[ "protein transport", "membrane" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM", "PIRSF", "PANTHER", "NCBIFAM" ]
[ "PF00344", "PIRSF004557", "PTHR10906", "TIGR00967" ]
[ "SecY", "SecY", "", "3a0501s007" ]
[ 39517, 33870, 40511, 33197 ]
4
[ "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GenProp0209", "PDOC00612", "R-HSA-1222387", "R-HSA-1236974", "R-HSA-1799339", "R-HSA-9760173" ]
[ "GP:GenProp0209", "PROSITEDOC:PDOC00612", "REACTOME:R-HSA-1222387", "REACTOME:R-HSA-1236974", "REACTOME:R-HSA-1799339", "REACTOME:R-HSA-9760173" ]
6
[ "1rh5", "1rhz", "2akh", "2aki", "2ww9", "2wwa", "2wwb", "2yxq", "2yxr", "2zjs", "2zqp", "3bo0", "3bo1", "3din", "3dkn", "3dl8", "3j45", "3j46", "3j7q", "3j7r", "3jc2", "3mp7", "4cg5", "4cg6", "4cg7", "4v4n", "4v6m", "4v7i", "5a6u", "5abb", "5aww", "5ch4"...
96
[ "PUB00000694", "PUB00001631", "PUB00003801", "PUB00003823", "PUB00007064", "PUB00007065", "PUB00007066", "PUB00007187" ]
[ "1764515", "1544427", "2110998", "1406280", "2202721", "11336818", "10418149", "12167867" ]
[ "Presence of a gene in the archaebacterium Methanococcus vannielii homologous to secY of eubacteria.", "A secY homologue is found in the plastid genome of Cryptomonas phi.", "Isolation of a secY homologue from Bacillus subtilis: evidence for a common protein export pathway in eubacteria.", "SecY and integral ...
[ 1991, 1992, 1990, 1992, 1990, 2001, 1999, 2002 ]
8
[]
[ "IPR014269", "IPR026593" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctHip2", "unclassified sequences" ]
[ 1081, 27167, 12479, 1, 684 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 21, 2, 3, 2, 1, 24, 7, 1, 30, 12, 2, 2, 36 ]
13
true
Family
SecY/SEC61-alpha family
SecY/SEC61-alpha family
SecY/SEC61-alpha
4
IPR002209
2,209
Fibroblast growth factor family
Fibroblast_GF_fam
Family
24,533
false
false
Fibroblast growth factors (FGFs) [ , ] are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [ , ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGF...
[ "GO:0008083" ]
[ "growth factor activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS", "PROSITE", "PANTHER", "SMART" ]
[ "PF00167", "PR00263", "PS00247", "PTHR11486", "SM00442" ]
[ "FGF", "HBGFFGF", "HBGF_FGF", "", "FGF" ]
[ 24479, 16811, 17784, 23425, 23347 ]
5
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-109704", "R-BTA-1257604", "R-BTA-190322", "R-BTA-190370", "R-BTA-190371", "R-BTA-190372", "R-BTA-190373", "R-BTA-190375", "R-BTA-190377", "R-BTA-3000170", "R-BTA-5654219", "R-BTA-5654221", "R-BTA-5654227", "R-BTA-5654228", "R-BTA-5654687", "R-BTA-5654688", "R-BTA-5654689", "...
[ "REACTOME:R-BTA-109704", "REACTOME:R-BTA-1257604", "REACTOME:R-BTA-190322", "REACTOME:R-BTA-190370", "REACTOME:R-BTA-190371", "REACTOME:R-BTA-190372", "REACTOME:R-BTA-190373", "REACTOME:R-BTA-190375", "REACTOME:R-BTA-190377", "REACTOME:R-BTA-3000170", "REACTOME:R-BTA-5654219", "REACTOME:R-BTA-...
301
[ "1afc", "1axm", "1bar", "1bas", "1bfb", "1bfc", "1bff", "1bfg", "1bla", "1bld", "1cvs", "1djs", "1dzc", "1dzd", "1e0o", "1ev2", "1evt", "1fga", "1fmm", "1fq9", "1g82", "1hkn", "1ihk", "1ii4", "1iil", "1ijt", "1jqz", "1jt3", "1jt4", "1jt5", "1jt7", "1jtc"...
172
[ "PUB00000068", "PUB00001036", "PUB00005334", "PUB00021048", "PUB00024683", "PUB00039267", "PUB00067626", "PUB00067627", "PUB00067628", "PUB00067629", "PUB00067630", "PUB00067631", "PUB00067632", "PUB00067633", "PUB00067634", "PUB00067635", "PUB00067636" ]
[ "2549857", "7583099", "3072709", "11276432", "10830168", "8652550", "1705486", "8760337", "23000357", "15689573", "10441498", "23108135", "23016864", "1649700", "11746231", "14745970", "8978613" ]
[ "The heparin-binding (fibroblast) growth factor family of proteins.", "Functions of fibroblast growth factors and their receptors.", "Transforming potential of fibroblast growth factor genes.", "Fibroblast growth factors.", "Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-rece...
[ 1989, 1995, 1988, 2001, 2000, 1996, 1990, 1996, 2012, 2005, 1999, 2013, 2013, 1991, 2001, 2003, 1996 ]
17
[]
[ "IPR035444" ]
0
1
0
[ "Eukaryota", "Pseudomonadati", "Viruses" ]
[ 24384, 4, 145 ]
3
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 88, 8, 76, 87, 85 ]
6
true
Family
Fibroblast growth factor family
Fibroblast growth factor family
Fibroblast_GF_fam
2
IPR002210
2,210
Major capsid L1 (late) protein, Papillomavirus
Capsid_L1_Papillomavir
Family
6,538
false
false
This entry represents the major late capsid protein L1 from Papillomaviruses, such as Human papillomavirus (HPV) [ ]. Papillomaviruses are members of the papovavirus superfamily. More than 70 different types of papillomavirus have been discovered in humans, some of which have been shown to cause genital carcinomas and ...
[ "GO:0005198", "GO:0019028" ]
[ "structural molecule activity", "viral capsid" ]
[ "molecular_function", "cellular_component" ]
2
[ "HAMAP", "PFAM", "PRINTS" ]
[ "MF_04002", "PF00500", "PR00865" ]
[ "PPV_L1", "Late_protein_L1", "HPVCAPSIDL1" ]
[ 2078, 6537, 5193 ]
3
[]
[]
[]
0
[ "1dzl", "2r5h", "2r5i", "2r5j", "2r5k", "3iyj", "3j6r", "3j7g", "3j8v", "3j8w", "3j8z", "3jba", "5j6r", "5jb1", "5kep", "5keq", "5w1o", "5w1x", "5y9c", "5y9e", "5y9f", "6bsp", "6bt3", "6igc", "6igd", "6ige", "6igf", "6l31", "7cn2", "7dn5", "7dnh", "7dnk"...
44
[ "PUB00003160", "PUB00024376", "PUB00035302", "PUB00035622" ]
[ "7561785", "10882140", "12620808", "17446671" ]
[ "Organization of the major and minor capsid proteins in human papillomavirus type 33 virus-like particles.", "Structure of small virus-like particles assembled from the L1 protein of human papillomavirus 16.", "The L1 major capsid protein of human papillomavirus type 11 interacts with Kap beta2 and Kap beta3 nu...
[ 1995, 2000, 2003, 2006 ]
4
[]
[]
0
0
null
[ "Homo sapiens", "Papillomaviridae" ]
[ 3, 6535 ]
2
[ "Homo sapiens" ]
[ 3 ]
1
true
Family
Major capsid L1 (late) protein, Papillomavirus
Major capsid L1 (late) protein, Papillomavirus
Capsid_L1_Papillomavir
5
IPR002211
2,211
Lymphocyte-specific protein
Lymphspecific
Family
1,047
false
false
Human and mouse LSP1 proteins consist of two domains: an N-terminal acidic domain and a C-terminal basic domain [ , ]. The C-terminal domains are highly conserved and include several putative Ser/Thr phosphorylation sites [ ]. Immunoprecipitation of LSP1 from 32P-orthophosphate-loaded cells indicates that LSP1 is a pho...
[ "GO:0003779", "GO:0007165" ]
[ "actin binding", "signal transduction" ]
[ "molecular_function", "biological_process" ]
2
[ "PRINTS" ]
[ "PR01083" ]
[ "LYMPHSPCIFIC" ]
[ 1047 ]
1
[]
[]
[]
0
[]
0
[ "PUB00003175", "PUB00003176", "PUB00003780" ]
[ "3263441", "2295815", "7935501" ]
[ "A new lymphocyte-specific gene which encodes a putative Ca2+-binding protein is not expressed in transformed T lymphocyte lines.", "Human and mouse LSP1 genes code for highly conserved phosphoproteins.", "The LSP1 gene is expressed in cultured normal and transformed mouse macrophages." ]
[ 1988, 1990, 1994 ]
3
[ "IPR006018" ]
[]
1
0
1
[ "Vertebrata" ]
[ 1047 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 15, 4, 11 ]
3
true
Family
Lymphocyte-specific protein
Lymphocyte-specific protein
Lymphspecific
2
IPR002213
2,213
UDP-glucuronosyl/UDP-glucosyltransferase
UDP_glucos_trans
Family
147,902
false
false
UDP glycosyltransferases (UGT) are a superfamily of enzymes that catalyse the addition of the glycosyl group from a UDP-sugar to a small hydrophobic molecule. This family currently consist of: Mammalian UDP-glucuronosyl transferases ( ) (UDPGT) [ ]. A large family of membrane-bound microsomal enzymes which catalyse the...
[ "GO:0008194" ]
[ "UDP-glycosyltransferase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "CDD" ]
[ "PF00201", "cd03784" ]
[ "UDPGT", "GT1_Gtf-like" ]
[ 115150, 137354 ]
2
[ "EC", "GP", "GP", "GP", "GP", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "2.4.1", "GenProp1261", "GenProp1547", "GenProp1591", "GenProp1600", "PDOC00359", "R-CEL-9840309", "R-HSA-156588", "R-HSA-189483", "R-HSA-1989781", "R-HSA-5579002", "R-HSA-5579016", "R-HSA-9623433", "R-HSA-9749641", "R-HSA-9753281", "R-HSA-9754706", "R-HSA-9757110", "R-HSA-9840309"...
[ "EC:2.4.1", "GP:GenProp1261", "GP:GenProp1547", "GP:GenProp1591", "GP:GenProp1600", "PROSITEDOC:PDOC00359", "REACTOME:R-CEL-9840309", "REACTOME:R-HSA-156588", "REACTOME:R-HSA-189483", "REACTOME:R-HSA-1989781", "REACTOME:R-HSA-5579002", "REACTOME:R-HSA-5579016", "REACTOME:R-HSA-9623433", "R...
32
[ "1iir", "1pn3", "1pnv", "1rrv", "2acv", "2acw", "2c1x", "2c1z", "2c9z", "2iya", "2iyf", "2o6l", "2p6p", "2pq6", "2vce", "2vch", "2vg8", "2yjn", "3d0q", "3d0r", "3h4i", "3h4t", "3hbf", "3hbj", "3ia7", "3iaa", "3otg", "3oth", "3oti", "3rsc", "3tsa", "3uyk"...
228
[ "PUB00001112", "PUB00001835", "PUB00004807", "PUB00005121", "PUB00094545", "PUB00095588", "PUB00097197", "PUB00097198", "PUB00097199", "PUB00100237", "PUB00100238" ]
[ "1909870", "8244027", "7694285", "2505387", "32047295", "32688778", "27227328", "17163637", "24960592", "30051576", "27696999" ]
[ "The UDP glucuronosyltransferase gene superfamily: suggested nomenclature based on evolutionary divergence.", "Characterization of a Streptomyces antibioticus gene cluster encoding a glycosyltransferase involved in oleandomycin inactivation.", "Ceramide UDPgalactosyltransferase from myelinating rat brain: purif...
[ 1991, 1993, 1993, 1989, 2020, 2008, 2016, 2006, 2014, 2018, 2017 ]
11
[]
[ "IPR006326", "IPR016224", "IPR050481" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 23, 22219, 125391, 198, 71 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 585, 83, 75, 64, 146, 49, 5, 562, 80, 1, 576 ]
11
true
Family
UDP-glucuronosyl/UDP-glucosyltransferase
UDP-glucuronosyl/UDP-glucosyltransferase
UDP_glucos_trans
6
IPR002214
2,214
Hantavirus nucleocapsid protein
Hanta_nucleocap
Family
3,684
false
false
Hantaviruses are ssRNA negative-strand viruses. The nucleocapsid protein is an internal protein of the virus particle [ , ].
[ "GO:0019013" ]
[ "viral nucleocapsid" ]
[ "cellular_component" ]
1
[ "PFAM", "PIRSF" ]
[ "PF00846", "PIRSF003949" ]
[ "Hanta_nucleocap", "N_HantaV" ]
[ 3684, 805 ]
2
[]
[]
[]
0
[ "2ic6", "2ic9", "2k48", "4fi5", "5e04", "5e05", "5e06", "5fsg", "6i2n" ]
9
[ "PUB00005633", "PUB00005638" ]
[ "9208453", "8578853" ]
[ "A major antigenic domain of hantaviruses is located on the aminoproximal site of the viral nucleocapsid protein.", "Nucleocapsid- and virus-like particles assemble in cells infected with recombinant baculoviruses or vaccinia viruses expressing the M and the S segments of Hantaan virus." ]
[ 1997, 1995 ]
2
[]
[]
0
0
null
[ "Elliovirales", "Eucarida" ]
[ 3681, 3 ]
2
[]
[]
0
true
Family
Hantavirus nucleocapsid protein
Hantavirus nucleocapsid protein
Hanta_nucleocap
1
IPR002217
2,217
Lipoprotein LPP20
Lipo_LPP20
Family
90
false
false
This entry represents LPP20, which belongs to the non-essential class of lipoproteins [ ].
[ "GO:0009279" ]
[ "cell outer membrane" ]
[ "cellular_component" ]
1
[ "PIRSF", "PRINTS" ]
[ "PIRSF011368", "PR01019" ]
[ "Lipo_LPP20", "LIPOLPP20" ]
[ 69, 90 ]
2
[]
[]
[]
0
[ "5ok8" ]
1
[ "PUB00002256" ]
[ "7928954" ]
[ "Molecular characterization of a conserved 20-kilodalton membrane-associated lipoprotein antigen of Helicobacter pylori." ]
[ 1994 ]
1
[]
[]
0
0
null
[ "Pseudomonadati" ]
[ 90 ]
1
[]
[]
0
true
Family
Lipoprotein LPP20
Lipoprotein LPP20
Lipo_LPP20
5
IPR002218
2,218
tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG-related
MnmG-rel
Family
34,167
false
false
MnmG (also known as GidA) is a tRNA modification enzyme found in bacteria and mitochondria. Though its precise molecular function of these proteins is not known, it is involved in the 5-carboxymethylaminomethyl modification of the wobble uridine base in some tRNAs [ , ]. Sequence variations in the human mitochondrial p...
[ "GO:0050660", "GO:0008033" ]
[ "flavin adenine dinucleotide binding", "tRNA processing" ]
[ "molecular_function", "biological_process" ]
2
[ "PANTHER" ]
[ "PTHR11806" ]
[ "" ]
[ 34167 ]
1
[ "GP", "GP", "PROSITEDOC", "REACTOME" ]
[ "GenProp1313", "GenProp1555", "PDOC00986", "R-HSA-6787450" ]
[ "GP:GenProp1313", "GP:GenProp1555", "PROSITEDOC:PDOC00986", "REACTOME:R-HSA-6787450" ]
4
[ "2cul", "2zxh", "2zxi", "3ces", "3cp2", "3cp8", "3g05", "3g5q", "3g5r", "3g5s", "8zu0", "9hip", "9hiq", "9hir" ]
14
[ "PUB00043571", "PUB00043572", "PUB00043573" ]
[ "15509579", "11544186", "15542390" ]
[ "Mitochondria-specific RNA-modifying enzymes responsible for the biosynthesis of the wobble base in mitochondrial tRNAs. Implications for the molecular pathogenesis of human mitochondrial diseases.", "Translational misreading: a tRNA modification counteracts a +2 ribosomal frameshift.", "Phenotype of non-syndro...
