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
IPR015422
15,422
Pyridoxal phosphate-dependent transferase, small domain
PyrdxlP-dep_Trfase_small
Homologous_superfamily
1,057,631
false
false
The monomer of PLP-dependent transferases consists of two domains, a large domain and a small domain. This entry represents small domain, which has a complex α/β structure [ ]. It can be found in the following PLP-dependent transferase families: Aspartate aminotransferase (AAT)-like enzymes, such as aromatic aminoacid ...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:3.90.1150.10" ]
[ "" ]
[ 1057631 ]
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-1483213", "R-BTA-1660661", "R-BTA-189451", "R-BTA-196757", "R-BTA-2408508", "R-BTA-389661", "R-BTA-70921", "R-BTA-8963684", "R-BTA-8963693", "R-BTA-8964539", "R-BTA-9013408", "R-BTA-9837999", "R-BTA-9856872", "R-CEL-1442490", "R-CEL-1483213", "R-CEL-1614558", "R-CEL-1614603", ...
[ "REACTOME:R-BTA-1483213", "REACTOME:R-BTA-1660661", "REACTOME:R-BTA-189451", "REACTOME:R-BTA-196757", "REACTOME:R-BTA-2408508", "REACTOME:R-BTA-389661", "REACTOME:R-BTA-70921", "REACTOME:R-BTA-8963684", "REACTOME:R-BTA-8963693", "REACTOME:R-BTA-8964539", "REACTOME:R-BTA-9013408", "REACTOME:R-B...
216
[ "1aam", "1aat", "1aaw", "1ahe", "1ahf", "1ahg", "1ahx", "1ahy", "1aia", "1aib", "1aic", "1ajr", "1ajs", "1aka", "1akb", "1akc", "1ama", "1amq", "1amr", "1ams", "1arg", "1arh", "1ari", "1ars", "1art", "1asa", "1asb", "1asc", "1asd", "1ase", "1asf", "1asg"...
1,667
[ "PUB00006322", "PUB00014087", "PUB00035504", "PUB00035505", "PUB00035506", "PUB00035507", "PUB00035508", "PUB00035511", "PUB00035512", "PUB00035513", "PUB00035514", "PUB00035515", "PUB00043268", "PUB00153780", "PUB00153781" ]
[ "7748903", "10666573", "15581583", "8690703", "15189147", "17109392", "16763894", "17300176", "16790938", "15690345", "17014820", "15848278", "17583737", "20142041", "36320885" ]
[ "Pyridoxal phosphate-dependent enzymes.", "Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a.", "Reaction specificity in pyridoxal phosphate enzymes.", "Pyridoxal enzymes: mechanistic diversity and uniformity.", "Pyridoxal phosphate enzymes: mechanis...
[ 1995, 1999, 2005, 1995, 2004, 2006, 2006, 2007, 2006, 2005, 2006, 2005, 2007, 2010, 2022 ]
15
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 18878, 802928, 218073, 220, 17532 ]
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",...
[ 367, 49, 98, 64, 36, 210, 117, 38, 263, 186, 30, 27, 580 ]
13
true
Homologous_superfamily
Pyridoxal phosphate-dependent transferase, small domain
Pyridoxal phosphate-dependent transferase, small domain
PyrdxlP-dep_Trfase_small
3
IPR015424
15,424
Pyridoxal phosphate-dependent transferase
PyrdxlP-dep_Trfase
Homologous_superfamily
1,222,161
false
false
This entry represents the major region of PLP-dependent transferases. This domain has a three layer α/β/α sandwich topology, with mixed β-sheets of 7 strands. The major region can be found in the following PLP-dependent transferase families: Aspartate aminotransferase (AAT)-like enzymes, such as aromatic aminoacid amin...
[]
[]
[]
0
[ "SSF" ]
[ "SSF53383" ]
[ "" ]
[ 1222161 ]
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-1483213", "R-BTA-1614558", "R-BTA-1660661", "R-BTA-189451", "R-BTA-196757", "R-BTA-2408508", "R-BTA-389661", "R-BTA-70921", "R-BTA-888568", "R-BTA-888590", "R-BTA-8963684", "R-BTA-8963693", "R-BTA-8964539", "R-BTA-9013408", "R-BTA-947581", "R-BTA-9837999", "R-BTA-9856872", "...
[ "REACTOME:R-BTA-1483213", "REACTOME:R-BTA-1614558", "REACTOME:R-BTA-1660661", "REACTOME:R-BTA-189451", "REACTOME:R-BTA-196757", "REACTOME:R-BTA-2408508", "REACTOME:R-BTA-389661", "REACTOME:R-BTA-70921", "REACTOME:R-BTA-888568", "REACTOME:R-BTA-888590", "REACTOME:R-BTA-8963684", "REACTOME:R-BTA...
240
[ "1aam", "1aat", "1aaw", "1ahe", "1ahf", "1ahg", "1ahx", "1ahy", "1aia", "1aib", "1aic", "1ajr", "1ajs", "1aka", "1akb", "1akc", "1ama", "1amq", "1amr", "1ams", "1arg", "1arh", "1ari", "1ars", "1art", "1asa", "1asb", "1asc", "1asd", "1ase", "1asf", "1asg"...
1,791
[ "PUB00006322", "PUB00014087", "PUB00035504", "PUB00035505", "PUB00035506", "PUB00035507", "PUB00035508", "PUB00035511", "PUB00035512", "PUB00035513", "PUB00035514", "PUB00035515", "PUB00153780", "PUB00153781" ]
[ "7748903", "10666573", "15581583", "8690703", "15189147", "17109392", "16763894", "17300176", "16790938", "15690345", "17014820", "15848278", "20142041", "36320885" ]
[ "Pyridoxal phosphate-dependent enzymes.", "Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a.", "Reaction specificity in pyridoxal phosphate enzymes.", "Pyridoxal enzymes: mechanistic diversity and uniformity.", "Pyridoxal phosphate enzymes: mechanis...
[ 1995, 1999, 2005, 1995, 2004, 2006, 2006, 2007, 2006, 2005, 2006, 2005, 2010, 2022 ]
14
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 20310, 907896, 272958, 295, 20702 ]
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",...
[ 412, 59, 130, 79, 41, 298, 164, 47, 329, 235, 34, 31, 753 ]
13
true
Homologous_superfamily
Pyridoxal phosphate-dependent transferase
Pyridoxal phosphate-dependent transferase
PyrdxlP-dep_Trfase
1
IPR015425
15,425
Formin, FH2 domain
FH2_Formin
Domain
48,294
false
false
Formin homology (FH) proteins play a crucial role in the reorganisation of the actin cytoskeleton, which mediates various functions of the cell cortex including motility, adhesion, and cytokinesis [ ]. Formins are multidomain proteins that interact with diverse signalling molecules and cytoskeletal proteins, although s...
[]
[]
[]
0
[ "PFAM", "PROFILE", "SMART" ]
[ "PF02181", "PS51444", "SM00498" ]
[ "FH2", "FH2", "FH2" ]
[ 46979, 47563, 43082 ]
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-5663220", "R-BTA-9013106", "R-CEL-5663220", "R-CEL-8980692", "R-CEL-9013149", "R-DME-5663220", "R-DME-6785631", "R-DME-6798695", "R-DME-8980692", "R-DME-9013026", "R-DME-9013149", "R-DME-9013404", "R-DME-9013405", "R-DME-9013406", "R-DME-9013408", "R-DME-9013423", "R-DME-90350...
[ "REACTOME:R-BTA-5663220", "REACTOME:R-BTA-9013106", "REACTOME:R-CEL-5663220", "REACTOME:R-CEL-8980692", "REACTOME:R-CEL-9013149", "REACTOME:R-DME-5663220", "REACTOME:R-DME-6785631", "REACTOME:R-DME-6798695", "REACTOME:R-DME-8980692", "REACTOME:R-DME-9013026", "REACTOME:R-DME-9013149", "REACTOM...
60
[ "1ux4", "1ux5", "1v9d", "1y64", "2j1d", "2z6e", "3o4x", "3obv", "4eah", "8rtt", "8rty", "8ru2", "8rv2", "9az4", "9azp", "9azq", "9b03", "9b0k", "9b27", "9b3d" ]
20
[ "PUB00014909", "PUB00014910", "PUB00014911", "PUB00014912", "PUB00014913" ]
[ "10631086", "12538772", "14576350", "14992721", "15006353" ]
[ "Formin family proteins in cytoskeletal control.", "ForC, a novel type of formin family protein lacking an FH1 domain, is involved in multicellular development in Dictyostelium discoideum.", "Fhos, a mammalian formin, directly binds to F-actin via a region N-terminal to the FH1 domain and forms a homotypic comp...
[ 2000, 2003, 2003, 2004, 2004 ]
5
[]
[]
0
0
null
[ "Bacteria", "Candidatus Heimdallarchaeum endolithica", "Eukaryota", "Viruses", "bird metagenome" ]
[ 27, 1, 48258, 6, 2 ]
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...
[ 110, 19, 176, 39, 89, 53, 1, 44, 73, 2, 3, 143 ]
12
true
Domain
Formin, FH2 domain
Formin, FH2 domain
FH2_Formin
2
IPR015426
15,426
Acetaldehyde dehydrogenase, C-terminal
Acetylaldehyde_DH_C
Domain
5,993
false
false
This C-terminal domain is found in prokaryotic acetaldehyde dehydrogenases, it adopts a structure consisting of an α-β-α-β(3) core, which mediates dimerisation of the protein [ ]. The acetaldehyde dehydrogenase family of bacterial enzymes catalyses the formation of acetyl-CoA from acetaldehyde in the 3-hydroxyphenylpro...
[ "GO:0008774", "GO:0009056" ]
[ "acetaldehyde dehydrogenase (acetylating) activity", "catabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PFAM", "CDD" ]
[ "PF09290", "cd23933" ]
[ "AcetDehyd-dimer", "ALDH_C" ]
[ 5993, 5915 ]
2
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]
[ "1.2.1.10", "PWY-5162", "PWY-5436", "PWY-5480", "PWY-6587", "PWY-7085", "PWY-7180", "PWY-8060", "PWY-8062" ]
[ "EC:1.2.1.10", "METACYC:PWY-5162", "METACYC:PWY-5436", "METACYC:PWY-5480", "METACYC:PWY-6587", "METACYC:PWY-7085", "METACYC:PWY-7180", "METACYC:PWY-8060", "METACYC:PWY-8062" ]
9
[ "1nvm", "4jn6", "4lrs", "4lrt", "7z3s", "8ih7" ]
6
[ "PUB00016385", "PUB00042979", "PUB00067280", "PUB00158508", "PUB00158509" ]
[ "12764229", "1732207", "23614353", "9169437", "16788178" ]
[ "Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate.", "Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600.", "Characterization of an aldolase-dehydrogenase complex fro...
[ 2003, 1992, 2013, 1997, 2006 ]
5
[]
[]
0
0
null
[ "Bacteria", "Bathycoccus sp. RCC716 virus 2", "Eukaryota", "Halobacteriales", "Sym plasmid", "unclassified sequences" ]
[ 5926, 1, 8, 13, 1, 44 ]
6
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Domain
Acetaldehyde dehydrogenase, C-terminal
Acetaldehyde dehydrogenase, C-terminal
Acetylaldehyde_DH_C
6
IPR015439
15,439
Integrin beta-2 superfamily
Integrin_b-2_sf
Homologous_superfamily
705
false
false
Integrins are the major metazoan receptors for cell adhesion to extracellular matrix proteins and, in vertebrates, also play important roles in certain cell-cell adhesions, make transmembrane connections to the cytoskeleton, and activate many intracellular signalling pathways [ , ]. An integrin receptor is a heterodime...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:6.20.50.10" ]
[ "" ]
[ 705 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-166016", "R-BTA-198933", "R-BTA-202733", "R-BTA-216083", "R-BTA-6798695", "R-HSA-166016", "R-HSA-198933", "R-HSA-202733", "R-HSA-216083", "R-HSA-6785807", "R-HSA-6798695", "R-MMU-166016", "R-MMU-198933", "R-MMU-202733", "R-MMU-216083", "R-MMU-6798695" ]
[ "REACTOME:R-BTA-166016", "REACTOME:R-BTA-198933", "REACTOME:R-BTA-202733", "REACTOME:R-BTA-216083", "REACTOME:R-BTA-6798695", "REACTOME:R-HSA-166016", "REACTOME:R-HSA-198933", "REACTOME:R-HSA-202733", "REACTOME:R-HSA-216083", "REACTOME:R-HSA-6785807", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-...
16
[ "1yuk", "2p26", "2p28", "3k6s", "3k71", "3k72", "4neh", "4nen", "5e6r", "5e6s", "5e6u", "5e6v", "5e6w", "5e6x", "5es4", "7p2d", "7usl", "7usm" ]
18
[ "PUB00009789", "PUB00015915", "PUB00015985", "PUB00035000", "PUB00035002", "PUB00035005", "PUB00035006", "PUB00035007" ]
[ "12297042", "14689578", "2467745", "12361595", "12234368", "10766246", "11812992", "12130787" ]
[ "Integrins: bidirectional, allosteric signaling machines.", "Integrin clipping: a novel adhesion switch?", "A novel vitronectin receptor integrin (alpha v beta x) is responsible for distinct adhesive properties of carcinoma cells.", "Integrins in development: moving on, responding to, and sticking to the extr...
[ 2002, 2004, 1989, 2002, 2002, 2000, 2002, 2002 ]
8
[]
[]
0
0
null
[ "Eukaryota" ]
[ 705 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 14, 7, 5 ]
3
true
Homologous_superfamily
Integrin beta-2 superfamily
Integrin beta-2 superfamily
Integrin_b-2_sf
9
IPR015445
15,445
TATA-Box binding protein-like 1
TBP-like
Family
1,417
false
false
This entry refers to TATA box-binding protein-like 1 proteins also known as TBP-like 1. TATA-Box binding protein (TBP) is a general factor that plays a central role in the activation of eukaryotic genes transcribed by RNA polymerase II [ , ]. TBP binds specifically to the TATA-box promoter element, which lies close to ...
[]
[]
[]
0
[ "CDD" ]
[ "cd04517" ]
[ "TLF" ]
[ 1417 ]
1
[]
[]
[]
0
[]
0
[ "PUB00004068", "PUB00004069", "PUB00017041", "PUB00044510", "PUB00080143", "PUB00080157", "PUB00080158", "PUB00080159" ]
[ "2374612", "2197561", "12878007", "16858867", "14685269", "11051541", "10470030", "15767669" ]
[ "Highly conserved core domain and unique N terminus with presumptive regulatory motifs in a human TATA factor (TFIID).", "Arabidopsis thaliana contains two genes for TFIID.", "The genetics of TBP and TBP-related factors.", "The general transcription machinery and general cofactors.", "The multicoloured worl...
[ 1990, 1990, 2003, 2006, 2004, 2000, 1999, 2005 ]
8
[ "IPR000814" ]
[]
1
0
1
[ "Eukaryota" ]
[ 1417 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 1, 5, 2, 2, 5 ]
6
true
Family
TATA-Box binding protein-like 1
TATA-Box binding protein-like 1
TBP-like
9
IPR015446
15,446
Bone morphogenetic protein 1/tolloid-like protein
BMP_1/tolloid-like
Family
4,731
false
false
This entry includes metalloproteases that serve as activators of a broader subset of the TGFbeta superfamily of proteins and are involved in the morphogenetic processes [ ]. Members of this family are bone morphogenetic protein 1 (BMP1), tolloid-like protein1/2 from mammals, dorsal-ventral patterning protein tolloid fr...
[ "GO:0004222" ]
[ "metalloendopeptidase activity" ]
[ "molecular_function" ]
1
[ "PIRSF" ]
[ "PIRSF001199" ]
[ "BMP_1/tolloid-like" ]
[ 4731 ]
1
[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.24.-", "PWY-8119", "R-CEL-1474228", "R-CEL-1650814", "R-CEL-2214320", "R-DME-1474228", "R-DME-1650814", "R-DME-2243919", "R-DRE-1650814", "R-DRE-2243919", "R-HSA-1474228", "R-HSA-1650814", "R-HSA-2214320", "R-HSA-2243919", "R-HSA-8963896", "R-MMU-1650814", "R-MMU-2214320", "R-...
[ "EC:3.4.24.-", "METACYC:PWY-8119", "REACTOME:R-CEL-1474228", "REACTOME:R-CEL-1650814", "REACTOME:R-CEL-2214320", "REACTOME:R-DME-1474228", "REACTOME:R-DME-1650814", "REACTOME:R-DME-2243919", "REACTOME:R-DRE-1650814", "REACTOME:R-DRE-2243919", "REACTOME:R-HSA-1474228", "REACTOME:R-HSA-1650814",...
19
[]
0
[ "PUB00072406" ]
[ "17560775" ]
[ "The bone morphogenetic protein 1/Tolloid-like metalloproteinases." ]
[ 2007 ]
1
[]
[]
0
0
null
[ "Eumetazoa" ]
[ 4731 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 6, 10, 7, 8, 9 ]
6
true
Family
Bone morphogenetic protein 1/tolloid-like protein
Bone morphogenetic protein 1/tolloid-like protein
BMP_1/tolloid-like
4
IPR015449
15,449
Potassium channel, calcium-activated, SK
K_chnl_Ca-activ_SK
Family
8,618
false
false
Potassium channels are the most diverse group of the ion channel family [ , ]. They are important in shaping the action potential, and in neuronal excitability and plasticity [ ]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [ ]: the pr...
[ "GO:0016286", "GO:0006813", "GO:0016020" ]
[ "small conductance calcium-activated potassium channel activity", "potassium ion transport", "membrane" ]
[ "molecular_function", "biological_process", "cellular_component" ]
3
[ "PFAM", "PRINTS", "PANTHER" ]
[ "PF03530", "PR01451", "PTHR10153" ]
[ "SK_channel", "SKCHANNEL", "" ]
[ 6271, 3424, 8553 ]
3
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CEL-1296052", "R-DME-1296052", "R-HSA-1296052", "R-HSA-9667769", "R-MMU-1296052", "R-RNO-1296052", "R-SSC-1296052" ]
[ "REACTOME:R-CEL-1296052", "REACTOME:R-DME-1296052", "REACTOME:R-HSA-1296052", "REACTOME:R-HSA-9667769", "REACTOME:R-MMU-1296052", "REACTOME:R-RNO-1296052", "REACTOME:R-SSC-1296052" ]
7
[ "1g4y", "1kkd", "1qx7", "3sjq", "4g27", "4g28", "4j9y", "4j9z", "4qnh", "5v02", "5v03", "5wbx", "5wc5", "6ale", "6cnm", "6cnn", "6cno", "6czq", "8v2g", "8v2h", "8v3g", "9ed1", "9eio", "9o48", "9o51", "9o52", "9o53", "9o5o", "9o7s", "9o85", "9o93", "9oa8"...
34
[ "PUB00001055", "PUB00001622", "PUB00002771", "PUB00004011", "PUB00004020", "PUB00006577", "PUB00008285", "PUB00009378", "PUB00035208", "PUB00035209", "PUB00035210", "PUB00035211", "PUB00035212", "PUB00035213", "PUB00036011" ]
[ "1772658", "1879548", "1373731", "2448635", "2451788", "2555158", "9687354", "11178249", "2432249", "7993625", "6099412", "2430185", "9280156", "10390643", "8781233" ]
[ "The molecular biology of K+ channels.", "Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.", "Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.", "Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Droso...
[ 1991, 1991, 1992, 1988, 1988, 1989, 1998, 2000, 1986, 1994, 1984, 1986, 1997, 1999, 1996 ]
15
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 85, 8533 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 20, 27, 10, 28, 18, 36 ]
6
true
Family
Potassium channel, calcium-activated, SK
Potassium channel, calcium-activated, SK
K_chnl_Ca-activ_SK
5
IPR015458
15,458
MDM4
MDM4
Family
872
false
false
MDM4, also known as MDMX, is a MDM2-related protein that has been shown to inhibit p53, although not as well as MDM2 [ , ].
[]
[]
[]
0
[ "PIRSF" ]
[ "PIRSF500699" ]
[ "MDM4" ]
[ 872 ]
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-DRE-2559580", "R-DRE-2559585", "R-DRE-6804757", "R-DRE-69541", "R-HSA-2559580", "R-HSA-2559585", "R-HSA-5689880", "R-HSA-6804756", "R-HSA-6804757", "R-HSA-6804760", "R-HSA-69541", "R-MMU-2559580", "R-MMU-2559585", "R-MMU-5689880", "R-MMU-6804756", "R-MMU-6804757", "R-MMU-6804760",...
[ "REACTOME:R-DRE-2559580", "REACTOME:R-DRE-2559585", "REACTOME:R-DRE-6804757", "REACTOME:R-DRE-69541", "REACTOME:R-HSA-2559580", "REACTOME:R-HSA-2559585", "REACTOME:R-HSA-5689880", "REACTOME:R-HSA-6804756", "REACTOME:R-HSA-6804757", "REACTOME:R-HSA-6804760", "REACTOME:R-HSA-69541", "REACTOME:R-...
25
[]
0
[ "PUB00059214", "PUB00059215" ]
[ "6163388", "16511572" ]
[ "Serum immunoreactive trypsin and trypsin inhibitors during acute pancreatitis.", "14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation." ]
[ 1980, 2006 ]
2
[ "IPR016495" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 872 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 3, 4, 6 ]
4
true
Family
MDM4
MDM4
MDM4
8
IPR015468
15,468
CD8 alpha subunit
CD8_asu
Family
1,222
false
false
The CD8 alpha subunit is a component of the CD8 α-β heterodimer and is additionally found as a homodimeric complex [ ]. Both of these species assist in the recognition of MHC class I-peptide complexes by the α-β T cell receptor (TCR). CD8 binds to constant regions of the peptide-MHC complex and augments antigen-specifi...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR10441" ]
[ "" ]
[ 1222 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CFA-198933", "R-HSA-198933", "R-MMU-198933", "R-RNO-198933" ]
[ "REACTOME:R-CFA-198933", "REACTOME:R-HSA-198933", "REACTOME:R-MMU-198933", "REACTOME:R-RNO-198933" ]
4
[ "1akj", "1bqh", "1cd8", "1nez", "2arj", "2atp", "2hp4", "2q3a", "3b9k", "3dmm", "3qzw", "5eb9", "5ebg", "5edx", "5z11", "6lhf", "6lhg", "7umg", "7uvf", "8ew6", "8hxs", "9jl0" ]
22
[ "PUB00034830", "PUB00034831", "PUB00034832" ]
[ "10493174", "12133804", "2107025" ]
[ "Molecular analysis of protein interactions mediating the function of the cell surface protein CD8.", "Molecular coordination of alphabeta T-cell receptors and coreceptors CD8 and CD4 in their recognition of peptide-MHC ligands.", "Interaction of the unique N-terminal region of tyrosine kinase p56lck with cytop...
[ 1999, 2002, 1990 ]
3
[]
[]
0
0
null
[ "Bilateria" ]
[ 1222 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 6, 9, 3 ]
4
true
Family
CD8 alpha subunit
CD8 alpha subunit
CD8_asu
6
IPR015476
15,476
Calcitonin gene-related peptide
Calcitonin_gene-rel_peptide
Family
816
false
false
The calcitonin (CT) gene is alternatively expressed in a tissue-specific manner, producing either the calcium regulatory hormone CT in the thyroid, or the neuropeptide calcitonin gene related peptide (CGRP) in the brain [ ]. In medullary carcinoma of the thyroid, both peptides are produced [ ]. The calcitonin regulator...
[ "GO:0005179", "GO:0005576" ]
[ "hormone activity", "extracellular region" ]
[ "molecular_function", "cellular_component" ]
2
[ "PRINTS" ]
[ "PR00817" ]
[ "CALCITONINB" ]
[ 816 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-CFA-419812", "R-HSA-418555", "R-HSA-419812", "R-MMU-418555", "R-MMU-419812", "R-RNO-419812", "R-SSC-418555", "R-SSC-419812" ]
[ "REACTOME:R-CFA-419812", "REACTOME:R-HSA-418555", "REACTOME:R-HSA-419812", "REACTOME:R-MMU-418555", "REACTOME:R-MMU-419812", "REACTOME:R-RNO-419812", "REACTOME:R-SSC-418555", "REACTOME:R-SSC-419812" ]
8
[ "6e3y", "7knu", "9auc" ]
3
[ "PUB00000335", "PUB00000353", "PUB00000472", "PUB00001543" ]
[ "1931969", "1988044", "3060108", "2985435" ]
[ "Solution conformation of salmon calcitonin in sodium dodecyl sulfate micelles as determined by two-dimensional NMR and distance geometry calculations.", "Solution structure of human calcitonin gene-related peptide by 1H NMR and distance geometry with restrained molecular dynamics.", "Peptides from the calciton...
[ 1991, 1991, 1988, 1985 ]
4
[ "IPR021117" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 816 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 3, 4, 7 ]
4
true
Family
Calcitonin gene-related peptide
Calcitonin gene-related peptide
Calcitonin_gene-rel_peptide
2
IPR015482
15,482
Syntrophin
Syntrophin
Family
6,800
false
false
The syntrophin family are intracellular membrane-associated proteins that interact with both ion channels and signalling proteins. As such, syntrophins appear to be important for linking ion channels to intracellular signalling pathways. Syntrophins are concentrated at postsynaptic sites at the neuromuscular junction a...
