RNF125
entrez
54941
canonical
uniprot
Q96EQ8
canonical
ensembl
ENSG00000101695
resolver
ensp
ENSP00000217740
resolver
ensp
ENSP00000520722
resolver
ensp
ENSP00000520723
resolver
ensp
ENSP00000579812
resolver
enst
ENST00000217740
resolver
enst
ENST00000718283
resolver
enst
ENST00000718284
resolver
genesymbol
RNF125
resolver
hgnc
HGNC:21150
resolver
uniprot
A0ABB0MVB3
resolver
uniprot
A0ABB0MVB6
resolver
uniprot
Q9NX39
resolver
uniprot_entry
A0ABB0MVB3_HUMAN
resolver
uniprot_entry
A0ABB0MVB6_HUMAN
resolver
uniprot_entry
RN125_HUMAN
resolver
uniprot_sec
Q9NX39
resolver
amino_acid_sequence
MGSVLSTDSGKSAPASATARALERRRDPELPVTSFDCAVCLEVLHQPVRTRCGHVFCRSCIATSLKNNKWTCPYCRAYLPSEGVPATDVAKRMKSEYKNCAECDTLVCLSEMRAHIRTCQKYIDKYGPLQELEETAARCVCPFCQRELYEDSLLDHCITHHRSERRPVFCPLCRLIPDENPSSFSGSLIRHLQVSHTLFYDDFIDFNIIEEALIRRVLDRSLLEYVNHSNTT
uniprot
proteins
disease_involvement
DISEASE: Tenorio syndrome (TNORS) [MIM:616260]: A disease characterized by overgrowth, macrocephaly, and intellectual disability. Some patients may have mild hydrocephaly, hypoglycemia, and inflammatory diseases resembling Sjogren syndrome. {ECO:0000269|PubMed:25196541}. 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 that mediates ubiquitination and subsequent proteasomal degradation of target proteins, such as RIGI, MAVS/IPS1, IFIH1/MDA5, JAK1 and p53/TP53 (PubMed:15843525, PubMed:17460044, PubMed:17643463, PubMed:25591766, PubMed:26027934, PubMed:26471729, PubMed:27411375). Acts as a negative regulator of type I interferon production by mediating ubiquitination of RIGI at 'Lys-181', leading to RIGI degradation (PubMed:17460044, PubMed:26471729). Mediates ubiquitination and subsequent degradation of p53/TP53 (PubMed:25591766). Mediates ubiquitination and subsequent degradation of JAK1 (PubMed:26027934). Acts as a positive regulator of T-cell activation (PubMed:15843525). {ECO:0000269|PubMed:15843525, ECO:0000269|PubMed:17460044, ECO:0000269|PubMed:17643463, ECO:0000269|PubMed:25591766, ECO:0000269|PubMed:26027934, ECO:0000269|PubMed:26471729, ECO:0000269|PubMed:27411375}.
uniprot
proteins
mass_dalton
26454
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="G->A: Abolishes ability to regulate T-cell activation but not E3 ligase activity in vitro. Also abolishes myristoylation and membrane localization."; /evidence="ECO:0000269|PubMed:15843525, ECO:0000269|PubMed:17643463, ECO:0000269|PubMed:17990982"; MUTAGEN 37; /note="C->A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-40."; /evidence="ECO:0000269|PubMed:15843525, ECO:0000269|PubMed:17643463, ECO:0000269|PubMed:17990982"; MUTAGEN 40; /note="C->A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-37."; /evidence="ECO:0000269|PubMed:15843525, ECO:0000269|PubMed:17990982"; MUTAGEN 54; /note="H->A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-57."; /evidence="ECO:0000269|PubMed:15843525"; MUTAGEN 57; /note="C->A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-54."; /evidence="ECO:0000269|PubMed:15843525"; MUTAGEN 72; /note="C->A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-75."; /evidence="ECO:0000269|PubMed:15843525, ECO:0000269|PubMed:17460044, ECO:0000269|PubMed:25591766"; MUTAGEN 75; /note="C->A: Abolishes ability to regulate T-cell activation and E3 ligase activity in vitro; when associated with A-72."; /evidence="ECO:0000269|PubMed:15843525, ECO:0000269|PubMed:17460044, ECO:0000269|PubMed:25591766"; MUTAGEN 100..103; /note="CAEC->AAEA: Abolished E3 ubiquitin-protein ligase activity in vitro."; /evidence="ECO:0000269|PubMed:27411375"; MUTAGEN 109..113; /note="LSEMR->ASEAA: Abolished E3 ubiquitin-protein ligase activity in vitro."; /evidence="ECO:0000269|PubMed:27411375"; MUTAGEN 217; /note="V->P: Reduced ubiquitination and reduced binding to ubiquitinated proteins; when associated with Q-221."; /evidence="ECO:0000269|PubMed:17990982"; MUTAGEN 221; /note="S->Q: Reduced ubiquitination and reduced binding to ubiquitinated proteins; when associated with P-217."; /evidence="ECO:0000269|PubMed:17990982
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:15843525, ECO:0000269|PubMed:17460044, ECO:0000269|PubMed:17643463, ECO:0000269|PubMed:25591766, ECO:0000269|PubMed:26027934, ECO:0000269|PubMed:26471729, ECO:0000269|PubMed:27411375}.
uniprot
proteins
post_translational_modification
PTM: Autoubiquitinated, leading to its subsequent proteasomal degradation. {ECO:0000269|PubMed:17990982}.
uniprot
proteins
pubmed
12974981
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15843525
uniprot
proteins
pubmed
17460044
uniprot
proteins
pubmed
17643463
uniprot
proteins
pubmed
17990982
uniprot
proteins
pubmed
25196541
uniprot
proteins
pubmed
25591766
uniprot
proteins
pubmed
26027934
uniprot
proteins
pubmed
26202983
uniprot
proteins
pubmed
26471729
uniprot
proteins
pubmed
27411375
uniprot
proteins
sequence_length
232
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:17990982}; Lipid-anchor {ECO:0000269|PubMed:17990982}. Note=Shows a reticular staining pattern within the cell and is probably expressed at other intracellular membranes in addition to the Golgi membrane. Not detected at the plasma membrane. {ECO:0000269|PubMed:17990982}.
uniprot
proteins