[ 2005, 2001, 2004 ]
3
[]
[ "IPR004416", "IPR004417" ]
0
2
0
[ "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "Stenosarchaea group", "unclassified sequences" ]
[ 28562, 4974, 1, 2, 628 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 6, 1, 8, 1, 1, 32, 4, 1, 3, 2, 1, 1, 21 ]
13
true
Family
tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG-related
tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG-related
MnmG-rel
8
IPR002219
2,219
Protein kinase C-like, phorbol ester/diacylglycerol-binding domain
PKC_DAG/PE
Domain
136,587
false
false
This entry represents the N-terminal region of PKC, known as C1. It has been shown to bind PE and DAG in a phospholipid and zinc-dependent fashion [ ]. The C1 region contains one or two copies (depending on the isozyme of PKC) of a cysteine-rich domain, which is about 50 amino-acid residues long, and which is essential...
[]
[]
[]
0
[ "PFAM", "PROSITE", "PROFILE", "SMART" ]
[ "PF00130", "PS00479", "PS50081", "SM00109" ]
[ "C1_1", "ZF_DAG_PE_1", "ZF_DAG_PE_2", "C1" ]
[ 104747, 104953, 130121, 123729 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00379", "R-BTA-114508", "R-BTA-114516", "R-BTA-114604", "R-BTA-1169091", "R-BTA-1257604", "R-BTA-1433557", "R-BTA-193648", "R-BTA-2029482", "R-BTA-2871796", "R-BTA-2871809", "R-BTA-354192", "R-BTA-389359", "R-BTA-392517", "R-BTA-416482", "R-BTA-416993", "R-BTA-4419969", "R-BTA...
[ "PROSITEDOC:PDOC00379", "REACTOME:R-BTA-114508", "REACTOME:R-BTA-114516", "REACTOME:R-BTA-114604", "REACTOME:R-BTA-1169091", "REACTOME:R-BTA-1257604", "REACTOME:R-BTA-1433557", "REACTOME:R-BTA-193648", "REACTOME:R-BTA-2029482", "REACTOME:R-BTA-2871796", "REACTOME:R-BTA-2871809", "REACTOME:R-BT...
570
[ "1faq", "1far", "1kbe", "1kbf", "1ptq", "1ptr", "1r79", "1rfh", "1tbn", "1tbo", "1xa6", "1y8f", "2db6", "2e73", "2eli", "2enn", "2enz", "2fnf", "2row", "2vrw", "2yuu", "3bji", "3cxl", "3ky9", "3pfq", "3uej", "3uey", "3uff", "3ugd", "3ugi", "3ugl", "4b6d"...
102
[ "PUB00000490", "PUB00000502", "PUB00000518", "PUB00001427", "PUB00004058", "PUB00004125", "PUB00004685", "PUB00119042", "PUB00160328", "PUB00160329" ]
[ "2268301", "1660266", "1445255", "1396661", "2156169", "1614545", "2500657", "18923184", "21215369", "7499357" ]
[ "Human brain n-chimaerin cDNA encodes a novel phorbol ester receptor.", "The cysteine-rich domain of human proteins, neuronal chimaerin, protein kinase C and diacylglycerol kinase binds zinc. Evidence for the involvement of a zinc-dependent structure in phorbol ester binding.", "The Caenorhabditis elegans unc-1...
[ 1990, 1991, 1992, 1992, 1990, 1992, 1989, 2008, 2011, 1995 ]
10
[]
[ "IPR047314", "IPR047469", "IPR047470", "IPR047471", "IPR047475", "IPR047477", "IPR047478", "IPR047480", "IPR047484", "IPR047485", "IPR047486", "IPR047487", "IPR047983" ]
0
13
0
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 13, 30, 136531, 13 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 208, 78, 785, 142, 327, 247, 4, 39, 386, 1, 5, 33 ]
12
true
Domain
Protein kinase C-like, phorbol ester/diacylglycerol-binding domain
Protein kinase C-like, phorbol ester/diacylglycerol-binding domain
PKC_DAG/PE
6
IPR002220
2,220
DapA-like
DapA-like
Family
86,270
false
false
Dihydrodipicolinate synthase ( ) (DHDPS, DapA) catalyses, in higher plants, some fungi and bacteria (gene dapA), the first reaction specific to the biosynthesis of lysine and of diaminopimelate [ ]. DHDPS is responsible for the condensation of aspartate semialdehyde and pyruvate by a ping-pong mechanism in which pyruva...
[ "GO:0016829" ]
[ "lyase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PIRSF", "PRINTS", "PANTHER", "SMART" ]
[ "PF00701", "PIRSF001365", "PR00146", "PTHR12128", "SM01130" ]
[ "DHDPS", "DHDPS", "DHPICSNTHASE", "", "DHDPS" ]
[ 85296, 76445, 68118, 77845, 84657 ]
5
[ "EC", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "4.3.3.7", "GenProp0715", "GenProp0717", "PWY-2941", "PWY-2942", "PWY-5097", "PWY-8088", "PDOC00569", "R-BTA-389661", "R-BTA-4085001", "R-DRE-389661", "R-DRE-4085001", "R-HSA-389661", "R-HSA-4085001", "R-MMU-389661", "R-MMU-4085001", "R-RNO-4085001", "R-SSC-4085001", "R-XTR-38966...
[ "EC:4.3.3.7", "GP:GenProp0715", "GP:GenProp0717", "METACYC:PWY-2941", "METACYC:PWY-2942", "METACYC:PWY-5097", "METACYC:PWY-8088", "PROSITEDOC:PDOC00569", "REACTOME:R-BTA-389661", "REACTOME:R-BTA-4085001", "REACTOME:R-DRE-389661", "REACTOME:R-DRE-4085001", "REACTOME:R-HSA-389661", "REACTOME...
20
[ "1dhp", "1f5z", "1f6k", "1f6p", "1f73", "1f74", "1f7b", "1fdy", "1fdz", "1hl2", "1nal", "1o5k", "1s5t", "1s5v", "1s5w", "1w37", "1w3i", "1w3n", "1w3t", "1xky", "1xl9", "1xxx", "1yxc", "1yxd", "2a6l", "2a6n", "2ats", "2ehh", "2hmc", "2nuw", "2nux", "2nuy"...
269
[ "PUB00000520", "PUB00002226", "PUB00024869", "PUB00049291", "PUB00067366", "PUB00067367" ]
[ "1463470", "8349559", "9047371", "18186475", "22949190", "20025926" ]
[ "Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization.", "The Rhizobium meliloti rhizopine mos locus is a mosaic structure facilitating its symbiotic regulation.", "Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase.", "Cryst...
[ 1992, 1993, 1997, 2008, 2012, 2010 ]
6
[]
[ "IPR005263", "IPR005264", "IPR017655", "IPR048038" ]
0
4
0
[ "Archaea", "Bacteria", "Eukaryota", "Megaviridae environmental sample", "plasmids", "unclassified sequences" ]
[ 1519, 70648, 12712, 1, 2, 1388 ]
6
[ "Arabidopsis thaliana", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 10, 5, 4, 6, 3, 4, 7, 8, 9 ]
9
true
Family
DapA-like
DapA-like
DapA-like
2
IPR002222
2,222
Small ribosomal subunit protein uS19
Ribosomal_uS19
Family
50,622
false
false
This entry represents the small ribosomal subunit protein uS19 family. The small subunit ribosomal proteins can be categorised as: primary binding proteins, which bind directly and independently to 16S rRNA; secondary binding proteins, which display no specific affinity for 16S rRNA, but its assembly is contingent upon...
[ "GO:0003735", "GO:0006412", "GO:0005840" ]
[ "structural constituent of ribosome", "translation", "ribosome" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "HAMAP", "PFAM", "PIRSF", "PRINTS", "PANTHER" ]
[ "MF_00531", "PF00203", "PIRSF002144", "PR00975", "PTHR11880" ]
[ "Ribosomal_uS19", "Ribosomal_S19", "Ribosomal_S19", "RIBOSOMALS19", "" ]
[ 48863, 50398, 47726, 49541, 49782 ]
5
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00288", "R-BTA-156827", "R-BTA-1799339", "R-BTA-6791226", "R-BTA-72649", "R-BTA-72689", "R-BTA-72695", "R-BTA-72702", "R-BTA-72706", "R-BTA-975956", "R-BTA-975957", "R-CEL-156827", "R-CEL-1799339", "R-CEL-72649", "R-CEL-72689", "R-CEL-72695", "R-CEL-72702", "R-CEL-72706", "R...
[ "PROSITEDOC:PDOC00288", "REACTOME:R-BTA-156827", "REACTOME:R-BTA-1799339", "REACTOME:R-BTA-6791226", "REACTOME:R-BTA-72649", "REACTOME:R-BTA-72689", "REACTOME:R-BTA-72695", "REACTOME:R-BTA-72702", "REACTOME:R-BTA-72706", "REACTOME:R-BTA-975956", "REACTOME:R-BTA-975957", "REACTOME:R-CEL-156827"...
101
[ "1fjg", "1fka", "1hnw", "1hnx", "1hnz", "1hr0", "1i94", "1i95", "1i96", "1i97", "1ibk", "1ibl", "1ibm", "1j5e", "1jgo", "1jgp", "1jgq", "1ml5", "1n32", "1n33", "1n34", "1n36", "1qkf", "1qkh", "1vvj", "1vy4", "1vy5", "1vy6", "1vy7", "1xmo", "1xmq", "1xnq"...
1,759
[ "PUB00001612", "PUB00004907", "PUB00007068", "PUB00007069", "PUB00007070" ]
[ "2044758", "9371771", "11297922", "11290319", "11114498" ]
[ "rig encodes ribosomal protein S15. The primary structure of mammalian ribosomal protein S15.", "Proteins on ribosome surface: measurements of protein exposure by hot tritium bombardment technique.", "Atomic structures at last: the ribosome in 2000.", "The ribosome in focus.", "The end of the beginning: str...
[ 1991, 1997, 2001, 2001, 2000 ]
5
[]
[ "IPR005713", "IPR005732" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 915, 23212, 26052, 443 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 35, 1, 1, 2, 1, 8, 4, 2, 10, 4, 2, 3, 39 ]
13
true
Family
Small ribosomal subunit protein uS19
Small ribosomal subunit protein uS19
Ribosomal_uS19
4
IPR002223
2,223
Pancreatic trypsin inhibitor Kunitz domain
Kunitz_BPTI
Domain
35,793
false
false
The majority of the sequences having this domain belong to the MEROPS inhibitor family I2, clan IB; the Kunitz/bovine pancreatic trypsin inhibitor family, they inhibit proteases of the S1 family [ ] and are restricted to the metazoa with a single exception: Amsacta moorei entomopoxvirus. They are short (~50 residue) α/...
[ "GO:0004867" ]
[ "serine-type endopeptidase inhibitor activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS", "PROFILE", "SMART" ]
[ "PF00014", "PR00759", "PS50279", "SM00131" ]
[ "Kunitz_BPTI", "BASICPTASE", "BPTI_KUNITZ_2", "KU" ]
[ 35309, 28460, 35086, 34414 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00252", "R-HSA-114608", "R-HSA-140834", "R-HSA-1442490", "R-HSA-1566977", "R-HSA-1650814", "R-HSA-186797", "R-HSA-2022090", "R-HSA-204005", "R-HSA-216083", "R-HSA-2168880", "R-HSA-2214320", "R-HSA-3000157", "R-HSA-3000178", "R-HSA-381426", "R-HSA-416476", "R-HSA-418594", "R-HS...
[ "PROSITEDOC:PDOC00252", "REACTOME:R-HSA-114608", "REACTOME:R-HSA-140834", "REACTOME:R-HSA-1442490", "REACTOME:R-HSA-1566977", "REACTOME:R-HSA-1650814", "REACTOME:R-HSA-186797", "REACTOME:R-HSA-2022090", "REACTOME:R-HSA-204005", "REACTOME:R-HSA-216083", "REACTOME:R-HSA-2168880", "REACTOME:R-HSA...
89
[ "1aal", "1aap", "1adz", "1b0c", "1bf0", "1bhc", "1bik", "1bpi", "1bpt", "1brb", "1brc", "1bth", "1bti", "1bun", "1bz5", "1bzx", "1ca0", "1cbw", "1co7", "1d0d", "1dem", "1den", "1dtk", "1dtx", "1eaw", "1ejm", "1f5r", "1f7z", "1fak", "1fan", "1fy8", "1g6x"...
222
[ "PUB00000032", "PUB00003271", "PUB00003421", "PUB00004837", "PUB00005002", "PUB00005362", "PUB00014133" ]
[ "6996568", "1714504", "1593645", "8159751", "1304909", "1703675", "14705960" ]
[ "Protein inhibitors of proteinases.", "Crystal structure of a Y35G mutant of bovine pancreatic trypsin inhibitor.", "Evolutionary origin of a Kunitz-type trypsin inhibitor domain inserted in the amyloid beta precursor protein of Alzheimer's disease.", "Molecular cloning, expression, and partial characterizati...
[ 1980, 1991, 1992, 1994, 1992, 1990, 2004 ]
7
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Betaentomopoxvirus", "Eukaryota", "marine metagenome" ]
[ 2, 134, 2, 35644, 11 ]
5
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 70, 67, 64, 72, 54, 63 ]
6
true
Domain
Pancreatic trypsin inhibitor Kunitz domain
Pancreatic trypsin inhibitor Kunitz domain
Kunitz_BPTI
6
IPR002225
2,225
3-beta hydroxysteroid dehydrogenase/isomerase
3Beta_OHSteriod_DH/Estase
Domain
19,020
false
false
The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyses the oxidation and isomerisation of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.
[ "GO:0016616", "GO:0006694" ]
[ "oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor", "steroid biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM" ]
[ "PF01073" ]
[ "3Beta_HSD" ]
[ 19020 ]
1
[ "EC", "GP", "GP", "GP", "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "1.1.1", "GenProp1217", "GenProp1246", "GenProp1364", "GenProp1385", "GenProp1473", "GenProp1742", "R-BTA-191273", "R-BTA-193048", "R-BTA-193993", "R-BTA-194002", "R-BTA-6807062", "R-CEL-191273", "R-CEL-6807062", "R-CFA-193048", "R-CFA-193993", "R-CFA-194002", "R-HSA-191273", "R-...
[ "EC:1.1.1", "GP:GenProp1217", "GP:GenProp1246", "GP:GenProp1364", "GP:GenProp1385", "GP:GenProp1473", "GP:GenProp1742", "REACTOME:R-BTA-191273", "REACTOME:R-BTA-193048", "REACTOME:R-BTA-193993", "REACTOME:R-BTA-194002", "REACTOME:R-BTA-6807062", "REACTOME:R-CEL-191273", "REACTOME:R-CEL-680...
48
[ "4pvc", "4pvd", "6jkg", "6jkh", "7ymb", "7ymu" ]
6
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Nucleocytoviricota", "metagenomes" ]
[ 14, 2409, 16305, 184, 108 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 24, 4, 17, 1, 23, 34, 2, 28, 34, 2, 1, 78 ]
12
true
Domain
3-beta hydroxysteroid dehydrogenase/isomerase
3-beta hydroxysteroid dehydrogenase/isomerase
3Beta_OHSteriod_DH/Estase
3
IPR002226
2,226
Catalase haem-binding site
Catalase_haem_BS
Binding_site
32,406
false
false
Catalases ( ) are antioxidant enzymes that catalyse the conversion of hydrogen peroxide to water and molecular oxygen, serving to protect cells from its toxic effects [ ]. Hydrogen peroxide is produced as a consequence of oxidative cellular metabolism and can be converted to the highly reactive hydroxyl radical via tra...
[ "GO:0020037" ]
[ "heme binding" ]
[ "molecular_function" ]
1
[ "PROSITE" ]
[ "PS00437" ]
[ "CATALASE_1" ]
[ 32406 ]
1
[ "EC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "1.11.1.6", "PDOC00395", "R-BTA-3299685", "R-BTA-6798695", "R-BTA-9033241", "R-CFA-3299685", "R-CFA-6798695", "R-CFA-9033241", "R-DDI-3299685", "R-DDI-6798695", "R-DDI-9033241", "R-DME-3299685", "R-DME-6798695", "R-DME-9033241", "R-DRE-3299685", "R-DRE-6798695", "R-HSA-3299685", "R...
[ "EC:1.11.1.6", "PROSITEDOC:PDOC00395", "REACTOME:R-BTA-3299685", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-9033241", "REACTOME:R-CFA-3299685", "REACTOME:R-CFA-6798695", "REACTOME:R-CFA-9033241", "REACTOME:R-DDI-3299685", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-9033241", "REACTOME:R-DME-32996...