[ "GO:0005198" ]
[ "structural molecule activity" ]
[ "molecular_function" ]
1
[ "PANTHER" ]
[ "PTHR10554" ]
[ "" ]
[ 6800 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-9913351", "R-CEL-9913351", "R-HSA-9913351", "R-MMU-9913351" ]
[ "REACTOME:R-BTA-9913351", "REACTOME:R-CEL-9913351", "REACTOME:R-HSA-9913351", "REACTOME:R-MMU-9913351" ]
4
[ "1qav", "1z86", "1z87", "2adz", "2pdz", "2vrf", "4hop" ]
7
[ "PUB00034889", "PUB00034890" ]
[ "7691103", "9210230" ]
[ "Two forms of mouse syntrophin, a 58 kd dystrophin-associated protein, differ in primary structure and tissue distribution.", "Syntrophins: modular adapter proteins at the neuromuscular junction and the sarcolemma." ]
[ 1993, 1997 ]
2
[]
[]
0
0
null
[ "Eukaryota" ]
[ 6800 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 16, 11, 33, 16, 18 ]
6
true
Family
Syntrophin
Syntrophin
Syntrophin
4
IPR015484
15,484
CD3 protein, epsilon/gamma/delta subunit
CD3_esu/gsu/dsu
Family
2,245
false
false
The closely related CD3 epsilon, gamma and delta subunits constitute part of the invariant portion of the T cell receptor (TCR) complex. Both are transmembrane proteins with immunoglobulin-like domains in their extracellular regions. Each protein contains a single immunoreceptor tyrosine-based activation motif (ITAM) i...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR10570" ]
[ "" ]
[ 2245 ]
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-198933", "R-BTA-202424", "R-BTA-202427", "R-BTA-202430", "R-BTA-202433", "R-BTA-389948", "R-BTA-8856825", "R-BTA-8856828", "R-CFA-198933", "R-CFA-202424", "R-CFA-202427", "R-CFA-202430", "R-CFA-202433", "R-CFA-389948", "R-HSA-198933", "R-HSA-202424", "R-HSA-202427", "R-HSA-2...
[ "REACTOME:R-BTA-198933", "REACTOME:R-BTA-202424", "REACTOME:R-BTA-202427", "REACTOME:R-BTA-202430", "REACTOME:R-BTA-202433", "REACTOME:R-BTA-389948", "REACTOME:R-BTA-8856825", "REACTOME:R-BTA-8856828", "REACTOME:R-CFA-198933", "REACTOME:R-CFA-202424", "REACTOME:R-CFA-202427", "REACTOME:R-CFA-2...
60
[ "1jbj", "1sy6", "1xiw", "1xmw", "2mim", "3r08", "6jxr", "7fjd", "7fje", "7fjf", "7phr", "8es7", "8es8", "8es9", "8jc0", "8jcb", "8tw4", "8tw6", "8wxe", "8wy0", "8wyi", "8yc0", "8za6", "9bbc", "9c3e", "9ci8", "9cia", "9cq4", "9ip8", "9ip9", "9ipa", "9ipc"...
37
[ "PUB00016636" ]
[ "14552840" ]
[ "T-cell receptor signal transmission: who gives an ITAM?" ]
[ 2003 ]
1
[]
[]
0
0
null
[ "Gnathostomata" ]
[ 2245 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 13, 14, 14 ]
4
true
Family
CD3 protein, epsilon/gamma/delta subunit
CD3 protein, epsilon/gamma/delta subunit
CD3_esu/gsu/dsu
9
IPR015495
15,495
Myb transcription factor, plants
Myb_TF_plants
Family
34,902
false
false
This entry represents a group of Myb transcription factors from plants which are involved in a variety of plant developmental processes and stress responses [ ]. Members of the family play crucial roles in anther development, microsporogenesis, and tapetal function, which are essential for pollen development. They are ...
[]
[]
[]
0
[ "PANTHER", "PANTHER", "PANTHER", "PANTHER" ]
[ "PTHR10641", "PTHR47994", "PTHR47998", "PTHR47999" ]
[ "", "", "", "" ]
[ 10597, 11460, 3554, 9291 ]
4
[]
[]
[]
0
[ "6kks", "7fdl", "7fdo" ]
3
[ "PUB00001152", "PUB00004032", "PUB00005459", "PUB00098010", "PUB00107896", "PUB00150143", "PUB00153079", "PUB00155084" ]
[ "2824190", "3185713", "8882580", "23943862", "15361138", "15728674", "26184177", "22814374" ]
[ "The highly conserved amino-terminal region of the protein encoded by the v-myb oncogene functions as a DNA-binding domain.", "Viral myb oncogene encodes a sequence-specific DNA-binding activity.", "The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional co-repressor...
[ 1987, 1988, 1996, 2013, 2004, 2005, 2015, 2012 ]
8
[]
[]
0
0
null
[ "Eukaryota" ]
[ 34902 ]
1
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 325, 144, 276 ]
3
true
Family
Myb transcription factor, plants
Myb transcription factor, plants
Myb_TF_plants
1
IPR015496
15,496
Ubiquilin
Ubiquilin
Family
11,619
false
false
Ubiquitin [ ] is a protein of seventy six amino acid residues, found in all eukaryotic cells and whose sequence is extremely well conserved from protozoan to vertebrates. It is widely known as a post-translational tag used to signal a protein's hydrolytic destruction. Other functions for ubiquitin, depend on its differ...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR10677" ]
[ "" ]
[ 11619 ]
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-1169408", "R-BTA-5656169", "R-BTA-936440", "R-BTA-9833482", "R-BTA-9909505", "R-CEL-8856825", "R-DDI-8856825", "R-HSA-1169408", "R-HSA-168276", "R-HSA-168928", "R-HSA-5205685", "R-HSA-5656169", "R-HSA-5675482", "R-HSA-5689877", "R-HSA-8856825", "R-HSA-909733", "R-HSA-936440", ...
[ "REACTOME:R-BTA-1169408", "REACTOME:R-BTA-5656169", "REACTOME:R-BTA-936440", "REACTOME:R-BTA-9833482", "REACTOME:R-BTA-9909505", "REACTOME:R-CEL-8856825", "REACTOME:R-DDI-8856825", "REACTOME:R-HSA-1169408", "REACTOME:R-HSA-168276", "REACTOME:R-HSA-168928", "REACTOME:R-HSA-5205685", "REACTOME:R...
42
[ "1iyf", "1j8c", "1mg8", "1vej", "1wx7", "1wx8", "1x1m", "1yqb", "1z2m", "2bwe", "2bwf", "2dah", "2jy5", "2jy6", "2klc", "2knb", "2knz", "2mlb", "2mqj", "2nbv", "2zeq", "3b1l", "3m63", "3pse", "3r66", "3rt3", "3sdl", "4k95", "4zyn", "5c1z", "5c23", "5chf"...
64
[ "PUB00000623", "PUB00034999" ]
[ "1647207", "12645912" ]
[ "Genetic analysis of the ubiquitin system.", "The ubiquitin superfamily: members, features, and phylogenies." ]
[ 1991, 2002 ]
2
[]
[]
0
0
null
[ "Caldiarchaeum subterraneum", "Eukaryota", "metagenomes", "unclassified Klosneuvirinae" ]
[ 4, 11610, 3, 2 ]
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...
[ 12, 2, 9, 4, 37, 29, 1, 11, 39, 1, 1, 37 ]
12
true
Family
Ubiquilin
Ubiquilin
Ubiquilin
9
IPR015499
15,499
Cholecystokinin-like
CCK-like
Family
1,229
false
false
Gastrin and cholecystokinin (CCK) are structurally and functionally related peptide hormones that function as hormonal regulators of various digestive processes and feeding behaviours. They are known to induce gastric secretion, stimulate pancreatic secretion, increase blood circulation and water secretion in the stoma...
[ "GO:0005184", "GO:0007586" ]
[ "neuropeptide hormone activity", "digestion" ]
[ "molecular_function", "biological_process" ]
2
[ "PANTHER" ]
[ "PTHR10786" ]
[ "" ]
[ 1229 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-375276", "R-BTA-416476", "R-HSA-375276", "R-HSA-416476", "R-MMU-375276", "R-MMU-416476", "R-RNO-375276", "R-RNO-416476", "R-SSC-375276", "R-SSC-416476" ]
[ "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", "REACTOME:R-SSC-375276", "REACTOME:R-SSC-416476" ]
10
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Gnathostomata" ]
[ 1229 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 3, 3, 6 ]
4
true
Family
Cholecystokinin-like
Cholecystokinin-like
CCK-like
4
IPR015505
15,505
Coronin
Coronin
Family
15,037
false
false
Coronins are evoluntionarily conserved WD-repeat-containing proteins mostly involved in actin cytoskeleton organisation. The WD40 motif is found in a multitude of eukaryotic proteins involved in a variety of cellular processes [ ]. Repeated WD40 motifs act as a site for protein-protein interaction, and proteins contain...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR10856" ]
[ "" ]
[ 15037 ]
1
[ "REACTOME" ]
[ "R-HSA-9636383" ]
[ "REACTOME:R-HSA-9636383" ]
1
[ "2aq5", "2b4e", "4ozu", "7kyx", "7sty", "9qey", "9qf2", "9qfb", "9qfe", "9qfg", "9qfk" ]
11
[ "PUB00014164", "PUB00035080", "PUB00035082", "PUB00039364", "PUB00063875", "PUB00063876", "PUB00063877", "PUB00063878", "PUB00063888", "PUB00063890", "PUB00063893" ]
[ "11761326", "10461187", "12499356", "16407068", "18925375", "15892111", "18925371", "18925376", "18775315", "17350576", "1661669" ]
[ "Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes.", "The coronin family of actin-associated proteins.", "Direct regulation of Arp2/3 complex activity and function by the actin binding protein coronin.", "The crystal structure of murine coronin-1: a regulator of actin cytoskeletal dynamics in lymphocyt...
[ 2001, 1999, 2002, 2006, 2008, 2005, 2008, 2008, 2008, 2007, 1991 ]
11
[]
[]
0
0
null
[ "Eukaryota" ]
[ 15037 ]
1
[ "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)", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strai...
[ 5, 41, 7, 65, 45, 1, 36, 1, 1 ]
9
true
Family
Coronin
Coronin
Coronin
7
IPR015507
15,507
Ribosomal RNA large subunit methyltransferase E
rRNA-MeTfrase_E
Family
22,125
false
false
The ribosomal RNA large subunit methyltransferase E ( ) methylates the 23S rRNA. It specifically methylates the uridine in position 2552 of 23s rRNA in the 50S particle using S-adenosyl-L-methionine as a substrate [ ]. It was previously known as cell division protein FtsJ. This entry represents the ribosomal RNA large ...
[ "GO:0008168", "GO:0001510" ]
[ "methyltransferase activity", "RNA methylation" ]
[ "molecular_function", "biological_process" ]
2
[ "HAMAP", "PIRSF" ]
[ "MF_01547", "PIRSF005461" ]
[ "RNA_methyltr_E", "23S_rRNA_mtase" ]
[ 21824, 12711 ]
2
[ "EC", "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.1.1", "2.1.1.166", "R-HSA-6782315", "R-HSA-6791226", "R-HSA-6793080", "R-MMU-6791226", "R-RNO-6791226" ]
[ "EC:2.1.1", "EC:2.1.1.166", "REACTOME:R-HSA-6782315", "REACTOME:R-HSA-6791226", "REACTOME:R-HSA-6793080", "REACTOME:R-MMU-6791226", "REACTOME:R-RNO-6791226" ]
7
[ "1eiz", "1ej0", "2nyu", "2plw", "3dou", "6elz", "6em5", "6jp6", "6jpl", "6ylx", "7nac", "7nad", "7naf", "7o9k", "7o9m", "7ods", "7ohr", "7ohv", "7r6k", "7r72", "7r7a", "7r7o", "7u0h", "8esq", "8esr", "8etc", "8etj", "8fkp", "8fkq", "8fkr", "8fks", "8fkt"...
48
[ "PUB00016804", "PUB00054996" ]
[ "10748051", "11927565" ]
[ "The FtsJ/RrmJ heat shock protein of Escherichia coli is a 23 S ribosomal RNA methyltransferase.", "Trm7p catalyses the formation of two 2'-O-methylriboses in yeast tRNA anticodon loop." ]
[ 2000, 2002 ]
2
[]
[ "IPR004512", "IPR028589", "IPR028590" ]
0
3
0
[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]
[ 703, 9534, 11735, 153 ]
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",...
[ 17, 5, 7, 5, 1, 9, 3, 4, 8, 6, 3, 3, 21 ]
13
true
Family
Ribosomal RNA large subunit methyltransferase E
Ribosomal RNA large subunit methyltransferase E
rRNA-MeTfrase_E
4
IPR015510
15,510
Peptidoglycan recognition protein
PGRP
Family
16,913
false
false
This is a group of animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme [ ]. The bacteriophage molecule, but not its moth homologue, has been shown to have N-acetylmuramoyl-L-alanine amidase activity. One member, Tag7, is a cytokine [ ].
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR11022" ]
[ "" ]
[ 16913 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-6798695", "R-BTA-6803157", "R-DME-209171", "R-DME-209266", "R-DME-214397", "R-DME-214399", "R-DME-214411", "R-DME-214416", "R-DME-6798695", "R-DME-6803157", "R-HSA-6798695", "R-HSA-6803157", "R-MMU-6798695", "R-MMU-6803157", "R-RNO-6798695", "R-RNO-6803157" ]
[ "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-6803157", "REACTOME:R-DME-209171", "REACTOME:R-DME-209266", "REACTOME:R-DME-214397", "REACTOME:R-DME-214399", "REACTOME:R-DME-214411", "REACTOME:R-DME-214416", "REACTOME:R-DME-6798695", "REACTOME:R-DME-6803157", "REACTOME:R-HSA-6798695", "REACTOME:R-HS...
16
[ "1aro", "1lba", "1oht", "1s2j", "1sk3", "1sk4", "1sxr", "1twq", "1yck", "1z6i", "2aph", "2cb3", "2eav", "2eax", "2f2l", "2r2k", "2r90", "2rkq", "2xz4", "2xz8", "2z9n", "3c2x", "3cg9", "3cor", "3cxa", "3ep1", "3ng4", "3nno", "3nw3", "3o4k", "3ogx", "3qj1"...
73
[ "PUB00009690", "PUB00009691" ]
[ "9707603", "9660837" ]
[ "A peptidoglycan recognition protein in innate immunity conserved from insects to humans.", "Molecular cloning and characterization of the mouse tag7 gene encoding a novel cytokine." ]
[ 1998, 1998 ]
2
[]
[ "IPR017331", "IPR034689" ]
0
2
0
[ "Bacteria", "Eukaryota", "Methanosarcina mazei", "Viruses", "metagenomes" ]
[ 9452, 6734, 2, 613, 112 ]
5
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 7, 36, 4, 12, 15 ]
5
true
Family
Peptidoglycan recognition protein
Peptidoglycan recognition protein
PGRP
1
IPR015513
15,513
Semaphorin 3E, Sema domain
Semaphorin_3E_Sema
Domain
555
false
false
This entry represents the Sema domain of Semaphorin 3E, a protein interacting module located at the N-terminal end that contain four disulfide bonds formed by eight conserved cysteine residues. It serves as a receptor-recognition and -binding module [ ]. Semaphorins were first cloned as recognised mediators of cellular...
[]
[]
[]
0
[ "CDD" ]
[ "cd11253" ]
[ "Sema_3E" ]
[ 555 ]
1
[ "REACTOME", "REACTOME" ]
[ "R-HSA-416700", "R-MMU-416700" ]
[ "REACTOME:R-HSA-416700", "REACTOME:R-MMU-416700" ]
2
[]
0
[ "PUB00015414", "PUB00034855", "PUB00034856", "PUB00034857", "PUB00034858", "PUB00034879" ]
[ "12925274", "11956234", "10520995", "10520994", "10934324", "12213213" ]
[ "Structure of the semaphorin-3A receptor binding module.", "Semaphorins as signals for cell repulsion and invasion.", "Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates.", "Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors.", ...
[ 2003, 2002, 1999, 1999, 2000, 2002 ]
6
[ "IPR001627" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 555 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 3, 1, 5 ]
4
true
Domain
Semaphorin 3E, Sema domain
Semaphorin 3E, Sema domain
Semaphorin_3E_Sema
9
IPR015517
15,517
Deoxycytidylate deaminase-related
dCMP_deaminase-rel
Family
17,605
false
false
Deoxycytidylate deaminase ( ) (dCMP deaminase) hydrolyzes deoxycytidylate mono phosphate (dCMP) into deoxyuridine mono phosphate (dUMP), thus providing the nucleotide substrate for thymidylate synthase. The enzyme requires zinc for catalytic activity which is regulated by the ratio of dCTP to dTTP, both the end product...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR11086" ]
[ "" ]
[ 17605 ]
1
[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.5.4.12", "PWY-7210", "R-HSA-499943", "R-MMU-499943", "R-RNO-499943" ]
[ "EC:3.5.4.12", "METACYC:PWY-7210", "REACTOME:R-HSA-499943", "REACTOME:R-MMU-499943", "REACTOME:R-RNO-499943" ]
5
[ "1vq2", "2hvv", "2hvw", "2w4l", "4p9c", "4p9d", "4p9e", "5c2o", "7fh4", "7fh9", "9hfq", "9hfr", "9hfs", "9hft" ]
14
[ "PUB00002807", "PUB00047647", "PUB00070796", "PUB00070799" ]
[ "8428902", "18255096", "7685356", "16955368" ]
[ "T4-phage deoxycytidylate deaminase is a metalloprotein containing two zinc atoms per subunit.", "Crystal structures of Streptococcus mutans 2'-deoxycytidylate deaminase and its complex with substrate analog and allosteric regulator dCTP x Mg2+.", "Primary structure of human deoxycytidylate deaminase and overex...
[ 1993, 2008, 1993, 2006 ]
4
[]
[ "IPR013404", "IPR016473" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 307, 9875, 5871, 1150, 402 ]
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...
[ 5, 1, 4, 2, 15, 7, 1, 5, 21, 1, 1, 9 ]
12
true
Family
Deoxycytidylate deaminase-related
Deoxycytidylate deaminase-related
dCMP_deaminase-rel
7
IPR015520
15,520
Imaginal disc growth factor
IDGF
Family
484
false
false
Imaginal disc growth factors (IDGFs), also known as chitinase-like proteins, are soluble factors involved in the regulation of proliferation in imaginal discs [ ]. They are a family of growth factors identified in insects that include at least five members, some of which are encoded by genes in a tight cluster [ ]. The...
[]
[]
[]
0
[ "CDD" ]
[ "cd02873" ]
[ "GH18_IDGF" ]
[ 484 ]
1
[ "REACTOME" ]
[ "R-DME-6798695" ]
[ "REACTOME:R-DME-6798695" ]
1
[ "1jnd", "1jne", "9g3q" ]
3
[ "PUB00026449", "PUB00034892", "PUB00085931", "PUB00085932" ]
[ "11821393", "11444043", "17594485", "12242232" ]
[ "Crystal structure of imaginal disc growth factor-2. A member of a new family of growth-promoting glycoproteins from Drosophila melanogaster.", "Growth factors controlling imaginal disc growth in Drosophila.", "Chitinase family GH18: evolutionary insights from the genomic history of a diverse protein family.", ...
[ 2002, 2001, 2007, 2002 ]
4
[ "IPR050314" ]
[]
1
0
1
[ "Neoptera" ]
[ 484 ]
1
[ "Drosophila melanogaster" ]
[ 20 ]
1
true
Family
Imaginal disc growth factor
Imaginal disc growth factor
IDGF
1
IPR015525
15,525
Breast cancer type 2 susceptibility protein
BRCA2
Family
4,600
false
false
The breast cancer type 2 susceptibility protein (BRCA2) is a breast tumour suppressor involved in double-strand break repair and/or homologous recombination [ ]. BRCA2 gene expression is regulated in a cell-cycle dependent manner and peak expression of BRCA2 mRNA occurring in S phase, suggesting BRCA2 may participate i...
[ "GO:0000724", "GO:0006281" ]
[ "double-strand break repair via homologous recombination", "DNA repair" ]
[ "biological_process", "biological_process" ]
2
[ "PIRSF", "PANTHER" ]
[ "PIRSF002397", "PTHR11289" ]
[ "BRCA2", "" ]
[ 1251, 4600 ]
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-HSA-5685939", "R-HSA-5685942", "R-HSA-5693554", "R-HSA-5693568", "R-HSA-5693579", "R-HSA-5693616", "R-HSA-912446", "R-HSA-9701192", "R-HSA-9704331", "R-HSA-9704646", "R-HSA-9709275", "R-HSA-9709570", "R-HSA-9709603", "R-HSA-9763198", "R-MMU-5685939", "R-MMU-5685942", "R-MMU-569356...
[ "REACTOME:R-HSA-5685939", "REACTOME:R-HSA-5685942", "REACTOME:R-HSA-5693554", "REACTOME:R-HSA-5693568", "REACTOME:R-HSA-5693579", "REACTOME:R-HSA-5693616", "REACTOME:R-HSA-912446", "REACTOME:R-HSA-9701192", "REACTOME:R-HSA-9704331", "REACTOME:R-HSA-9704646", "REACTOME:R-HSA-9709275", "REACTOME...
24
[ "1iyj", "1miu", "1mje" ]
3
[ "PUB00003901", "PUB00005803", "PUB00005815", "PUB00005834", "PUB00007172", "PUB00027524", "PUB00066909", "PUB00085103" ]
[ "8673099", "9405383", "9560268", "9811893", "10551859", "12442171", "20513136", "22077663" ]
[ "Internal repeats in the BRCA2 protein sequence.", "RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene brca2.", "The BRC repeats in BRCA2 are critical for RAD51 binding and resistance to methyl methanesulfonate treatment.", "The BRCA2 gene product funct...
[ 1996, 1997, 1998, 1998, 1999, 2002, 2010, 2012 ]
8
[]
[]
0
0
null
[ "Eukaryota" ]
[ 4600 ]
1
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 18, 3, 1, 92, 5, 7, 7, 34 ]
8
true
Family
Breast cancer type 2 susceptibility protein
Breast cancer type 2 susceptibility protein
BRCA2
8
IPR015526
15,526
Frizzled/secreted frizzled-related protein
Frizzled/SFRP
Family
21,842
false
false
This entry includes both frizzled proteins and secreted frizzled-related proteins (SFRP). Frizzleds are seven transmembrane-spanning proteins that constitute an unconventional class of G protein-coupled receptors [ ]. They have important regulatory roles during embryonic development [ , ]. Frizzleds expose their large ...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR11309" ]
[ "" ]
[ 21842 ]
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-4086398", "R-CEL-4086400", "R-CEL-4608870", "R-CEL-4641262", "R-CEL-4641263", "R-CEL-5140745", "R-DME-209214", "R-DME-209338", "R-DME-209387", "R-DME-209440", "R-DME-209472", "R-DME-216119", "R-DME-216217", "R-DME-350368", "R-DME-350376", "R-DME-350379", "R-DME-350411", "R-D...
[ "REACTOME:R-CEL-4086398", "REACTOME:R-CEL-4086400", "REACTOME:R-CEL-4608870", "REACTOME:R-CEL-4641262", "REACTOME:R-CEL-4641263", "REACTOME:R-CEL-5140745", "REACTOME:R-DME-209214", "REACTOME:R-DME-209338", "REACTOME:R-DME-209387", "REACTOME:R-DME-209440", "REACTOME:R-DME-209472", "REACTOME:R-D...
79
[ "1ijx", "1ijy", "2mah", "4c79", "4c7a", "4f0a", "4jkv", "4n4w", "4o9r", "4qim", "4qin", "5bpb", "5bpq", "5bqc", "5bqe", "5cl1", "5cm4", "5kzv", "5kzy", "5kzz", "5l7d", "5l7i", "5t44", "5un5", "5un6", "5urv", "5ury", "5urz", "5uwg", "5v56", "5v57", "5wbs"...
81
[ "PUB00001934", "PUB00004042", "PUB00033723", "PUB00060605", "PUB00060609", "PUB00060610", "PUB00061907" ]
[ "2174014", "2493583", "11452312", "10347172", "17884187", "21314612", "9288750" ]
[ "Molecular structure of frizzled, a Drosophila tissue polarity gene.", "A Drosophila tissue polarity locus encodes a protein containing seven potential transmembrane domains.", "Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains.", "Interaction of frizzled relat...
[ 1990, 1989, 2001, 1999, 2007, 2010, 1997 ]
7
[]
[]
0
0
null
[ "Eukaryota", "Kangiella spongicola" ]
[ 21841, 1 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 9, 39, 22, 44, 40, 45 ]
6
true
Family
Frizzled/secreted frizzled-related protein
Frizzled/secreted frizzled-related protein
Frizzled/SFRP
3
IPR015527
15,527
Peptidase C26, gamma-glutamyl hydrolase
Pept_C26_g-glut_hydrolase
Family
4,228
false
false
Gamma-glutamyl hydrolase (GH) is a lysosomal and secreted glycoprotein that hydrolyses the gamma-glutamyl tail of antifolate and folate polyglutamates. Tumour cells that have high levels of GH are inherently resistant to classical antifolates, and further resistance can be acquired by elevations in GH following exposur...
