TRIM37
entrez
4591
canonical
uniprot
O94972
canonical
ensembl
ENSG00000108395
resolver
ensp
ENSP00000262294
resolver
ensp
ENSP00000376784
resolver
ensp
ENSP00000376785
resolver
ensp
ENSP00000555302
resolver
ensp
ENSP00000555303
resolver
ensp
ENSP00000555304
resolver
ensp
ENSP00000555306
resolver
ensp
ENSP00000555307
resolver
ensp
ENSP00000555311
resolver
ensp
ENSP00000555315
resolver
ensp
ENSP00000555318
resolver
ensp
ENSP00000608689
resolver
ensp
ENSP00000608693
resolver
ensp
ENSP00000634708
resolver
ensp
ENSP00000713371
resolver
ensp
ENSP00000713372
resolver
ensp
ENSP00000713373
resolver
ensp
ENSP00000747670
resolver
ensp
ENSP00000747673
resolver
genesymbol
TRIM37
resolver
genesymbol_syn
KIAA0898
resolver
genesymbol_syn
MUL
resolver
genesymbol_syn
POB1
resolver
hgnc
HGNC:7523
resolver
uniprot
A8K0V9
resolver
uniprot
A8K8U4
resolver
uniprot
A8MZ79
resolver
uniprot
B4DGZ3
resolver
uniprot
F8WEE6
resolver
uniprot
Q7Z3E6
resolver
uniprot
Q8IYF7
resolver
uniprot
Q8WYF7
resolver
uniprot_entry
TRI37_HUMAN
resolver
uniprot_sec
A8K0V9
resolver
uniprot_sec
A8K8U4
resolver
uniprot_sec
A8MZ79
resolver
uniprot_sec
B4DGZ3
resolver
uniprot_sec
F8WEE6
resolver
uniprot_sec
Q7Z3E6
resolver
uniprot_sec
Q8IYF7
resolver
uniprot_sec
Q8WYF7
resolver
amino_acid_sequence
MDEQSVESIAEVFRCFICMEKLRDARLCPHCSKLCCFSCIRRWLTEQRAQCPHCRAPLQLRELVNCRWAEEVTQQLDTLQLCSLTKHEENEKDKCENHHEKLSVFCWTCKKCICHQCALWGGMHGGHTFKPLAEIYEQHVTKVNEEVAKLRRRLMELISLVQEVERNVEAVRNAKDERVREIRNAVEMMIARLDTQLKNKLITLMGQKTSLTQETELLESLLQEVEHQLRSCSKSELISKSSEILMMFQQVHRKPMASFVTTPVPPDFTSELVPSYDSATFVLENFSTLRQRADPVYSPPLQVSGLCWRLKVYPDGNGVVRGYYLSVFLELSAGLPETSKYEYRVEMVHQSCNDPTKNIIREFASDFEVGECWGYNRFFRLDLLANEGYLNPQNDTVILRFQVRSPTFFQKSRDQHWYITQLEAAQTSYIQQINNLKERLTIELSRTQKSRDLSPPDNHLSPQNDDALETRAKKSACSDMLLEGGPTTASVREAKEDEEDEEKIQNEDYHHELSDGDLDLDLVYEDEVNQLDGSSSSASSTATSNTEENDIDEETMSGENDVEYNNMELEEGELMEDAAAAGPAGSSHGYVGSSSRISRRTHLCSAATSSLLDIDPLILIHLLDLKDRSSIENLWGLQPRPPASLLQPTASYSRKDKDQRKQQAMWRVPSDLKMLKRLKTQMAEVRCMKTDVKNTLSEIKSSSAASGDMQTSLFSADQAALAACGTENSGRLQDLGMELLAKSSVANCYIRNSTNKKSNSPKPARSSVAGSLSLRRAVDPGENSRSKGDCQTLSEGSPGSSQSGSRHSSPRALIHGSIGDILPKTEDRQCKALDSDAVVVAVFSGLPAVEKRRKMVTLGANAKGGHLEGLQMTDLENNSETGELQPVLPEGASAAPEEGMSSDSDIECDTENEEQEEHTSVGGFHDSFMVMTQPPDEDTHSSFPDGEQIGPEDLSFNTDENSGR
uniprot
proteins
disease_involvement
DISEASE: Mulibrey nanism (MUL) [MIM:253250]: An autosomal recessive growth disorder characterized by severe growth failure of prenatal onset, constrictive pericardium and progressive cardiomyopathy, facial dysmorphism, and failure of sexual maturation. Additional clinical features include hepatomegaly, muscle hypotonia, J-shaped sella turcica, yellowish dots in the ocular fundi, hypoplasia of various endocrine glands, insulin resistance with type 2 diabetes, and an increased risk for Wilms' tumor. {ECO:0000269|PubMed:10888877, ECO:0000269|PubMed:12754710, ECO:0000269|PubMed:15108285, ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:17100991, ECO:0000269|PubMed:17551331, ECO:0000269|PubMed:21865362, ECO:0000269|PubMed:23385855}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase required to prevent centriole reduplication (PubMed:15885686, PubMed:23769972). Probably acts by ubiquitinating positive regulators of centriole reduplication (PubMed:23769972). Mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression: associates with some Polycomb group (PcG) multiprotein PRC2-like complex and mediates repression of target genes (PubMed:25470042). Also acts as a positive regulator of peroxisome import by mediating monoubiquitination of PEX5 at 'Lys-472': monoubiquitination promotes PEX5 stabilitation by preventing its polyubiquitination and degradation by the proteasome (PubMed:28724525). Has anti-HIV activity (PubMed:24317724). {ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:23769972, ECO:0000269|PubMed:24317724, ECO:0000269|PubMed:25470042, ECO:0000269|PubMed:28724525}.
uniprot
proteins
mass_dalton
107906
uniprot
proteins
mutagenesis
MUTAGEN 18; /note="C->R: Abolishes ability to monoubiquitinate 'Lys-119' of histone H2A (H2AK119Ub)."; /evidence="ECO:0000269|PubMed:25470042"; MUTAGEN 35..36; /note="CC->SS: Reduces ubiquitination and abolishes the formation of perinuclear aggregates."; /evidence="ECO:0000269|PubMed:15885686
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:25470042, ECO:0000269|PubMed:28724525}.
uniprot
proteins
post_translational_modification
PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:15885686}.
uniprot
proteins
protein_family
TRIM/RBCC family
uniprot
proteins
pubmed
10048485
uniprot
proteins
pubmed
10888877
uniprot
proteins
pubmed
11938494
uniprot
proteins
pubmed
12754710
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15108285
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15885686
uniprot
proteins
pubmed
16310976
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17100991
uniprot
proteins
pubmed
17551331
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
21865362
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23385855
uniprot
proteins
pubmed
23769972
uniprot
proteins
pubmed
24317724
uniprot
proteins
pubmed
25470042
uniprot
proteins
pubmed
26697951
uniprot
proteins
pubmed
28724525
uniprot
proteins
sequence_length
964
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:25470042}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15885686}. Peroxisome membrane {ECO:0000269|PubMed:11938494, ECO:0000269|PubMed:28724525}; Peripheral membrane protein {ECO:0000269|PubMed:28724525}. Note=Found in vesicles of the peroxisome. Aggregates as aggresomes, a perinuclear region where certain misfolded or aggregated proteins are sequestered for proteasomal degradation. {ECO:0000269|PubMed:15885686}.
uniprot
proteins