33
[ "1a4e", "1cf9", "1dgb", "1dgf", "1dgg", "1dgh", "1e93", "1f4j", "1gg9", "1gge", "1ggf", "1ggh", "1ggj", "1ggk", "1gwe", "1gwf", "1gwh", "1h6n", "1h7k", "1hbz", "1iph", "1m7s", "1m85", "1mqf", "1nm0", "1p7y", "1p7z", "1p80", "1p81", "1qf7", "1qqw", "1qwl"...
140
[ "PUB00012765", "PUB00015054", "PUB00027249", "PUB00056180" ]
[ "11351128", "14745498", "12557185", "9287428" ]
[ "Mitochondrial catalase and oxidative injury.", "Diversity of structures and properties among catalases.", "Structure of the Clade 1 catalase, CatF of Pseudomonas syringae, at 1.8 A resolution.", "Phylogenetic relationships among prokaryotic and eukaryotic catalases." ]
[ 2001, 2004, 2003, 1997 ]
4
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Tupanvirus", "unclassified sequences" ]
[ 154, 21525, 10646, 4, 77 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...
[ 22, 4, 2, 6, 1, 4, 7, 1, 6, 2, 2, 1, 14 ]
13
true
Binding_site
Catalase haem-binding site
Catalase haem-binding site
Catalase_haem_BS
4
IPR002227
2,227
Tyrosinase copper-binding domain
Tyrosinase_Cu-bd
Domain
35,011
false
false
Tyrosinase ( ) [ ] is a copper monooxygenases that catalyses the hydroxylation of monophenols and the oxidation of o-diphenols to o-quinols. This enzyme, found in prokaryotes as well as in eukaryotes, is involved in the formation of pigments such as melanins and other polyphenolic compounds. Tyrosinase binds two copper...
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PFAM", "PRINTS", "PROSITE", "PROSITE" ]
[ "PF00264", "PR00092", "PS00497", "PS00498" ]
[ "Tyrosinase", "TYROSINASE", "TYROSINASE_1", "TYROSINASE_2" ]
[ 32753, 26098, 21944, 24219 ]
4
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "PDOC00398", "R-CEL-5662702", "R-HSA-5662702", "R-HSA-9824585", "R-MMU-5662702", "R-SSC-5662702" ]
[ "PROSITEDOC:PDOC00398", "REACTOME:R-CEL-5662702", "REACTOME:R-HSA-5662702", "REACTOME:R-HSA-9824585", "REACTOME:R-MMU-5662702", "REACTOME:R-SSC-5662702" ]
6
[ "1bt1", "1bt2", "1bt3", "1bug", "1hc1", "1hcy", "1js8", "1ll1", "1lla", "1lnl", "1nol", "1oxy", "1wx2", "1wx4", "1wx5", "1wxc", "2ahk", "2ahl", "2p3x", "2y9w", "2y9x", "2zmx", "2zmy", "2zmz", "2zwd", "2zwe", "2zwf", "2zwg", "3aws", "3awt", "3awu", "3awv"...
145
[ "PUB00000238", "PUB00000492", "PUB00001230", "PUB00001267", "PUB00004295", "PUB00004557", "PUB00004733", "PUB00004934" ]
[ "7980602", "1901488", "1537334", "7813420", "2664531", "1391768", "1898774", "3130643" ]
[ "Dopachrome tautomerase is a zinc-containing enzyme.", "Albino mutants of Streptomyces glaucescens tyrosinase.", "A second tyrosinase-related protein, TRP-2, maps to and is mutated at the mouse slaty locus.", "Tyrosinase related protein 1 (TRP1) functions as a DHICA oxidase in melanin biosynthesis.", "[Blue...
[ 1994, 1991, 1992, 1994, 1989, 1992, 1991, 1988 ]
8
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Perinereis aibuhitensis marna-like virus 5", "metagenomes" ]
[ 13, 2885, 32080, 1, 32 ]
5
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 7, 9, 6, 15, 14, 8, 21, 8, 18 ]
9
true
Domain
Tyrosinase copper-binding domain
Tyrosinase copper-binding domain
Tyrosinase_Cu-bd
7
IPR002228
2,228
Muscarinic acetylcholine receptor M1
Musac_Ach_M1_rcpt
Family
216
false
false
Muscarinic acetylcholine receptors are members of rhodopsin-like G-protein coupled receptor family. They play several important roles; they mediate many of the effects of acetylcholine in the central and peripheral nervous system and modulate a variety of physiological functions, such as airway, eye and intestinal smoo...
[ "GO:0016907", "GO:0007186", "GO:0040012", "GO:0046541", "GO:0050890", "GO:0005886" ]
[ "G protein-coupled acetylcholine receptor activity", "G protein-coupled receptor signaling pathway", "regulation of locomotion", "saliva secretion", "cognition", "plasma membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "biological_process", "cellular_component" ]
6
[ "PRINTS", "CDD" ]
[ "PR00538", "cd17790" ]
[ "MUSCRINICM1R", "7tmA_mAChR_M1" ]
[ 173, 209 ]
2
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "13", "R-HSA-390648", "R-HSA-416476", "R-MMU-390648", "R-MMU-416476", "R-RNO-390648", "R-RNO-416476", "R-SSC-390648", "R-SSC-416476" ]
[ "IUPHAR:13", "REACTOME:R-HSA-390648", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-390648", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-390648", "REACTOME:R-RNO-416476", "REACTOME:R-SSC-390648", "REACTOME:R-SSC-416476" ]
9
[ "5cxv", "6oij", "6wjc", "9jea", "9uap", "9uaz", "9ucp" ]
7
[ "PUB00064316", "PUB00064317", "PUB00064318", "PUB00064319", "PUB00064320", "PUB00064321", "PUB00064322", "PUB00064323", "PUB00064324", "PUB00064325", "PUB00064326", "PUB00064327", "PUB00064328", "PUB00064329", "PUB00064330", "PUB00064331", "PUB00064332", "PUB00064333", "PUB000643...
[ "3443095", "3272174", "3037705", "9647869", "2470172", "8853955", "10841527", "14641022", "12725869", "17762886", "15850824", "3753655", "7560279", "240249", "15661360", "7751967", "11082420", "16952712", "14744253", "15474550", "15266016", "11714883", "18431815" ]
[ "Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors.", "Cloning and expression of the human and rat m5 muscarinic acetylcholine receptor genes.", "Identification of a family of muscarinic acetylcholine receptor genes.", "Inter...
[ 1987, 1988, 1987, 1998, 1989, 1996, 2000, 2003, 2003, 2007, 2005, 1986, 1995, 1975, 2005, 1995, 2000, 2006, 2004, 2004, 2004, 2001, 2008 ]
23
[ "IPR000995" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 216 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 1, 2 ]
3
true
Family
Muscarinic acetylcholine receptor M1
Muscarinic acetylcholine receptor M1
Musac_Ach_M1_rcpt
9
IPR002229
2,229
Blood group Rhesus C/E/D polypeptide
RhesusRHD
Family
16,568
false
false
Proteins in this group are responsible for the molecular basis of the blood group antigens, surface markers on the outside of the red blood cell membrane. Most of these markers are proteins, but some are carbohydrates attached to lipids or proteins [Reid M.E., Lomas-Francis C. The Blood Group Antigen Facts Book Academi...
[ "GO:0005886" ]
[ "plasma membrane" ]
[ "cellular_component" ]
1
[ "PRINTS" ]
[ "PR00342" ]
[ "RHESUSRHD" ]
[ 16568 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-444411", "R-CFA-444411", "R-DDI-1237044", "R-DDI-1247673", "R-DDI-444411", "R-DRE-444411", "R-HSA-1237044", "R-HSA-1247673", "R-HSA-444411", "R-HSA-5619042", "R-HSA-9037628", "R-MMU-1237044", "R-MMU-1247673", "R-MMU-444411", "R-RNO-1237044", "R-RNO-1247673", "R-RNO-444411", ...
[ "REACTOME:R-BTA-444411", "REACTOME:R-CFA-444411", "REACTOME:R-DDI-1237044", "REACTOME:R-DDI-1247673", "REACTOME:R-DDI-444411", "REACTOME:R-DRE-444411", "REACTOME:R-HSA-1237044", "REACTOME:R-HSA-1247673", "REACTOME:R-HSA-444411", "REACTOME:R-HSA-5619042", "REACTOME:R-HSA-9037628", "REACTOME:R-M...
19
[ "3b9w", "3b9y", "3b9z", "3bhs", "3hd6", "6eu6", "7uzq", "7v0k", "7v0s", "8crt", "8cs9", "8csl", "8csx", "8cte" ]
14
[ "PUB00004766", "PUB00093983", "PUB00093985" ]
[ "1438298", "11062476", "11861637" ]
[ "Molecular cloning and primary structure of the human blood group RhD polypeptide.", "The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast.", "Identification of the erythrocyte Rh blood group glycoprotein as a mammalian ammonium transporter." ]
[ 1992, 2000, 2002 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Megaviridae environmental sample", "metagenomes" ]
[ 102, 5431, 10931, 1, 103 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 4, 4, 25, 3, 558, 14, 7, 12, 10 ]
9
true
Family
Blood group Rhesus C/E/D polypeptide
Blood group Rhesus C/E/D polypeptide
RhesusRHD
1
IPR002230
2,230
Cannabinoid receptor family
Cnbnoid_rcpt
Family
2,123
false
false
Cannabinoid receptors are a class of cell membrane receptors that belong to the rhodopsin-like G-protein coupled receptor (GPCR) family [ , , ]. Typical of G protein-coupled receptors, cannabinoid receptors contain seven transmembrane spanning domains [ ]. Cannabinoid receptors are activated by three major groups of li...
[ "GO:0004949", "GO:0007186", "GO:0016020" ]
[ "cannabinoid receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR00362" ]
[ "CANNABINOIDR" ]
[ 2123 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-373076", "R-HSA-418594", "R-MMU-373076", "R-MMU-418594", "R-RNO-373076", "R-RNO-418594" ]
[ "REACTOME:R-HSA-373076", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-373076", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-373076", "REACTOME:R-RNO-418594" ]
6
[ "5tgz", "5u09", "5xr8", "5xra", "6kpf", "6kpg", "6kqi", "6n4b", "6pt0", "7fee", "7v3z", "7wv9", "8gag", "8ghv", "8guq", "8gur", "8gus", "8gut", "8ikg", "8ikh", "8k8j", "8wrz", "8wu1", "8x3l", "9b54", "9b65", "9b9y", "9b9z", "9ba0", "9dgi", "9ego", "9erx"...
32
[ "PUB00068045", "PUB00068114", "PUB00068115", "PUB00068116", "PUB00068117", "PUB00068118", "PUB00068119", "PUB00068120", "PUB00068121" ]
[ "21079038", "12432948", "18426493", "19273110", "6268916", "5538858", "7565624", "2165569", "7689702" ]
[ "International Union of Basic and Clinical Pharmacology. LXXIX. Cannabinoid receptors and their ligands: beyond CB₁ and CB₂.", "The cannabinoid receptors.", "Cannabinoid receptors: where they are and what they do.", "Cannabinoid receptors: a brief history and \"what's hot\".", "Behavioral comparisons of the...
[ 2010, 2002, 2008, 2009, 1981, 1971, 1995, 1990, 1993 ]
9
[ "IPR000276" ]
[ "IPR000810", "IPR001551" ]
1
2
0
[ "Vertebrata" ]
[ 2123 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 6, 4, 7 ]
4
true
Family
Cannabinoid receptor family
Cannabinoid receptor family
Cnbnoid_rcpt
6
IPR002231
2,231
5-hydroxytryptamine receptor family
5HT_rcpt
Family
7,854
false
false
5-hydroxytryptamine (5-HT) or serotonin, is a neurotransmitter that it is primarily found in the gastrointestinal (GI) tract, platelets, and in the central nervous system (CNS). It is implicated in a vast array of physiological and pathophysiological pathways. Receptors for 5-HT mediate both excitatory and inhibitory n...
[ "GO:0004993", "GO:0007186", "GO:0005886" ]
[ "G protein-coupled serotonin receptor activity", "G protein-coupled receptor signaling pathway", "plasma membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01101" ]
[ "5HTRECEPTOR" ]
[ 7854 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CFA-390666", "R-CFA-416476", "R-CFA-418594", "R-HSA-390666", "R-HSA-416476", "R-HSA-418594", "R-MMU-390666", "R-MMU-416476", "R-MMU-418594", "R-RNO-390666", "R-RNO-416476", "R-RNO-418594" ]
[ "REACTOME:R-CFA-390666", "REACTOME:R-CFA-416476", "REACTOME:R-CFA-418594", "REACTOME:R-HSA-390666", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-390666", "REACTOME:R-MMU-416476", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-390666", "REACTOME:R-RNO-416476", "REACTOME:R-RNO-418...
12
[ "4iaq", "4iar", "4ib4", "4nc3", "5tud", "5tvn", "5v54", "6a93", "6a94", "6bqg", "6bqh", "6drx", "6dry", "6drz", "6ds0", "6g79", "6wgt", "6wh4", "6wha", "7c61", "7e2x", "7e2y", "7e2z", "7e32", "7e33", "7exd", "7ran", "7srr", "7um4", "7um5", "7um6", "7um7"...
88
[ "PUB00064376", "PUB00066704" ]
[ "18476671", "11989819" ]
[ "Serotonin receptors.", "The molecular basis of the structure and function of the 5-HT3 receptor: a model ligand-gated ion channel (review)." ]
[ 2008, 2002 ]
2
[ "IPR000276" ]
[ "IPR000377", "IPR000431", "IPR000455", "IPR000482", "IPR000505", "IPR000610", "IPR001397", "IPR002147" ]
1
8
0
[ "Bilateria" ]
[ 7854 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 24, 16, 18, 25 ]
5
true
Family
5-hydroxytryptamine receptor family
5-hydroxytryptamine receptor family
5HT_rcpt
3
IPR002232
2,232
5-Hydroxytryptamine 6 receptor
5HT6_rcpt
Family
390
false
false
5-hydroxytryptamine (5-HT) or serotonin, is a neurotransmitter that it is primarily found in the gastrointestinal (GI) tract, platelets, and in the central nervous system (CNS). It is implicated in a vast array of physiological and pathophysiological pathways. Receptors for 5-HT mediate both excitatory and inhibitory n...
[ "GO:0004993", "GO:0007186", "GO:0016020" ]
[ "G protein-coupled serotonin receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "CDD" ]
[ "cd15054" ]
[ "7tmA_5-HT6" ]
[ 390 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "11", "R-HSA-390666", "R-HSA-418555", "R-MMU-390666", "R-MMU-418555", "R-RNO-390666" ]
[ "IUPHAR:11", "REACTOME:R-HSA-390666", "REACTOME:R-HSA-418555", "REACTOME:R-MMU-390666", "REACTOME:R-MMU-418555", "REACTOME:R-RNO-390666" ]
6
[ "7xtb", "7ys6", "8jlz" ]
3
[ "PUB00003456", "PUB00064376", "PUB00064510", "PUB00064511", "PUB00064512", "PUB00064513", "PUB00064514", "PUB00064515", "PUB00064516", "PUB00064517", "PUB00064518", "PUB00064519", "PUB00064520", "PUB00064521", "PUB00064522", "PUB00064523", "PUB00066704" ]
[ "8522988", "18476671", "10780993", "11682249", "1522329", "17625499", "18625457", "14618683", "14965245", "8389146", "9037500", "10432491", "7908055", "20217056", "11489457", "11163639", "11989819" ]
[ "Cloning, characterization, and chromosomal localization of a human 5-HT6 serotonin receptor.", "Serotonin receptors.", "In vivo effects of the 5-HT(6) antagonist SB-271046 on striatal and frontal cortex extracellular concentrations of noradrenaline, dopamine, 5-HT, glutamate and aspartate.", "The 5-HT(6) rec...
[ 1996, 2008, 2000, 2001, 1992, 2008, 2008, 2004, 2004, 1993, 1997, 1999, 1994, 2011, 2001, 2001, 2002 ]
17
[ "IPR000276" ]
[]
1
0
1
[ "Chordata" ]
[ 390 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 1, 2, 4 ]
4
true
Family
5-Hydroxytryptamine 6 receptor
5-Hydroxytryptamine 6 receptor
5HT6_rcpt
3
IPR002233
2,233
Adrenoceptor family
ADR_fam
Family
8,682
false
false
The adrenoceptors (or adrenergic receptors) are rhodopsin-like G protein-coupled receptors that are targets of the catecholamines, especially norepinephrine (noradrenaline) and epinephrine (adrenaline). Many cells possess these receptors, and the binding of a catecholamine to the receptor will generally stimulate the s...