[ "GO:0008242" ]
[ "omega peptidase activity" ]
[ "molecular_function" ]
1
[ "PROFILE", "PANTHER" ]
[ "PS51275", "PTHR11315" ]
[ "PEPTIDASE_C26_GGH", "" ]
[ 4084, 4179 ]
2
[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.4.19.9", "PWY-2161", "R-BTA-6798695", "R-DDI-6798695", "R-HSA-6798695", "R-MMU-6798695", "R-RNO-6798695" ]
[ "EC:3.4.19.9", "METACYC:PWY-2161", "REACTOME:R-BTA-6798695", "REACTOME:R-DDI-6798695", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-6798695" ]
7
[ "1l9x", "4l7q", "4l8f", "4l8w", "4l8y", "4l95" ]
6
[ "PUB00015219", "PUB00034829" ]
[ "11953431", "10739875" ]
[ "Three-dimensional structure of human gamma -glutamyl hydrolase. A class I glatamine amidotransferase adapted for a complex substate.", "Glutamyl hydrolase. pharmacological role and enzymatic characterization." ]
[ 2002, 2000 ]
2
[ "IPR011697" ]
[]
1
0
1
[ "Eukaryota", "Megaviricetes", "metagenomes" ]
[ 4196, 6, 26 ]
3
[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 17, 5, 3, 7, 3, 3, 2, 16 ]
8
true
Family
Peptidase C26, gamma-glutamyl hydrolase
Peptidase C26, gamma-glutamyl hydrolase
Pept_C26_g-glut_hydrolase
3
IPR015528
15,528
Interleukin-12 beta
IL-12_beta
Family
1,304
false
false
This entry represents Interleukin-12 beta. Interleukins are a group of cytokines that have important roles in cell growth, differentiation, and motility, and in the functioning of the immune system. Interleukin-12 (also known as natural killer cell stimulatory factor, and cytotoxic lymphocyte maturation factor) is a 75...
[]
[]
[]
0
[ "PIRSF", "PRINTS" ]
[ "PIRSF038007", "PR01928" ]
[ "IL_12_beta", "INTRLEUKN12B" ]
[ 943, 1277 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-6783783", "R-HSA-6785807", "R-HSA-9020591", "R-HSA-9020933", "R-MMU-9020591", "R-MMU-9020933", "R-SSC-9020591", "R-SSC-9020933" ]
[ "REACTOME:R-HSA-6783783", "REACTOME:R-HSA-6785807", "REACTOME:R-HSA-9020591", "REACTOME:R-HSA-9020933", "REACTOME:R-MMU-9020591", "REACTOME:R-MMU-9020933", "REACTOME:R-SSC-9020591", "REACTOME:R-SSC-9020933" ]
8
[ "1f42", "1f45", "3d85", "3d87", "3duh", "3hmx", "3qwr", "4grw", "5mj3", "5mj4", "5mxa", "5mzv", "5njd", "6sff", "6smc", "6sp3", "6uib", "6wdq", "7pur", "7r3n", "8cr5", "8cr6", "8cr8", "8odz", "8oe0", "8oe4", "8pb1", "8uui", "8xrp", "8yi7" ]
30
[ "PUB00013064", "PUB00043736", "PUB00043737" ]
[ "11114383", "10426995", "18490716" ]
[ "Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with biological activities similar as well as distinct from IL-12.", "Host defense mechanisms triggered by microbial lipoproteins through toll-like receptors.", "Tumor-secreted lactic acid promotes IL-23/IL-17 proinflammatory pathway." ]
[ 2000, 1999, 2008 ]
3
[]
[]
0
0
null
[ "Gnathostomata" ]
[ 1304 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 18, 1, 2, 4 ]
4
true
Family
Interleukin-12 beta
Interleukin-12 beta
IL-12_beta
3
IPR015529
15,529
Interleukin-18
IL-18
Family
743
false
false
Interleukins (IL) are a group of cytokines that play an important role in the immune system. They modulate inflammation and immunity by regulating growth, mobility and differentiation of lymphoid and other cells. Interleukin-18 (IL-18) is a potent proinflammatory cytokine that induces interferon-gamma (IFN-gamma) produ...
[]
[]
[]
0
[ "PIRSF", "PRINTS" ]
[ "PIRSF015162", "PR01933" ]
[ "Interleukin_18", "INTRLEUKIN18" ]
[ 679, 706 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-448706", "R-BTA-5620971", "R-BTA-9012546", "R-HSA-448706", "R-HSA-5620971", "R-HSA-6783783", "R-HSA-6785807", "R-HSA-9012546", "R-HSA-9660826", "R-MMU-448706", "R-MMU-5620971", "R-MMU-9012546", "R-RNO-448706", "R-RNO-5620971", "R-RNO-9012546", "R-SSC-448706", "R-SSC-5620971", ...
[ "REACTOME:R-BTA-448706", "REACTOME:R-BTA-5620971", "REACTOME:R-BTA-9012546", "REACTOME:R-HSA-448706", "REACTOME:R-HSA-5620971", "REACTOME:R-HSA-6783783", "REACTOME:R-HSA-6785807", "REACTOME:R-HSA-9012546", "REACTOME:R-HSA-9660826", "REACTOME:R-MMU-448706", "REACTOME:R-MMU-5620971", "REACTOME:R...
18
[ "1j0s", "2vxt", "3f62", "3wo2", "3wo3", "3wo4", "4eee", "4ekx", "4hjj", "4r6u", "4xfs", "4xft", "4xfu", "7al7", "8j6k", "8spb", "8sv1", "8urv", "9od7", "9od9" ]
20
[ "PUB00026216", "PUB00034867", "PUB00034868", "PUB00034869" ]
[ "14528293", "14744554", "15464021", "15174967" ]
[ "The structure and binding mode of interleukin-18.", "A potential role of interleukin 18 in severe falciparum malaria.", "Interleukin-18 bioactivity: a novel target for immunopharmacological anti-inflammatory intervention.", "Therapeutic potential of targeting IL-1 and IL-18 in inflammation." ]
[ 2003, 2004, 2004, 2004 ]
4
[ "IPR000975" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 743 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 6, 4 ]
3
true
Family
Interleukin-18
Interleukin-18
IL-18
8
IPR015550
15,550
Glucagon
Glucagon
Family
1,286
false
false
A number of polypeptidic hormones, mainly expressed in the intestine or the pancreas, belong to a group of structurally related peptides [ , ]. Once such hormone, glucagon is widely distributed and produced in the alpha-cells of pancreatic islets [ ]. It affects glucose metabolism in the liver [ ] by inhibiting glycoge...
[ "GO:0005179" ]
[ "hormone activity" ]
[ "molecular_function" ]
1
[ "PANTHER" ]
[ "PTHR11418" ]
[ "" ]
[ 1286 ]
1
[ "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "GenProp2087", "GenProp2089", "GenProp2092", "R-BTA-163359", "R-BTA-381676", "R-BTA-381771", "R-BTA-416476", "R-BTA-418555", "R-BTA-420092", "R-BTA-422085", "R-GGA-163359", "R-GGA-381771", "R-GGA-416476", "R-GGA-418555", "R-GGA-420092", "R-GGA-422085", "R-HSA-163359", "R-HSA-381676...
[ "GP:GenProp2087", "GP:GenProp2089", "GP:GenProp2092", "REACTOME:R-BTA-163359", "REACTOME:R-BTA-381676", "REACTOME:R-BTA-381771", "REACTOME:R-BTA-416476", "REACTOME:R-BTA-418555", "REACTOME:R-BTA-420092", "REACTOME:R-BTA-422085", "REACTOME:R-GGA-163359", "REACTOME:R-GGA-381771", "REACTOME:R-G...
43
[ "1bh0", "1d0r", "1gcn", "1kx6", "1nau", "2g49", "2l63", "2l64", "2m5p", "2m5q", "3iol", "4apd", "4zgm", "5otu", "5otv", "5otw", "5otx", "5vai", "5yqz", "6eds", "6lmk", "6lml", "6nzn", "6phi", "6phj", "6phk", "6phl", "6phm", "6phn", "6pho", "6php", "6phq"...
56
[ "PUB00000024", "PUB00000025", "PUB00001745", "PUB00002491", "PUB00004603", "PUB00088953" ]
[ "3133967", "3291691", "4076759", "3260236", "6577439", "17167473" ]
[ "Vasoactive intestinal polypeptide and related peptides. Isolation and chemistry.", "Glucagon and related peptides. Molecular structure and biological specificity.", "Primary structure of glucagon from an elasmobranchian fish. Torpedo marmorata.", "Isolation of peptide hormones from the pancreas of the bullfr...
[ 1988, 1988, 1985, 1988, 1983, 2006 ]
6
[]
[]
0
0
null
[ "Opisthokonta" ]
[ 1286 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 1, 2, 3 ]
4
true
Family
Glucagon
Glucagon
Glucagon
5
IPR015556
15,556
Plasminogen activator inhibitor-2
PAI-2
Family
61
false
false
Plasminogen activator inhibitor 2 (PAI-2; MEROPS identifier I04.007) is a serpin (SERine Proteinase INhibitor). Serpins belong to MEROPS inhibitor family I4 (clan ID) [ ]. PAI-2 has antiapoptosis activity, probably related to its interaction with the proteasome subunit PSMbeta1 [ ]. PAI-2 might be an important factor i...
[ "GO:0004867", "GO:0043066" ]
[ "serine-type endopeptidase inhibitor activity", "negative regulation of apoptotic process" ]
[ "molecular_function", "biological_process" ]
2
[ "CDD" ]
[ "cd19562" ]
[ "serpinB2_PAI-2" ]
[ 61 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-75205", "R-HSA-8950505", "R-MMU-75205", "R-RNO-75205" ]
[ "REACTOME:R-HSA-75205", "REACTOME:R-HSA-8950505", "REACTOME:R-MMU-75205", "REACTOME:R-RNO-75205" ]
4
[ "1by7", "1jrr", "2arq", "2arr" ]
4
[ "PUB00014133", "PUB00021278", "PUB00067573", "PUB00067574" ]
[ "14705960", "10368272", "14732874", "7499264" ]
[ "Evolutionary families of peptidase inhibitors.", "The crystal structure of plasminogen activator inhibitor 2 at 2.0 A resolution: implications for serpin function.", "Interaction of plasminogen activator inhibitor-2 and proteasome subunit, beta type 1.", "Plasminogen activator inhibitor type 2 inhibits tumor...
[ 2004, 1999, 2004, 1995 ]
4
[]
[]
0
0
null
[ "Boreoeutheria" ]
[ 61 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 2, 2, 2 ]
3
true
Family
Plasminogen activator inhibitor-2
Plasminogen activator inhibitor-2
PAI-2
3
IPR015576
15,576
Spermine synthase, animal
Spermine_synthase_animal
Family
1,759
false
false
The polyamines putrescine, spermidine and spermine represent a group of naturally occurring compounds exerting a bewildering number of biological effects. Their biosynthesis is accomplished by a concerted action of four different enzymes: ornithine decarboxylase, adenosylmethionine decarboxylase, spermidine synthase an...
[ "GO:0016768", "GO:0006597" ]
[ "spermine synthase activity", "spermine biosynthetic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PANTHER" ]
[ "PTHR46315" ]
[ "" ]
[ 1759 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.5.1.22", "R-BTA-351202", "R-HSA-351202", "R-MMU-351202" ]
[ "EC:2.5.1.22", "REACTOME:R-BTA-351202", "REACTOME:R-HSA-351202", "REACTOME:R-MMU-351202" ]
4
[ "3c6k", "3c6m" ]
2
[ "PUB00034968", "PUB00034969", "PUB00034970" ]
[ "1930914", "9467015", "7546290" ]
[ "Polyamines: from molecular biology to clinical applications.", "Spermine deficiency in Gy mice caused by deletion of the spermine synthase gene.", "Molecular cloning of a cDNA encoding human spermine synthase." ]
[ 1991, 1998, 1995 ]
3
[ "IPR001045" ]
[]
1
0
1
[ "Bacteria", "Opisthokonta" ]
[ 21, 1738 ]
2
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 5, 3, 3, 5 ]
5
true
Family
Spermine synthase, animal
Spermine synthase, animal
Spermine_synthase_animal
7
IPR015578
15,578
Neurotrophin-3
Neurotrophin-3
Family
3,256
false
false
During the development of the vertebrate nervous system, many neurons become redundant (because they have died, failed to connect to target cells, etc.) and are eliminated. At the same time, developing neurons send out axon outgrowths that contact their target cells [ ]. Such cells control their degree of innervation (...
[ "GO:0005165" ]
[ "neurotrophin receptor binding" ]
[ "molecular_function" ]
1
[ "PRINTS" ]
[ "PR01914" ]
[ "NEUROTROPHN3" ]
[ 3256 ]
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-1257604", "R-BTA-6811558", "R-BTA-9034013", "R-BTA-9034793", "R-BTA-9603381", "R-HSA-1257604", "R-HSA-2219530", "R-HSA-6811558", "R-HSA-9025046", "R-HSA-9034013", "R-HSA-9034015", "R-HSA-9034793", "R-HSA-9034864", "R-HSA-9603381", "R-MMU-1257604", "R-MMU-6811558", "R-MMU-90340...
[ "REACTOME:R-BTA-1257604", "REACTOME:R-BTA-6811558", "REACTOME:R-BTA-9034013", "REACTOME:R-BTA-9034793", "REACTOME:R-BTA-9603381", "REACTOME:R-HSA-1257604", "REACTOME:R-HSA-2219530", "REACTOME:R-HSA-6811558", "REACTOME:R-HSA-9025046", "REACTOME:R-HSA-9034013", "REACTOME:R-HSA-9034015", "REACTOM...
24
[]
0
[ "PUB00000638", "PUB00001187", "PUB00001600", "PUB00005102", "PUB00005408", "PUB00034812", "PUB00034813", "PUB00034814", "PUB00034815", "PUB00034816" ]
[ "1477101", "2369898", "1995338", "3589669", "8488558", "2321006", "12914971", "14507970", "14499950", "14519521" ]
[ "Purification and amino-acid sequence of a nerve growth factor from the venom of Vipera russelli russelli.", "Regional distribution of brain-derived neurotrophic factor mRNA in the adult mouse brain.", "Amino acid sequences of nerve growth factors derived from cobra venoms.", "Recruitment of enzymes as lens s...
[ 1992, 1990, 1991, 1987, 1993, 1990, 2003, 2003, 2003, 2003 ]
10
[ "IPR020408" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 3256 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 11, 1, 2, 5 ]
4
true
Family
Neurotrophin-3
Neurotrophin-3
Neurotrophin-3
9
IPR015590
15,590
Aldehyde dehydrogenase domain
Aldehyde_DH_dom
Domain
404,013
false
false
Aldehyde dehydrogenases ( and ) are enzymes that oxidize a wide variety of aliphatic and aromatic aldehydes using NADP as a cofactor. In mammals at least four different forms of the enzyme are known [ ]: class-1 (or Ald C) a tetrameric cytosolic enzyme, class-2 (or Ald M) a tetrameric mitochondrial enzyme, class- 3 (or...
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PFAM" ]
[ "PF00171" ]
[ "Aldedh" ]
[ 404013 ]
1
[ "EC", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "1.2.1", "GenProp0292", "GenProp0294", "GenProp0457", "GenProp0715", "GenProp0717", "GenProp1226", "GenProp1267", "GenProp1276", "GenProp1297", "GenProp1321", "GenProp1370", "GenProp1379", "GenProp1390", "GenProp1401", "GenProp1402", "GenProp1425", "GenProp1434", "GenProp1437", ...
[ "EC:1.2.1", "GP:GenProp0292", "GP:GenProp0294", "GP:GenProp0457", "GP:GenProp0715", "GP:GenProp0717", "GP:GenProp1226", "GP:GenProp1267", "GP:GenProp1276", "GP:GenProp1297", "GP:GenProp1321", "GP:GenProp1370", "GP:GenProp1379", "GP:GenProp1390", "GP:GenProp1401", "GP:GenProp1402", "G...
156
[ "1a4s", "1a4z", "1ad3", "1ag8", "1bi9", "1bpw", "1bxs", "1cw3", "1euh", "1eyy", "1ez0", "1ky8", "1nzw", "1nzx", "1nzz", "1o00", "1o01", "1o02", "1o04", "1o05", "1o20", "1o9j", "1qi1", "1qi6", "1t90", "1uxn", "1uxp", "1uxq", "1uxr", "1uxt", "1uxu", "1uxv"...
522
[ "PUB00000303", "PUB00015186" ]
[ "2713359", "7920024" ]
[ "Inducible (class 3) aldehyde dehydrogenase from rat hepatocellular carcinoma and 2,3,7,8-tetrachlorodibenzo-p-dioxin-treated liver: distant relationship to the class 1 and 2 enzymes from mammalian liver cytosol/mitochondria.", "Allergen nomenclature. WHO/IUIS Allergen Nomenclature Subcommittee." ]
[ 1989, 1994 ]
2
[]
[ "IPR000965", "IPR005933", "IPR044086", "IPR044148" ]
0
4
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "plasmids", "unclassified sequences" ]
[ 3550, 302042, 93798, 3, 6, 4614 ]
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",...
[ 75, 24, 49, 48, 14, 138, 77, 15, 81, 110, 10, 8, 221 ]
13
true
Domain
Aldehyde dehydrogenase domain
Aldehyde dehydrogenase domain
Aldehyde_DH_dom
1
IPR015615
15,615
Transforming growth factor-beta-like
TGF-beta-like
Family
36,105
false
false
The transforming growth factor-beta (TGF-beta) superfamily comprises a number of structurally related, secreted polypeptides that regulate a multitude of cellular processes including proliferation, differentiation, cell invasion, immune regulation, and neoplastic transformation [ , ]. Family members include the activin...
[ "GO:0005576" ]
[ "extracellular region" ]
[ "cellular_component" ]
1
[ "PANTHER" ]
[ "PTHR11848" ]
[ "" ]
[ 36105 ]
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-114608", "R-BTA-1502540", "R-BTA-201451", "R-BTA-209822", "R-BTA-2129379", "R-BTA-2173789", "R-BTA-2473224", "R-BTA-381426", "R-BTA-8957275", "R-BTA-9839389", "R-BTA-9839406", "R-CEL-114608", "R-CEL-201451", "R-CEL-2129379", "R-CEL-2173788", "R-CEL-2173789", "R-CEL-2173791", ...
[ "REACTOME:R-BTA-114608", "REACTOME:R-BTA-1502540", "REACTOME:R-BTA-201451", "REACTOME:R-BTA-209822", "REACTOME:R-BTA-2129379", "REACTOME:R-BTA-2173789", "REACTOME:R-BTA-2473224", "REACTOME:R-BTA-381426", "REACTOME:R-BTA-8957275", "REACTOME:R-BTA-9839389", "REACTOME:R-BTA-9839406", "REACTOME:R-...
134
[ "1bmp", "1es7", "1kla", "1klc", "1kld", "1ktz", "1lx5", "1lxi", "1m4u", "1nys", "1nyu", "1reu", "1rew", "1s4y", "1tfg", "1tgj", "1tgk", "1waq", "1zkz", "2arp", "2arv", "2b0u", "2bhk", "2goo", "2h62", "2h64", "2p6a", "2pjy", "2qcq", "2qcw", "2qj9", "2qja"...
152
[ "PUB00000211", "PUB00004939", "PUB00005153", "PUB00007614", "PUB00035159", "PUB00035160", "PUB00043835", "PUB00096668", "PUB00096669", "PUB00097278" ]
[ "1575734", "8199356", "1631557", "8679613", "15032667", "15180456", "18662538", "29109152", "30696809", "24086041" ]
[ "Evolutionary grouping of the transforming growth factor-beta superfamily.", "Evolution of the transforming growth factor-beta superfamily.", "Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily.", "Transforming growth factor beta 1: three-dimensional structure in solut...
[ 1992, 1994, 1992, 1996, 2004, 2004, 2008, 2018, 2019, 2013 ]
10
[]
[ "IPR000491", "IPR001318", "IPR003942", "IPR016319", "IPR017175", "IPR017197" ]
0
6
0
[ "Bacteria", "Chordopoxvirinae", "Eukaryota", "bird metagenome" ]
[ 10, 24, 36070, 1 ]
4
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 96, 11, 128, 82, 91 ]
6
true
Family
Transforming growth factor-beta-like
Transforming growth factor-beta-like
TGF-beta-like
5
IPR015616
15,616
Growth/differentiation factor 8, C-terminal domain
GDF8_C
Domain
1,639
false
false
This entry represents Growth/differentiation factor 8. Growth and differentiation 8 (GDF-8), or myostatin, is a member of this superfamily with a role in the control and maintenance of skeletal muscle mass. Myostatin knockout in mice increases myogenesis and decreases adipogenesis [ ]. Frequent sequence variation in th...
[ "GO:0005102", "GO:0008083" ]
[ "signaling receptor binding", "growth factor activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "CDD" ]
[ "cd19388" ]
[ "TGF_beta_GDF8" ]
[ 1639 ]
1
[ "REACTOME" ]
[ "R-HSA-9617828" ]
[ "REACTOME:R-HSA-9617828" ]
1
[ "3hh2", "3sek", "5f3b", "5f3h", "5ji1", "5ntu", "5nxs", "6umx" ]
8
[ "PUB00000211", "PUB00004939", "PUB00005153", "PUB00007614", "PUB00035159", "PUB00035160", "PUB00035187", "PUB00035188", "PUB00043835", "PUB00096668", "PUB00096669", "PUB00097278" ]
[ "1575734", "8199356", "1631557", "8679613", "15032667", "15180456", "11855847", "10610713", "18662538", "29109152", "30696809", "24086041" ]
[ "Evolutionary grouping of the transforming growth factor-beta superfamily.", "Evolution of the transforming growth factor-beta superfamily.", "Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily.", "Transforming growth factor beta 1: three-dimensional structure in solut...
[ 1992, 1994, 1992, 1996, 2004, 2004, 2002, 1999, 2008, 2018, 2019, 2013 ]
12
[ "IPR001839" ]
[]
1
0
1
[ "Vertebrata" ]
[ 1639 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 11, 5, 3 ]
4
true
Domain
Growth/differentiation factor 8, C-terminal domain
Growth/differentiation factor 8, C-terminal domain
GDF8_C
1
IPR015618
15,618
Transforming growth factor beta-3
TGFB3
Family
1,052
false
false
The transforming growth factors-beta (TGF-beta 1-5) constitute of a family of multi-functional cytokines that regulate cell growth and differentiation [ ]. Many cells synthesise TGF-beta, and essentially all have specific receptors for this peptide [ ]. TGF-beta regulates the actions of many other peptide growth factor...
[ "GO:0005160" ]
[ "transforming growth factor beta receptor binding" ]
[ "molecular_function" ]
1
[ "PRINTS" ]
[ "PR01426" ]
[ "TGFBETA3" ]
[ 1052 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-114608", "R-HSA-2129379", "R-HSA-2173789", "R-HSA-3000178", "R-MMU-114608", "R-MMU-2129379", "R-MMU-2173789", "R-RNO-114608", "R-RNO-2129379", "R-RNO-2173789", "R-SSC-114608", "R-SSC-2129379", "R-SSC-2173789" ]
[ "REACTOME:R-HSA-114608", "REACTOME:R-HSA-2129379", "REACTOME:R-HSA-2173789", "REACTOME:R-HSA-3000178", "REACTOME:R-MMU-114608", "REACTOME:R-MMU-2129379", "REACTOME:R-MMU-2173789", "REACTOME:R-RNO-114608", "REACTOME:R-RNO-2129379", "REACTOME:R-RNO-2173789", "REACTOME:R-SSC-114608", "REACTOME:R-...
13
[ "8vs6", "8vsb" ]
2
[ "PUB00007611", "PUB00007612", "PUB00007613", "PUB00007628", "PUB00007629" ]
[ "8424942", "2879635", "8819159", "2628730", "7852342" ]
[ "Transforming growth factor beta 1: NMR signal assignments of the recombinant protein expressed and isotopically enriched using Chinese hamster ovary cells.", "The transforming growth factor-beta system, a complex pattern of cross-reactive ligands and receptors.", "The crystal structure of TGF-beta 3 and compar...
[ 1993, 1987, 1996, 1989, 1995 ]
5
[ "IPR016319" ]
[]
1
0
1
[ "Chordata" ]
[ 1052 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 6, 7, 3 ]
4
true
Family
Transforming growth factor beta-3
Transforming growth factor beta-3
TGFB3
2
IPR015621
15,621
Interleukin-1 receptor family
IL-1_rcpt_fam
Family
11,915
false
false
Interleukin-1 alpha and interleukin-1 beta (IL-1 alpha and IL-1 beta) are cytokines that participate in the regulation of immune responses, inflammatory reactions, and hematopoiesis [ ]. Two types of IL-1 receptor, each with three extracellular immunoglobulin (Ig)-like domains, limited sequence similarity (28%) and dif...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR11890" ]
[ "" ]
[ 11915 ]
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-DRE-9007892", "R-HSA-1257604", "R-HSA-166058", "R-HSA-2132295", "R-HSA-388844", "R-HSA-6783783", "R-HSA-6811558", "R-HSA-9007892", "R-HSA-9008059", "R-HSA-9012546", "R-HSA-9014826", "R-HSA-9014843", "R-HSA-9020702", "R-HSA-9679191", "R-MMU-1257604", "R-MMU-2132295", "R-MMU-388844"...
[ "REACTOME:R-DRE-9007892", "REACTOME:R-HSA-1257604", "REACTOME:R-HSA-166058", "REACTOME:R-HSA-2132295", "REACTOME:R-HSA-388844", "REACTOME:R-HSA-6783783", "REACTOME:R-HSA-6811558", "REACTOME:R-HSA-9007892", "REACTOME:R-HSA-9008059", "REACTOME:R-HSA-9012546", "REACTOME:R-HSA-9014826", "REACTOME:...
31
[ "1g0y", "1ira", "1itb", "1t3g", "3o4o", "3oq3", "3wo3", "3wo4", "4dep", "4gaf", "4kc3", "4r6u", "4yfd", "4yh6", "4yh7", "5vi4", "5wy8", "5y32", "6kn9", "6u6u", "7fcc", "7fch", "7fcj", "7fcl", "7fd3", "7szl", "7tze", "7tzg", "8dgg", "8so3", "8sr0", "9bf9"...
36
[ "PUB00007346", "PUB00007347", "PUB00007348", "PUB00007351" ]
[ "2969618", "8702856", "1833184", "9062194" ]
[ "cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily.", "Cloning and characterization of an alternatively processed human type II interleukin-1 receptor mRNA.", "A novel IL-1 receptor, cloned from B cells by mammalian expression, is expressed in many cell types.", "A new c...
