Rnf115
entrez
67845
canonical
uniprot
Q9D0C1
canonical
ensembl
ENSMUSG00000028098
resolver
ensp
ENSMUSP00000029740
resolver
ensp
ENSMUSP00000335714
resolver
enst
ENSMUST00000029740
resolver
genesymbol
Rnf115
resolver
genesymbol_syn
Zfp364
resolver
genesymbol_syn
Znf364
resolver
uniprot
Q8R5A1
resolver
uniprot
Q9D885
resolver
uniprot_entry
RN115_MOUSE
resolver
uniprot_sec
Q8R5A1
resolver
uniprot_sec
Q9D885
resolver
amino_acid_sequence
MAEASAAGADAGSAVAAHRFFCHFCKGEVNPKLPEYICPRCDSGFIEEVTDDSSFLGGGGSRTDNSTATHFAELWDHLDHTMFLQDFRPFLSSNPLDQDNRANERGHQTHTDFWGPSRPPRLPMTRRYRSRGSTRPDRSPAIEGIIQQIFAGFFANSAIPGSPHPFSWSGMLHSNPGDYAWGQTGLDAIVTQLLGQLENTGPPPADKEKITSLPTVTVTQEQVNTGLECPVCKEDYTVEEKVRQLPCNHFFHSSCIVPWLELHDTCPVCRKSLNGEDSTRQTQSSEASASNRFSNDSQLHDRWTF
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:36281581). 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. Also possesses an antiviral activity independently of BST2 by promoting retroviral GAG proteins ubiquitination, redistribution to endo-lysosomal compartments and, ultimately, lysosomal degradation. Catalyzes distinct types of ubiquitination on MAVS and STING1 at different phases of viral infection to promote innate antiviral response. 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. 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. {ECO:0000250|UniProtKB:Q9Y4L5, ECO:0000269|PubMed:33139700, ECO:0000269|PubMed:36281581}.
uniprot
proteins
mass_dalton
33859
uniprot
proteins
mutagenesis
MUTAGEN 22; /note="C->A: Loss of interaction with EGFR and FLT3. No effect on E3 ubiquitin protein ligase activity; when associated with A-25."; /evidence="ECO:0000269|PubMed:23418353"; MUTAGEN 25; /note="C->A: Loss of interaction with EGFR and FLT3. No effect on E3 ubiquitin protein ligase activity; when associated with A-22."; /evidence="ECO:0000269|PubMed:23418353"; MUTAGEN 229; /note="C->S: Loss of E3 ubiquitin protein ligase activity."; /evidence="ECO:0000269|PubMed:17462600, ECO:0000269|PubMed:23418353
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:17462600, ECO:0000269|PubMed:23418353}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by AKT1, allowing association with the 14-3-3 chaperones that facilitates associating with TLRs. {ECO:0000250|UniProtKB:Q9Y4L5}.; PTM: Deubiquitinated by USP9X; antogonizing its autoubiquitination and subsequent proteasomal degradation. {ECO:0000250|UniProtKB:Q9Y4L5}.; PTM: RING-type zinc finger-dependent and E2-dependent autoubiquitination. {ECO:0000269|PubMed:17462600}.
uniprot
proteins
pubmed
12972561
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17462600
uniprot
proteins
pubmed
23418353
uniprot
proteins
pubmed
33139700
uniprot
proteins
pubmed
36281581
uniprot
proteins
sequence_length
305
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12972561}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:36281581}. Nucleus {ECO:0000250|UniProtKB:Q9Y4L5}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y4L5}. Golgi apparatus {ECO:0000250|UniProtKB:Q9Y4L5}. Note=The GTP-bound form of RAB7A recruits RNF115 from the cytosol onto late endosomes/lysosomes. {ECO:0000269|PubMed:12972561}.
uniprot
proteins