[ "GO:0004935", "GO:0007186", "GO:0016020" ]
[ "adrenergic receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01103" ]
[ "ADRENERGICR" ]
[ 8682 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-390696", "R-BTA-392023", "R-BTA-400042", "R-BTA-418555", "R-BTA-418594", "R-BTA-418597", "R-BTA-5683826", "R-BTA-5689880", "R-BTA-8856825", "R-BTA-8856828", "R-DME-390651", "R-DME-390696", "R-DME-418555", "R-DME-5689880", "R-DME-8856825", "R-DME-8856828", "R-DRE-390696", "R-...
[ "REACTOME:R-BTA-390696", "REACTOME:R-BTA-392023", "REACTOME:R-BTA-400042", "REACTOME:R-BTA-418555", "REACTOME:R-BTA-418594", "REACTOME:R-BTA-418597", "REACTOME:R-BTA-5683826", "REACTOME:R-BTA-5689880", "REACTOME:R-BTA-8856825", "REACTOME:R-BTA-8856828", "REACTOME:R-DME-390651", "REACTOME:R-DME...
65
[ "2r4r", "2r4s", "2vt4", "2y00", "2y01", "2y02", "2y03", "2y04", "2ycw", "2ycx", "2ycy", "2ycz", "3kj6", "3zpq", "3zpr", "4ami", "4amj", "4bvn", "4gpo", "5a8e", "5f8u", "6h7j", "6h7l", "6h7m", "6h7n", "6h7o", "6ibl", "6kr8", "6kux", "6kuy", "6tko", "7b6w"...
144
[ "PUB00066376", "PUB00066377" ]
[ "18882199", "2855960" ]
[ "A study of the adrenotropic receptors.", "Subtypes of alpha 2-adrenoceptors: pharmacological and molecular biological evidence converge." ]
[ 1948, 1988 ]
2
[ "IPR000276" ]
[ "IPR000207", "IPR000332", "IPR000363", "IPR000507", "IPR000681", "IPR000735", "IPR001004", "IPR001115", "IPR001946" ]
1
9
0
[ "Eumetazoa" ]
[ 8682 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 22, 5, 18, 22, 25 ]
5
true
Family
Adrenoceptor family
Adrenoceptor family
ADR_fam
6
IPR002234
2,234
Anaphylatoxin chemotactic receptor, C3a/C5a1/C5a2
Anphylx_rcpt_C3a/C5a1-2
Family
1,409
false
false
The activation of the complement cascade produces a number of small fragments that are bioactive: potent chemoattractants and secretagogues that act on immune and non-immune cells [ ]. Similar peptides can also be released by the actions of non-complement proteases, for instance during clotting [ ]. Initially these wer...
[ "GO:0004875", "GO:0006935", "GO:0016020" ]
[ "complement receptor activity", "chemotaxis", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS", "PRINTS" ]
[ "PR00426", "PR01104" ]
[ "C5ANPHYLTXNR", "ANPHYLATOXNR" ]
[ 1093, 1081 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-375276", "R-HSA-418594", "R-HSA-6798695", "R-HSA-9660826", "R-HSA-977606", "R-MMU-375276", "R-MMU-418594", "R-MMU-6798695", "R-MMU-977606", "R-RNO-375276", "R-RNO-418594", "R-RNO-6798695", "R-RNO-977606" ]
[ "REACTOME:R-HSA-375276", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-9660826", "REACTOME:R-HSA-977606", "REACTOME:R-MMU-375276", "REACTOME:R-MMU-418594", "REACTOME:R-MMU-6798695", "REACTOME:R-MMU-977606", "REACTOME:R-RNO-375276", "REACTOME:R-RNO-418594", "REACTOME:R-RNO-...
13
[ "5o9h", "6c1q", "6c1r", "7y64", "7y65", "7y66", "7y67", "8hk2", "8hk3", "8hk5", "8hpt", "8hqc", "8i95", "8i97", "8i9a", "8i9l", "8i9s", "8ia2", "8ia8", "8j6d", "8jzp", "8jzz", "8zwf", "8zwg", "9ipv", "9ipy", "9isi" ]
27
[ "PUB00002962", "PUB00066912", "PUB00066913", "PUB00066914", "PUB00066915", "PUB00066916", "PUB00066917", "PUB00066919", "PUB00066920", "PUB00066921", "PUB00066922", "PUB00066923", "PUB00066924", "PUB00066925", "PUB00066926", "PUB00066928", "PUB00066929", "PUB00066930" ]
[ "8702752", "17603557", "19025115", "19601884", "22118769", "19477527", "9725198", "2528484", "11165367", "8011297", "8605247", "1847994", "12429062", "15833747", "17322907", "11342658", "16154494", "14570896" ]
[ "Molecular cloning and characterization of the human anaphylatoxin C3a receptor.", "Function, structure and therapeutic potential of complement C5a receptors.", "Interaction between the coagulation and complement system.", "The role of anaphylatoxins C3a and C5a in regulating innate and adaptive immune respon...
[ 1996, 2007, 2008, 2009, 2011, 2009, 1998, 1989, 2001, 1994, 1996, 1991, 2002, 2005, 2007, 2001, 2005, 2004 ]
18
[ "IPR000826" ]
[ "IPR001644" ]
1
1
0
[ "Gnathostomata" ]
[ 1409 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 8, 10, 9 ]
4
true
Family
Anaphylatoxin chemotactic receptor, C3a/C5a1/C5a2
Anaphylatoxin chemotactic receptor, C3a/C5a1/C5a2
Anphylx_rcpt_C3a/C5a1-2
7
IPR002236
2,236
CC chemokine receptor 1
Chemokine_CCR1
Family
918
false
false
Chemokines (chemotactic cytokines) are a family of chemoattractant molecules. They attract leukocytes to areas of inflammation and lesions, and play a key role in leukocyte activation. Originally defined as host defense proteins, chemokines are now known to play a much broader biological role [ ]. They have a wide rang...
[ "GO:0016493", "GO:0006954", "GO:0006955", "GO:0007186", "GO:0090026", "GO:0016020" ]
[ "C-C chemokine receptor activity", "inflammatory response", "immune response", "G protein-coupled receptor signaling pathway", "positive regulation of monocyte chemotaxis", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "biological_process", "cellular_component" ]
6
[ "PRINTS" ]
[ "PR01106" ]
[ "CHEMOKINER1" ]
[ 918 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "58", "R-HSA-380108", "R-HSA-418594", "R-HSA-6783783", "R-MMU-418594" ]
[ "IUPHAR:58", "REACTOME:R-HSA-380108", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-6783783", "REACTOME:R-MMU-418594" ]
5
[ "7vl8", "7vl9", "7vla" ]
3
[ "PUB00009401", "PUB00064589", "PUB00064612", "PUB00064613", "PUB00064614", "PUB00064615", "PUB00064619", "PUB00064621", "PUB00064622", "PUB00064623", "PUB00064624", "PUB00064625", "PUB00064626", "PUB00064627", "PUB00064628", "PUB00064648", "PUB00067945", "PUB00067946" ]
[ "11544102", "10714678", "11110672", "9269754", "12270118", "10619859", "10587518", "10601351", "9500790", "12381680", "9514408", "7542241", "11943214", "10734056", "9166425", "18587271", "9689100", "7592998" ]
[ "Chemokine receptors.", "Chemokines: a new classification system and their role in immunity.", "Functional expression of CCR1, CCR3, CCR4, and CXCR4 chemokine receptors on human platelets.", "Human immunodeficiency virus-1 entry into purified blood dendritic cells through CC and CXC chemokine coreceptors.", ...
[ 2001, 2000, 2000, 1997, 2002, 2000, 1999, 1999, 1998, 2002, 1998, 1995, 2002, 2000, 1997, 2008, 1998, 1995 ]
18
[ "IPR000355" ]
[]
1
0
1
[ "Equid gammaherpesvirus 2", "Euteleostomi" ]
[ 19, 899 ]
2
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 5, 4 ]
3
true
Family
CC chemokine receptor 1
CC chemokine receptor 1
Chemokine_CCR1
9
IPR002237
2,237
CC chemokine receptor 2
Chemokine_CCR2
Family
199
false
false
Chemokines (chemotactic cytokines) are a family of chemoattractant molecules. They attract leukocytes to areas of inflammation and lesions, and play a key role in leukocyte activation. Originally defined as host defense proteins, chemokines are now known to play a much broader biological role [ ]. They have a wide rang...
[ "GO:0016493", "GO:0001974", "GO:0006954", "GO:0006955", "GO:0007186", "GO:0090026", "GO:0016020" ]
[ "C-C chemokine receptor activity", "blood vessel remodeling", "inflammatory response", "immune response", "G protein-coupled receptor signaling pathway", "positive regulation of monocyte chemotaxis", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "biological_process", "biological_process", "cellular_component" ]
7
[ "PRINTS" ]
[ "PR01107" ]
[ "CHEMOKINER2" ]
[ 199 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "59", "R-HSA-1461957", "R-HSA-380108", "R-HSA-418594", "R-HSA-6783783" ]
[ "IUPHAR:59", "REACTOME:R-HSA-1461957", "REACTOME:R-HSA-380108", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-6783783" ]
5
[ "6gps", "7xa3" ]
2
[ "PUB00009401", "PUB00064589", "PUB00064621", "PUB00064622", "PUB00064624", "PUB00064636", "PUB00064637", "PUB00064642", "PUB00064643", "PUB00064644", "PUB00064645", "PUB00064646", "PUB00064647", "PUB00067945", "PUB00067946" ]
[ "11544102", "10714678", "10601351", "9500790", "9514408", "8146186", "10587439", "14674010", "16215992", "17351623", "20136653", "22607625", "17479183", "9689100", "7592998" ]
[ "Chemokine receptors.", "Chemokines: a new classification system and their role in immunity.", "Macrophage inflammatory protein 3alpha is involved in the constitutive trafficking of epidermal langerhans cells.", "Flexible programs of chemokine receptor expression on human polarized T helper 1 and 2 lymphocyte...
[ 2001, 2000, 1999, 1998, 1998, 1994, 1999, 2003, 2006, 2007, 2010, 2012, 2007, 1998, 1995 ]
15
[ "IPR000355" ]
[]
1
0
1
[ "Eutheria" ]
[ 199 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 3, 2 ]
3
true
Family
CC chemokine receptor 2
CC chemokine receptor 2
Chemokine_CCR2
4
IPR002238
2,238
CC chemokine receptor 3
Chemokine_CCR3
Family
202
false
false
Chemokines (chemotactic cytokines) are a family of chemoattractant molecules. They attract leukocytes to areas of inflammation and lesions, and play a key role in leukocyte activation. Originally defined as host defense proteins, chemokines are now known to play a much broader biological role [ ]. They have a wide rang...
[ "GO:0016493", "GO:0006935", "GO:0006954", "GO:0007186", "GO:0016020" ]
[ "C-C chemokine receptor activity", "chemotaxis", "inflammatory response", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "cellular_component" ]
5
[ "PRINTS" ]
[ "PR01108" ]
[ "CHEMOKINER3" ]
[ 202 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "60", "R-HSA-380108", "R-HSA-418594", "R-MMU-380108", "R-MMU-418594", "R-RNO-380108", "R-RNO-418594" ]
[ "IUPHAR:60", "REACTOME:R-HSA-380108", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-380108", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-380108", "REACTOME:R-RNO-418594" ]
7
[ "7x9y" ]
1
[ "PUB00009401", "PUB00064589", "PUB00064621", "PUB00064622", "PUB00064634", "PUB00064658", "PUB00064659", "PUB00064660", "PUB00064661", "PUB00064662", "PUB00064663", "PUB00064664", "PUB00064665", "PUB00064666", "PUB00064667", "PUB00067945", "PUB00067946" ]
[ "11544102", "10714678", "10601351", "9500790", "9276730", "9933081", "9480044", "11099305", "11830666", "16210640", "16453027", "10640766", "10984371", "16978084", "9182688", "9689100", "7592998" ]
[ "Chemokine receptors.", "Chemokines: a new classification system and their role in immunity.", "Macrophage inflammatory protein 3alpha is involved in the constitutive trafficking of epidermal langerhans cells.", "Flexible programs of chemokine receptor expression on human polarized T helper 1 and 2 lymphocyte...
[ 2001, 2000, 1999, 1998, 1997, 1999, 1997, 2000, 2002, 2005, 2006, 2000, 2000, 2006, 1997, 1998, 1995 ]
17
[ "IPR000355" ]
[]
1
0
1
[ "Equid gammaherpesvirus 2", "Tetrapoda" ]
[ 1, 201 ]
2
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 3, 4 ]
3
true
Family
CC chemokine receptor 3
CC chemokine receptor 3
Chemokine_CCR3
5
IPR002240
2,240
CC chemokine receptor 5
Chemokine_CCR5
Family
570
false
false
CC chemokine receptor 5 (CCR5) is found on the surface of white blood cells, such as macrophages [ ], T cells [ ] and dendritic cells [ , ], and expressed in lymphoid organs [ ]. Transfected cells expressing CCR5 receptor bind CCL5 (RANTES), CCL4 (MIP-1beta) and CCL3 (MIP-1alpha), and generate inositol phosphates in re...
[ "GO:0016493", "GO:0006935", "GO:0006954", "GO:0006955", "GO:0007186", "GO:0016020" ]
[ "C-C chemokine receptor activity", "chemotaxis", "inflammatory response", "immune response", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "biological_process", "biological_process", "biological_process", "cellular_component" ]
6
[ "PRINTS" ]
[ "PR01110" ]
[ "CHEMOKINER5" ]
[ 570 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "62", "R-BTA-380108", "R-BTA-418594", "R-CFA-418594", "R-HSA-173107", "R-HSA-380108", "R-HSA-418594", "R-HSA-6783783", "R-MMU-380108", "R-MMU-418594", "R-RNO-380108", "R-RNO-418594" ]
[ "IUPHAR:62", "REACTOME:R-BTA-380108", "REACTOME:R-BTA-418594", "REACTOME:R-CFA-418594", "REACTOME:R-HSA-173107", "REACTOME:R-HSA-380108", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-6783783", "REACTOME:R-MMU-380108", "REACTOME:R-MMU-418594", "REACTOME:R-RNO-380108", "REACTOME:R-RNO-418594" ]
12
[ "4mbs", "5uiw", "6akx", "6aky", "6meo", "6met" ]
6
[ "PUB00002958", "PUB00009401", "PUB00064589", "PUB00064613", "PUB00064621", "PUB00064622", "PUB00064681", "PUB00064683", "PUB00064684", "PUB00067945", "PUB00067946", "PUB00073726" ]
[ "8663314", "11544102", "10714678", "9269754", "10601351", "9500790", "9655467", "11994538", "12682253", "9689100", "7592998", "24855645" ]
[ "Molecular cloning and functional characterization of a novel human CC chemokine receptor (CCR5) for RANTES, MIP-1beta, and MIP-1alpha.", "Chemokine receptors.", "Chemokines: a new classification system and their role in immunity.", "Human immunodeficiency virus-1 entry into purified blood dendritic cells thr...
[ 1996, 2001, 2000, 1997, 1999, 1998, 1998, 2002, 2003, 1998, 1995, 2014 ]
12
[ "IPR000355" ]
[]
1
0
1
[ "Amniota" ]
[ 570 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 89, 2, 3 ]
3
true
Family
CC chemokine receptor 5
CC chemokine receptor 5
Chemokine_CCR5
5
IPR002241
2,241
Glycoside hydrolase, family 27
Glyco_hydro_27
Family
22,021
false
false
O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,...
[ "GO:0004553", "GO:0005975" ]
[ "hydrolase activity, hydrolyzing O-glycosyl compounds", "carbohydrate metabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "PRINTS", "PANTHER", "CDD" ]
[ "PF16499", "PR00740", "PTHR11452", "cd14792" ]
[ "Melibiase_2", "GLHYDRLASE27", "", "GH27" ]
[ 20791, 19520, 21767, 19307 ]
4
[ "CAZY", "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "GH27", "3.2.1.22", "PWY-6527", "R-DDI-6798695", "R-DDI-9840310", "R-HSA-6798695", "R-HSA-9840310", "R-MMU-6798695", "R-MMU-9840310", "R-SPO-6798695" ]
[ "CAZY:GH27", "EC:3.2.1.22", "METACYC:PWY-6527", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-9840310", "REACTOME:R-HSA-6798695", "REACTOME:R-HSA-9840310", "REACTOME:R-MMU-6798695", "REACTOME:R-MMU-9840310", "REACTOME:R-SPO-6798695" ]
10
[ "1ktb", "1ktc", "1r46", "1r47", "1szn", "1t0o", "1uas", "3a21", "3a22", "3a23", "3a5v", "3cc1", "3gxn", "3gxp", "3gxt", "3h53", "3h54", "3h55", "3hg2", "3hg3", "3hg4", "3hg5", "3igu", "3lrk", "3lrl", "3lrm", "3lx9", "3lxa", "3lxb", "3lxc", "3s5y", "3s5z"...