[ 1988, 1996, 1991, 1997 ]
4
[]
[ "IPR004074" ]
0
1
0
[ "Chordopoxvirinae", "Metazoa" ]
[ 265, 11650 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 46, 49, 36, 64 ]
4
true
Family
Interleukin-1 receptor family
Interleukin-1 receptor family
IL-1_rcpt_fam
1
IPR015631
15,631
CD2/SLAM family receptor
CD2/SLAM_rcpt
Family
12,751
false
false
The SLAM/CD2 family of receptors plays important roles in regulating multiple cellular interactions in the adaptive and innate immune systems [ ]. Signalling lymphocyte activation molecule (SLAM) receptors are expressed in multiple cells of the immune system, including natural killer cells, T cells, and B cells [ , , ,...
[ "GO:0016020" ]
[ "membrane" ]
[ "cellular_component" ]
1
[ "PANTHER" ]
[ "PTHR12080" ]
[ "" ]
[ 12751 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-198933", "R-HSA-202733", "R-HSA-6798695", "R-MMU-198933", "R-MMU-202733", "R-RNO-202733" ]
[ "REACTOME:R-HSA-198933", "REACTOME:R-HSA-202733", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-198933", "REACTOME:R-MMU-202733", "REACTOME:R-RNO-202733" ]
6
[ "1ccz", "1ci5", "1hnf", "1hng", "1qa9", "2dru", "2edo", "2if7", "2pkd", "2ptt", "2ptv" ]
11
[ "PUB00034934", "PUB00034935", "PUB00090162", "PUB00155119", "PUB00155120", "PUB00155121", "PUB00155122" ]
[ "12787752", "11034354", "21094032", "20818396", "22184727", "27249817", "27683913" ]
[ "The SLAM family of immune-cell receptors.", "Defective NK cell activation in X-linked lymphoproliferative disease.", "The role of SLAM/CD2 polymorphisms in systemic autoimmunity.", "SLAM is a microbial sensor that regulates bacterial phagosome functions in macrophages.", "Increased expression of SLAM recep...
[ 2003, 2000, 2010, 2010, 2012, 2016, 2016 ]
7
[]
[]
0
0
null
[ "Eumetazoa", "Viruses" ]
[ 12717, 34 ]
2
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 73, 40, 58, 37 ]
4
true
Family
CD2/SLAM family receptor
CD2/SLAM family receptor
CD2/SLAM_rcpt
4
IPR015632
15,632
T-cell surface antigen CD2
CD2
Family
368
false
false
The CD2 adhesion molecule is a cell surface protein expressed by T cells and natural killer cells. CD2's extracellular domain contains immunoglobulin-like domains that are glycosylated at two sites and can mediate homodimerisation [ ]. Ligation of CD2 by CD58 in humans or CD48 in mice helps T cells adhere to antigen-pr...
[]
[]
[]
0
[ "PRINTS" ]
[ "PR01870" ]
[ "CD2ANTIGEN" ]
[ 368 ]
1
[ "REACTOME" ]
[ "R-HSA-202733" ]
[ "REACTOME:R-HSA-202733" ]
1
[ "1a64", "1a6p", "1a7b", "1cdb", "1cdc", "1gya", "1hnf", "1hng", "1qa9", "1t6w" ]
10
[ "PUB00034961", "PUB00034962", "PUB00034963" ]
[ "12475217", "1358605", "9794375" ]
[ "The pH dependence of CD2 domain 1 self-association and 15N chemical exchange broadening is correlated with the anomalous pKa of Glu41.", "Development and function of T cells in mice with a disrupted CD2 gene.", "Uncoupling activation-dependent HS1 phosphorylation from nuclear factor of activated T cells transc...
[ 2002, 1992, 1998 ]
3
[]
[]
0
0
null
[ "Euteleostomi" ]
[ 368 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 5, 4, 2 ]
3
true
Family
T-cell surface antigen CD2
T-cell surface antigen CD2
CD2
1
IPR015633
15,633
E2F Family
E2F
Family
14,379
false
false
The E2F family of transcription factors plays a crucial role in the control of cell cycle [ , ] and action of tumour suppressor proteins. This family consists of eight members and is divided into activators (E2F1-3) and repressors (E2F4-8) depending on cellular context, target gene and cofactors [ ]. The E2F proteins c...
[ "GO:0000978", "GO:0006357" ]
[ "RNA polymerase II cis-regulatory region sequence-specific DNA binding", "regulation of transcription by RNA polymerase II" ]
[ "molecular_function", "biological_process" ]
2
[ "PANTHER" ]
[ "PTHR12081" ]
[ "" ]
[ 14379 ]
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-8953750", "R-DME-1538133", "R-DME-2173796", "R-DME-68911", "R-DME-69231", "R-DME-8953750", "R-DRE-6804116", "R-HSA-111448", "R-HSA-113501", "R-HSA-1362277", "R-HSA-1362300", "R-HSA-139915", "R-HSA-1538133", "R-HSA-1912408", "R-HSA-2173796", "R-HSA-2559580", "R-HSA-2559585", ...
[ "REACTOME:R-BTA-8953750", "REACTOME:R-DME-1538133", "REACTOME:R-DME-2173796", "REACTOME:R-DME-68911", "REACTOME:R-DME-69231", "REACTOME:R-DME-8953750", "REACTOME:R-DRE-6804116", "REACTOME:R-HSA-111448", "REACTOME:R-HSA-113501", "REACTOME:R-HSA-1362277", "REACTOME:R-HSA-1362300", "REACTOME:R-HS...
38
[ "1cf7", "2aze", "4yo2", "5tuu", "5tuv" ]
5
[ "PUB00008097", "PUB00096666", "PUB00096667" ]
[ "7739537", "22903062", "20040599" ]
[ "In vivo association of E2F and DP family proteins.", "E2F7 and E2F8 promote angiogenesis through transcriptional activation of VEGFA in cooperation with HIF1.", "Regulation of E2F1-induced apoptosis by the nucleolar protein RRP1B." ]
[ 1995, 2012, 2010 ]
3
[]
[]
0
0
null
[ "Eukaryota", "bird metagenome" ]
[ 14377, 2 ]
2
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 29, 3, 17, 5, 28, 24, 21, 25, 59 ]
9
true
Family
E2F Family
E2F Family
E2F
6
IPR015637
15,637
Uracil DNA glycosylase family 2
MUG/TDG
Family
9,586
false
false
G:U mismatches resulting from deamination of cytosine are the most common pro-mutagenic lesions occurring in DNA. Uracil is removed in a base-excision repair pathway by uracil DNA-glycosylase (UDG), which excises uracil from both single- and double-stranded DNA. The uracil DNA glycosylase family 2 consists of thymine D...
[ "GO:0000700", "GO:0006285" ]
[ "mismatch base pair DNA N-glycosylase activity", "base-excision repair, AP site formation" ]
[ "molecular_function", "biological_process" ]
2
[ "PANTHER", "CDD" ]
[ "PTHR12159", "cd10028" ]
[ "", "UDG-F2_TDG_MUG" ]
[ 9536, 9268 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "3.2.2.28", "R-HSA-110328", "R-HSA-110329", "R-HSA-110357", "R-HSA-3108214", "R-HSA-5221030", "R-MMU-110329", "R-MMU-110357", "R-MMU-3108214", "R-MMU-5221030", "R-SPO-110329", "R-SPO-3108214", "R-SPO-5221030" ]
[ "EC:3.2.2.28", "REACTOME:R-HSA-110328", "REACTOME:R-HSA-110329", "REACTOME:R-HSA-110357", "REACTOME:R-HSA-3108214", "REACTOME:R-HSA-5221030", "REACTOME:R-MMU-110329", "REACTOME:R-MMU-110357", "REACTOME:R-MMU-3108214", "REACTOME:R-MMU-5221030", "REACTOME:R-SPO-110329", "REACTOME:R-SPO-3108214",...
13
[ "1mtl", "1mug", "1mwi", "1mwj", "1wyw", "2c2p", "2c2q", "2d07", "2rba", "3ufj", "3uo7", "3uob", "4fnc", "4jgc", "4xeg", "4z3a", "4z47", "4z7b", "4z7z", "5cys", "5ff8", "5hf7", "5jxy", "5t2w", "6u15", "6u16", "6u17" ]
27
[ "PUB00008091", "PUB00080609", "PUB00095804" ]
[ "9489705", "19909758", "18789404" ]
[ "Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions.", "Uracil-DNA glycosylase: Structural, thermodynamic and kinetic aspects of lesion search and recognition.", "Repair of deaminated base damage by Schizosaccharomyces pombe thymine DNA glyc...
[ 1998, 2010, 2008 ]
3
[]
[ "IPR003310", "IPR023502" ]
0
2
0
[ "Archaea", "Bacteria", "Eukaryota", "Peduoviridae", "metagenomes" ]
[ 10, 5503, 4020, 2, 51 ]
5
[ "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)", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 7, 3, 1, 10, 6, 1, 8, 1 ]
8
true
Family
Uracil DNA glycosylase family 2
Uracil DNA glycosylase family 2
MUG/TDG
8
IPR015646
15,646
Nuclear factor of activated T-cells 5, Rel homology domain, DNA-binding domain
NFAT5_RHD_DNA-bd
Domain
1,825
false
false
Nuclear factor of activated T-cells 5 (NFAT5) is a member of the nuclear factors of activated T cells (NFAT) of transcription factors. Proteins belonging to this family play a central role in inducible gene transcription during the immune response. This protein regulates gene expression induced by osmotic stress in mam...
[ "GO:0000978" ]
[ "RNA polymerase II cis-regulatory region sequence-specific DNA binding" ]
[ "molecular_function" ]
1
[ "CDD" ]
[ "cd07882" ]
[ "RHD-n_TonEBP" ]
[ 1825 ]
1
[]
[]
[]
0
[ "1imh" ]
1
[ "PUB00004201", "PUB00011687", "PUB00035152", "PUB00049544", "PUB00095357" ]
[ "7830764", "10652349", "11528118", "17869269", "22266867" ]
[ "Structure of the NF-kappa B p50 homodimer bound to DNA.", "Identification of amino acid residues and protein kinases involved in the regulation of NFATc subcellular localization.", "Genomic organization of the human NFAT5 gene: exon-intron structure of the 14-kb transcript and CpG-island analysis of the promot...
[ 1995, 2000, 2001, 2007, 2012 ]
5
[ "IPR011539" ]
[]
1
0
1
[ "Bilateria" ]
[ 1825 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 20, 8, 1, 6, 4 ]
5
true
Domain
Nuclear factor of activated T-cells 5, Rel homology domain, DNA-binding domain
Nuclear factor of activated T-cells 5, Rel homology domain, DNA-binding domain
NFAT5_RHD_DNA-bd
5
IPR015648
15,648
Transcription factor DP
Transcrpt_fac_DP
Family
5,702
false
false
The DP proteins function as binding partners for E2F transcription factors. The association of DP with E2F can either enhances or repress E2F-dependent transcriptional activity. The activities of both DP and E2F proteins are under cell cycle control, being influenced by the level of phosphorylation imparted through the...
[ "GO:0051726", "GO:0005667" ]
[ "regulation of cell cycle", "transcription regulator complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PIRSF", "PANTHER" ]
[ "PIRSF009404", "PTHR12548" ]
[ "Transcription_factor_DP", "" ]
[ 3665, 5702 ]
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-1538133", "R-BTA-2173796", "R-BTA-69231", "R-BTA-8953750", "R-CEL-1538133", "R-CEL-2173796", "R-DME-1538133", "R-DME-2173796", "R-DME-69231", "R-DME-8953750", "R-HSA-111448", "R-HSA-113501", "R-HSA-1362277", "R-HSA-1362300", "R-HSA-139915", "R-HSA-1538133", "R-HSA-1912408", ...
[ "REACTOME:R-BTA-1538133", "REACTOME:R-BTA-2173796", "REACTOME:R-BTA-69231", "REACTOME:R-BTA-8953750", "REACTOME:R-CEL-1538133", "REACTOME:R-CEL-2173796", "REACTOME:R-DME-1538133", "REACTOME:R-DME-2173796", "REACTOME:R-DME-69231", "REACTOME:R-DME-8953750", "REACTOME:R-HSA-111448", "REACTOME:R-H...
32
[ "1cf7", "2aze", "5tuu", "5tuv" ]
4
[ "PUB00035117", "PUB00035118", "PUB00035119" ]
[ "8674727", "9670325", "7880534" ]
[ "E2F and the molecular mechanisms of early cell-cycle control.", "Growth regulation by the E2F and DP transcription factor families.", "DP and E2F proteins: coordinating transcription with cell cycle progression." ]
[ 1996, 1998, 1994 ]
3
[]
[]
0
0
null
[ "Eukaryota" ]
[ 5702 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 6, 1, 4, 2, 11, 22, 10, 16, 19 ]
9
true
Family
Transcription factor DP
Transcription factor DP
Transcrpt_fac_DP
7
IPR015654
15,654
Mandelate racemase
Mandelate_racemase
Family
8
false
false
Mandelate racemase ( ) (MR) in certain bacteria, including Pseudomonas putida, utilise D or L mandelic acid as sole carbon source for energy. Mandelate racemase and muconate lactonizing enzyme ( ) (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet ...
[ "GO:0018838" ]
[ "mandelate racemase activity" ]
[ "molecular_function" ]
1
[ "SFLD" ]
[ "SFLDF00004" ]
[ "mandelate_racemase" ]
[ 8 ]
1
[]
[]
[]
0
[ "1mdr", "1mns", "2mnr", "3uxk", "3uxl", "4fp1", "4m6u", "4x2p", "6vim", "7mqx" ]
10
[ "PUB00004081", "PUB00005404", "PUB00034787" ]
[ "2215699", "8256284", "1892834" ]
[ "Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous.", "On the origin of enzymatic species.", "Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5-A resolution: identification of the active site and...
[ 1990, 1993, 1991 ]
3
[ "IPR046945" ]
[]
1
0
1
[ "Pseudomonadota" ]
[ 8 ]
1
[]
[]
0
true
Family
Mandelate racemase
Mandelate racemase
Mandelate_racemase
6
IPR015655
15,655
Protein phosphatase 2C
PP2C
Family
110,598
false
false
Protein phosphatase 2C (PP2C) is one of the four major classes of mammalian serine/threonine specific protein phosphatases ( ). PP2C [ ] is a monomeric enzyme of about 42kDa, that shows broad substrate specificity and is dependent on divalent cations (mainly manganese and magnesium) for its activity. The exact physiolo...
[ "GO:0004722", "GO:0006470" ]
[ "protein serine/threonine phosphatase activity", "protein dephosphorylation" ]
[ "molecular_function", "biological_process" ]
2
[ "PANTHER", "PANTHER" ]
[ "PTHR13832", "PTHR47992" ]
[ "", "" ]
[ 45661, 64937 ]
2
[ "EC", "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "3.1.3", "3.1.3.16", "R-BTA-1169408", "R-BTA-204174", "R-BTA-2173795", "R-BTA-380972", "R-BTA-70895", "R-CEL-1169408", "R-CEL-2173795", "R-CEL-380972", "R-HSA-1169408", "R-HSA-1660661", "R-HSA-168638", "R-HSA-204174", "R-HSA-2173795", "R-HSA-2871837", "R-HSA-380972", "R-HSA-445989"...
[ "EC:3.1.3", "EC:3.1.3.16", "REACTOME:R-BTA-1169408", "REACTOME:R-BTA-204174", "REACTOME:R-BTA-2173795", "REACTOME:R-BTA-380972", "REACTOME:R-BTA-70895", "REACTOME:R-CEL-1169408", "REACTOME:R-CEL-2173795", "REACTOME:R-CEL-380972", "REACTOME:R-HSA-1169408", "REACTOME:R-HSA-1660661", "REACTOME:...
60
[ "1a6q", "1txo", "2cm1", "2i0o", "2i44", "2iq1", "2irm", "2isn", "2j4o", "2j82", "2j86", "2jfr", "2jfs", "2jft", "2p8e", "2pk0", "2pnq", "2pom", "2pop", "2v06", "2xzv", "2y09", "3d8k", "3fxj", "3fxk", "3fxl", "3fxm", "3fxo", "3jrq", "3kb3", "3kdj", "3mq3"...
108
[ "PUB00000387", "PUB00001629", "PUB00003690", "PUB00005194", "PUB00155069", "PUB00155070" ]
[ "8396421", "1312947", "8395005", "7973632", "11559703", "18930133" ]
[ "Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C.", "Molecular cloning and primary structure of a protein phosphatase 2C isoform.", "Mutations in a protein tyrosine phosphatase gene (PTP2) and a protein se...
[ 1993, 1992, 1993, 1994, 2001, 2009 ]
6
[]
[ "IPR016660" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]
[ 142, 19359, 90656, 89, 352 ]
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...
[ 312, 9, 50, 28, 68, 49, 5, 181, 75, 6, 5, 598 ]
12
true
Family
Protein phosphatase 2C
Protein phosphatase 2C
PP2C
5
IPR015657
15,657
Aminobutyraldehyde dehydrogenase
Aminobutyraldehyde_DH
Family
6,379
false
false
Aminobutyraldehyde dehydrogenase functions in the putrescine degradation pathway. It catalyses the oxidation of 4 aminobutyraldehyde to 4 aminobutyrate, a neurotransmitter. YdcW encodes gamma-aminobutyraldehyde dehydrogenase (ABALDH) in the wild-type Escherichia coli (strain K12). It is a tetramer and when coupled with...
[]
[]
[]
0
[ "CDD" ]
[ "cd07092" ]
[ "ALDH_ABALDH-YdcW" ]
[ 6379 ]
1
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "...
[ "1.2.1.-", "1.2.1.19", "PWY-1121", "PWY-2", "PWY-2724", "PWY-282", "PWY-3", "PWY-3162", "PWY-321", "PWY-5168", "PWY-5305", "PWY-5875", "PWY-5885", "PWY-6309", "PWY-6322", "PWY-6328", "PWY-6681", "PWY-6713", "PWY-6832", "PWY-6863", "PWY-6926", "PWY-6948", "PWY-7033", "PW...
[ "EC:1.2.1.-", "EC:1.2.1.19", "METACYC:PWY-1121", "METACYC:PWY-2", "METACYC:PWY-2724", "METACYC:PWY-282", "METACYC:PWY-3", "METACYC:PWY-3162", "METACYC:PWY-321", "METACYC:PWY-5168", "METACYC:PWY-5305", "METACYC:PWY-5875", "METACYC:PWY-5885", "METACYC:PWY-6309", "METACYC:PWY-6322", "META...
34
[ "1wnb", "1wnd", "4dal", "4f3x", "6c43" ]
5
[ "PUB00032275", "PUB00042939", "PUB00043488" ]
[ "15381418", "16023116", "12186751" ]
[ "Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase.", "Identification of Escherichia coli K12 YdcW protein as a gamma-aminobutyraldehyde dehydrogenase.", "Purification and characterization of aminobutyraldehyde dehydrogenase from Arthrobacter Sp....
[ 2004, 2005, 2002 ]
3
[]
[ "IPR017749" ]
0
1
0
[ "Bacteria", "Eukaryota", "metagenomes" ]
[ 6222, 6, 151 ]
3
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Aminobutyraldehyde dehydrogenase
Aminobutyraldehyde dehydrogenase
Aminobutyraldehyde_DH
4
IPR015659
15,659
Proline oxidase family
Proline_oxidase
Family
17,334
false
false
This entry includes a group of proline dehydrogenases (proline oxidases) found in bacteria, archaea and eukaryotes (mitochondria).
[ "GO:0004657", "GO:0006562" ]
[ "proline dehydrogenase activity", "L-proline catabolic process" ]
[ "molecular_function", "biological_process" ]
2
[ "PANTHER" ]
[ "PTHR13914" ]
[ "" ]
[ 17334 ]
1
[ "EC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.5.5.2", "PWY-5737", "PWY-6922", "R-CEL-389661", "R-CEL-70688", "R-DDI-389661", "R-DDI-70688", "R-DME-389661", "R-DME-70688", "R-HSA-389661", "R-HSA-70688", "R-MMU-389661", "R-MMU-70688", "R-RNO-389661", "R-RNO-70688", "R-SCE-389661", "R-SCE-70688", "R-SPO-389661", "R-SPO-70688...
[ "EC:1.5.5.2", "METACYC:PWY-5737", "METACYC:PWY-6922", "REACTOME:R-CEL-389661", "REACTOME:R-CEL-70688", "REACTOME:R-DDI-389661", "REACTOME:R-DDI-70688", "REACTOME:R-DME-389661", "REACTOME:R-DME-70688", "REACTOME:R-HSA-389661", "REACTOME:R-HSA-70688", "REACTOME:R-MMU-389661", "REACTOME:R-MMU-7...
19
[ "1tiw", "1tj0", "1tj1", "1tj2", "2ekg", "2fzm", "2fzn", "2g37", "3e2q", "3e2r", "3e2s", "3itg", "4h6q", "4h6r", "4o8a", "5m42", "7mwt", "7mwu", "7mwv", "7sqn", "8dko", "8dkp", "8dkq", "8upz", "8uq0", "8uq1", "8w0k", "9c8a", "9c8b", "9d7l" ]
30
[ "PUB00083173", "PUB00083174", "PUB00085164" ]
[ "17536821", "8096642", "25697095" ]
[ "Delta1-pyrroline-5-carboxylic acid formed by proline dehydrogenase from the Bacillus subtilis ssp. natto expressed in Escherichia coli as a precursor for 2-acetyl-1-pyrroline.", "The sluggish-A gene of Drosophila melanogaster is expressed in the nervous system and encodes proline oxidase, a mitochondrial enzyme ...
[ 2007, 1993, 2015 ]
3
[]
[ "IPR008219" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Megaviricetes", "unclassified sequences" ]
[ 485, 8186, 8541, 5, 117 ]
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...
[ 11, 1, 8, 4, 12, 11, 1, 4, 11, 1, 1, 6 ]
12
true
Family
Proline oxidase family
Proline oxidase family
Proline_oxidase
9
IPR015660
15,660
Achaete-scute transcription factor-related
MASH1/Ascl1a-like
Family
8,778
false
false
Basic helix-loop-helix proteins (bHLH) are a group of eukaryotic transcription factors that exert a determinative influence in a variety of developmental pathways. These transcription factors are characterised by a highly evolutionary conserved bHLH domain that mediates specific dimerisation [ ]. They facilitate the co...
[ "GO:0003700", "GO:0006357" ]
[ "DNA-binding transcription factor activity", "regulation of transcription by RNA polymerase II" ]
[ "molecular_function", "biological_process" ]
2
[ "PANTHER" ]
[ "PTHR13935" ]
[ "" ]
[ 8778 ]
1
[ "REACTOME" ]
[ "R-HSA-9031628" ]
[ "REACTOME:R-HSA-9031628" ]
1
[]
0
[ "PUB00000717", "PUB00004974", "PUB00085017", "PUB00085019" ]
[ "1755826", "7553065", "25751153", "26700681" ]
[ "The helix-loop-helix domain: a common motif for bristles, muscles and sex.", "Transcription factors 2: helix-loop-helix.", "MASH1/Ascl1a leads to GAP43 expression and axon regeneration in the adult CNS.", "A novel role for Ascl1 in the regulation of mesendoderm formation via HDAC-dependent antagonism of VegT...
[ 1991, 1995, 2015, 2016 ]
4
[]
[]
0
0
null
[ "Eukaryota" ]
[ 8778 ]
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", "Zea mays" ]
[ 69, 2, 2, 3, 2, 5, 1, 13, 5, 16 ]
10
true
Family
Achaete-scute transcription factor-related
Achaete-scute transcription factor-related
MASH1/Ascl1a-like
6
IPR015661
15,661
Mitotic spindle checkpoint protein Bub1/Mad3
Bub1/Mad3
Family
7,703
false
false
This represents the mitotic checkpoint serine/threonine-protein kinase Bub1.
[ "GO:0007094" ]
[ "mitotic spindle assembly checkpoint signaling" ]
[ "biological_process" ]
1
[ "PANTHER" ]
[ "PTHR14030" ]
[ "" ]
[ 7703 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.11.1", "R-CEL-141430", "R-DDI-141430", "R-DDI-174184", "R-DDI-176409", "R-DDI-179409", "R-HSA-141430", "R-HSA-141444", "R-HSA-174184", "R-HSA-176409", "R-HSA-179409", "R-HSA-2467813", "R-HSA-2500257", "R-HSA-5663220", "R-HSA-68877", "R-HSA-9648025", "R-MMU-141430", "R-MMU-1414...
[ "EC:2.7.11.1", "REACTOME:R-CEL-141430", "REACTOME:R-DDI-141430", "REACTOME:R-DDI-174184", "REACTOME:R-DDI-176409", "REACTOME:R-DDI-179409", "REACTOME:R-HSA-141430", "REACTOME:R-HSA-141444", "REACTOME:R-HSA-174184", "REACTOME:R-HSA-176409", "REACTOME:R-HSA-179409", "REACTOME:R-HSA-2467813", "...
28
[ "2lah", "2wvi", "3esl", "3si5", "4a1g", "4aez", "4qpm", "4r8q", "5dmz", "5khu", "5lcw", "6f7b", "6jkk", "6jkm", "6tlj" ]
15
[ "PUB00017177", "PUB00063118", "PUB00074625", "PUB00074626", "PUB00074627", "PUB00074628" ]
[ "10704439", "12769845", "10395177", "9521327", "17369399", "19503101" ]
[ "MAD3 encodes a novel component of the spindle checkpoint which interacts with Bub3p, Cdc20p, and Mad2p.", "Requirement of Skp1-Bub1 interaction for kinetochore-mediated activation of the spindle checkpoint.", "Mutation analysis of hBUB1 in aneuploid HNSCC and lung cancer cell lines.", "Mutations of mitotic c...
