RNF115
entrez
27246
canonical
uniprot
Q9Y4L5
canonical
ensembl
ENSG00000265491
resolver
ensp
ENSP00000463650
resolver
ensp
ENSP00000561165
resolver
ensp
ENSP00000657476
resolver
enst
ENST00000582693
resolver
genesymbol
RNF115
resolver
genesymbol_syn
ZNF364
resolver
hgnc
HGNC:18154
resolver
uniprot
A8K3Y4
resolver
uniprot
Q5T2V9
resolver
uniprot
Q7Z2J2
resolver
uniprot_entry
RN115_HUMAN
resolver
uniprot_sec
A8K3Y4
resolver
uniprot_sec
Q5T2V9
resolver
uniprot_sec
Q7Z2J2
resolver
amino_acid_sequence
MAEASAAGADSGAAVAAHRFFCHFCKGEVSPKLPEYICPRCESGFIEEVTDDSSFLGGGGSRIDNTTTTHFAELWGHLDHTMFFQDFRPFLSSSPLDQDNRANERGHQTHTDFWGARPPRLPLGRRYRSRGSSRPDRSPAIEGILQHIFAGFFANSAIPGSPHPFSWSGMLHSNPGDYAWGQTGLDAIVTQLLGQLENTGPPPADKEKITSLPTVTVTQEQVDMGLECPVCKEDYTVEEEVRQLPCNHFFHSSCIVPWLELHDTCPVCRKSLNGEDSTRQSQSTEASASNRFSNDSQLHDRWTF
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase that catalyzes the 'Lys-48'- and/or 'Lys-63'-linked polyubiquitination of various substrates and thereby plays a role in a number of signaling pathways including autophagy, innate immunity, cell proliferation and cell death (PubMed:20019814, PubMed:30689267). Plays a role in the endosomal trafficking and degradation of membrane receptors including EGFR, FLT3, MET and CXCR4 through their polyubiquitination. Participates together with BST2 in antiviral immunity by facilitating the internalization of HIV-1 virions into intracellular vesicles leading to their lysosomal degradation (PubMed:20019814). Also possesses an antiviral activity independently of BST2 by promoting retroviral GAG proteins ubiquitination, redistribution to endo-lysosomal compartments and, ultimately, lysosomal degradation (PubMed:24852021). Catalyzes distinct types of ubiquitination on MAVS and STING1 at different phases of viral infection to promote innate antiviral response (PubMed:33139700). Mediates the 'Lys-48'-linked ubiquitination of MAVS leading to its proteasomal degradation and ubiquitinates STING1 via 'Lys-63'-linked polyubiquitination, critical for its oligomerization and the subsequent recruitment of TBK1 (PubMed:33139700). Plays a positive role in the autophagosome-lysosome fusion by interacting with STX17 and enhancing its stability without affecting 'Lys-48'- or 'Lys-63'-linked polyubiquitination levels, which in turn promotes autophagosome maturation (PubMed:32980859). Negatively regulates TLR-induced expression of proinflammatory cytokines by catalyzing 'Lys-11'-linked ubiquitination of RAB1A and RAB13 to inhibit post-ER trafficking of TLRs to the Golgi by RAB1A and subsequently from the Golgi apparatus to the cell surface by RAB13 (PubMed:35343654). {ECO:0000269|PubMed:16288031, ECO:0000269|PubMed:18819927, ECO:0000269|PubMed:20019814, ECO:0000269|PubMed:24852021, ECO:0000269|PubMed:32980859, ECO:0000269|PubMed:33139700, ECO:0000269|PubMed:35343654, ECO:0000303|PubMed:23418353}.
uniprot
proteins
mass_dalton
33703
uniprot
proteins
mutagenesis
MUTAGEN 26; /note="K->R: Loss of autoubiquitination; when associated with R-32."; /evidence="ECO:0000269|PubMed:18819927"; MUTAGEN 32; /note="K->R: Loss of autoubiquitination; when associated with R-26."; /evidence="ECO:0000269|PubMed:18819927"; MUTAGEN 132; /note="S->A: About 50% loss of phosphorylation; when associated with A-133."; /evidence="ECO:0000269|PubMed:35343654"; MUTAGEN 133; /note="S->A: About 50% loss of phosphorylation; when associated with A-132."; /evidence="ECO:0000269|PubMed:35343654"; MUTAGEN 228; /note="C->A: Loss of autoubiquitination."; /evidence="ECO:0000269|PubMed:18819927"; MUTAGEN 228; /note="C->A: Loss of E3 ligase activity. Maintains the ability to restrict viral particle production; when associated with A-232."; /evidence="ECO:0000269|PubMed:20019814, ECO:0000269|PubMed:33139700"; MUTAGEN 231; /note="C->A: Loss of autoubiquitination."; /evidence="ECO:0000269|PubMed:18819927"; MUTAGEN 231; /note="C->A: Loss of E3 ligase activity. Maintains the ability to restrict viral particle production; when associated with A-228."; /evidence="ECO:0000269|PubMed:20019814, ECO:0000269|PubMed:33139700
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:18819927}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by AKT1, allowing association with the 14-3-3 chaperones that facilitates associating with TLRs. {ECO:0000269|PubMed:35343654}.; PTM: RING-type zinc finger-dependent and E2-dependent autoubiquitination. {ECO:0000269|PubMed:16288031, ECO:0000269|PubMed:18819927}.; PTM: Deubiquitinated by USP9X; antogonizing its autoubiquitination and subsequent proteasomal degradation. {ECO:0000269|PubMed:30689267}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16288031
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16925951
uniprot
proteins
pubmed
18819927
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20019814
uniprot
proteins
pubmed
23418353
uniprot
proteins
pubmed
24852021
uniprot
proteins
pubmed
30689267
uniprot
proteins
pubmed
32980859
uniprot
proteins
pubmed
33139700
uniprot
proteins
pubmed
35343654
uniprot
proteins
sequence_length
304
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20019814, ECO:0000269|PubMed:24852021}. Nucleus {ECO:0000269|PubMed:24852021}. Endoplasmic reticulum {ECO:0000269|PubMed:35343654}. Golgi apparatus {ECO:0000269|PubMed:35343654}. Note=The GTP-bound form of RAB7A recruits RNF115 from the cytosol onto late endosomes/lysosomes. {ECO:0000269|PubMed:20019814, ECO:0000269|PubMed:24852021}.
uniprot
proteins