60
[ "PUB00002595", "PUB00004870", "PUB00005266", "PUB00005652" ]
[ "2174888", "7624375", "8535779", "7725791" ]
[ "Human alpha-N-acetylgalactosaminidase-molecular cloning, nucleotide sequence, and expression of a full-length cDNA. Homology with human alpha-galactosidase A suggests evolution from a common ancestral gene.", "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydr...
[ 1990, 1995, 1995, 1994 ]
4
[]
[ "IPR006215" ]
0
1
0
[ "Bacteria", "Eukaryota", "Halobacteriales", "Viruses", "unclassified sequences" ]
[ 7832, 14097, 21, 2, 69 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]
[ 18, 1, 2, 3, 16, 13, 19, 10, 1, 72 ]
10
true
Family
Glycoside hydrolase, family 27
Glycoside hydrolase, family 27
Glyco_hydro_27
1
IPR002242
2,242
Chloride channel ClC-0
Cl_channel-0
Family
2
false
false
Chloride channels (CLCs) constitute an evolutionarily well-conserved family of voltage-gated channels that are structurally unrelated to the other known voltage-gated channels. They are found in organisms ranging from bacteria to yeasts and plants, and also to animals. Their functions in higher animals likely include t...
[ "GO:0005247", "GO:0006821", "GO:0016020" ]
[ "voltage-gated chloride channel activity", "chloride transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01111" ]
[ "CLCHANNEL0" ]
[ 2 ]
1
[]
[]
[]
0
[]
0
[ "PUB00000734", "PUB00001999", "PUB00004085", "PUB00004230", "PUB00004243", "PUB00004244", "PUB00004913", "PUB00155406" ]
[ "9046241", "7581380", "2174129", "8559248", "8848046", "8848047", "9207144", "29845874" ]
[ "Chloride channels: an emerging molecular picture.", "Myotonia levior is a chloride channel disorder.", "Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes.", "A common molecular basis for three inherited kidney stone diseases.", "Homodimeric architectu...
[ 1997, 1995, 1990, 1996, 1996, 1996, 1997, 2018 ]
8
[ "IPR001807" ]
[]
1
0
1
[ "Torpedinidae" ]
[ 2 ]
1
[]
[]
0
true
Family
Chloride channel ClC-0
Chloride channel ClC-0
Cl_channel-0
1
IPR002243
2,243
Chloride channel ClC-1
Cl_channel-1
Family
397
false
false
Chloride channels (CLCs) constitute an evolutionarily well-conserved family of voltage-gated channels that are structurally unrelated to the other known voltage-gated channels. They are found in organisms ranging from bacteria to yeasts and plants, and also to animals. Their functions in higher animals likely include t...
[ "GO:0005247", "GO:0006821", "GO:0016020" ]
[ "voltage-gated chloride channel activity", "chloride transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01112" ]
[ "CLCHANNEL1" ]
[ 397 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CFA-2672351", "R-HSA-2672351", "R-MMU-2672351", "R-RNO-2672351" ]
[ "REACTOME:R-CFA-2672351", "REACTOME:R-HSA-2672351", "REACTOME:R-MMU-2672351", "REACTOME:R-RNO-2672351" ]
4
[ "6coy", "6coz", "6qv6", "6qvb", "6qvc", "6qvd", "6qvu", "8wxi", "8wxj" ]
9
[ "PUB00000734", "PUB00001999", "PUB00004085", "PUB00004108", "PUB00004230", "PUB00004913", "PUB00155406" ]
[ "9046241", "7581380", "2174129", "1659664", "8559248", "9207144", "29845874" ]
[ "Chloride channels: an emerging molecular picture.", "Myotonia levior is a chloride channel disorder.", "Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes.", "Primary structure and functional expression of a developmentally regulated skeletal muscle chlo...
[ 1997, 1995, 1990, 1991, 1996, 1997, 2018 ]
7
[ "IPR001807" ]
[]
1
0
1
[ "Tetrapoda" ]
[ 397 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 10, 12 ]
3
true
Family
Chloride channel ClC-1
Chloride channel ClC-1
Cl_channel-1
4
IPR002244
2,244
Chloride channel ClC-2
Cl-channel-2
Family
986
false
false
Chloride channels (CLCs) constitute an evolutionarily well-conserved family of voltage-gated channels that are structurally unrelated to the other known voltage-gated channels. They are found in organisms ranging from bacteria to yeasts and plants, and also to animals. Their functions in higher animals likely include t...
[ "GO:0005247", "GO:0006821", "GO:0016020" ]
[ "voltage-gated chloride channel activity", "chloride transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01113" ]
[ "CLCHANNEL2" ]
[ 986 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-2672351", "R-MMU-2672351", "R-RNO-2672351" ]
[ "REACTOME:R-HSA-2672351", "REACTOME:R-MMU-2672351", "REACTOME:R-RNO-2672351" ]
3
[ "7xf5", "7xja", "8gqu", "8ta2", "8ta3", "8ta4", "8ta5", "8ta6" ]
8
[ "PUB00000734", "PUB00001999", "PUB00004085", "PUB00004139", "PUB00004230", "PUB00004913", "PUB00155406" ]
[ "9046241", "7581380", "2174129", "1334533", "8559248", "9207144", "29845874" ]
[ "Chloride channels: an emerging molecular picture.", "Myotonia levior is a chloride channel disorder.", "Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes.", "Regions involved in the opening of CIC-2 chloride channel by voltage and cell volume.", "A co...
[ 1997, 1995, 1990, 1992, 1996, 1997, 2018 ]
7
[ "IPR001807" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 986 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 6, 5, 8 ]
4
true
Family
Chloride channel ClC-2
Chloride channel ClC-2
Cl-channel-2
5
IPR002245
2,245
H(+)/Cl(-) exchange transporter 3
ClC3
Family
2,056
false
false
CLC-3/ClC3 is a member of the CLC family initially cloned from rat kidney [ , ] and localised to chromosome 4 in humans [ ]; the human isoform contains 762 amino acid residues. Together with CLC-4 and CLC-5, it forms a distinct branch of the CLC gene family, the three members showing ~80% residue identity. CLC-3is an o...
[ "GO:0062158", "GO:0006821", "GO:0016020" ]
[ "chloride:proton antiporter activity", "chloride transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01114" ]
[ "CLCHANNEL3" ]
[ 2056 ]
1
[ "REACTOME" ]
[ "R-HSA-2672351" ]
[ "REACTOME:R-HSA-2672351" ]
1
[ "8jev", "8jgj", "8jgk", "8jgl", "8jgs", "8jgv", "9dnw", "9dnx", "9dny", "9dnz", "9do0" ]
11
[ "PUB00000734", "PUB00001964", "PUB00001999", "PUB00003044", "PUB00004085", "PUB00004230", "PUB00004266", "PUB00004913", "PUB00155406" ]
[ "9046241", "7665160", "7581380", "9873029", "2174129", "8559248", "9389484", "9207144", "29845874" ]
[ "Chloride channels: an emerging molecular picture.", "Characterization of a human and murine gene (CLCN3) sharing similarities to voltage-gated chloride channels and to a yeast integral membrane protein.", "Myotonia levior is a chloride channel disorder.", "Mutational analysis demonstrates that ClC-4 and ClC-...
[ 1997, 1995, 1995, 1999, 1990, 1996, 1997, 1997, 2018 ]
9
[ "IPR001807" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 2056 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 9, 6, 11, 5 ]
4
true
Family
H(+)/Cl(-) exchange transporter 3
H(+)/Cl(-) exchange transporter 3
ClC3
6
IPR002247
2,247
Chloride channel ClC-5
Cl_channel-5
Family
794
false
false
Chloride channels (CLCs) constitute an evolutionarily well-conserved family of voltage-gated channels that are structurally unrelated to the other known voltage-gated channels. They are found in organisms ranging from bacteria to yeasts and plants, and also to animals. Their functions in higher animals likely include t...
[ "GO:0005247", "GO:0006821", "GO:0016020" ]
[ "voltage-gated chloride channel activity", "chloride transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01116" ]
[ "CLCHANNEL5" ]
[ 794 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-2672351", "R-MMU-2672351", "R-RNO-2672351", "R-SSC-2672351" ]
[ "REACTOME:R-HSA-2672351", "REACTOME:R-MMU-2672351", "REACTOME:R-RNO-2672351", "REACTOME:R-SSC-2672351" ]
4
[]
0
[ "PUB00000734", "PUB00001999", "PUB00002941", "PUB00003044", "PUB00004085", "PUB00004230", "PUB00004913", "PUB00004923", "PUB00155406" ]
[ "9046241", "7581380", "8537381", "9873029", "2174129", "8559248", "9207144", "9653142", "29845874" ]
[ "Chloride channels: an emerging molecular picture.", "Myotonia levior is a chloride channel disorder.", "Cloning and functional expression of rat CLC-5, a chloride channel related to kidney disease.", "Mutational analysis demonstrates that ClC-4 and ClC-5 directly mediate plasma membrane currents.", "Primar...
[ 1997, 1995, 1995, 1999, 1990, 1996, 1997, 1998, 2018 ]
9
[ "IPR001807" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 794 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 3, 4 ]
3
true
Family
Chloride channel ClC-5
Chloride channel ClC-5
Cl_channel-5
5
IPR002248
2,248
Chloride channel ClC-6
Cl_channel-6
Family
1,143
false
false
Chloride channels (CLCs) constitute an evolutionarily well-conserved family of voltage-gated channels that are structurally unrelated to the other known voltage-gated channels. They are found in organisms ranging from bacteria to yeasts and plants, and also to animals. Their functions in higher animals likely include t...
[ "GO:0005247", "GO:0006821", "GO:0016020" ]
[ "voltage-gated chloride channel activity", "chloride transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01117" ]
[ "CLCHANNEL6" ]
[ 1143 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-2672351", "R-HSA-6802952", "R-MMU-2672351" ]
[ "REACTOME:R-HSA-2672351", "REACTOME:R-HSA-6802952", "REACTOME:R-MMU-2672351" ]
3
[ "8jpj", "8jpo", "8jpr" ]
3
[ "PUB00000549", "PUB00000734", "PUB00001698", "PUB00001999", "PUB00004085", "PUB00004230", "PUB00004913", "PUB00100240", "PUB00100241", "PUB00155406" ]
[ "9224655", "9046241", "8543009", "7581380", "2174129", "8559248", "9207144", "20466723", "16950870", "29845874" ]
[ "Alternative splicing of ClC-6 (a member of the CIC chloride-channel family) transcripts generates three truncated isoforms one of which, ClC-6c, is kidney-specific.", "Chloride channels: an emerging molecular picture.", "ClC-6 and ClC-7 are two novel broadly expressed members of the CLC chloride channel family...
[ 1997, 1997, 1995, 1995, 1990, 1996, 1997, 2010, 2006, 2018 ]
10
[ "IPR001807" ]
[]
1
0
1
[ "Metazoa" ]
[ 1143 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 2, 6, 2 ]
4
true
Family
Chloride channel ClC-6
Chloride channel ClC-6
Cl_channel-6
3
IPR002249
2,249
H(+)/Cl(-) exchange transporter 7
CIC-7
Family
1,398
false
false
CLC-7 is a CLC that functions as antiporter and contributes to the acidification of the lysosome lumen and may be involved in maintaining lysosomal pH [ , , ]. Chloride channels (CLCs) constitute an evolutionarily well-conserved family of voltage-gated channels that are structurally unrelated to the other known voltage...
[ "GO:0062158", "GO:0006821", "GO:0016020" ]
[ "chloride:proton antiporter activity", "chloride transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01118" ]
[ "CLCHANNEL7" ]
[ 1398 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-2672351", "R-HSA-2672351", "R-MMU-2672351", "R-RNO-2672351" ]
[ "REACTOME:R-BTA-2672351", "REACTOME:R-HSA-2672351", "REACTOME:R-MMU-2672351", "REACTOME:R-RNO-2672351" ]
4
[ "7bxu", "7cq5", "7cq6", "7cq7", "7jm6", "7jm7", "8hvt", "9g6c", "9g6d", "9g6e" ]
10
[ "PUB00000734", "PUB00001999", "PUB00004085", "PUB00004230", "PUB00004913", "PUB00155406", "PUB00155407", "PUB00155408", "PUB00155409" ]
[ "9046241", "7581380", "2174129", "8559248", "9207144", "29845874", "18449189", "21527911", "31155284" ]
[ "Chloride channels: an emerging molecular picture.", "Myotonia levior is a chloride channel disorder.", "Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes.", "A common molecular basis for three inherited kidney stone diseases.", "Transmembrane topology...
[ 1997, 1995, 1990, 1996, 1997, 2018, 2008, 2011, 2019 ]
9
[ "IPR001807" ]
[]
1
0
1
[ "Bilateria" ]
[ 1398 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 10, 6, 4 ]
4
true
Family
H(+)/Cl(-) exchange transporter 7
H(+)/Cl(-) exchange transporter 7
CIC-7
8
IPR002250
2,250
Chloride channel ClC-K
Cl_channel-K
Family
552
false
false
Chloride channels (CLCs) constitute an evolutionarily well-conserved family of voltage-gated channels that are structurally unrelated to the other known voltage-gated channels. They are found in organisms ranging from bacteria to yeasts and plants, and also to animals. Their functions in higher animals likely include t...
[ "GO:0005247", "GO:0006821", "GO:0016020" ]
[ "voltage-gated chloride channel activity", "chloride transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01119" ]
[ "CLCHANNELKDY" ]
[ 552 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-2672351", "R-MMU-2672351", "R-RNO-2672351" ]
[ "REACTOME:R-HSA-2672351", "REACTOME:R-MMU-2672351", "REACTOME:R-RNO-2672351" ]
3
[ "5tqq", "5tr1" ]
2
[ "PUB00000734", "PUB00001999", "PUB00002854", "PUB00003906", "PUB00003910", "PUB00004085", "PUB00004230", "PUB00004845", "PUB00004913", "PUB00155406" ]
[ "9046241", "7581380", "8021279", "9326936", "9916798", "2174129", "8559248", "8041726", "9207144", "29845874" ]
[ "Chloride channels: an emerging molecular picture.", "Myotonia levior is a chloride channel disorder.", "Two isoforms of a chloride channel predominantly expressed in thick ascending limb of Henle's loop and collecting ducts of rat kidney.", "Mutations in the chloride channel gene, CLCNKB, cause Bartter's syn...
[ 1997, 1995, 1994, 1997, 1999, 1990, 1996, 1994, 1997, 2018 ]
10
[ "IPR001807" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 552 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 3, 9 ]
3
true
Family
Chloride channel ClC-K
Chloride channel ClC-K
Cl_channel-K
6
IPR002251
2,251
Chloride channel ClC-plant
Cl_channel_pln
Family
3,427
false
false
Chloride channels (CLCs) constitute an evolutionarily well-conserved family of voltage-gated channels that are structurally unrelated to the other known voltage-gated channels. They are found in organisms ranging from bacteria to yeasts and plants, and also to animals. Their functions in higher animals likely include t...
[ "GO:0005247", "GO:0006821", "GO:0016020" ]
[ "voltage-gated chloride channel activity", "chloride transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01120" ]
[ "CLCHANNELPLT" ]
[ 3427 ]
1
[]
[]
[]
0
[ "7xa9", "8iab", "8iad" ]
3
[ "PUB00000734", "PUB00001999", "PUB00002978", "PUB00004085", "PUB00004230", "PUB00004523", "PUB00004913", "PUB00155406" ]
[ "9046241", "7581380", "8969232", "2174129", "8559248", "8624442", "9207144", "29845874" ]
[ "Chloride channels: an emerging molecular picture.", "Myotonia levior is a chloride channel disorder.", "A family of putative chloride channels from Arabidopsis and functional complementation of a yeast strain with a CLC gene disruption.", "Primary structure of Torpedo marmorata chloride channel isolated by e...