[ 2000, 2003, 1999, 1998, 2007, 2009 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 6, 7697 ]
2
[ "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...
[ 12, 2, 19, 4, 10, 10, 2, 13, 6, 2, 2, 20 ]
12
true
Family
Mitotic spindle checkpoint protein Bub1/Mad3
Mitotic spindle checkpoint protein Bub1/Mad3
Bub1/Mad3
6
IPR015662
15,662
Promotilin
Promotilin
Family
565
false
false
Promotilin can be cleaved into two chains: motilin and motilin-associated peptide. Motilin plays an important role in the regulation of interdigestive gastrointestinal motility and indirectly causes rhythmic contraction of duodenal and colonic smooth muscle [ ].
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR14156" ]
[ "" ]
[ 565 ]
1
[ "REACTOME", "REACTOME" ]
[ "R-HSA-375276", "R-HSA-416476" ]
[ "REACTOME:R-HSA-375276", "REACTOME:R-HSA-416476" ]
2
[]
0
[ "PUB00074886" ]
[ "4941085" ]
[ "The further purification of motilin, a gastric motor activity stimulating polypeptide from the mucosa of the small intestine of hogs." ]
[ 1971 ]
1
[]
[]
0
0
null
[ "Gnathostomata" ]
[ 565 ]
1
[ "Homo sapiens" ]
[ 1 ]
1
true
Family
Promotilin
Promotilin
Promotilin
3
IPR015664
15,664
P53-induced protein
P53_induced
Family
3,173
false
false
This entry includes p53-induced proteins that are members of the Pmp22 family of tetraspan membrane proteins.
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR14399" ]
[ "" ]
[ 3173 ]
1
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-6803205", "R-HSA-6809371", "R-MMU-6809371" ]
[ "REACTOME:R-HSA-6803205", "REACTOME:R-HSA-6809371", "REACTOME:R-MMU-6809371" ]
3
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Ciceribacter ferrooxidans", "Eumetazoa" ]
[ 1, 3172 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 3, 2, 2, 2, 5 ]
6
true
Family
P53-induced protein
P53-induced protein
P53_induced
7
IPR015666
15,666
Sarcoplasmic reticulum histidine-rich calcium-binding protein
HRC
Family
558
false
false
The histidine-rich calcium-binding protein of sarcoplasmic reticulum (HRC) may play a role in the regulation of calcium sequestration or release in the SR of skeletal and cardiac muscle [ ]. This protein is very acidic (31% of Asp and Glu) and rich in histidine (13%). The sequence of HRC contains 10 tandem repeats of a...
[ "GO:0005509" ]
[ "calcium ion binding" ]
[ "molecular_function" ]
1
[ "PANTHER" ]
[ "PTHR15054" ]
[ "" ]
[ 558 ]
1
[ "REACTOME", "REACTOME" ]
[ "R-HSA-381426", "R-HSA-8957275" ]
[ "REACTOME:R-HSA-381426", "REACTOME:R-HSA-8957275" ]
2
[]
0
[ "PUB00002520" ]
[ "2808365" ]
[ "Molecular cloning of a histidine-rich Ca2+-binding protein of sarcoplasmic reticulum that contains highly conserved repeated elements." ]
[ 1989 ]
1
[]
[]
0
0
null
[ "Eukaryota" ]
[ 558 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 7, 5, 7 ]
4
true
Family
Sarcoplasmic reticulum histidine-rich calcium-binding protein
Sarcoplasmic reticulum histidine-rich calcium-binding protein
HRC
8
IPR015667
15,667
Telethonin
Telethonin
Family
870
false
false
Telethonin is found at the Z-disc of sarcomeres. It is the phosphorylation target of the kinase domain of titin, and is thought to play a role in muscle development [ , ]. Deletion of the C terminus of titin, including the kinase domain, has been found to impair myofibrillogenesis [ ]. Mutations of telethonin cause lim...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF09470", "PTHR15143" ]
[ "Telethonin", "" ]
[ 870, 853 ]
2
[ "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-390522", "R-HSA-390522", "R-MMU-390522" ]
[ "REACTOME:R-BTA-390522", "REACTOME:R-HSA-390522", "REACTOME:R-MMU-390522" ]
3
[ "1ya5", "2f8v" ]
2
[ "PUB00034631", "PUB00035182", "PUB00035183", "PUB00035184", "PUB00040581" ]
[ "9804419", "10481174", "14600266", "12379311", "16713295" ]
[ "Structural basis for activation of the titin kinase domain during myofibrillogenesis.", "Titin: a molecular control freak.", "A targeted deletion of the C-terminal end of titin, including the titin kinase domain, impairs myofibrillogenesis.", "Telethonin protein expression in neuromuscular disorders.", "Ev...
[ 1998, 1999, 2003, 2002, 2006 ]
5
[]
[]
0
0
null
[ "Vertebrata" ]
[ 870 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 25, 4, 3, 3 ]
4
true
Family
Telethonin
Telethonin
Telethonin
3
IPR015668
15,668
B Cell Lymphoma 9
Bcl-9/Bcl-9l
Family
2,254
false
false
BCL9 is associated with B-cell acute lymphoblastic leukemia [ ]. This entry includes BCL9 and BCL9L. They are tissue-specific transcriptional cofactors that cooperate with beta-catenin. In the nucleus, Bcl9 and Bcl9l simultaneously bind beta-catenin and the transcriptional activator Pygo2 to promote the transcription o...
[ "GO:0003713", "GO:0008013", "GO:0060070" ]
[ "transcription coactivator activity", "beta-catenin binding", "canonical Wnt signaling pathway" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PANTHER" ]
[ "PTHR15185" ]
[ "" ]
[ 2254 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DRE-201722", "R-HSA-201722", "R-HSA-3769402", "R-MMU-201722" ]
[ "REACTOME:R-DRE-201722", "REACTOME:R-HSA-201722", "REACTOME:R-HSA-3769402", "REACTOME:R-MMU-201722" ]
4
[ "2gl7", "2vp7", "2vpb", "2vpd", "2vpe", "2vpg", "3sl9" ]
7
[ "PUB00035231", "PUB00084974" ]
[ "9490669", "28174279" ]
[ "Molecular cloning of translocation t(1;14)(q21;q32) defines a novel gene (BCL9) at chromosome 1q21.", "A cytoplasmic role of Wnt/β-catenin transcriptional cofactors Bcl9, Bcl9l, and Pygopus in tooth enamel formation." ]
[ 1998, 2017 ]
2
[]
[]
0
0
null
[ "Bilateria" ]
[ 2254 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 10, 7, 4, 7 ]
4
true
Family
B Cell Lymphoma 9
B Cell Lymphoma 9
Bcl-9/Bcl-9l
3
IPR015669
15,669
Endothelial protein C receptor
Endothetial_C_recpt
Family
652
false
false
Upon vascular injury, flowing blood is exposed to cells expressing tissue factor (TF) on their surfaces and FVII/FVIIa binds to its receptor/cofactor TF and is rapidly activated to FVIIa and the activity of bound FVIIa is dramatically enhanced. The TF/FVIIa complex activates zymogens factor X (FX) and factor IX (FIX). ...
[ "GO:0038023" ]
[ "signaling receptor activity" ]
[ "molecular_function" ]
1
[ "PANTHER" ]
[ "PTHR15349" ]
[ "" ]
[ 652 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-BTA-140875", "R-BTA-202733", "R-HSA-140875", "R-HSA-202733", "R-MMU-140875", "R-MMU-202733", "R-RNO-140875", "R-RNO-202733" ]
[ "REACTOME:R-BTA-140875", "REACTOME:R-BTA-202733", "REACTOME:R-HSA-140875", "REACTOME:R-HSA-202733", "REACTOME:R-MMU-140875", "REACTOME:R-MMU-202733", "REACTOME:R-RNO-140875", "REACTOME:R-RNO-202733" ]
8
[ "1l8j", "1lqv", "3jtc", "4v3d", "4v3e", "6sny", "7oks", "7okt", "7oku", "7okv", "7q5d", "8c44" ]
12
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Amniota" ]
[ 652 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 3, 4 ]
3
true
Family
Endothelial protein C receptor
Endothelial protein C receptor
Endothetial_C_recpt
4
IPR015671
15,671
GLTSCR protein, conserved domain
GSCR1_dom
Domain
3,867
false
false
This domain is found in glioma tumour suppressor candidate region gene 1 (GLTSCR1, also known as BICRAL) protein, and is typically between 105 and 124 amino acids in length. GLTSCR1 is a component of SWI/SNF chromatin remodeling subcomplex GBAF that carries out key enzymatic activities, changing chromatin structure by ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF15249" ]
[ "GLTSCR1" ]
[ 3867 ]
1
[ "REACTOME", "REACTOME" ]
[ "R-HSA-9933947", "R-MMU-9933947" ]
[ "REACTOME:R-HSA-9933947", "REACTOME:R-MMU-9933947" ]
2
[]
0
[ "PUB00034953", "PUB00045218", "PUB00088478" ]
[ "15834925", "17474147", "29374058" ]
[ "Polymorphisms in GLTSCR1 and ERCC2 are associated with the development of oligodendrogliomas.", "Systematic identification of SH3 domain-mediated human protein-protein interactions by peptide array target screening.", "Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog GLTSCR1-like form ...
[ 2005, 2007, 2018 ]
3
[]
[]
0
0
null
[ "Eukaryota" ]
[ 3867 ]
1
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 7, 1, 14, 4, 4, 4, 12, 9, 8 ]
9
true
Domain
GLTSCR protein, conserved domain
GLTSCR protein, conserved domain
GSCR1_dom
7
IPR015672
15,672
The Golgi pH regulator/GPCR-type G protein
GPHR/GTG
Family
4,820
false
false
This entry include human Golgi pH regulators (GPHR) and GPCR-type G proteins (GTG1 and GTG2) from Arabidopsis.
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR15948" ]
[ "" ]
[ 4820 ]
1
[]
[]
[]
0
[]
0
[ "PUB00059166", "PUB00059167" ]
[ "19135895", "18794847" ]
[ "Two novel GPCR-type G proteins are abscisic acid receptors in Arabidopsis.", "GPHR is a novel anion channel critical for acidification and functions of the Golgi apparatus." ]
[ 2009, 2008 ]
2
[]
[]
0
0
null
[ "Eukaryota" ]
[ 4820 ]
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...
[ 16, 4, 2, 1, 13, 2, 1, 1, 7, 1, 18 ]
11
true
Family
The Golgi pH regulator/GPCR-type G protein
The Golgi pH regulator/GPCR-type G protein
GPHR/GTG
6
IPR015673
15,673
Enamelin
Enamelin
Family
556
false
false
Enamelin is a secreted structural protein that acts to create dental enamel matrix. Enamelin protein is proteolytically cleaved into several products, which are identified by their molecular weights and appear to have different functions in different enamel compartments. It is not currently known how enamelin interacts...
[]
[]
[]
0
[ "PFAM", "PANTHER" ]
[ "PF15362", "PTHR16784" ]
[ "Enamelin", "" ]
[ 538, 556 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-381426", "R-HSA-8957275", "R-MMU-381426", "R-MMU-8957275" ]
[ "REACTOME:R-HSA-381426", "REACTOME:R-HSA-8957275", "REACTOME:R-MMU-381426", "REACTOME:R-MMU-8957275" ]
4
[]
0
[ "PUB00035154", "PUB00035155" ]
[ "14656895", "11037750" ]
[ "Enamelin and autosomal-dominant amelogenesis imperfecta.", "Enamelin maps to human chromosome 4q21 within the autosomal dominant amelogenesis imperfecta locus." ]
[ 2003, 2000 ]
2
[]
[]
0
0
null
[ "Tetrapoda" ]
[ 556 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 3, 4 ]
3
true
Family
Enamelin
Enamelin
Enamelin
4
IPR015675
15,675
Secretin precursor
Prosecretin
Family
530
false
false
A number of polypeptidic hormones, mainly expressed in the intestine or the pancreas, belong to a group of structurally related peptides [ , ]. Members of the structurally similar group include glucagon, glicentin precursor, secretin, gastric inhibitory protein, vasoactive intestinal peptide (VIP), prealbumin, peptide ...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR17378" ]
[ "" ]
[ 530 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-418555", "R-HSA-420092", "R-MMU-418555", "R-MMU-420092", "R-RNO-420092", "R-SSC-418555", "R-SSC-420092" ]
[ "REACTOME:R-HSA-418555", "REACTOME:R-HSA-420092", "REACTOME:R-MMU-418555", "REACTOME:R-MMU-420092", "REACTOME:R-RNO-420092", "REACTOME:R-SSC-418555", "REACTOME:R-SSC-420092" ]
7
[ "6wi9", "6wzg", "7d3s" ]
3
[ "PUB00000024", "PUB00000025", "PUB00035042", "PUB00035043", "PUB00035044", "PUB00070144", "PUB00095381", "PUB00095382" ]
[ "3133967", "3291691", "2315322", "11060443", "7612008", "2395872", "25332973", "30449620" ]
[ "Vasoactive intestinal polypeptide and related peptides. Isolation and chemistry.", "Glucagon and related peptides. Molecular structure and biological specificity.", "Secretin: structure of the precursor and tissue distribution of the mRNA.", "Human secretin (SCT): gene structure, chromosome location, and dis...
[ 1988, 1988, 1990, 2000, 1995, 1990, 2013, 2018 ]
8
[]
[]
0
0
null
[ "Amniota" ]
[ 530 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 5, 2 ]
3
true
Family
Secretin precursor
Secretin precursor
Prosecretin
8
IPR015676
15,676
Tob1/2
Tob1/2
Family
2,472
false
false
Tob1 and Tob2 are members of the BTG/Tob family. The BTG/Tob family members contain an conserved N-terminal domain, known as APRO domain (AntiPROliferative) or BTG domain. In mammals, six family members have been identified: BTG1, BTG2/PC3/Tis21, BTG3/ANA, BTG4/PC3B, Tob1/Tob and Tob2. They interact with CAF1, a subuni...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR17537" ]
[ "" ]
[ 2472 ]
1
[]
[]
[]
0
[ "2d5r", "2z15", "5ci8", "5ci9", "5td6" ]
5
[ "PUB00078467" ]
[ "19746446" ]
[ "The mammalian anti-proliferative BTG/Tob protein family." ]
[ 2010 ]
1
[]
[]
0
0
null
[ "Eumetazoa" ]
[ 2472 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 6, 4, 5, 7, 7 ]
6
true
Family
Tob1/2
Tob1/2
Tob1/2
4
IPR015679
15,679
Phospholipase D family
PLipase_D_fam
Family
24,004
false
false
Phospholipase D (PLD) catalyses the hydrolysis of the phosphodiester bond of glycerophospholipids to generate phosphatidic acid and a free head group. Phospholipase D activities have been detected in simple to complex organisms from viruses and bacteria to yeast, plants, and mammals [ ]. In higher organisms, PLD specif...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR18896" ]
[ "" ]
[ 24004 ]
1
[ "EC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "R...
[ "3.1.4.4", "PWY-3561", "PWY-7039", "R-DDI-1483166", "R-DDI-2029485", "R-DDI-6798695", "R-DDI-9013149", "R-DDI-9013404", "R-DDI-9013408", "R-HSA-1483148", "R-HSA-1483166", "R-HSA-2029485", "R-HSA-6798695", "R-HSA-8980692", "R-HSA-9013148", "R-HSA-9013149", "R-HSA-9013404", "R-HSA-90...
[ "EC:3.1.4.4", "METACYC:PWY-3561", "METACYC:PWY-7039", "REACTOME:R-DDI-1483166", "REACTOME:R-DDI-2029485", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-9013149", "REACTOME:R-DDI-9013404", "REACTOME:R-DDI-9013408", "REACTOME:R-HSA-1483148", "REACTOME:R-HSA-1483166", "REACTOME:R-HSA-2029485", "REA...
40
[ "6kz8", "6kz9", "6ohm", "6oho", "6ohp", "6ohq", "6ohr", "6ohs", "6u8z", "7svp", "7v53", "7v55", "7wdk" ]
13
[ "PUB00034910", "PUB00034911", "PUB00034912", "PUB00053993" ]
[ "15052340", "10818442", "14517341", "19439403" ]
[ "Phospholipase D.", "Phospholipase D.", "Phospholipase D in cell proliferation and cancer.", "A eukaryote-like cardiolipin synthase is present in Streptomyces coelicolor and in most actinobacteria." ]
[ 2004, 2000, 2003, 2009 ]
4
[]
[ "IPR011402", "IPR016555" ]
0
2
0
[ "Bacteria", "Eukaryota", "Methanobacteriota", "metagenomes" ]
[ 4067, 19902, 14, 21 ]
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...
[ 67, 1, 21, 6, 9, 11, 3, 60, 13, 1, 1, 125 ]
12
true
Family
Phospholipase D family
Phospholipase D family
PLipase_D_fam
3
IPR015683
15,683
Ionotropic glutamate receptor
Ionotropic_Glu_rcpt
Family
61,666
false
false
Ionotropic glutamate receptors (iGluRs) are a highly conserved family of ligand-gated ion channels present in animals, plants, and bacteria, which are best characterised for their roles in synaptic communication in vertebrate nervous systems [ ]. A variant subfamily of iGluRs, the Ionotropic Receptors (IRs), consist of...
[]
[]
[]
0
[ "PANTHER", "PANTHER" ]
[ "PTHR18966", "PTHR34836" ]
[ "", "" ]
[ 55096, 6570 ]
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-CEL-204005", "R-CEL-399710", "R-CEL-438066", "R-CEL-5694530", "R-CEL-8849932", "R-CFA-3928662", "R-CFA-438066", "R-CFA-5673001", "R-CFA-8849932", "R-CFA-9609736", "R-DME-204005", "R-DME-3928662", "R-DME-399710", "R-DME-416993", "R-DME-438066", "R-DME-5694530", "R-DME-8849932", "...
[ "REACTOME:R-CEL-204005", "REACTOME:R-CEL-399710", "REACTOME:R-CEL-438066", "REACTOME:R-CEL-5694530", "REACTOME:R-CEL-8849932", "REACTOME:R-CFA-3928662", "REACTOME:R-CFA-438066", "REACTOME:R-CFA-5673001", "REACTOME:R-CFA-8849932", "REACTOME:R-CFA-9609736", "REACTOME:R-DME-204005", "REACTOME:R-D...
63
[ "1ftj", "1ftk", "1ftl", "1ftm", "1fto", "1fw0", "1gr2", "1lb8", "1lb9", "1lbb", "1lbc", "1m5b", "1m5c", "1m5d", "1m5e", "1m5f", "1mm6", "1mm7", "1mqd", "1mqg", "1mqh", "1mqi", "1mqj", "1ms7", "1mxu", "1mxv", "1mxw", "1mxx", "1mxy", "1mxz", "1my0", "1my1"...
815
[ "PUB00072709", "PUB00072710" ]
[ "14977400", "20808886" ]
[ "Structure and function of glutamate receptor ion channels.", "Ancient protostome origin of chemosensory ionotropic glutamate receptors and the evolution of insect taste and olfaction." ]
[ 2004, 2010 ]
2
[]
[ "IPR001508", "IPR017103" ]
0
2
0
[ "Bacteria", "Eukaryota", "Paramecium bursaria Chlorella virus 1", "metagenomes", "unclassified Candidatus Methanogaster" ]
[ 1174, 60470, 1, 19, 2 ]
5
[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]
[ 136, 17, 238, 47, 124, 82, 88, 106, 92 ]
9
true
Family
Ionotropic glutamate receptor
Ionotropic glutamate receptor
Ionotropic_Glu_rcpt
3
IPR015685
15,685
Aquaporin 9
Aquaporin_9
Family
630
false
false
Aquaporins are water channels, present in both higher and lower organisms, that belong to the major intrinsic protein family. Most aquaporins are highly selective for water, though some also facilitate the movement of small uncharged molecules such as glycerol [ ]. In higher eukaryotes these proteins play diverse roles...
[]
[]
[]
0
[ "PRINTS" ]
[ "PR02021" ]
[ "AQUAPORIN9" ]
[ 630 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-432030", "R-HSA-432047", "R-MMU-432030", "R-MMU-432047", "R-RNO-432030", "R-RNO-432047" ]
[ "REACTOME:R-HSA-432030", "REACTOME:R-HSA-432047", "REACTOME:R-MMU-432030", "REACTOME:R-MMU-432047", "REACTOME:R-RNO-432030", "REACTOME:R-RNO-432047" ]
6
[]
0
[ "PUB00028718", "PUB00031522", "PUB00033222", "PUB00033223", "PUB00033224", "PUB00035072", "PUB00035073", "PUB00043535", "PUB00083165", "PUB00095345" ]
[ "11780053", "15377788", "15340377", "16406529", "14691544", "9514918", "12594337", "16650285", "10872456", "30420639" ]
[ "Structural basis of water-specific transport through the AQP1 water channel.", "The channel architecture of aquaporin 0 at a 2.2-A resolution.", "From structure to disease: the evolving tale of aquaporin biology.", "Why do microorganisms have aquaporins?", "Architecture and selectivity in aquaporins: 2.5 a...
[ 2001, 2004, 2004, 2006, 2003, 1998, 2003, 2006, 1999, 2018 ]
10
[ "IPR000425" ]
[]
1
0
1
[ "Bilateria" ]
[ 630 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 5, 4 ]
3
true
Family
Aquaporin 9
Aquaporin 9
Aquaporin_9
9
IPR015688
15,688
Elongation Factor 3, ABC2 domain, chromodomain-like insertion
eEF3_ABC2_chromodomain-like
Domain
3,316
false
false
This entry includes members of the EF3 (Elongation Factor 3) family, which contain the ABC transporter domains and belong to the family of ABC (ATP-binding cassette) proteins. Yef3 (elongation factor 3A) and Hef3 (elongation factor 3B) are included in this entry. The ribosomal elongation cycle requires two elongation f...
[]
[]
[]
0
[ "CDD" ]
[ "cd18626" ]
[ "CD_eEF3" ]
[ 3316 ]
1
[ "EC", "METACYC", "REACTOME" ]
[ "3.6.4.-", "PWY-7250", "R-SCE-382556" ]
[ "EC:3.6.4.-", "METACYC:PWY-7250", "REACTOME:R-SCE-382556" ]
3
[ "2iw3", "2iwh", "2ix3", "2ix8", "6s47", "7b7d", "8yld", "8ylr", "8z71" ]
9
[ "PUB00041798", "PUB00095258" ]
[ "16929303", "22888004" ]
[ "Structure of eEF3 and the mechanism of transfer RNA release from the E-site.", "Overexpression of eukaryotic translation elongation factor 3 impairs Gcn2 protein activation." ]
[ 2006, 2012 ]
2
[]
[]
0
0
null
[ "Chlorovirus", "Eukaryota", "viral metagenome" ]
[ 8, 3305, 3 ]
3
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]
[ 2, 3, 1 ]
3
true
Domain
Elongation Factor 3, ABC2 domain, chromodomain-like insertion
Elongation Factor 3, ABC2 domain, chromodomain-like insertion
eEF3_ABC2_chromodomain-like
6
IPR015700
15,700
DNA-directed RNA polymerase III subunit RPC1
RPC1
Family
6,226
false
false
This entry represents the DNA-directed RNA polymerase III subunit RPC1. DNA-directed RNA polymerases (also known as DNA-dependent RNA polymerases) are responsible for the polymerisation of ribonucleotides into a sequence complementary to the template DNA. In eukaryotes, there are three different forms of DNA-directed R...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR48446" ]
[ "" ]
[ 6226 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.7.6", "R-BTA-76061", "R-BTA-76066", "R-BTA-76071", "R-DDI-76061", "R-DDI-76066", "R-HSA-1834949", "R-HSA-73780", "R-HSA-73980", "R-HSA-749476", "R-HSA-76061", "R-HSA-76066", "R-HSA-76071", "R-SCE-76066", "R-SPO-76061", "R-SPO-76066" ]
[ "EC:2.7.7.6", "REACTOME:R-BTA-76061", "REACTOME:R-BTA-76066", "REACTOME:R-BTA-76071", "REACTOME:R-DDI-76061", "REACTOME:R-DDI-76066", "REACTOME:R-HSA-1834949", "REACTOME:R-HSA-73780", "REACTOME:R-HSA-73980", "REACTOME:R-HSA-749476", "REACTOME:R-HSA-76061", "REACTOME:R-HSA-76066", "REACTOME:R...
16
[ "5fj8", "5fj9", "5fja", "6cnb", "6cnc", "6cnd", "6cnf", "6eu0", "6eu1", "6eu2", "6eu3", "6f40", "6f41", "6f42", "6f44", "6tut", "7a6h", "7ae1", "7ae3", "7aea", "7ast", "7d58", "7d59", "7dn3", "7du2", "7fji", "7fjj", "7z0h", "7z1l", "7z1m", "7z1n", "7z1o"...
54
[ "PUB00000061", "PUB00033173" ]
[ "3052291", "10499798" ]
[ "Structure and function of bacterial sigma factors.", "Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution." ]
[ 1988, 1999 ]
2
[]
[]
0
0
null
[ "Archaea", "Eukaryota", "ecological metagenomes" ]
[ 4, 6219, 3 ]
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...