[ 1997, 1995, 1996, 1990, 1996, 1996, 1997, 2018 ]
8
[ "IPR001807" ]
[]
1
0
1
[ "Viridiplantae" ]
[ 3427 ]
1
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 25, 23, 45 ]
3
true
Family
Chloride channel ClC-plant
Chloride channel ClC-plant
Cl_channel_pln
4
IPR002252
2,252
Glycoside hydrolase family 36
Glyco_hydro_36
Family
15,340
false
false
O-Glycosyl hydrolases ( ) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [ ,...
[ "GO:0004557", "GO:0016052" ]
[ "alpha-galactosidase activity", "carbohydrate catabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PIRSF", "PRINTS", "CDD" ]
[ "PIRSF005536", "PR00743", "cd14791" ]
[ "Agal", "GLHYDRLASE36", "GH36" ]
[ 8958, 12630, 15187 ]
3
[ "CAZY", "EC", "METACYC" ]
[ "GH36", "3.2.1.22", "PWY-6527" ]
[ "CAZY:GH36", "EC:3.2.1.22", "METACYC:PWY-6527" ]
3
[ "2xn0", "2xn1", "2xn2", "2yfn", "2yfo", "3mi6", "4fnp", "4fnq", "4fnr", "4fns", "4fnt", "4fnu", "6jhp", "6lcj", "6lck", "6lcl", "6phu", "6phv", "6phw", "6phx", "6phy", "6pi0", "8k1a", "8k7u", "8k7v" ]
25
[ "PUB00004870", "PUB00005266", "PUB00083912", "PUB00083913", "PUB00083914" ]
[ "7624375", "8535779", "20681989", "12123797", "21931163" ]
[ "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.", "Structures and mechanisms of glycosyl hydrolases.", "Aspergillus nidulans alpha-galactosidase of glycoside hydrolase family 36 catalyses the formation of alpha-galacto-oligosaccharides by transglyc...
[ 1995, 1995, 2010, 2002, 2011 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 32, 13758, 1435, 115 ]
4
[]
[]
0
true
Family
Glycoside hydrolase family 36
Glycoside hydrolase family 36
Glyco_hydro_36
1
IPR002253
2,253
Flavin monooxygenase (FMO) 1
Flavin_mOase_1
Family
2,237
false
false
Flavin-containing monooxygenases (FMOs) constitute a family of xenobiotic- metabolising enzymes [ ]. Using an NADPH cofactor and FAD prosthetic group, these microsomal proteins catalyse the oxygenation of nucleophilic nitrogen, sulphur, phosphorous and selenium atoms in a range of structurally diverse compounds. FMOs h...
[ "GO:0004499" ]
[ "N,N-dimethylaniline monooxygenase activity" ]
[ "molecular_function" ]
1
[ "PRINTS" ]
[ "PR01121" ]
[ "FMOXYGENASE1" ]
[ 2237 ]
1
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.14.13.148", "1.14.13.8", "PWY-5331", "PWY-6968", "PWY-7850", "PWY-8292", "R-CFA-1614558", "R-CFA-217271", "R-HSA-1614558", "R-HSA-217271", "R-MMU-1614558", "R-MMU-217271", "R-RNO-1614558", "R-RNO-217271", "R-SSC-1614558", "R-SSC-217271" ]
[ "EC:1.14.13.148", "EC:1.14.13.8", "METACYC:PWY-5331", "METACYC:PWY-6968", "METACYC:PWY-7850", "METACYC:PWY-8292", "REACTOME:R-CFA-1614558", "REACTOME:R-CFA-217271", "REACTOME:R-HSA-1614558", "REACTOME:R-HSA-217271", "REACTOME:R-MMU-1614558", "REACTOME:R-MMU-217271", "REACTOME:R-RNO-1614558",...
16
[ "7al4" ]
1
[ "PUB00000158", "PUB00000516", "PUB00002549", "PUB00002611", "PUB00002642", "PUB00002834", "PUB00004772", "PUB00005489" ]
[ "8311461", "1417778", "2355001", "2318837", "1712018", "8486656", "1542660", "9538688" ]
[ "A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities.", "Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family.", "Covalent structure of liver microsomal flavin-containing...
[ 1994, 1992, 1990, 1990, 1991, 1993, 1992, 1998 ]
8
[ "IPR000960" ]
[]
1
0
1
[ "Eukaryota", "Rhodothermus marinus" ]
[ 2236, 1 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 2, 6, 8 ]
4
true
Family
Flavin monooxygenase (FMO) 1
Flavin monooxygenase (FMO) 1
Flavin_mOase_1
2
IPR002254
2,254
Flavin monooxygenase (FMO) 2
Flavin_mOase_2
Family
280
false
false
Flavin-containing monooxygenases (FMOs) constitute a family of xenobiotic- metabolising enzymes [ ]. Using an NADPH cofactor and FAD prosthetic group, these microsomal proteins catalyse the oxygenation of nucleophilic nitrogen, sulphur, phosphorous and selenium atoms in a range of structurally diverse compounds. Five m...
[ "GO:0004499" ]
[ "N,N-dimethylaniline monooxygenase activity" ]
[ "molecular_function" ]
1
[ "PRINTS" ]
[ "PR01122" ]
[ "FMOXYGENASE2" ]
[ 280 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC"...
[ "1.14.13.-", "PWY-1381", "PWY-2421", "PWY-2467", "PWY-2724", "PWY-321", "PWY-5317", "PWY-5318", "PWY-5412", "PWY-5413", "PWY-5414", "PWY-5421", "PWY-5422", "PWY-5434", "PWY-5706", "PWY-581", "PWY-5846", "PWY-5855", "PWY-5856", "PWY-5857", "PWY-5870", "PWY-5871", "PWY-5872...
[ "EC:1.14.13.-", "METACYC:PWY-1381", "METACYC:PWY-2421", "METACYC:PWY-2467", "METACYC:PWY-2724", "METACYC:PWY-321", "METACYC:PWY-5317", "METACYC:PWY-5318", "METACYC:PWY-5412", "METACYC:PWY-5413", "METACYC:PWY-5414", "METACYC:PWY-5421", "METACYC:PWY-5422", "METACYC:PWY-5434", "METACYC:PWY-...
120
[ "6sem", "6sf0" ]
2
[ "PUB00000158", "PUB00000356", "PUB00000516", "PUB00002549", "PUB00002611", "PUB00002642", "PUB00002834", "PUB00004507", "PUB00004772", "PUB00005489" ]
[ "8311461", "1911780", "1417778", "2355001", "2318837", "1712018", "8486656", "1306120", "1542660", "9538688" ]
[ "A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities.", "Evidence for complex formation between rabbit lung flavin-containing monooxygenase and calreticulin.", "Cloning, primary sequence and chromosomal localization of human FMO2, a new member of ...
[ 1994, 1991, 1992, 1990, 1990, 1991, 1993, 1992, 1992, 1998 ]
10
[ "IPR000960" ]
[]
1
0
1
[ "Bilateria" ]
[ 280 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 2, 4 ]
3
true
Family
Flavin monooxygenase (FMO) 2
Flavin monooxygenase (FMO) 2
Flavin_mOase_2
3
IPR002255
2,255
Flavin monooxygenase (FMO) 3
Flavin_mOase_3
Family
557
false
false
Flavin-containing monooxygenases (FMOs) constitute a family of xenobiotic- metabolising enzymes [ ]. Using an NADPH cofactor and FAD prosthetic group, these microsomal proteins catalyse the oxygenation of nucleophilic nitrogen, sulphur, phosphorous and selenium atoms in a range of structurally diverse compounds. Five m...
[ "GO:0004499" ]
[ "N,N-dimethylaniline monooxygenase activity" ]
[ "molecular_function" ]
1
[ "PRINTS" ]
[ "PR01123" ]
[ "FMOXYGENASE3" ]
[ 557 ]
1
[ "EC", "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.14.13.148", "1.14.13.32", "1.14.13.8", "PWY-5331", "PWY-6968", "PWY-7850", "PWY-8292", "R-BTA-217271", "R-CFA-217271", "R-HSA-217271", "R-HSA-5579019", "R-MMU-217271", "R-RNO-217271" ]
[ "EC:1.14.13.148", "EC:1.14.13.32", "EC:1.14.13.8", "METACYC:PWY-5331", "METACYC:PWY-6968", "METACYC:PWY-7850", "METACYC:PWY-8292", "REACTOME:R-BTA-217271", "REACTOME:R-CFA-217271", "REACTOME:R-HSA-217271", "REACTOME:R-HSA-5579019", "REACTOME:R-MMU-217271", "REACTOME:R-RNO-217271" ]
13
[ "6se3" ]
1
[ "PUB00000158", "PUB00000166", "PUB00000516", "PUB00001464", "PUB00002004", "PUB00002549", "PUB00002611", "PUB00002642", "PUB00002834", "PUB00004772", "PUB00005489" ]
[ "8311461", "9344459", "1417778", "8654418", "9536088", "2355001", "2318837", "1712018", "8486656", "1542660", "9538688" ]
[ "A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities.", "Molecular cloning, sequencing, and expression in Escherichia coli of mouse flavin-containing monooxygenase 3 (FMO3): comparison with the human isoform.", "Cloning, primary sequence and chrom...
[ 1994, 1997, 1992, 1996, 1998, 1990, 1990, 1991, 1993, 1992, 1998 ]
11
[ "IPR000960" ]
[]
1
0
1
[ "Tetrapoda" ]
[ 557 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 4, 6 ]
3
true
Family
Flavin monooxygenase (FMO) 3
Flavin monooxygenase (FMO) 3
Flavin_mOase_3
5
IPR002256
2,256
Flavin monooxygenase (FMO) 4
Flavin_mOase_4
Family
238
false
false
null
[ "GO:0004499" ]
[ "N,N-dimethylaniline monooxygenase activity" ]
[ "molecular_function" ]
1
[ "PRINTS" ]
[ "PR01124" ]
[ "FMOXYGENASE4" ]
[ 238 ]
1
[ "EC", "METACYC", "METACYC" ]
[ "1.14.13.8", "PWY-5331", "PWY-7850" ]
[ "EC:1.14.13.8", "METACYC:PWY-5331", "METACYC:PWY-7850" ]
3
[]
0
[ "PUB00000158", "PUB00000516", "PUB00001464", "PUB00002549", "PUB00002611", "PUB00002642", "PUB00002834", "PUB00002842", "PUB00004772", "PUB00005489" ]
[ "8311461", "1417778", "8654418", "2355001", "2318837", "1712018", "8486656", "8188717", "1542660", "9538688" ]
[ "A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities.", "Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family.", "Differential developmental and tissue-specific regulatio...
[ 1994, 1992, 1996, 1990, 1990, 1991, 1993, 1994, 1992, 1998 ]
10
[ "IPR000960" ]
[]
1
0
1
[ "Mammalia" ]
[ 238 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 3, 6 ]
3
true
Family
Flavin monooxygenase (FMO) 4
Flavin monooxygenase (FMO) 4
Flavin_mOase_4
5
IPR002258
2,258
Chemerin-like receptor 1
CML1
Family
595
false
false
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...
[ "GO:0004930", "GO:0007186", "GO:0016020" ]
[ "G protein-coupled receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01126" ]
[ "DEZORPHANR" ]
[ 595 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-373076", "R-HSA-373076", "R-MMU-373076", "R-RNO-373076", "R-SSC-373076" ]
[ "REACTOME:R-BTA-373076", "REACTOME:R-HSA-373076", "REACTOME:R-MMU-373076", "REACTOME:R-RNO-373076", "REACTOME:R-SSC-373076" ]
5
[ "7ykd", "8sg1", "8zjg", "9l3w", "9l3z" ]
5
[ "PUB00000131", "PUB00002477", "PUB00004960", "PUB00004961", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816", "PUB00092626", "PUB00092627", "PUB00092628", "PUB00092629", "PUB00092630", "PUB00099598" ]
[ "2111655", "2830256", "8386361", "8170923", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293", "25637017", "29848608", "30588761", "26718448", "14530373", "27716822" ]
[ "G proteins in signal transduction.", "G protein involvement in receptor-effector coupling.", "Design of a discriminating fingerprint for G-protein-coupled receptors.", "Fingerprinting G-protein-coupled receptors.", "The G protein-coupled receptor repertoires of human and mouse.", "GCRDb: a G-protein-coup...
[ 1990, 1988, 1993, 1994, 2003, 1994, 2005, 2009, 2006, 2013, 2015, 2018, 2018, 2016, 2003, 2016 ]
16
[ "IPR000826" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 595 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 4, 1 ]
3
true
Family
Chemerin-like receptor 1
Chemerin-like receptor 1
CML1
1
IPR002259
2,259
Equilibrative nucleoside transporter
Eqnu_transpt
Family
14,969
false
false
Nucleosides are hydrophilic molecules and require specialised transport proteins for permeation of cell membranes. There are two types of nucleoside transport processes: equilibrative bidirectional processes driven by chemical gradients and inwardly directed concentrative processes driven by an electrochemical gradient...
[ "GO:0005337", "GO:1901642", "GO:0016020" ]
[ "nucleoside transmembrane transporter activity", "nucleoside transmembrane transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PIRSF", "PRINTS", "PANTHER" ]
[ "PF01733", "PIRSF016379", "PR01130", "PTHR10332" ]
[ "Nucleoside_tran", "ENT", "DERENTRNSPRT", "" ]
[ 14061, 9288, 9617, 14682 ]
4
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DRE-83936", "R-HSA-5619063", "R-HSA-83936", "R-HSA-9748787", "R-HSA-9755088", "R-MMU-83936", "R-MMU-9748787", "R-MMU-9755088", "R-RNO-83936", "R-RNO-9748787", "R-RNO-9755088" ]
[ "REACTOME:R-DRE-83936", "REACTOME:R-HSA-5619063", "REACTOME:R-HSA-83936", "REACTOME:R-HSA-9748787", "REACTOME:R-HSA-9755088", "REACTOME:R-MMU-83936", "REACTOME:R-MMU-9748787", "REACTOME:R-MMU-9755088", "REACTOME:R-RNO-83936", "REACTOME:R-RNO-9748787", "REACTOME:R-RNO-9755088" ]
11
[ "6ob6", "6ob7", "7wn0", "7wn1", "7ydq", "8tzi" ]
6
[ "PUB00009774", "PUB00033989", "PUB00071908", "PUB00152815" ]
[ "12446811", "10353709", "23506887", "36977719" ]
[ "Molecular evolution of the equilibrative nucleoside transporter family: identification of novel family members in prokaryotes and eukaryotes.", "Recent advances in the molecular biology of nucleoside transporters of mammalian cells.", "The human concentrative and equilibrative nucleoside transporter families, ...
[ 2002, 1998, 2013, 2023 ]
4
[]
[ "IPR034764" ]
0
1
0
[ "Bacteria", "Eukaryota", "Herpesvirales", "hydrothermal vent metagenome" ]
[ 26, 14935, 7, 1 ]
4
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...
[ 32, 13, 13, 6, 27, 19, 1, 14, 20, 1, 23 ]
11
true
Family
Equilibrative nucleoside transporter
Equilibrative nucleoside transporter
Eqnu_transpt
4
IPR002260
2,260
Gap junction delta-2 protein (Cx36)
Connexin36
Family
194
false
false
The connexins are a family of integral membrane proteins that oligomerise to form intercellular channels that are clustered at gap junctions. These channels are specialised sites of cell-cell contact that allow the passage of ions, intracellular metabolites and messenger molecules (with molecular weight less than 1-2kD...
[ "GO:0007154", "GO:0005922" ]
[ "cell communication", "connexin complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01131" ]
[ "CONNEXIN36" ]
[ 194 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-112303", "R-BTA-190861", "R-HSA-112303", "R-HSA-190861", "R-MMU-112303", "R-MMU-190861", "R-RNO-112303", "R-RNO-190861" ]
[ "REACTOME:R-BTA-112303", "REACTOME:R-BTA-190861", "REACTOME:R-HSA-112303", "REACTOME:R-HSA-190861", "REACTOME:R-MMU-112303", "REACTOME:R-MMU-190861", "REACTOME:R-RNO-112303", "REACTOME:R-RNO-190861" ]
8
[ "7xkk", "7xl8", "7xnh", "7xnv", "8hkp", "8iyg", "8qoj", "8r7p", "8r7q", "8r7r", "8xgd", "8xge", "8xgf", "8xgg", "8xgj", "8xh8", "8xh9" ]
17
[ "PUB00000087", "PUB00000926", "PUB00001482", "PUB00005237", "PUB00005511", "PUB00005532", "PUB00005545", "PUB00005549" ]
[ "8811187", "8608591", "9753189", "1320430", "9861669", "9769729", "7685944", "7570999" ]
[ "Connexins, connexons, and intercellular communication.", "The gap junction communication channel.", "Cloning of a new gap junction gene (Cx36) highly expressed in mammalian brain neurons.", "Molecular biology and genetics of gap junction channels.", "Diverse functions of vertebrate gap junctions.", "Inne...
[ 1996, 1996, 1998, 1992, 1998, 1998, 1993, 1995 ]
8
[ "IPR000500" ]
[]
1
0
1
[ "Microvirga lotononidis", "Theria" ]
[ 1, 193 ]
2
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 2, 3 ]
3
true
Family
Gap junction delta-2 protein (Cx36)
Gap junction delta-2 protein (Cx36)
Connexin36
4
IPR002261
2,261
Gap junction alpha-1 protein (Cx43)
Connexin43
Family
922
false
false
The connexins are a family of integral membrane proteins that oligomerise to form intercellular channels that are clustered at gap junctions. These channels are specialised sites of cell-cell contact that allow the passage of ions, intracellular metabolites and messenger molecules (with molecular weight less than 1-2kD...
[ "GO:0022857", "GO:0007267", "GO:0007507", "GO:0005922" ]
[ "transmembrane transporter activity", "cell-cell signaling", "heart development", "connexin complex" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR01132" ]
[ "CONNEXINA1" ]
[ 922 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...
[ "R-BTA-190840", "R-BTA-190861", "R-BTA-190873", "R-BTA-191650", "R-BTA-196025", "R-BTA-9013406", "R-DRE-190840", "R-DRE-190861", "R-DRE-191650", "R-DRE-9013406", "R-HSA-190704", "R-HSA-190827", "R-HSA-190840", "R-HSA-190861", "R-HSA-190873", "R-HSA-191650", "R-HSA-196025", "R-HSA-9...
[ "REACTOME:R-BTA-190840", "REACTOME:R-BTA-190861", "REACTOME:R-BTA-190873", "REACTOME:R-BTA-191650", "REACTOME:R-BTA-196025", "REACTOME:R-BTA-9013406", "REACTOME:R-DRE-190840", "REACTOME:R-DRE-190861", "REACTOME:R-DRE-191650", "REACTOME:R-DRE-9013406", "REACTOME:R-HSA-190704", "REACTOME:R-HSA-1...
33
[ "1r5s", "7f92", "7f93", "7xq9", "7xqb", "7z1t", "7z22", "7z23", "8qko" ]
9
[ "PUB00000087", "PUB00000926", "PUB00005237", "PUB00005511", "PUB00005532", "PUB00005545", "PUB00005549" ]
[ "8811187", "8608591", "1320430", "9861669", "9769729", "7685944", "7570999" ]
[ "Connexins, connexons, and intercellular communication.", "The gap junction communication channel.", "Molecular biology and genetics of gap junction channels.", "Diverse functions of vertebrate gap junctions.", "Innexins: a family of invertebrate gap-junction proteins.", "Gap junctions in the brain: where...
[ 1996, 1996, 1992, 1998, 1998, 1993, 1995 ]
7
[ "IPR000500" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 922 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 9, 4, 3 ]
4
true
Family
Gap junction alpha-1 protein (Cx43)
Gap junction alpha-1 protein (Cx43)
Connexin43
7
IPR002262
2,262
Gap junction alpha-3 protein (Cx46)
Connexin46
Family
144
false
false
Gap junction alpha-3 protein (also called connexin46, or Cx46) is a connexin of ~415 amino acid residues. The bovine form is slightly shorter (401 residues) and is hence known as Cx44, having a molecular mass of ~44 kD. Cx46 (together with Cx50) is a connexin isoform expressed in the lens fibres of the eye. Here, gap j...
[ "GO:0005243", "GO:0007154", "GO:0007601", "GO:0005921" ]
[ "gap junction channel activity", "cell communication", "visual perception", "gap junction" ]
[ "molecular_function", "biological_process", "biological_process", "cellular_component" ]
4
[ "PRINTS" ]
[ "PR01133" ]
[ "CONNEXINA3" ]
[ 144 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-190861", "R-HSA-190861", "R-MMU-190861", "R-RNO-190861" ]
[ "REACTOME:R-BTA-190861", "REACTOME:R-HSA-190861", "REACTOME:R-MMU-190861", "REACTOME:R-RNO-190861" ]
4
[ "6mhq", "7jkc", "7jmd", "7jn0", "7jn1" ]
5
[ "PUB00087465", "PUB00087466" ]
[ "9413992", "25404239" ]
[ "Disruption of alpha3 connexin gene leads to proteolysis and cataractogenesis in mice.", "The connexin46 mutant, Cx46T19M, causes loss of gap junction function and alters hemi-channel gating." ]
[ 1997, 2015 ]
2
[ "IPR000500" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 144 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 2, 3 ]
3
true
Family
Gap junction alpha-3 protein (Cx46)
Gap junction alpha-3 protein (Cx46)
Connexin46
3
IPR002263
2,263
Gap junction alpha-4 protein (Cx37)
Connexin37
Family
181
false
false
The connexins are a family of integral membrane proteins that oligomerise to form intercellular channels that are clustered at gap junctions. These channels are specialised sites of cell-cell contact that allow the passage of ions, intracellular metabolites and messenger molecules (with molecular weight less than 1-2kD...
[ "GO:0007154", "GO:0005922" ]
[ "cell communication", "connexin complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01134" ]
[ "CONNEXINA4" ]
[ 181 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-190861", "R-HSA-190861", "R-MMU-190861", "R-RNO-190861" ]
[ "REACTOME:R-BTA-190861", "REACTOME:R-HSA-190861", "REACTOME:R-MMU-190861", "REACTOME:R-RNO-190861" ]
4
[]
0
[ "PUB00000087", "PUB00000926", "PUB00005237", "PUB00005511", "PUB00005532", "PUB00005545", "PUB00005549" ]
[ "8811187", "8608591", "1320430", "9861669", "9769729", "7685944", "7570999" ]
[ "Connexins, connexons, and intercellular communication.", "The gap junction communication channel.", "Molecular biology and genetics of gap junction channels.", "Diverse functions of vertebrate gap junctions.", "Innexins: a family of invertebrate gap-junction proteins.", "Gap junctions in the brain: where...
[ 1996, 1996, 1992, 1998, 1998, 1993, 1995 ]
7
[ "IPR000500" ]
[]
1
0
1
[ "Amniota" ]
[ 181 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 3, 2 ]
3
true
Family
Gap junction alpha-4 protein (Cx37)
Gap junction alpha-4 protein (Cx37)
Connexin37
7
IPR002264
2,264
Gap junction alpha-5 protein (Cx40)
Connexin40
Family
664
false
false
The connexins are a family of integral membrane proteins that oligomerise to form intercellular channels that are clustered at gap junctions. These channels are specialised sites of cell-cell contact that allow the passage of ions, intracellular metabolites and messenger molecules (with molecular weight less than 1-2kD...
[ "GO:0007154", "GO:0005922" ]
[ "cell communication", "connexin complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01135" ]
[ "CONNEXINA5" ]
[ 664 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CFA-190861", "R-HSA-190861", "R-MMU-190861", "R-RNO-190861" ]
[ "REACTOME:R-CFA-190861", "REACTOME:R-HSA-190861", "REACTOME:R-MMU-190861", "REACTOME:R-RNO-190861" ]
4
[ "2k7m" ]
1
[ "PUB00000087", "PUB00000926", "PUB00005237", "PUB00005511", "PUB00005532", "PUB00005545", "PUB00005549" ]
[ "8811187", "8608591", "1320430", "9861669", "9769729", "7685944", "7570999" ]
[ "Connexins, connexons, and intercellular communication.", "The gap junction communication channel.", "Molecular biology and genetics of gap junction channels.", "Diverse functions of vertebrate gap junctions.", "Innexins: a family of invertebrate gap-junction proteins.", "Gap junctions in the brain: where...
[ 1996, 1996, 1992, 1998, 1998, 1993, 1995 ]
7
[ "IPR000500" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 664 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 2, 3, 3 ]
4
true
Family
Gap junction alpha-5 protein (Cx40)
Gap junction alpha-5 protein (Cx40)
Connexin40
2
IPR002265
2,265
Gap junction alpha-6 protein (Cx45)
Connexin45
Family
576
false
false
The connexins are a family of integral membrane proteins that oligomerise to form intercellular channels that are clustered at gap junctions. These channels are specialised sites of cell-cell contact that allow the passage of ions, intracellular metabolites and messenger molecules (with molecular weight less than 1-2kD...
[ "GO:0007154", "GO:0005922" ]
[ "cell communication", "connexin complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01136" ]
[ "CONNEXINA6" ]
[ 576 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-112303", "R-BTA-190861", "R-GGA-112303", "R-GGA-190861", "R-HSA-112303", "R-HSA-190861", "R-MMU-112303", "R-MMU-190861", "R-RNO-112303", "R-RNO-190861", "R-SSC-112303", "R-SSC-190861" ]
[ "REACTOME:R-BTA-112303", "REACTOME:R-BTA-190861", "REACTOME:R-GGA-112303", "REACTOME:R-GGA-190861", "REACTOME:R-HSA-112303", "REACTOME:R-HSA-190861", "REACTOME:R-MMU-112303", "REACTOME:R-MMU-190861", "REACTOME:R-RNO-112303", "REACTOME:R-RNO-190861", "REACTOME:R-SSC-112303", "REACTOME:R-SSC-190...
12
[]
0
[ "PUB00000087", "PUB00000926", "PUB00005237", "PUB00005511", "PUB00005532", "PUB00005545", "PUB00005549" ]
[ "8811187", "8608591", "1320430", "9861669", "9769729", "7685944", "7570999" ]
[ "Connexins, connexons, and intercellular communication.", "The gap junction communication channel.", "Molecular biology and genetics of gap junction channels.", "Diverse functions of vertebrate gap junctions.", "Innexins: a family of invertebrate gap-junction proteins.", "Gap junctions in the brain: where...
[ 1996, 1996, 1992, 1998, 1998, 1993, 1995 ]
7
[ "IPR000500" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 576 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 3, 3 ]
3
true
Family
Gap junction alpha-6 protein (Cx45)
Gap junction alpha-6 protein (Cx45)
Connexin45
9
IPR002267
2,267
Gap junction beta-1 protein (Cx32)
Connexin32
Family
578
false
false
The connexins are a family of integral membrane proteins that oligomerise to form intercellular channels that are clustered at gap junctions. These channels are specialised sites of cell-cell contact that allow the passage of ions, intracellular metabolites and messenger molecules (with molecular weight less than 1-2kD...
[ "GO:0007154", "GO:0005922" ]
[ "cell communication", "connexin complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01138" ]
[ "CONNEXINB1" ]
[ 578 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-190704", "R-HSA-190704", "R-HSA-190827", "R-HSA-190861", "R-MMU-190704", "R-RNO-190704" ]
[ "REACTOME:R-BTA-190704", "REACTOME:R-HSA-190704", "REACTOME:R-HSA-190827", "REACTOME:R-HSA-190861", "REACTOME:R-MMU-190704", "REACTOME:R-RNO-190704" ]
6
[ "7zxm", "7zxn", "7zxo", "7zxp", "7zxq", "7zxt", "8qjf", "8qjh", "8qk6", "8qki" ]
10
[ "PUB00000087", "PUB00000926", "PUB00003056", "PUB00005237", "PUB00005511", "PUB00005532", "PUB00005545", "PUB00005549" ]
[ "8811187", "8608591", "2843548", "1320430", "9861669", "9769729", "7685944", "7570999" ]
[ "Connexins, connexons, and intercellular communication.", "The gap junction communication channel.", "Sequence and developmental expression of mRNA coding for a gap junction protein in Xenopus.", "Molecular biology and genetics of gap junction channels.", "Diverse functions of vertebrate gap junctions.", ...
[ 1996, 1996, 1988, 1992, 1998, 1998, 1993, 1995 ]
8
[ "IPR000500" ]
[]
1
0
1
[ "Tetrapoda" ]
[ 578 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 2, 2 ]
3
true
Family
Gap junction beta-1 protein (Cx32)
Gap junction beta-1 protein (Cx32)
Connexin32
3
IPR002268
2,268
Connexin 26
Connexin26
Family
196
false
false
Gap junction beta-2 protein (also called connexin26, or Cx26) is a connexin of 226 amino acid residues that is often found together with Cx32 in epithelial tissues. In rodents, it seems essential for normal embryonic development; mice lacking Cx26 die in utero at about embryonic day 11. Absence of Cx26 impairs transpla...
[ "GO:0007154", "GO:0005922" ]
[ "cell communication", "connexin complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01139" ]
[ "CONNEXINB2" ]
[ 196 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-190872", "R-HSA-190704", "R-HSA-190827", "R-HSA-190861", "R-HSA-190872", "R-MMU-190872", "R-RNO-190872" ]
[ "REACTOME:R-BTA-190872", "REACTOME:R-HSA-190704", "REACTOME:R-HSA-190827", "REACTOME:R-HSA-190861", "REACTOME:R-HSA-190872", "REACTOME:R-MMU-190872", "REACTOME:R-RNO-190872" ]
7
[ "2zw3", "3iz1", "3iz2", "5er7", "5era", "6uvr", "6uvs", "6uvt", "7qeo", "7qeq", "7qer", "7qes", "7qet", "7qeu", "7qev", "7qew", "8q9z", "8qa0", "8qa1", "8qa2", "8qa3" ]
21
[ "PUB00000087", "PUB00000926", "PUB00005237", "PUB00005511", "PUB00005532", "PUB00005545", "PUB00005549" ]
[ "8811187", "8608591", "1320430", "9861669", "9769729", "7685944", "7570999" ]
[ "Connexins, connexons, and intercellular communication.", "The gap junction communication channel.", "Molecular biology and genetics of gap junction channels.", "Diverse functions of vertebrate gap junctions.", "Innexins: a family of invertebrate gap-junction proteins.", "Gap junctions in the brain: where...
[ 1996, 1996, 1992, 1998, 1998, 1993, 1995 ]
7
[ "IPR000500" ]
[]
1
0
1
[ "Bilateria" ]
[ 196 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 9, 5, 4 ]
3
true
Family
Connexin 26
Connexin 26
Connexin26
4
IPR002269
2,269
Gap junction beta-3 protein (Cx31)
Connexin31
Family
251
false
false
The connexins are a family of integral membrane proteins that oligomerise to form intercellular channels that are clustered at gap junctions. These channels are specialised sites of cell-cell contact that allow the passage of ions, intracellular metabolites and messenger molecules (with molecular weight less than 1-2kD...
[ "GO:0007154", "GO:0005922" ]
[ "cell communication", "connexin complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01140" ]
[ "CONNEXINB3" ]
[ 251 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-190861", "R-HSA-190861", "R-HSA-9725554", "R-MMU-190861", "R-RNO-190861" ]
[ "REACTOME:R-BTA-190861", "REACTOME:R-HSA-190861", "REACTOME:R-HSA-9725554", "REACTOME:R-MMU-190861", "REACTOME:R-RNO-190861" ]
5
[]
0
[ "PUB00000087", "PUB00000926", "PUB00005237", "PUB00005511", "PUB00005532", "PUB00005545", "PUB00005549", "PUB00006063" ]
[ "8811187", "8608591", "1320430", "9861669", "9769729", "7685944", "7570999", "2168416" ]
[ "Connexins, connexons, and intercellular communication.", "The gap junction communication channel.", "Molecular biology and genetics of gap junction channels.", "Diverse functions of vertebrate gap junctions.", "Innexins: a family of invertebrate gap-junction proteins.", "Gap junctions in the brain: where...
[ 1996, 1996, 1992, 1998, 1998, 1993, 1995, 1990 ]
8
[ "IPR000500" ]
[]
1
0
1
[ "Tetrapoda" ]
[ 251 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 2, 2 ]
3
true
Family
Gap junction beta-3 protein (Cx31)
Gap junction beta-3 protein (Cx31)
Connexin31
5
IPR002270
2,270
Gap junction beta-4 protein (Cx30.3)
Connexin-30.3
Family
166
false
false
The connexins are a family of integral membrane proteins that oligomerise to form intercellular channels that are clustered at gap junctions. These channels are specialised sites of cell-cell contact that allow the passage of ions, intracellular metabolites and messenger molecules (with molecular weight less than 1-2kD...