[ 4, 1, 2, 4, 10, 2, 1, 3, 4, 1, 1, 18 ]
12
true
Family
DNA-directed RNA polymerase III subunit RPC1
DNA-directed RNA polymerase III subunit RPC1
RPC1
4
IPR015701
15,701
Ferredoxin--NADP reductase
FNR
Family
3,999
false
false
null
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PIRSF", "PANTHER" ]
[ "PIRSF000361", "PTHR43314" ]
[ "Frd-NADP+_RD", "" ]
[ 3249, 3988 ]
2
[ "EC", "METACYC", "METACYC" ]
[ "1.18.1.2", "PWY-101", "PWY-8271" ]
[ "EC:1.18.1.2", "METACYC:PWY-101", "METACYC:PWY-8271" ]
3
[ "1b2r", "1bjk", "1bqe", "1bx0", "1bx1", "1e62", "1e63", "1e64", "1ewy", "1fnb", "1fnc", "1fnd", "1frn", "1frq", "1gaq", "1gaw", "1gjr", "1go2", "1gr1", "1h42", "1h85", "1jb9", "1ogi", "1ogj", "1qfy", "1qfz", "1qg0", "1qga", "1qgy", "1qgz", "1qh0", "1que"...
83
[ "PUB00001372", "PUB00001683", "PUB00002328", "PUB00002509", "PUB00002674", "PUB00003255", "PUB00004098", "PUB00005007", "PUB00005135", "PUB00005247", "PUB00005356", "PUB00005367", "PUB00043075" ]
[ "2924777", "7890048", "3700359", "2550423", "1748631", "2319593", "1712077", "8298460", "1986412", "7812715", "2204158", "1908607", "15458418" ]
[ "cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases.", "Specific arrangement of three amino acid residues for flavin-binding barrel structures in NADH-cytochrome b5 reductase and the other flavin-dependent reductases.", "Complete amino acid sequence of NADH-cytochrom...
[ 1989, 1995, 1986, 1989, 1991, 1990, 1991, 1993, 1991, 1994, 1990, 1991, 2004 ]
13
[]
[ "IPR017634", "IPR035442" ]
0
2
0
[ "Bacteria", "Eukaryota", "Halorussus caseinilyticus", "unclassified sequences" ]
[ 1343, 2646, 1, 9 ]
4
[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]
[ 20, 8, 34 ]
3
true
Family
Ferredoxin--NADP reductase
Ferredoxin--NADP reductase
FNR
4
IPR015707
15,707
Beta-2-Microglobulin
B2Microglobulin
Family
394
false
false
Beta-2-microglobulin (Beta2m) constitutes the 12kDa light chain of the class I major histocompatibility complex (MHC-I) on the surface of many cells, to which it is non-covalently associated. It is also found in the serum in a free form. Beta-2-microglobulin co-association with the MHC class I heavy chain is prerequisi...
[ "GO:0006955", "GO:0042612" ]
[ "immune response", "MHC class I protein complex" ]
[ "biological_process", "cellular_component" ]
2
[ "CDD" ]
[ "cd05770" ]
[ "IgC1_beta2m" ]
[ 394 ]
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-1236974", "R-BTA-1236977", "R-BTA-198933", "R-BTA-2424491", "R-BTA-6798695", "R-BTA-983170", "R-DRE-1236974", "R-DRE-1236977", "R-DRE-2132295", "R-DRE-6798695", "R-DRE-983170", "R-GGA-1236974", "R-GGA-1236977", "R-GGA-198933", "R-GGA-2424491", "R-GGA-6798695", "R-GGA-983170", ...
[ "REACTOME:R-BTA-1236974", "REACTOME:R-BTA-1236977", "REACTOME:R-BTA-198933", "REACTOME:R-BTA-2424491", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-983170", "REACTOME:R-DRE-1236974", "REACTOME:R-DRE-1236977", "REACTOME:R-DRE-2132295", "REACTOME:R-DRE-6798695", "REACTOME:R-DRE-983170", "REACTOME:R...
50
[ "1a1m", "1a1n", "1a1o", "1a6z", "1a9b", "1a9e", "1agb", "1agc", "1agd", "1age", "1agf", "1akj", "1ao7", "1b0g", "1b0r", "1bd2", "1bii", "1bmg", "1bqh", "1bz9", "1c16", "1cd1", "1ce6", "1cg9", "1ddh", "1de4", "1duy", "1duz", "1e27", "1e28", "1ed3", "1eey"...
1,737
[ "PUB00029693" ]
[ "14595439" ]
[ "Variable MHC class I engagement by Ly49 natural killer cell receptors demonstrated by the crystal structure of Ly49C bound to H-2K(b)." ]
[ 2003 ]
1
[]
[]
0
0
null
[ "Bilateria" ]
[ 394 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 4, 3, 3, 3 ]
4
true
Family
Beta-2-Microglobulin
Beta-2-Microglobulin
B2Microglobulin
6
IPR015712
15,712
DNA-directed RNA polymerase, subunit 2
DNA-dir_RNA_pol_su2
Family
125,802
false
false
This entry represents the beta subunit (also referred to as subunit 2) from DNA-dependent RNA polymerases. RNA polymerases catalyse the DNA dependent polymerization of RNA. Prokaryotes contain a single RNA polymerase compared to three in eukaryotes (not including mitochondrial and chloroplast polymerases). Each RNA pol...
[ "GO:0003899", "GO:0032549", "GO:0006351" ]
[ "DNA-directed RNA polymerase activity", "ribonucleoside binding", "DNA-templated transcription" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "PANTHER", "CDD" ]
[ "PTHR20856", "cd00653" ]
[ "", "RNA_pol_B_RPB2" ]
[ 125444, 61643 ]
2
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", ...
[ "2.7.7.6", "R-BTA-112382", "R-BTA-113418", "R-BTA-5578749", "R-BTA-674695", "R-BTA-6781823", "R-BTA-6782135", "R-BTA-6782210", "R-BTA-6796648", "R-BTA-6803529", "R-BTA-6807505", "R-BTA-72086", "R-BTA-72163", "R-BTA-72165", "R-BTA-72203", "R-BTA-73776", "R-BTA-73779", "R-BTA-75953",...
[ "EC:2.7.7.6", "REACTOME:R-BTA-112382", "REACTOME:R-BTA-113418", "REACTOME:R-BTA-5578749", "REACTOME:R-BTA-674695", "REACTOME:R-BTA-6781823", "REACTOME:R-BTA-6782135", "REACTOME:R-BTA-6782210", "REACTOME:R-BTA-6796648", "REACTOME:R-BTA-6803529", "REACTOME:R-BTA-6807505", "REACTOME:R-BTA-72086",...
214
[ "1hqm", "1i3q", "1i50", "1i6h", "1i6v", "1iw7", "1k83", "1l9u", "1l9z", "1nik", "1nt9", "1pqv", "1r5u", "1r9s", "1r9t", "1sfo", "1smy", "1twa", "1twc", "1twf", "1twg", "1twh", "1wcm", "1y1v", "1y1w", "1y1y", "1y77", "1ynj", "1ynn", "1zyr", "2a68", "2a69"...
1,220
[ "PUB00000061", "PUB00010734", "PUB00011749", "PUB00013986", "PUB00022053", "PUB00025919", "PUB00028105", "PUB00033173", "PUB00079994", "PUB00079995", "PUB00080226" ]
[ "3052291", "11909517", "12000971", "12191485", "12016307", "11313499", "10684922", "10499798", "11839495", "11297923", "10066472" ]
[ "Structure and function of bacterial sigma factors.", "The RNA polymerase II machinery: structure illuminates function.", "Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution.", "Structure of the yeast RNA polymerase II holoenzyme: Mediator conformation and polymerase interaction.",...
[ 1988, 2002, 2002, 2002, 2002, 2001, 2000, 1999, 2002, 2001, 1998 ]
11
[]
[ "IPR010243" ]
0
1
0
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 1881, 41392, 80650, 535, 1344 ]
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",...
[ 32, 3, 4, 4, 1, 21, 9, 3, 30, 9, 3, 3, 107 ]
13
true
Family
DNA-directed RNA polymerase, subunit 2
DNA-directed RNA polymerase, subunit 2
DNA-dir_RNA_pol_su2
2
IPR015720
15,720
Transmembrane emp24 domain-containing protein
Emp24-like
Family
27,582
false
false
This group of proteins consists of TMP21 (also known as transmembrane emp24 domain-containing protein 10) and related proteins, which are members of the p24 family. The p24 family is a widely conserved family of transmembrane proteins that plays a functional role in the initiation of assembly of COPI (Coat protein I) c...
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR22811" ]
[ "" ]
[ 27582 ]
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-204005", "R-BTA-3238698", "R-BTA-5694530", "R-BTA-6807878", "R-BTA-6811434", "R-CEL-1912420", "R-CEL-6807878", "R-CEL-6811434", "R-DDI-6807878", "R-DDI-6811434", "R-DME-6807878", "R-DME-6811434", "R-HSA-1912420", "R-HSA-204005", "R-HSA-3238698", "R-HSA-5694530", "R-HSA-6807878...
[ "REACTOME:R-BTA-204005", "REACTOME:R-BTA-3238698", "REACTOME:R-BTA-5694530", "REACTOME:R-BTA-6807878", "REACTOME:R-BTA-6811434", "REACTOME:R-CEL-1912420", "REACTOME:R-CEL-6807878", "REACTOME:R-CEL-6811434", "REACTOME:R-DDI-6807878", "REACTOME:R-DDI-6811434", "REACTOME:R-DME-6807878", "REACTOME...
34
[ "5azw", "5azx", "5azy", "5gu5", "7rrm", "9cjk", "9cjl" ]
7
[ "PUB00003083", "PUB00009426", "PUB00009427", "PUB00034783", "PUB00034784" ]
[ "9472029", "8947548", "8663407", "15145531", "9681629" ]
[ "gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP I and II coatomer.", "A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding.", "Tmp21 and p24A, two type I proteins enriched in pancreatic microsomal membranes, are members of a protein fami...
[ 1998, 1996, 1996, 2004, 1998 ]
5
[]
[]
0
0
null
[ "Eukaryota", "Vibrio" ]
[ 27569, 13 ]
2
[ "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...
[ 40, 6, 19, 12, 38, 41, 4, 29, 39, 8, 4, 40 ]
12
true
Family
Transmembrane emp24 domain-containing protein
Transmembrane emp24 domain-containing protein
Emp24-like
5
IPR015725
15,725
Myosin Light Chain Kinase 1, Kinase domain
MLCK1_kinase_dom
Domain
681
false
false
Smooth muscle myosin light chain kinase (also known as MLCK1) is a Ser/Thr protein kinase that phosphorylates phosphorylates the 20kDa myosin regulatory light chain (RLC) of smooth and nonmuscle myosin II in the presence of Ca2+ and calmodulin, which facilitates myosin interaction with actin filaments [ , ]. In mice, t...
[ "GO:0004672", "GO:0006468" ]
[ "protein kinase activity", "protein phosphorylation" ]
[ "molecular_function", "biological_process" ]
2
[ "CDD" ]
[ "cd14191" ]
[ "STKc_MLCK1" ]
[ 681 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.11.18", "R-BTA-445355", "R-BTA-5627123", "R-HSA-445355", "R-HSA-5627123", "R-MMU-445355", "R-MMU-5627123" ]
[ "EC:2.7.11.18", "REACTOME:R-BTA-445355", "REACTOME:R-BTA-5627123", "REACTOME:R-HSA-445355", "REACTOME:R-HSA-5627123", "REACTOME:R-MMU-445355", "REACTOME:R-MMU-5627123" ]
7
[]
0
[ "PUB00083900", "PUB00083901" ]
[ "18053800", "16774989" ]
[ "Role of non-kinase activity of myosin light-chain kinase in regulating smooth muscle contraction, a review dedicated to Dr. Setsuro Ebashi.", "Regulation of myosin light chain kinase and telokin expression in smooth muscle tissues." ]
[ 2008, 2006 ]
2
[ "IPR000719" ]
[]
1
0
1
[ "Euteleostomi" ]
[ 681 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 14, 4, 2, 4 ]
4
true
Domain
Myosin Light Chain Kinase 1, Kinase domain
Myosin Light Chain Kinase 1, Kinase domain
MLCK1_kinase_dom
4
IPR015753
15,753
Leucine-rich repeat-containing protein 37
LRRC37
Family
1,445
false
false
This entry represents the leucine-rich repeat-containing protein 37. They are single-pass type I membrane proteins with unknown function.
[]
[]
[]
0
[ "PANTHER" ]
[ "PTHR23045" ]
[ "" ]
[ 1445 ]
1
[]
[]
[]
0
[]
0
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Bilateria" ]
[ 1445 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 43, 4, 8 ]
3
true
Family
Leucine-rich repeat-containing protein 37
Leucine-rich repeat-containing protein 37
LRRC37
8
IPR015758
15,758
Ral guanine nucleotide dissociation stimulator, RA domain
RalGDS_RA
Domain
1,722
false
false
RalGDS family members can act both as Ras effectors and as guanine nucleotide exchange factors (GEFs) for Ral. They act downstream of Ras and bind to the GTP-bound active form of Ras or Ras family members. They also promote the GDP to GTP exchange for Ral small GTPase, member of the Ras family [ ]. Due to their double ...
[]
[]
[]
0
[ "CDD" ]
[ "cd17209" ]
[ "RA_RalGDS" ]
[ 1722 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-171007", "R-HSA-5673001", "R-MMU-171007", "R-MMU-5673001", "R-RNO-171007", "R-RNO-5673001" ]
[ "REACTOME:R-HSA-171007", "REACTOME:R-HSA-5673001", "REACTOME:R-MMU-171007", "REACTOME:R-MMU-5673001", "REACTOME:R-RNO-171007", "REACTOME:R-RNO-5673001" ]
6
[ "1lfd", "1lxd", "1rax", "2b3a", "2rgf", "3kh0" ]
6
[ "PUB00073922", "PUB00073925", "PUB00073929", "PUB00074235", "PUB00101735" ]
[ "10760592", "20478380", "15766660", "9099691", "26469971" ]
[ "The human RGL (RalGDS-like) gene: cloning, expression analysis and genomic organization.", "RalGDS family members couple Ras to Ral signalling and that's not all.", "RalGDS is required for tumor formation in a model of skin carcinogenesis.", "Characterization of Ral GDP dissociation stimulator-like (RGL) act...
[ 2000, 2010, 2005, 1997, 2015 ]
5
[ "IPR000159" ]
[]
1
0
1
[ "Gnathostomata" ]
[ 1722 ]
1
[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 8, 6, 8, 7 ]
4
true
Domain
Ral guanine nucleotide dissociation stimulator, RA domain
Ral guanine nucleotide dissociation stimulator, RA domain
RalGDS_RA
3
IPR015771
15,771
Anti-muellerian hormone receptor, type II
Anti-muellerian_hrmn_rcpt_II
Family
282
false
false
Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substra...
[ "GO:0004675", "GO:0005524", "GO:0006468", "GO:0016020" ]
[ "transmembrane receptor protein serine/threonine kinase activity", "ATP binding", "protein phosphorylation", "membrane" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PIRSF" ]
[ "PIRSF037392" ]
[ "AMHRII" ]
[ 282 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.7.11.30", "R-HSA-201451", "R-MMU-201451", "R-RNO-201451" ]
[ "EC:2.7.11.30", "REACTOME:R-HSA-201451", "REACTOME:R-MMU-201451", "REACTOME:R-RNO-201451" ]
4
[]
0
[ "PUB00005115", "PUB00015362", "PUB00020114", "PUB00034898", "PUB00034899", "PUB00034960" ]
[ "3291115", "12368087", "12471243", "15078142", "15320712", "14656470" ]
[ "The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.", "Evolution of protein kinase signaling from yeast to man.", "The protein kinase complement of the human genome.", "High-throughput structural biology in drug discovery: protein kinases.", "Creating chemical dive...
[ 1988, 2002, 2002, 2004, 2004, 2003 ]
6
[ "IPR000333" ]
[]
1
0
1
[ "Theria" ]
[ 282 ]
1
[ "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 1, 6 ]
3
true
Family
Anti-muellerian hormone receptor, type II
Anti-muellerian hormone receptor, type II
Anti-muellerian_hrmn_rcpt_II
4
IPR015789
15,789
Twist-related, basic helix-loop-helix domain
Twist-rel_bHLH
Domain
211
false
false
The bHLH (basic Helix-Loop-Helix) proteins contain the bHLH domain that is approximately 60 amino acids long and consists of a DNA-binding basic region followed by two α-helices separated by a variable loop region (HLH). The HLH domain promotes dimerisation, allowing the formation of homo- or heterodimeric complexes be...
[]
[]
[]
0
[ "CDD" ]
[ "cd11464" ]
[ "bHLH_TS_TWIST" ]
[ 211 ]
1
[ "REACTOME" ]
[ "R-DME-9764725" ]
[ "REACTOME:R-DME-9764725" ]
1
[]
0
[ "PUB00035177", "PUB00076628", "PUB00086584", "PUB00086585" ]
[ "15294153", "12806077", "3416836", "9716413" ]
[ "Epithelial-mesenchymal transitions: twist in development and metastasis.", "The evolution of the neural basic Helix-Loop-Helix proteins.", "Sequence of the twist gene and nuclear localization of its protein in endomesodermal cells of early Drosophila embryos.", "Analysis of a Caenorhabditis elegans Twist hom...
[ 2004, 2001, 1988, 1998 ]
4
[ "IPR011598" ]
[]
1
0
1
[ "Eumetazoa" ]
[ 211 ]
1
[ "Caenorhabditis elegans", "Drosophila melanogaster" ]
[ 1, 2 ]
2
true
Domain
Twist-related, basic helix-loop-helix domain
Twist-related, basic helix-loop-helix domain
Twist-rel_bHLH
3
IPR015791
15,791
Antimicrobial/protein inhibitor, gamma-crystallin-like
Antimic/Inh_G_crystallin-like
Homologous_superfamily
927
false
false
This structural domain is found in a family of proteins with a Greek key motif [ ] that are related in structure to the beta/gamma crystallins. This group of proteins includes: Streptomyces killer toxin-like protein SKLP Antifungal protein, AFP1 Plant antimicrobial protein, MIAMP1 Streptomyces metalloproteinase inhibit...
[]
[]
[]
0
[ "CATHGENE3D" ]
[ "G3DSA:2.60.20.30" ]
[ "" ]
[ 927 ]
1
[]
[]
[]
0
[ "1bhu", "1c01", "1f53", "1g6e", "1gh5" ]
5
[ "PUB00014133", "PUB00014340", "PUB00014341" ]
[ "14705960", "8506258", "9735297" ]
[ "Evolutionary families of peptidase inhibitors.", "The Greek key motif: extraction, classification and analysis.", "NMR structure of the Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23: another example of an ancestral beta gamma-crystallin precursor structure." ]
[ 2004, 1993, 1998 ]
3
[]
[]
0
0
null
[ "Bacillati", "Eukaryota" ]
[ 513, 414 ]
2
[ "Zea mays" ]
[ 4 ]
1
true
Homologous_superfamily
Antimicrobial/protein inhibitor, gamma-crystallin-like
Antimicrobial/protein inhibitor, gamma-crystallin-like
Antimic/Inh_G_crystallin-like
8
IPR015793
15,793
Pyruvate kinase, barrel
Pyrv_Knase_brl
Domain
50,689
false
false
Pyruvate kinase ( ) (PK) catalyses the final step in glycolysis [ , ], the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP: ADP + phosphoenolpyruvate = ATP + pyruvate The enzyme, which is found in all living organisms, requires both magnesium and potassium ions for its activ...
[ "GO:0000287", "GO:0004743", "GO:0030955", "GO:0006096" ]
[ "magnesium ion binding", "pyruvate kinase activity", "potassium ion binding", "glycolytic process" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
4
[ "PFAM" ]
[ "PF00224" ]
[ "PK" ]
[ 50689 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME...
[ "2.7.1.40", "PWY-1042", "PWY-2221", "PWY-5484", "PWY-5723", "PWY-6886", "PWY-6901", "PWY-7003", "PWY-7218", "PWY-7383", "PWY-8004", "PWY-8404", "PDOC00101", "R-CFA-70171", "R-CFA-70268", "R-DDI-6798695", "R-DDI-70171", "R-DDI-70268", "R-DDI-9861718", "R-DME-6798695", "R-DME-7...
[ "EC:2.7.1.40", "METACYC:PWY-1042", "METACYC:PWY-2221", "METACYC:PWY-5484", "METACYC:PWY-5723", "METACYC:PWY-6886", "METACYC:PWY-6901", "METACYC:PWY-7003", "METACYC:PWY-7218", "METACYC:PWY-7383", "METACYC:PWY-8004", "METACYC:PWY-8404", "PROSITEDOC:PDOC00101", "REACTOME:R-CFA-70171", "REAC...
50
[ "1a3w", "1a3x", "1a49", "1a5u", "1aqf", "1e0t", "1e0u", "1f3w", "1f3x", "1pkl", "1pkm", "1pkn", "1pky", "1t5a", "1zjh", "2e28", "2g50", "2vgb", "2vgf", "2vgg", "2vgi", "3bjf", "3bjt", "3e0v", "3e0w", "3eoe", "3g2g", "3gg8", "3gqy", "3gr4", "3h6o", "3hqn"...
211
[ "PUB00000569", "PUB00014134", "PUB00014243", "PUB00024392", "PUB00100069" ]
[ "2379684", "11960989", "12798932", "10751408", "29748232" ]
[ "Isoenzymes of pyruvate kinase.", "Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.", "Pyruvate kinase: current status of regulatory and functional properties.", "The allosteric regulation of pyruvate kinase.", "An allostatic mechanism for M2 p...
[ 1990, 2002, 2003, 2000, 2018 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctNmW2", "unclassified sequences" ]
[ 711, 31239, 18115, 1, 623 ]
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",...
[ 53, 8, 9, 10, 2, 24, 14, 1, 38, 16, 2, 1, 84 ]
13
true
Domain
Pyruvate kinase, barrel
Pyruvate kinase, barrel
Pyrv_Knase_brl
2
IPR015795
15,795
Pyruvate kinase, C-terminal
Pyrv_Knase_C
Domain
45,685
false
false
Pyruvate kinase ( ) (PK) catalyses the final step in glycolysis [ , ], the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP: ADP + phosphoenolpyruvate = ATP + pyruvate The enzyme, which is found in all living organisms, requires both magnesium and potassium ions for its activ...
[]
[]
[]
0
[ "PFAM" ]
[ "PF02887" ]
[ "PK_C" ]
[ 45685 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME",...
[ "2.7.1.40", "PWY-1042", "PWY-2221", "PWY-5484", "PWY-5723", "PWY-6886", "PWY-6901", "PWY-7003", "PWY-7218", "PWY-7383", "PWY-8004", "PWY-8404", "R-CFA-70171", "R-CFA-70268", "R-DDI-6798695", "R-DDI-70171", "R-DDI-70268", "R-DDI-9861718", "R-DME-6798695", "R-DME-70171", "R-DME...
[ "EC:2.7.1.40", "METACYC:PWY-1042", "METACYC:PWY-2221", "METACYC:PWY-5484", "METACYC:PWY-5723", "METACYC:PWY-6886", "METACYC:PWY-6901", "METACYC:PWY-7003", "METACYC:PWY-7218", "METACYC:PWY-7383", "METACYC:PWY-8004", "METACYC:PWY-8404", "REACTOME:R-CFA-70171", "REACTOME:R-CFA-70268", "REAC...
49
[ "1a3w", "1a3x", "1a49", "1a5u", "1aqf", "1e0t", "1e0u", "1f3w", "1f3x", "1pkl", "1pkm", "1pkn", "1pky", "1t57", "1t5a", "1vp8", "1zjh", "2e28", "2g50", "2vgb", "2vgf", "2vgg", "2vgi", "3bjf", "3bjt", "3e0v", "3e0w", "3eoe", "3g2g", "3gg8", "3gqy", "3gr4"...
212
[ "PUB00000569", "PUB00014134", "PUB00014243", "PUB00024392", "PUB00100069" ]
[ "2379684", "11960989", "12798932", "10751408", "29748232" ]
[ "Isoenzymes of pyruvate kinase.", "Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.", "Pyruvate kinase: current status of regulatory and functional properties.", "The allosteric regulation of pyruvate kinase.", "An allostatic mechanism for M2 p...
[ 1990, 2002, 2003, 2000, 2018 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctNmW2", "unclassified sequences" ]
[ 940, 28703, 15478, 1, 563 ]
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",...
[ 46, 8, 9, 11, 2, 15, 7, 1, 32, 12, 2, 1, 65 ]
13
true
Domain
Pyruvate kinase, C-terminal
Pyruvate kinase, C-terminal
Pyrv_Knase_C
9
IPR015796
15,796
Impact YigZ-like
Impact_YigZ-like
Family
9,456
false
false
The Impact protein is a translational regulator that ensures constant high levels of translation under amino acid starvation. It acts by interacting with Gcn1/Gcn1L1, thereby preventing activation of Gcn2 protein kinases (EIF2AK1 to 4) and subsequent down-regulation of protein synthesis. It is evolutionary conserved fr...
[]
[]
[]
0
[ "NCBIFAM" ]
[ "TIGR00257" ]
[ "IMPACT_YIGZ" ]
[ 9456 ]
1
[]
[]
[]
0
[ "1vi7" ]
1
[ "PUB00032088", "PUB00046141" ]
[ "15103642", "11116084" ]
[ "Crystal structure of YIGZ, a conserved hypothetical protein from Escherichia coli k12 with a novel fold.", "Comparative genome analysis of the mouse imprinted gene impact and its nonimprinted human homolog IMPACT: toward the structural basis for species-specific imprinting." ]
[ 2004, 2000 ]
2
[ "IPR023582" ]
[]
1
0
1
[ "Bacteria", "Eukaryota", "Methanobacteriota", "metagenomes" ]
[ 9354, 7, 56, 39 ]
4
[ "Escherichia coli (strain K12)" ]
[ 1 ]
1
true
Family
Impact YigZ-like
Impact YigZ-like
Impact_YigZ-like
7
IPR015797
15,797
NUDIX hydrolase-like domain superfamily
NUDIX_hydrolase-like_dom_sf
Homologous_superfamily
398,767
false
false
MutT is a small bacterial protein (~12-15Kd) involved in the GO system [ ] responsible for removing an oxidatively damaged form of guanine (8-hydroxy-guanine or 7,8-dihydro-8-oxoguanine) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with near equal efficiency, lead...
[]
[]
[]
0
[ "SSF" ]
[ "SSF55811" ]
[ "" ]
[ 398767 ]
1
[ "EC", "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "R...
[ "3.6.1", "3.6.1.-", "PWY-5757", "PWY-6147", "PWY-6383", "PWY-6797", "PWY-7206", "PWY-7419", "PWY-7539", "PWY-7719", "PWY-7821", "PWY-8289", "R-BTA-1855167", "R-BTA-196807", "R-BTA-2393930", "R-BTA-3299685", "R-BTA-480985", "R-BTA-5389840", "R-BTA-5419276", "R-BTA-72187", "R-B...
[ "EC:3.6.1", "EC:3.6.1.-", "METACYC:PWY-5757", "METACYC:PWY-6147", "METACYC:PWY-6383", "METACYC:PWY-6797", "METACYC:PWY-7206", "METACYC:PWY-7419", "METACYC:PWY-7539", "METACYC:PWY-7719", "METACYC:PWY-7821", "METACYC:PWY-8289", "REACTOME:R-BTA-1855167", "REACTOME:R-BTA-196807", "REACTOME:R...
129
[ "1f3y", "1g0s", "1g9q", "1ga7", "1hx3", "1hzt", "1i9a", "1iry", "1jkn", "1jrk", "1k26", "1k2e", "1khz", "1kt9", "1ktg", "1mk1", "1mp2", "1mqe", "1mqw", "1mr2", "1mut", "1nfs", "1nfz", "1nqy", "1nqz", "1ow2", "1ppv", "1ppw", "1ppx", "1pun", "1puq", "1pus"...
838
[ "PUB00002202", "PUB00002808", "PUB00003856", "PUB00004433", "PUB00006662", "PUB00006677" ]
[ "1328155", "8226881", "8170394", "8233837", "8810257", "10373642" ]
[ "The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine).", "Cloning and expression of cDNA for a human enzyme that hydrolyzes 8-oxo-dGTP, a mutagenic substrate for DNA synthesis.", "Characterization of the mutX gene of Streptococcus pneum...
[ 1992, 1993, 1994, 1993, 1996, 1999 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 5627, 299473, 87865, 1296, 4506 ]
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",...
[ 174, 14, 71, 34, 15, 88, 78, 18, 78, 113, 7, 9, 189 ]
13
true
Homologous_superfamily
NUDIX hydrolase-like domain superfamily
NUDIX hydrolase-like domain superfamily
NUDIX_hydrolase-like_dom_sf
7
IPR015798
15,798
Copper amine oxidase, catalytic domain
Cu_amine_oxidase_C
Domain
19,407
false
false
This entry represents the C-terminal catalytic domain of copper amine oxidases, and has a super-sandwich fold consisting of 18 β-strands in 2 sheets [ ]. A domain with a similar structural fold can be found as the third domain in lysyl oxidase PplO [ ]. Amine oxidases (AO) are enzymes that catalyse the oxidation of a w...
[ "GO:0005507", "GO:0008131", "GO:0048038", "GO:0009308" ]
[ "copper ion binding", "primary methylamine oxidase activity", "quinone binding", "amine metabolic process" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
4
[ "PFAM" ]
[ "PF01179" ]
[ "Cu_amine_oxid" ]
[ 19407 ]
1
[ "EC", "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.4.3", "1.4.3.21", "GenProp1402", "R-BTA-211945", "R-HSA-211945", "R-HSA-6798695", "R-MMU-211945", "R-MMU-6798695", "R-RNO-211945", "R-RNO-6798695", "R-SSC-211945", "R-SSC-6798695" ]
[ "EC:1.4.3", "EC:1.4.3.21", "GP:GenProp1402", "REACTOME:R-BTA-211945", "REACTOME:R-HSA-211945", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-211945", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-211945", "REACTOME:R-RNO-6798695", "REACTOME:R-SSC-211945", "REACTOME:R-SSC-6798695" ]
12
[ "1a2v", "1av4", "1avk", "1avl", "1d6u", "1d6y", "1d6z", "1dyu", "1ekm", "1iqx", "1iqy", "1iu7", "1ivu", "1ivv", "1ivw", "1ivx", "1jrq", "1ksi", "1lvn", "1n9e", "1oac", "1pu4", "1qaf", "1qak", "1qal", "1rjo", "1rky", "1sih", "1sii", "1spu", "1tu5", "1ui7"...
151
[ "PUB00005251", "PUB00010699", "PUB00010700", "PUB00010701", "PUB00016565", "PUB00027613" ]
[ "8591028", "9048544", "9405045", "8805580", "10576737", "14690425" ]
[ "Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.", "Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction.", "Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the...
[ 1995, 1997, 1997, 1996, 1999, 2003 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Klosneuvirinae", "metagenomes" ]
[ 57, 3642, 15637, 3, 68 ]
5
[ "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", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)",...
[ 45, 2, 1, 10, 18, 2, 25, 13, 2, 17 ]
10
true
Domain
Copper amine oxidase, catalytic domain
Copper amine oxidase, catalytic domain
Cu_amine_oxidase_C
6
IPR015799
15,799
Influenza matrix M1, N-terminal subdomain 2
Flu_matrix_M1_N_sub2
Homologous_superfamily
69,987
false
false
Matrix protein (M1) of Influenza virus is a bifunctional membrane/RNA-binding protein that mediates the encapsidation of RNA-nucleoprotein cores into the membrane envelope. It is therefore required that M1 binds both membrane and RNA simultaneously [ ]. M1 is comprised of two domains connected by a linker sequence. The...
[ "GO:0003723", "GO:0005198" ]
[ "RNA binding", "structural molecule activity" ]
[ "molecular_function", "molecular_function" ]
2
[ "CATHGENE3D" ]
[ "G3DSA:1.10.10.180" ]
[ "" ]
[ 69987 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-168255", "R-HSA-168275", "R-HSA-168288", "R-HSA-168298", "R-HSA-168302", "R-HSA-168303", "R-HSA-168316", "R-HSA-168330", "R-HSA-168333", "R-HSA-168336", "R-HSA-192823" ]
[ "REACTOME:R-HSA-168255", "REACTOME:R-HSA-168275", "REACTOME:R-HSA-168288", "REACTOME:R-HSA-168298", "REACTOME:R-HSA-168302", "REACTOME:R-HSA-168303", "REACTOME:R-HSA-168316", "REACTOME:R-HSA-168330", "REACTOME:R-HSA-168333", "REACTOME:R-HSA-168336", "REACTOME:R-HSA-192823" ]
11
[ "1aa7", "1ea3", "2z16", "3md2", "3vdx", "4d9j", "4iq4", "4itv", "4ivj", "4pus", "4qes", "4qf0", "4qff", "5cqe", "5v6g", "5v7b", "5v7s", "5v8a", "6i3h", "6z5j", "6z5l", "7jm3" ]
22
[ "PUB00003941", "PUB00024486" ]
[ "9164466", "11162800" ]
[ "Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1.", "Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer." ]
[ 1997, 2001 ]
2
[]
[]
0
0
null
[ "Bacteria", "Orthomyxoviridae" ]
[ 12, 69975 ]
2
[]
[]
0
true
Homologous_superfamily
Influenza matrix M1, N-terminal subdomain 2
Influenza matrix M1, N-terminal subdomain 2
Flu_matrix_M1_N_sub2
7
IPR015800
15,800
Copper amine oxidase, N2-terminal
Cu_amine_oxidase_N2
Domain
11,890
false
false
This entry represents one (N2) of the two N-terminal domains (N2/N3) that share a similar structure. Amine oxidases (AO) are enzymes that catalyse the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. There are two classes of amine oxidases: flavin-containin...
[ "GO:0005507", "GO:0008131", "GO:0048038", "GO:0009308" ]
[ "copper ion binding", "primary methylamine oxidase activity", "quinone binding", "amine metabolic process" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
4
[ "PFAM" ]
[ "PF02727" ]
[ "Cu_amine_oxidN2" ]
[ 11890 ]
1
[ "EC", "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.4.3", "1.4.3.21", "GenProp1402", "R-BTA-211945", "R-HSA-211945", "R-HSA-6798695", "R-MMU-211945", "R-MMU-6798695", "R-RNO-211945", "R-RNO-6798695", "R-SSC-211945", "R-SSC-6798695" ]
[ "EC:1.4.3", "EC:1.4.3.21", "GP:GenProp1402", "REACTOME:R-BTA-211945", "REACTOME:R-HSA-211945", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-211945", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-211945", "REACTOME:R-RNO-6798695", "REACTOME:R-SSC-211945", "REACTOME:R-SSC-6798695" ]
12
[ "1a2v", "1d6u", "1d6y", "1d6z", "1dyu", "1ekm", "1jrq", "1ksi", "1lvn", "1n9e", "1oac", "1pu4", "1qaf", "1qak", "1qal", "1rky", "1spu", "1tu5", "1us1", "1w2z", "1w7c", "2c10", "2c11", "2oov", "2oqe", "2pnc", "2w0q", "2wgq", "2wo0", "2wof", "2woh", "2y73"...
56
[ "PUB00005251", "PUB00010699", "PUB00010700", "PUB00010701", "PUB00016565" ]
[ "8591028", "9048544", "9405045", "8805580", "10576737" ]
[ "Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.", "Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction.", "Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the...
[ 1995, 1997, 1997, 1996, 1999 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Klosneuvirinae", "metagenomes" ]
[ 45, 1146, 10679, 2, 18 ]
5
[ "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", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)",...
[ 36, 2, 1, 7, 15, 1, 13, 12, 2, 7 ]
10
true
Domain
Copper amine oxidase, N2-terminal
Copper amine oxidase, N2-terminal
Cu_amine_oxidase_N2
5
IPR015802
15,802
Copper amine oxidase, N3-terminal
Cu_amine_oxidase_N3
Domain
12,510
false
false
Amine oxidases (AO) are enzymes that catalyse the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. There are two classes of amine oxidases: flavin-containing ( ) and copper-containing ( ). Copper-containing AO act as a disulphide-linked homodimer. They cata...
[ "GO:0005507", "GO:0008131", "GO:0048038", "GO:0009308" ]
[ "copper ion binding", "primary methylamine oxidase activity", "quinone binding", "amine metabolic process" ]
[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]
4
[ "PFAM" ]
[ "PF02728" ]
[ "Cu_amine_oxidN3" ]
[ 12510 ]
1
[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.4.3.21", "GenProp1402", "R-BTA-211945", "R-HSA-211945", "R-HSA-6798695", "R-MMU-211945", "R-MMU-6798695", "R-RNO-211945", "R-RNO-6798695", "R-SSC-211945", "R-SSC-6798695" ]
[ "EC:1.4.3.21", "GP:GenProp1402", "REACTOME:R-BTA-211945", "REACTOME:R-HSA-211945", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-211945", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-211945", "REACTOME:R-RNO-6798695", "REACTOME:R-SSC-211945", "REACTOME:R-SSC-6798695" ]
11
[ "1a2v", "1d6u", "1d6y", "1d6z", "1dyu", "1ekm", "1jrq", "1ksi", "1lvn", "1oac", "1pu4", "1qaf", "1qak", "1qal", "1spu", "1tu5", "1us1", "1w2z", "2c10", "2c11", "2oov", "2oqe", "2pnc", "2w0q", "2wgq", "2wo0", "2wof", "2woh", "2y73", "2y74", "3ala", "3hi7"...
53
[ "PUB00005251", "PUB00010699", "PUB00010700", "PUB00010701", "PUB00016565" ]
[ "8591028", "9048544", "9405045", "8805580", "10576737" ]
[ "Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.", "Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction.", "Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the...
[ 1995, 1997, 1997, 1996, 1999 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]
[ 54, 2778, 9628, 50 ]
4
[ "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", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)",...
[ 42, 2, 1, 8, 15, 1, 19, 11, 2, 10 ]
10
true
Domain
Copper amine oxidase, N3-terminal
Copper amine oxidase, N3-terminal
Cu_amine_oxidase_N3
2
IPR015803
15,803
Cysteine-tRNA ligase
Cys-tRNA-ligase
Family
36,121
false
false
Cysteine-tRNA ligase (also known as Cysteinyl-tRNA synthetase) ( ) is an alpha monomer and belongs to class Ia [ ]. It is highly specific despite not possessing the amino acid editing activity characteristic of many other tRNA ligases [ ]. Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the a...
[ "GO:0004817", "GO:0005524", "GO:0006423" ]
[ "cysteine-tRNA ligase activity", "ATP binding", "cysteinyl-tRNA aminoacylation" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "NCBIFAM" ]
[ "MF_00041", "TIGR00435" ]
[ "Cys_tRNA_synth", "cysS" ]
[ 35221, 35873 ]
2
[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME" ]
[ "6.1.1.16", "GenProp0258", "R-HSA-379716", "R-HSA-379726", "R-HSA-9725370" ]
[ "EC:6.1.1.16", "GP:GenProp0258", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726", "REACTOME:R-HSA-9725370" ]
5
[ "1li5", "1li7", "1u0b", "3sp1", "3tqo", "6ujd", "8qhp", "9yru", "9yrw", "9yrx", "9yrz", "9ys0", "9ys1", "9ys2", "9yt2", "9yt3", "9yt5" ]
17
[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00028887", "PUB00056788", "PUB00079872", "PUB00079873" ]
[ "8364025", "8274143", "1852601", "2053131", "10673435", "2203971", "10447505", "12032090", "1992490", "10704480", "12458790" ]
[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...
[ 1993, 1993, 1991, 1991, 2000, 1990, 1999, 2002, 1991, 2000, 2002 ]
11
[ "IPR024909" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "Mimiviridae", "unclassified sequences" ]
[ 841, 26864, 7791, 9, 616 ]
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",...
[ 11, 4, 4, 2, 1, 8, 7, 1, 9, 13, 1, 1, 28 ]
13
true
Family
Cysteine-tRNA ligase
Cysteine-tRNA ligase
Cys-tRNA-ligase
1
IPR015806
15,806
Pyruvate kinase, insert domain superfamily
Pyrv_Knase_insert_dom_sf
Homologous_superfamily
47,762
false
false
Pyruvate kinase ( ) (PK) catalyses the final step in glycolysis [ , ], the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP: ADP + phosphoenolpyruvate = ATP + pyruvate The enzyme, which is found in all living organisms, requires both magnesium and potassium ions for its activ...
[ "GO:0004743", "GO:0006096" ]
[ "pyruvate kinase activity", "glycolytic process" ]
[ "molecular_function", "biological_process" ]
2
[ "CATHGENE3D" ]
[ "G3DSA:2.40.33.10" ]
[ "" ]
[ 47762 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME",...
[ "2.7.1.40", "PWY-1042", "PWY-2221", "PWY-5484", "PWY-5723", "PWY-6886", "PWY-6901", "PWY-7003", "PWY-7218", "PWY-7383", "PWY-8004", "PWY-8404", "R-CFA-70171", "R-CFA-70268", "R-DDI-6798695", "R-DDI-70171", "R-DDI-70268", "R-DDI-9861718", "R-DME-6798695", "R-DME-70171", "R-DME...
[ "EC:2.7.1.40", "METACYC:PWY-1042", "METACYC:PWY-2221", "METACYC:PWY-5484", "METACYC:PWY-5723", "METACYC:PWY-6886", "METACYC:PWY-6901", "METACYC:PWY-7003", "METACYC:PWY-7218", "METACYC:PWY-7383", "METACYC:PWY-8004", "METACYC:PWY-8404", "REACTOME:R-CFA-70171", "REACTOME:R-CFA-70268", "REAC...
49
[ "1a3w", "1a3x", "1a49", "1a5u", "1aqf", "1e0t", "1e0u", "1f3w", "1f3x", "1pkl", "1pkm", "1pkn", "1pky", "1t5a", "1zjh", "2e28", "2g50", "2vgb", "2vgf", "2vgg", "2vgi", "3bjf", "3bjt", "3e0v", "3e0w", "3eoe", "3g2g", "3gg8", "3gqy", "3gr4", "3h6o", "3hqn"...
170
[ "PUB00000569", "PUB00014134", "PUB00014243", "PUB00024392", "PUB00100069" ]
[ "2379684", "11960989", "12798932", "10751408", "29748232" ]
[ "Isoenzymes of pyruvate kinase.", "Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.", "Pyruvate kinase: current status of regulatory and functional properties.", "The allosteric regulation of pyruvate kinase.", "An allostatic mechanism for M2 p...
[ 1990, 2002, 2003, 2000, 2018 ]
5
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctNmW2", "unclassified sequences" ]
[ 694, 30373, 16182, 1, 512 ]
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",...
[ 52, 8, 9, 8, 2, 18, 11, 1, 35, 15, 2, 1, 67 ]
13
true
Homologous_superfamily
Pyruvate kinase, insert domain superfamily
Pyruvate kinase, insert domain superfamily
Pyrv_Knase_insert_dom_sf
8
IPR015807
15,807
Histidine-tRNA ligase
His-tRNA-ligase
Family
33,536
false
false
Histidine-tRNA ligase (also known as histidyl-tRNA synthetase) ( ) is an alpha2 dimer that belongs to class IIa. Every completed genome includes a histidine-tRNA ligase. Apparent second copies from Bacillus subtilis, Synechocystis sp. (strain PCC 6803), and Aquifex aeolicus are slightly shorter, more closely related to...
[ "GO:0004821", "GO:0005524", "GO:0006427" ]
[ "histidine-tRNA ligase activity", "ATP binding", "histidyl-tRNA aminoacylation" ]
[ "molecular_function", "molecular_function", "biological_process" ]
3
[ "HAMAP", "NCBIFAM" ]
[ "MF_00127", "TIGR00442" ]
[ "His_tRNA_synth", "hisS" ]
[ 28488, 33088 ]
2
[ "EC", "GP", "REACTOME", "REACTOME" ]
[ "6.1.1.21", "GenProp0258", "R-HSA-379716", "R-HSA-379726" ]
[ "EC:6.1.1.21", "GP:GenProp0258", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726" ]
4
[ "1adj", "1ady", "1h4v", "1htt", "1kmm", "1kmn", "1qe0", "1wu7", "2el9", "3hri", "3hrk", "3lc0", "3net", "4e51", "4g84", "4g85", "4phc", "4rdx", "4x5o", "4yp0", "4ypf", "4yrc", "4yre", "4yrf", "4yrg", "4yri", "4yrj", "4yrk", "4yrl", "4yrm", "4yrn", "4yro"...
41
[]
[]
[]
[]
0
[ "IPR004516" ]
[]
1
0
1
[ "Archaea", "Bacteria", "Eukaryota", "Megaviricetes", "unclassified sequences" ]
[ 911, 26624, 5482, 11, 508 ]
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",...
[ 12, 1, 2, 3, 1, 8, 7, 1, 6, 6, 1, 1, 18 ]
13
true
Family
Histidine-tRNA ligase
Histidine-tRNA ligase
His-tRNA-ligase
1
IPR015810
15,810
Photosynthetic reaction centre, H subunit, N-terminal
Photo_RC_H_N
Domain
652
false
false
This entry represents the N-terminal domain of the photosynthetic reaction centre H subunit, which includes the transmembrane domain and part of the cytoplasmic domain [ ]. The photosynthetic apparatus in non-oxygenic bacteria consists of light-harvesting (LH) protein-pigment complexes LH1 and LH2, which use carotenoid...
[ "GO:0019684", "GO:0030077" ]
[ "photosynthesis, light reaction", "plasma membrane light-harvesting complex" ]
[ "biological_process", "cellular_component" ]
2
[ "PFAM" ]
[ "PF03967" ]
[ "PRCH" ]
[ 652 ]
1
[]
[]
[]
0
[ "1aig", "1aij", "1ds8", "1dv3", "1dv6", "1dxr", "1e14", "1e6d", "1eys", "1f6n", "1fnp", "1fnq", "1jgw", "1jgx", "1jgy", "1jgz", "1jh0", "1k6l", "1k6n", "1kby", "1l9b", "1l9j", "1m3x", "1mps", "1ogv", "1pcr", "1prc", "1pss", "1pst", "1qov", "1r2c", "1rg5"...
219
[ "PUB00014111", "PUB00014116", "PUB00014117", "PUB00015279", "PUB00015395", "PUB00034760", "PUB00034761", "PUB00034762" ]
[ "11095707", "11005826", "10611277", "2676514", "12872158", "15329728", "16931113", "8027023" ]
[ "Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer.", "Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described...
[ 2000, 2000, 1999, 1989, 2003, 2004, 2006, 1994 ]
8
[]
[]
0
0
null
[ "Bacteria", "Eukaryota", "freshwater sediment metagenome" ]
[ 648, 3, 1 ]
3
[]
[]
0
true
Domain
Photosynthetic reaction centre, H subunit, N-terminal
Photosynthetic reaction centre, H subunit, N-terminal
Photo_RC_H_N
4
IPR015811
15,811
Methyl-coenzyme M reductase, alpha subunit, N-terminal subdomain 1
Me_CoM_Rdtase_asu_N_sub1
Homologous_superfamily
822
false
false
Methyl-coenzyme M reductase (MCR) catalyses the reduction of methyl-coenzyme M (CH3-SCoM) and coenzyme B (HS-CoB) to methane and the corresponding heterosulphide CoM-S-S-CoB ( ), the final step in methane biosynthesis. This reaction proceeds under anaerobic conditions by methanogenic Archaea [ ], and requires a nickel-...
[ "GO:0050524", "GO:0015948" ]
[ "coenzyme-B sulfoethylthiotransferase activity", "methanogenesis" ]
[ "molecular_function", "biological_process" ]
2
[ "CATHGENE3D" ]
[ "G3DSA:3.90.390.10" ]
[ "" ]
[ 822 ]
1
[ "EC" ]
[ "2.8.4.1" ]
[ "EC:2.8.4.1" ]
1
[ "1e6v", "1e6y", "1hbm", "1hbn", "1hbo", "1hbu", "1mro", "3m1v", "3m2r", "3m2u", "3m2v", "3m30", "3m32", "3pot", "3sqg", "5a0y", "5a8k", "5a8r", "5a8w", "5g0r", "5n1q", "5n28", "5n2a", "7b1s", "7b2c", "7b2h", "7nkg", "7suc", "7sxm", "8gf5", "8gf6", "8s7v"...
39
[ "PUB00006391", "PUB00010614", "PUB00035993", "PUB00035994" ]
[ "9367957", "11491299", "16260307", "16234924" ]
[ "Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.", "On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding.", "Methyl-coenzyme M reductase genes: unique functional ma...
[ 1997, 2001, 2005, 2005 ]
4
[]
[]
0
0
null
[ "Archaea", "ecological metagenomes" ]
[ 817, 5 ]
2
[]
[]
0
true
Homologous_superfamily
Methyl-coenzyme M reductase, alpha subunit, N-terminal subdomain 1
Methyl-coenzyme M reductase, alpha subunit, N-terminal subdomain 1
Me_CoM_Rdtase_asu_N_sub1
1
IPR015812
15,812
Integrin beta subunit
Integrin_bsu
Family
17,132
false
false
This entry represents the family of integrin beta subunit proteins and integrin beta-like proteins. It also includes integrin beta-pat-3 (pat-3) from Caenorhabditis elegans. Integrin alpha ina-1/beta pat-3 are receptors for laminin. Pat-3 is required for muscle development and maintenance and plays a role in axon regen...
[]
[]
[]
0
[ "PIRSF", "PRINTS", "PANTHER" ]
[ "PIRSF002512", "PR01186", "PTHR10082" ]
[ "Integrin_B", "INTEGRINB", "" ]
[ 9356, 14988, 17013 ]
3
[ "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACT...
[ "PDOC00216", "R-BTA-1566948", "R-BTA-166016", "R-BTA-198933", "R-BTA-202733", "R-BTA-2129379", "R-BTA-216083", "R-BTA-2173789", "R-BTA-3000178", "R-BTA-6798695", "R-CEL-114608", "R-CEL-1236973", "R-CEL-1566977", "R-CEL-198933", "R-CEL-202733", "R-CEL-210991", "R-CEL-2129379", "R-CE...
[ "PROSITEDOC:PDOC00216", "REACTOME:R-BTA-1566948", "REACTOME:R-BTA-166016", "REACTOME:R-BTA-198933", "REACTOME:R-BTA-202733", "REACTOME:R-BTA-2129379", "REACTOME:R-BTA-216083", "REACTOME:R-BTA-2173789", "REACTOME:R-BTA-3000178", "REACTOME:R-BTA-6798695", "REACTOME:R-CEL-114608", "REACTOME:R-CEL...
171
[ "1jv2", "1l5g", "1m1x", "1tye", "1u8c", "1yuk", "2iue", "2k9j", "2knc", "2kv9", "2l91", "2n9y", "2p26", "2p28", "2rmz", "2rn0", "2vc2", "2vdk", "2vdl", "2vdm", "2vdn", "2vdo", "2vdp", "2vdq", "2vdr", "3fcs", "3fcu", "3ije", "3k6s", "3k71", "3k72", "3nid"...
180
[ "PUB00000811", "PUB00001505", "PUB00006148", "PUB00009789", "PUB00015915", "PUB00015985", "PUB00035000", "PUB00035002", "PUB00057248", "PUB00101472", "PUB00160072", "PUB00160424", "PUB00160425" ]
[ "3028640", "2199285", "9009218", "12297042", "14689578", "2467745", "12361595", "12234368", "12388743", "22253611", "11572973", "31109965", "28510180" ]
[ "Integrins: a family of cell surface receptors.", "Integrins and other cell adhesion molecules.", "A structure prediction for the ligand-binding region of the integrin beta subunit: evidence for the presence of a von Willebrand factor A domain.", "Integrins: bidirectional, allosteric signaling machines.", "...