[ "GO:0005243", "GO:0007154", "GO:0005922" ]
[ "gap junction channel activity", "cell communication", "connexin complex" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01142" ]
[ "CONNEXINB5" ]
[ 166 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-190861", "R-MMU-190861", "R-RNO-190861" ]
[ "REACTOME:R-HSA-190861", "REACTOME:R-MMU-190861", "REACTOME:R-RNO-190861" ]
3
[]
0
[ "PUB00000087", "PUB00000926", "PUB00002737", "PUB00005237", "PUB00005511", "PUB00005532", "PUB00005545", "PUB00005549", "PUB00095326" ]
[ "8811187", "8608591", "1512260", "1320430", "9861669", "9769729", "7685944", "7570999", "20184948" ]
[ "Connexins, connexons, and intercellular communication.", "The gap junction communication channel.", "Two gap junction genes, connexin 31.1 and 30.3, are closely linked on mouse chromosome 4 and preferentially expressed in skin.", "Molecular biology and genetics of gap junction channels.", "Diverse function...
[ 1996, 1996, 1992, 1992, 1998, 1998, 1993, 1995, 2010 ]
9
[ "IPR000500" ]
[]
1
0
1
[ "Eutheria" ]
[ 166 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 3, 4 ]
3
true
Family
Gap junction beta-4 protein (Cx30.3)
Gap junction beta-4 protein (Cx30.3)
Connexin-30.3
6
IPR002271
2,271
Gap junction beta-5 protein (Cx31.1)
Connexin311
Family
151
false
false
The connexins are a family of integral membrane proteins that oligomerise to form intercellular channels that are clustered at gap junctions. These channels are specialised sites of cell-cell contact that allow the passage of ions, intracellular metabolites and messenger molecules (with molecular weight less than 1-2kD...
[ "GO:0007154", "GO:0005922" ]
[ "cell communication", "connexin complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR01141" ]
[ "CONNEXINB4" ]
[ 151 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-190861", "R-MMU-190861", "R-RNO-190861" ]
[ "REACTOME:R-HSA-190861", "REACTOME:R-MMU-190861", "REACTOME:R-RNO-190861" ]
3
[]
0
[ "PUB00000087", "PUB00000926", "PUB00002737", "PUB00005237", "PUB00005511", "PUB00005532", "PUB00005545", "PUB00005549", "PUB00095414" ]
[ "8811187", "8608591", "1512260", "1320430", "9861669", "9769729", "7685944", "7570999", "25388970" ]
[ "Connexins, connexons, and intercellular communication.", "The gap junction communication channel.", "Two gap junction genes, connexin 31.1 and 30.3, are closely linked on mouse chromosome 4 and preferentially expressed in skin.", "Molecular biology and genetics of gap junction channels.", "Diverse function...
[ 1996, 1996, 1992, 1992, 1998, 1998, 1993, 1995, 2015 ]
9
[ "IPR000500" ]
[]
1
0
1
[ "Eutheria" ]
[ 151 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 3, 2 ]
3
true
Family
Gap junction beta-5 protein (Cx31.1)
Gap junction beta-5 protein (Cx31.1)
Connexin311
6
IPR002272
2,272
Follicle stimulating hormone receptor
FSH_rcpt
Family
939
false
false
Glycoprotein hormone receptors are members the rhodopsin-like G-protein coupled receptor (GPCR) family. They function as receptors for the pituitary hormones thyrotropin (TSH receptor), follitropin (FSH receptor) and lutropin (LH receptor). In mammals the LH receptor is also the receptor for the placental hormone, huma...
[ "GO:0004963", "GO:0007186", "GO:0016020" ]
[ "follicle-stimulating hormone receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01143" ]
[ "FSHRECEPTOR" ]
[ 939 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "253", "R-HSA-375281", "R-HSA-418555", "R-MMU-375281", "R-MMU-418555", "R-RNO-375281" ]
[ "IUPHAR:253", "REACTOME:R-HSA-375281", "REACTOME:R-HSA-418555", "REACTOME:R-MMU-375281", "REACTOME:R-MMU-418555", "REACTOME:R-RNO-375281" ]
6
[ "1xwd", "2v9s", "2v9t", "4ay9", "4mqw", "8i2g", "8i2h" ]
7
[ "PUB00005254", "PUB00067404", "PUB00067405", "PUB00067406", "PUB00067407", "PUB00067408", "PUB00067409", "PUB00067410", "PUB00067411", "PUB00067412", "PUB00067413" ]
[ "8747461", "9408742", "8855829", "7553856", "12059813", "9811848", "10803590", "16026112", "1723141", "9707177", "12039074" ]
[ "Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions.", "The follicle-stimulating hormone receptor: biochemistry, molecular biology, physiology, and pathophysiology.", "Clinical features of primary ovarian failure caused by a poi...
[ 1995, 1997, 1996, 1995, 2002, 1998, 2000, 2004, 1991, 1998, 2002 ]
11
[ "IPR002131" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 939 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 8, 2, 3 ]
3
true
Family
Follicle stimulating hormone receptor
Follicle stimulating hormone receptor
FSH_rcpt
7
IPR002273
2,273
Lutropin-choriogonadotropic hormone receptor
LSH_rcpt
Family
1,065
false
false
Glycoprotein hormone receptors are members the rhodopsin-like G-protein coupled receptor (GPCR) family. They function as receptors for the pituitary hormones thyrotropin (TSH receptor), follitropin (FSH receptor) and lutropin (LH receptor). In mammals the LH receptor is also the receptor for the placental hormone, huma...
[ "GO:0004964", "GO:0007186", "GO:0016020" ]
[ "luteinizing hormone receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01144" ]
[ "LSHRECEPTOR" ]
[ 1065 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "254", "R-HSA-375281", "R-HSA-418555", "R-MMU-375281", "R-MMU-418555", "R-RNO-375281", "R-SSC-375281", "R-SSC-418555" ]
[ "IUPHAR:254", "REACTOME:R-HSA-375281", "REACTOME:R-HSA-418555", "REACTOME:R-MMU-375281", "REACTOME:R-MMU-418555", "REACTOME:R-RNO-375281", "REACTOME:R-SSC-375281", "REACTOME:R-SSC-418555" ]
8
[ "7fig", "7fih", "7fii", "7fij" ]
4
[ "PUB00005254", "PUB00067425", "PUB00067426", "PUB00067427", "PUB00067428" ]
[ "8747461", "12816543", "11133673", "9582090", "10493819" ]
[ "Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions.", "Multiple luteinizing hormone receptor (LHR) protein variants, interspecies reactivity of anti-LHR mAb clone 3B5, subcellular localization of LHR in human placenta, pelvic flo...
[ 1995, 2003, 2001, 1998, 1999 ]
5
[ "IPR002131" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 1065 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 9, 2, 5 ]
4
true
Family
Lutropin-choriogonadotropic hormone receptor
Lutropin-choriogonadotropic hormone receptor
LSH_rcpt
2
IPR002274
2,274
Thyrotropin receptor
TSH_rcpt
Family
1,778
false
false
Glycoprotein hormone receptors are members the rhodopsin-like G-protein coupled receptor (GPCR) family. They function as receptors for the pituitary hormones thyrotropin (TSH receptor), follitropin (FSH receptor) and lutropin (LH receptor). In mammals the LH receptor is also the receptor for the placental hormone, huma...
[ "GO:0004996", "GO:0007186", "GO:0016020" ]
[ "thyroid-stimulating hormone receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01145" ]
[ "TSHRECEPTOR" ]
[ 1778 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "255", "R-CFA-375281", "R-HSA-375281", "R-HSA-418555", "R-MMU-375281", "R-MMU-418555", "R-RNO-375281" ]
[ "IUPHAR:255", "REACTOME:R-CFA-375281", "REACTOME:R-HSA-375281", "REACTOME:R-HSA-418555", "REACTOME:R-MMU-375281", "REACTOME:R-MMU-418555", "REACTOME:R-RNO-375281" ]
7
[ "2xwt", "3g04", "7t9i", "7t9m", "7t9n", "7utz", "7xw5", "7xw6", "7xw7" ]
9
[ "PUB00005254", "PUB00067432", "PUB00067433", "PUB00067434", "PUB00067435", "PUB00067436", "PUB00067437" ]
[ "8747461", "2610690", "2558651", "15231707", "20378719", "23105486", "11444165" ]
[ "Structural predictions for the ligand-binding region of glycoprotein hormone receptors and the nature of hormone-receptor interactions.", "Cloning, sequencing and expression of the human thyrotropin (TSH) receptor: evidence for binding of autoantibodies.", "Molecular cloning, sequence and functional expression...
[ 1995, 1989, 1989, 2004, 2010, 2005, 2001 ]
7
[ "IPR002131" ]
[]
1
0
1
[ "Bilateria" ]
[ 1778 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 13, 10, 2, 7 ]
4
true
Family
Thyrotropin receptor
Thyrotropin receptor
TSH_rcpt
9
IPR002276
2,276
G protein-coupled receptor 4 orphan
GPR4_orph
Family
417
false
false
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...
[ "GO:0004930", "GO:0007186", "GO:0016020" ]
[ "G protein-coupled receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01147" ]
[ "GPR4RECEPTOR" ]
[ 417 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-373076", "R-BTA-416476", "R-HSA-373076", "R-HSA-416476", "R-MMU-373076", "R-MMU-416476", "R-RNO-373076", "R-RNO-416476" ]
[ "REACTOME:R-BTA-373076", "REACTOME:R-BTA-416476", "REACTOME:R-HSA-373076", "REACTOME:R-HSA-416476", "REACTOME:R-MMU-373076", "REACTOME:R-MMU-416476", "REACTOME:R-RNO-373076", "REACTOME:R-RNO-416476" ]
8
[ "8z3m", "8z3q", "8z3y", "8z65", "8z66", "8z67", "8z9o", "8z9p", "8zce", "8zcf", "8zf4", "8zf6", "8zf7", "8zf9", "8zfa", "8zfb", "8zfc", "8zfd", "8zfe", "8zfz", "9bip", "9iv6", "9j31", "9jco", "9jcp", "9jcq", "9jfu", "9jfv", "9jfw", "9jfx", "9jfz", "9jhp"...
38
[ "PUB00000131", "PUB00001118", "PUB00001970", "PUB00002477", "PUB00004960", "PUB00004961", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "2111655", "7832990", "8595909", "2830256", "8386361", "8170923", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "G proteins in signal transduction.", "Isolation of three novel human genes encoding G protein-coupled receptors.", "Isolation of a novel G protein-coupled receptor (GPR4) localized to chromosome 19q13.3.", "G protein involvement in receptor-effector coupling.", "Design of a discriminating fingerprint for G...
[ 1990, 1995, 1995, 1988, 1993, 1994, 2003, 1994, 2005, 2009, 2006, 2013 ]
12
[ "IPR000276" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 417 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 1, 2, 2 ]
4
true
Family
G protein-coupled receptor 4 orphan
G protein-coupled receptor 4 orphan
GPR4_orph
2
IPR002277
2,277
Lysophosphatidic acid receptor EDG-2
LPA_rcpt_EDG2
Family
1,724
false
false
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups [ ]. The term clan can...
[ "GO:0070915", "GO:0007186", "GO:0016020" ]
[ "lysophosphatidic acid receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS", "CDD" ]
[ "PR01148", "cd15344" ]
[ "EDG2RECEPTOR", "7tmA_LPAR1_Edg2" ]
[ 1722, 755 ]
2
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "272", "R-HSA-416476", "R-HSA-418594", "R-HSA-419408", "R-MMU-416476", "R-MMU-418594", "R-MMU-419408", "R-RNO-416476", "R-RNO-418594", "R-RNO-419408" ]
[ "IUPHAR:272", "REACTOME:R-HSA-416476", "REACTOME:R-HSA-418594", "REACTOME:R-HSA-419408", "REACTOME:R-MMU-416476", "REACTOME:R-MMU-418594", "REACTOME:R-MMU-419408", "REACTOME:R-RNO-416476", "REACTOME:R-RNO-418594", "REACTOME:R-RNO-419408" ]
10
[ "4z34", "4z35", "4z36", "7td0", "7td1", "7td2", "7yu3", "7yu4", "7yu5", "7yu6", "7yu7", "7yu8", "9izf", "9izg", "9izh", "9j5v" ]
16
[ "PUB00000131", "PUB00002477", "PUB00004960", "PUB00004961", "PUB00007103", "PUB00007104", "PUB00007190", "PUB00053635", "PUB00063577", "PUB00063578", "PUB00063579", "PUB00063580", "PUB00063816" ]
[ "2111655", "2830256", "8386361", "8170923", "11264467", "10603487", "11093753", "12679517", "8081729", "15914470", "18948278", "16753280", "23020293" ]
[ "G proteins in signal transduction.", "G protein involvement in receptor-effector coupling.", "Design of a discriminating fingerprint for G-protein-coupled receptors.", "Fingerprinting G-protein-coupled receptors.", "Lysophospholipid receptors.", "Life on the edg.", "Lysophosphatidic acid receptors.", ...
[ 1990, 1988, 1993, 1994, 2001, 1999, 2000, 2003, 1994, 2005, 2009, 2006, 2013 ]
13
[ "IPR004065" ]
[]
1
0
1
[ "Vertebrata", "bird metagenome" ]
[ 1723, 1 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 10, 5, 5, 2 ]
4
true
Family
Lysophosphatidic acid receptor EDG-2
Lysophosphatidic acid receptor EDG-2
LPA_rcpt_EDG2
4
IPR002278
2,278
Melatonin receptor 1A/1B
Mel_1A/1B_rcpt
Family
1,692
false
false
Melatonin is a naturally occurring compound found in animals, plants, and microbes [ , ]. In animals melatonin is secreted by the pineal gland during darkness [ , ]. It regulates a variety of neuroendocrine functions and is thought to play an essential role in circadian rhythms [ ]. Drugs that modify the action of mela...
[ "GO:0008502", "GO:0007186", "GO:0016020" ]
[ "melatonin receptor activity", "G protein-coupled receptor signaling pathway", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PRINTS" ]
[ "PR01149" ]
[ "MELATONIN1AR" ]
[ 1692 ]
1
[ "IUPHAR", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "287", "R-DRE-373076", "R-DRE-418594", "R-GGA-373076", "R-GGA-418594", "R-HSA-373076", "R-HSA-418594", "R-MMU-373076", "R-MMU-418594" ]
[ "IUPHAR:287", "REACTOME:R-DRE-373076", "REACTOME:R-DRE-418594", "REACTOME:R-GGA-373076", "REACTOME:R-GGA-418594", "REACTOME:R-HSA-373076", "REACTOME:R-HSA-418594", "REACTOME:R-MMU-373076", "REACTOME:R-MMU-418594" ]
9
[ "7db6", "7vgy", "7vgz", "7vh0" ]
4
[ "PUB00062419", "PUB00064597", "PUB00064598", "PUB00064599", "PUB00064600", "PUB00064601", "PUB00064602", "PUB00064603", "PUB00064604", "PUB00064605", "PUB00064606", "PUB00064607", "PUB00066873", "PUB00066874", "PUB00066875", "PUB00066876", "PUB00066877", "PUB00066878", "PUB000668...
[ "20605968", "15617532", "14987948", "15620576", "7946354", "7568007", "10413300", "9247266", "9737724", "9089668", "12183692", "9593596", "15206778", "19033551", "1649044", "17901231", "17298593", "16473858", "15992934", "8936344", "15357831", "9933574", "9051762", "118...
[ "International Union of Basic and Clinical Pharmacology. LXXV. Nomenclature, classification, and pharmacology of G protein-coupled melatonin receptors.", "Reduced hippocampal MT2 melatonin receptor expression in Alzheimer's disease.", "Expression of membrane and nuclear melatonin receptors in mouse peripheral o...
[ 2010, 2005, 2004, 2005, 1994, 1995, 1999, 1997, 1998, 1997, 2002, 1998, 2003, 2009, 1991, 2007, 2007, 2006, 2005, 1996, 2004, 1999, 1996, 2002, 1996 ]
25
[ "IPR000025" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 1692 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 4, 2, 4 ]
4
true
Family
Melatonin receptor 1A/1B
Melatonin receptor 1A/1B
Mel_1A/1B_rcpt
6