[ 1987, 1990, 1997, 2002, 2004, 1989, 2002, 2002, 2002, 2012, 2001, 2019, 2014 ]
13
[]
[ "IPR012013" ]
0
1
0
[ "Bacteria", "Eukaryota" ]
[ 54, 17078 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 3, 34, 8, 97, 29, 40 ]
6
true
Family
Integrin beta subunit
Integrin beta subunit
Integrin_bsu
5
IPR015813
15,813
Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily
Pyrv/PenolPyrv_kinase-like_dom
Homologous_superfamily
266,070
false
false
Pyruvate kinase controls the exit from the glysolysis pathway, catalysing the transfer of phosphate from phosphooenolpyruvate (PEP) to ADP. Mammalian pyruvate kinase is a homotetramer, where each polypeptide subunit consists of four domains: N-terminal, A domain, B domain and C-terminal. Activation of the enzyme is bel...
[]
[]
[]
0
[ "SSF" ]
[ "SSF51621" ]
[ "" ]
[ 266070 ]
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-CFA-70171", "R-CFA-70268", "R-DDI-6798695", "R-DDI-70171", "R-DDI-70268", "R-DDI-9861718", "R-DME-6798695", "R-DME-70171", "R-DME-70268", "R-DME-9861718", "R-GGA-352882", "R-GGA-6798695", "R-GGA-70171", "R-GGA-70268", "R-GGA-9861718", "R-HSA-163765", "R-HSA-210745", "R-HSA-67986...
[ "REACTOME:R-CFA-70171", "REACTOME:R-CFA-70268", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-70171", "REACTOME:R-DDI-70268", "REACTOME:R-DDI-9861718", "REACTOME:R-DME-6798695", "REACTOME:R-DME-70171", "REACTOME:R-DME-70268", "REACTOME:R-DME-9861718", "REACTOME:R-GGA-352882", "REACTOME:R-GGA-67986...
37
[ "1a3w", "1a3x", "1a49", "1a5u", "1aqf", "1dik", "1dqu", "1dxe", "1dxf", "1e0t", "1e0u", "1f3w", "1f3x", "1f61", "1f8i", "1f8m", "1fiy", "1ggo", "1igw", "1izc", "1jde", "1jqn", "1jqo", "1kbl", "1kc7", "1m1b", "1m3u", "1mum", "1o5q", "1o66", "1o68", "1oqf"...
413
[ "PUB00022133", "PUB00024777", "PUB00026498", "PUB00026675", "PUB00028676", "PUB00035541" ]
[ "12906829", "11563914", "12467579", "11790099", "11526312", "7064730" ]
[ "Structure of E. coli ketopantoate hydroxymethyl transferase complexed with ketopantoate and Mg2+, solved by locating 160 selenomethionine sites.", "Structural and functional linkages between subunit interfaces in mammalian pyruvate kinase.", "Crystal structures of C4 form maize and quaternary complex of E. col...
[ 2003, 2001, 2002, 2002, 2001, 1982 ]
6
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 5068, 206054, 50871, 13, 4064 ]
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",...
[ 125, 10, 12, 8, 14, 29, 16, 8, 96, 19, 5, 3, 289 ]
13
true
Homologous_superfamily
Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily
Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily
Pyrv/PenolPyrv_kinase-like_dom
2
IPR015814
15,814
Phosphogluconate dehydrogenase, NAD-binding, putative, C-terminal
Pgluconate_DH_NAD-bd_C
Domain
4,079
false
false
This domain has been found in a number of eukaryotic and prokaryotic proteins, some of which are predicted to be 6-phosphogluconate dehydrogenase, NAD-binding proteins.
[]
[]
[]
0
[ "PFAM" ]
[ "PF09130" ]
[ "DUF1932" ]
[ 4079 ]
1
[]
[]
[]
0
[ "1i36", "3qsg", "4ezb" ]
3
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "ecological metagenomes" ]
[ 30, 2874, 1140, 35 ]
4
[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)" ]
[ 1 ]
1
true
Domain
Phosphogluconate dehydrogenase, NAD-binding, putative, C-terminal
Phosphogluconate dehydrogenase, NAD-binding, putative, C-terminal
Pgluconate_DH_NAD-bd_C
6
IPR015815
15,815
3-hydroxyisobutyrate dehydrogenase-related
HIBADH-related
Family
64,980
false
false
This entry contains related reductases/dehydrogenases: 3-hydroxyisobutyrate dehydrogenase (HIBADH) ( ) catalyzes 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 [ ] (gene ...
[ "GO:0016491" ]
[ "oxidoreductase activity" ]
[ "molecular_function" ]
1
[ "PIRSF" ]
[ "PIRSF000103" ]
[ "HIBADH" ]
[ 64980 ]
1
[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "1.1.1", "R-BTA-70895", "R-CEL-70895", "R-DDI-70895", "R-DME-70895", "R-HSA-70895", "R-MMU-70895", "R-RNO-70895" ]
[ "EC:1.1.1", "REACTOME:R-BTA-70895", "REACTOME:R-CEL-70895", "REACTOME:R-DDI-70895", "REACTOME:R-DME-70895", "REACTOME:R-HSA-70895", "REACTOME:R-MMU-70895", "REACTOME:R-RNO-70895" ]
8
[ "1vpd", "1wp4", "1yb4", "2cvz", "2gf2", "2i9p", "2uyy", "3cky", "3doj", "3g0o", "3l6d", "3obb", "3pdu", "3pef", "3q3c", "3qha", "3w6u", "3w6z", "3ws7", "3zgy", "3zhb", "4d3d", "4d3f", "4d3s", "4dll", "4ezb", "4gbj", "4oqy", "4oqz", "5a9r", "5a9s", "5a9t"...
122
[ "PUB00002541", "PUB00002721", "PUB00051037", "PUB00057919", "PUB00085179" ]
[ "2647728", "1339433", "18680749", "16352664", "27402745" ]
[ "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, 2008, 2006, 2016 ]
5
[]
[ "IPR006398", "IPR011548", "IPR030876", "IPR050006" ]
0
4
0
[ "Archaea", "Bacteria", "Escherichia phage RCS47", "Eukaryota", "unclassified sequences" ]
[ 405, 55266, 1, 8807, 501 ]
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",...
[ 20, 1, 2, 2, 4, 2, 2, 2, 10, 4, 21 ]
11
true
Family
3-hydroxyisobutyrate dehydrogenase-related
3-hydroxyisobutyrate dehydrogenase-related
HIBADH-related
2
IPR015816
15,816
Vitellinogen, beta-sheet N-terminal
Vitellinogen_b-sht_N
Homologous_superfamily
10,724
false
false
Vitellinogen precursors provide the major egg yolk proteins that are a source of nutrients during early development of oviparous vertebrates and invertebrates. Vitellinogen precursors are multi-domain apolipoproteins that are cleaved into distinct yolk proteins. Different vitellinogen precursors exist, which are compos...
[ "GO:0005319", "GO:0006869" ]
[ "lipid transporter activity", "lipid transport" ]
[ "molecular_function", "biological_process" ]
2
[ "CATHGENE3D" ]
[ "G3DSA:2.30.230.10" ]
[ "" ]
[ 10724 ]
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-8964041", "R-DRE-8964041", "R-HSA-202733", "R-HSA-3000471", "R-HSA-3000480", "R-HSA-3000484", "R-HSA-3000497", "R-HSA-381426", "R-HSA-432142", "R-HSA-5686938", "R-HSA-8856825", "R-HSA-8856828", "R-HSA-8866423", "R-HSA-8957275", "R-HSA-8963888", "R-HSA-8963901", "R-HSA-8964026"...
[ "REACTOME:R-DME-8964041", "REACTOME:R-DRE-8964041", "REACTOME:R-HSA-202733", "REACTOME:R-HSA-3000471", "REACTOME:R-HSA-3000480", "REACTOME:R-HSA-3000484", "REACTOME:R-HSA-3000497", "REACTOME:R-HSA-381426", "REACTOME:R-HSA-432142", "REACTOME:R-HSA-5686938", "REACTOME:R-HSA-8856825", "REACTOME:R...
63
[ "1lsh", "6i7s", "8eoj", "9bd1", "9bd8", "9bde", "9bdt", "9coo", "9e9r", "9ea7", "9eag", "9enr", "9ens" ]
13
[ "PUB00005307", "PUB00007158", "PUB00035546", "PUB00035547", "PUB00035548", "PUB00035549" ]
[ "9687371", "12135361", "17314313", "9692232", "17189915", "8838584" ]
[ "The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein.", "Lipid-protein interactions in lipovitellin.", "Vertebrate yolk complexes and the functional implications of phosvitins and other subdomains in vitellogenins.", "Molecular characteristics of insect vitellogenins and vitellog...
[ 1998, 2002, 2007, 1998, 2006, 1996 ]
6
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 7, 10717 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 27, 7, 14, 5, 5 ]
6
true
Homologous_superfamily
Vitellinogen, beta-sheet N-terminal
Vitellinogen, beta-sheet N-terminal
Vitellinogen_b-sht_N
1
IPR015817
15,817
Vitellinogen, open beta-sheet, subdomain 1
Vitellinogen_open_b-sht_sub1
Homologous_superfamily
5,201
false
false
Vitellinogen precursors provide the major egg yolk proteins that are a source of nutrients during early development of oviparous vertebrates and invertebrates. Vitellinogen precursors are multi-domain apolipoproteins that are cleaved into distinct yolk proteins. Different vitellinogen precursors exist, which are compos...
[ "GO:0005319" ]
[ "lipid transporter activity" ]
[ "molecular_function" ]
1
[ "CATHGENE3D" ]
[ "G3DSA:2.20.50.20" ]
[ "" ]
[ 5201 ]
1
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-HSA-202733", "R-HSA-3000471", "R-HSA-3000480", "R-HSA-3000484", "R-HSA-3000497", "R-HSA-381426", "R-HSA-432142", "R-HSA-5686938", "R-HSA-8856825", "R-HSA-8856828", "R-HSA-8866423", "R-HSA-8957275", "R-HSA-8963888", "R-HSA-8963901", "R-HSA-8964026", "R-HSA-8964038", "R-HSA-8964041"...
[ "REACTOME:R-HSA-202733", "REACTOME:R-HSA-3000471", "REACTOME:R-HSA-3000480", "REACTOME:R-HSA-3000484", "REACTOME:R-HSA-3000497", "REACTOME:R-HSA-381426", "REACTOME:R-HSA-432142", "REACTOME:R-HSA-5686938", "REACTOME:R-HSA-8856825", "REACTOME:R-HSA-8856828", "REACTOME:R-HSA-8866423", "REACTOME:R...
20
[ "1lsh", "9bd1", "9bd8", "9bde", "9bdt", "9coo", "9e9r", "9ea7", "9eag" ]
9
[ "PUB00005307", "PUB00007158", "PUB00035546", "PUB00035547", "PUB00035548", "PUB00035549" ]
[ "9687371", "12135361", "17314313", "9692232", "17189915", "8838584" ]
[ "The structural basis of lipid interactions in lipovitellin, a soluble lipoprotein.", "Lipid-protein interactions in lipovitellin.", "Vertebrate yolk complexes and the functional implications of phosvitins and other subdomains in vitellogenins.", "Molecular characteristics of insect vitellogenins and vitellog...
[ 1998, 2002, 2007, 1998, 2006, 1996 ]
6
[]
[]
0
0
null
[ "Opisthokonta" ]
[ 5201 ]
1
[ "Danio rerio", "Drosophila melanogaster", "Homo sapiens" ]
[ 22, 4, 5 ]
3
true
Homologous_superfamily
Vitellinogen, open beta-sheet, subdomain 1
Vitellinogen, open beta-sheet, subdomain 1
Vitellinogen_open_b-sht_sub1
6
IPR015819
15,819
Lipid transport protein, beta-sheet shell
Lipid_transp_b-sht_shell
Homologous_superfamily
11,882
false
false
This superfamily represents β-sheet shell domains found in lipid transport proteins such as vitellinogen. Vitellinogen precursors provide the major egg yolk proteins that are a source of nutrients during early development of oviparous vertebrates and invertebrates. Vitellinogen precursors are multi-domain apolipoprotei...
[ "GO:0005319", "GO:0006869" ]
[ "lipid transporter activity", "lipid transport" ]
[ "molecular_function", "biological_process" ]
2
[ "SSF" ]
[ "SSF56968" ]
[ "" ]
[ 11882 ]
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-8964041", "R-DRE-8964041", "R-HSA-202733", "R-HSA-3000471", "R-HSA-3000480", "R-HSA-3000484", "R-HSA-3000497", "R-HSA-381426", "R-HSA-432142", "R-HSA-5686938", "R-HSA-8856825", "R-HSA-8856828", "R-HSA-8866423", "R-HSA-8957275", "R-HSA-8963888", "R-HSA-8963901", "R-HSA-8964026"...
[ "REACTOME:R-DME-8964041", "REACTOME:R-DRE-8964041", "REACTOME:R-HSA-202733", "REACTOME:R-HSA-3000471", "REACTOME:R-HSA-3000480", "REACTOME:R-HSA-3000484", "REACTOME:R-HSA-3000497", "REACTOME:R-HSA-381426", "REACTOME:R-HSA-432142", "REACTOME:R-HSA-5686938", "REACTOME:R-HSA-8856825", "REACTOME:R...
63
[ "1lsh", "6i7s", "8eoj", "9bd1", "9bd8", "9bde", "9bdt", "9coo", "9e9r", "9ea7", "9eag", "9enr", "9ens" ]
13
[ "PUB00007158", "PUB00035546" ]
[ "12135361", "17314313" ]
[ "Lipid-protein interactions in lipovitellin.", "Vertebrate yolk complexes and the functional implications of phosvitins and other subdomains in vitellogenins." ]
[ 2002, 2007 ]
2
[]
[]
0
0
null
[ "Bacteria", "Eukaryota" ]
[ 8, 11874 ]
2
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 6, 29, 7, 14, 5, 5 ]
6
true
Homologous_superfamily
Lipid transport protein, beta-sheet shell
Lipid transport protein, beta-sheet shell
Lipid_transp_b-sht_shell
1
IPR015823
15,823
Methyl-coenzyme M reductase, alpha subunit, N-terminal subdomain 2
Me_CoM_Rdtase_asu_N_sub2
Homologous_superfamily
2,191
false
false
Methyl-coenzyme M reductase (MCR) catalyses the reduction of methyl-coenzyme M (CH3-SCoM) and coenzyme B (HS-CoB) to methane and the corresponding heterosulphide CoM-S-S-CoB ( ), the final step in methane biosynthesis. This reaction proceeds under anaerobic conditions by methanogenic Archaea [ ], and requires a nickel-...
[ "GO:0050524", "GO:0015948" ]
[ "coenzyme-B sulfoethylthiotransferase activity", "methanogenesis" ]
[ "molecular_function", "biological_process" ]
2
[ "CATHGENE3D" ]
[ "G3DSA:3.30.70.470" ]
[ "" ]
[ 2191 ]
1
[ "EC" ]
[ "2.8.4.1" ]
[ "EC:2.8.4.1" ]
1
[ "1e6v", "1e6y", "1hbm", "1hbn", "1hbo", "1hbu", "1mro", "3m1v", "3m2r", "3m2u", "3m2v", "3m30", "3m32", "3pot", "3sqg", "5a0y", "5a8k", "5a8r", "5a8w", "5g0r", "5n1q", "5n28", "5n2a", "7b1s", "7b2c", "7b2h", "7nkg", "7suc", "7sxm", "8gf5", "8gf6", "8s7v"...
39
[ "PUB00006391", "PUB00010614", "PUB00035993", "PUB00035994" ]
[ "9367957", "11491299", "16260307", "16234924" ]
[ "Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.", "On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding.", "Methyl-coenzyme M reductase genes: unique functional ma...
[ 1997, 2001, 2005, 2005 ]
4
[]
[]
0
0
null
[ "Archaea", "unclassified sequences", "uncultured rumen bacterium" ]
[ 2033, 141, 17 ]
3
[]
[]
0
true
Homologous_superfamily
Methyl-coenzyme M reductase, alpha subunit, N-terminal subdomain 2
Methyl-coenzyme M reductase, alpha subunit, N-terminal subdomain 2
Me_CoM_Rdtase_asu_N_sub2
4
IPR015824
15,824
Phosphoglycerate kinase, N-terminal
Phosphoglycerate_kinase_N
Homologous_superfamily
38,125
false
false
Phosphoglycerate kinase ( ) (PGK) is an enzyme that catalyses the formation of ATP to ADP and vice versa. In the second step of the second phase in glycolysis, 1,3-diphosphoglycerate is converted to 3-phosphoglycerate, forming one molecule of ATP. If the reverse were to occur, one molecule of ADP would be formed. This ...
[ "GO:0004618", "GO:0006096" ]
[ "phosphoglycerate kinase activity", "glycolytic process" ]
[ "molecular_function", "biological_process" ]
2
[ "CATHGENE3D" ]
[ "G3DSA:3.40.50.1260" ]
[ "" ]
[ 38125 ]
1
[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTO...
[ "2.7.2.3", "PWY-1042", "PWY-5484", "PWY-6886", "PWY-6901", "PWY-7003", "PWY-8004", "PWY-8404", "R-BTA-70171", "R-BTA-70263", "R-CEL-70171", "R-CEL-70263", "R-DDI-70171", "R-DDI-70263", "R-DME-70171", "R-DME-70263", "R-GGA-352875", "R-GGA-352882", "R-HSA-70171", "R-HSA-70263", ...
[ "EC:2.7.2.3", "METACYC:PWY-1042", "METACYC:PWY-5484", "METACYC:PWY-6886", "METACYC:PWY-6901", "METACYC:PWY-7003", "METACYC:PWY-8004", "METACYC:PWY-8404", "REACTOME:R-BTA-70171", "REACTOME:R-BTA-70263", "REACTOME:R-CEL-70171", "REACTOME:R-CEL-70263", "REACTOME:R-DDI-70171", "REACTOME:R-DDI-...
33
[ "13pk", "16pk", "1fw8", "1hdi", "1kf0", "1ltk", "1php", "1qpg", "1v6s", "1vjc", "1vjd", "1vpe", "1zmr", "2cun", "2ie8", "2p9q", "2p9t", "2paa", "2wzb", "2wzc", "2wzd", "2x13", "2x14", "2x15", "2xe6", "2xe7", "2xe8", "2y3i", "2ybe", "2zgv", "3c39", "3c3a"...
68
[ "PUB00006255", "PUB00006482", "PUB00006511" ]
[ "2124145", "6689547", "10593256" ]
[ "Flexibility and folding of phosphoglycerate kinase.", "Phosphoglycerate kinase abnormalities: functional, structural and genomic aspects.", "Folding funnels and conformational transitions via hinge-bending motions." ]
[ 1990, 1983, 1999 ]
3
[]
[]
0
0
null
[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]
[ 956, 26516, 9799, 2, 852 ]
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",...
[ 8, 1, 1, 6, 1, 10, 4, 1, 16, 8, 1, 1, 33 ]
13
true
Homologous_superfamily
Phosphoglycerate kinase, N-terminal
Phosphoglycerate kinase, N-terminal
Phosphoglycerate_kinase_N
2
IPR015827
15,827
Alpha-(1,6)-fucosyltransferase
Fut8
Family
1,153
false
false
Alpha-(1,6)-fucosyltransferase Fut8 catalyses the alpha1,6-linkage of a fucose residue from a donor substrate to N-linked oligosaccharides on glycoproteins in a process called core fucosylation, which is crucial for growth factor receptor-mediated biological functions. Fut8-deficient mice show severe growth retardation...
[ "GO:0008424", "GO:0009101", "GO:0016020", "GO:0032580" ]
[ "glycoprotein 6-alpha-L-fucosyltransferase activity", "glycoprotein biosynthetic process", "membrane", "Golgi cisterna membrane" ]
[ "molecular_function", "biological_process", "cellular_component", "cellular_component" ]
4
[ "PIRSF" ]
[ "PIRSF000472" ]
[ "Alpha1_6FUT_euk" ]
[ 1153 ]
1
[ "EC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "2.4.1.68", "PWY-7426", "R-CEL-975578", "R-DME-975578", "R-HSA-9694548", "R-HSA-975578", "R-MMU-975578", "R-RNO-975578", "R-XTR-975578" ]
[ "EC:2.4.1.68", "METACYC:PWY-7426", "REACTOME:R-CEL-975578", "REACTOME:R-DME-975578", "REACTOME:R-HSA-9694548", "REACTOME:R-HSA-975578", "REACTOME:R-MMU-975578", "REACTOME:R-RNO-975578", "REACTOME:R-XTR-975578" ]
9
[ "2de0", "6vlf", "6vlg", "6x5h", "6x5r", "6x5t", "6x5u" ]
7
[ "PUB00040227", "PUB00085809", "PUB00085810", "PUB00085811" ]
[ "17172260", "17132494", "21951615", "14568171" ]
[ "Crystal structure of mammalian alpha1,6-fucosyltransferase, FUT8.", "Phenotype changes of Fut8 knockout mouse: core fucosylation is crucial for the function of growth factor receptor(s).", "Alteration in N-glycomics during mouse aging: a role for FUT8.", "Expression of alpha1,6-fucosyltransferase (FUT8) in p...
[ 2007, 2006, 2011, 2003 ]
4
[]
[]
0
0
null
[ "Bilateria" ]
[ 1153 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 7, 1, 3, 2, 4 ]
6
true
Family
Alpha-(1,6)-fucosyltransferase
Alpha-(1,6)-fucosyltransferase
Fut8
3
IPR015828
15,828
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
NDUFA10
Family
1,652
false
false
This entry represents the subunit 10 (also known as CI-42kD) of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). It is an accessory subunit that is believed not to be involved in catalysis [ ].
[ "GO:0006120" ]
[ "mitochondrial electron transport, NADH to ubiquinone" ]
[ "biological_process" ]
1
[ "PIRSF", "CDD" ]
[ "PIRSF000543", "cd02030" ]
[ "NADH_UQ_42KD", "NDUO42" ]
[ 1596, 1162 ]
2
[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]
[ "R-DME-611105", "R-DME-6799198", "R-HSA-611105", "R-HSA-6799198", "R-MMU-611105", "R-MMU-6799198", "R-RNO-611105", "R-RNO-6799198" ]
[ "REACTOME:R-DME-611105", "REACTOME:R-DME-6799198", "REACTOME:R-HSA-611105", "REACTOME:R-HSA-6799198", "REACTOME:R-MMU-611105", "REACTOME:R-MMU-6799198", "REACTOME:R-RNO-611105", "REACTOME:R-RNO-6799198" ]
8
[ "5gpn", "5gup", "5lnk", "5o31", "5xtc", "5xtd", "5xth", "5xti", "6g2j", "6g72", "6q9b", "6qa9", "6qbx", "6qc2", "6qc3", "6qc4", "6qc5", "6qc6", "6qc7", "6qc8", "6qc9", "6qca", "6qcf", "6zka", "6zkb", "6zkc", "6zkd", "6zke", "6zkf", "6zkg", "6zkh", "6zki"...
205
[ "PUB00005074", "PUB00011390", "PUB00043561", "PUB00045437" ]
[ "1470679", "9878551", "10940377", "18394423" ]
[ "The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.", "cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed.", "The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubuni...
[ 1992, 1998, 2000, 2008 ]
4
[]
[]
0
0
null
[ "Bilateria" ]
[ 1652 ]
1
[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]
[ 1, 1, 2, 25, 1, 13 ]
6
true
Family
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial
NDUFA10
4
IPR015832
15,832
MTH_1235/AF_1403/MJ1458
MTH_1235-like
Family
195
false
false
This entry includes Uncharacterized protein MTH_1235, AF_1403 and MJ1458. They are predicted ligand-binding protein with an N-terminal ACT domain, AF1403 type. The ACT domain generally has a regulatory role that is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration.
[]
[]
[]
0
[ "PIRSF" ]
[ "PIRSF006363" ]
[ "UCP006363_ACT" ]
[ 195 ]
1
[]
[]
[]
0
[ "1y7p" ]
1
[]
[]
[]
[]
0
[]
[]
0
0
null
[ "Archaea", "Bacteria", "ecological metagenomes" ]
[ 167, 19, 9 ]
3
[]
[]
0
true
Family
MTH_1235/AF_1403/MJ1458
MTH_1235/AF_1403/MJ1458
MTH_1235-like
2
IPR015833
15,833
DNA-directed DNA polymerase, family B, mitochondrial linear plasmid
DNA-dir_DNA_pol_B_mt_lin_plsmd
Family
79
false
false
This group represents a family B type DNA-directed DNA polymerase which is encoded on mitochondrial linear plasmids [ ].
[ "GO:0003677", "GO:0003887", "GO:0006260", "GO:0005739" ]
[ "DNA binding", "DNA-directed DNA polymerase activity", "DNA replication", "mitochondrion" ]
[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]
4
[ "PIRSF" ]
[ "PIRSF006517" ]
[ "DPol_mt_plasmid" ]
[ 79 ]
1
[ "EC" ]
[ "2.7.7.7" ]
[ "EC:2.7.7.7" ]
1
[]
0
[ "PUB00016902" ]
[ "1782679" ]
[ "The linear plasmid pMC3-2 from Morchella conica is structurally related to adenoviruses." ]
[ 1991 ]
1
[ "IPR006172" ]
[]
1
0
1
[ "Eukaryota" ]
[ 79 ]
1
[ "Zea mays" ]
[ 5 ]
1
true
Family
DNA-directed DNA polymerase, family B, mitochondrial linear plasmid
DNA-directed DNA polymerase, family B, mitochondrial linear plasmid
DNA-dir_DNA_pol_B_mt_lin_plsmd
6