RNF167
entrez
26001
canonical
uniprot
Q9H6Y7
canonical
ensembl
ENSG00000108523
resolver
ensp
ENSP00000262482
resolver
ensp
ENSP00000458189
resolver
ensp
ENSP00000458794
resolver
ensp
ENSP00000459324
resolver
ensp
ENSP00000460190
resolver
ensp
ENSP00000538776
resolver
ensp
ENSP00000538777
resolver
ensp
ENSP00000538778
resolver
ensp
ENSP00000538779
resolver
ensp
ENSP00000538780
resolver
ensp
ENSP00000538781
resolver
ensp
ENSP00000538782
resolver
genesymbol
RNF167
resolver
genesymbol_syn
RING105
resolver
hgnc
HGNC:24544
resolver
uniprot
D3DTK8
resolver
uniprot
I3L0L6
resolver
uniprot
Q6XYE0
resolver
uniprot
Q8NDC1
resolver
uniprot
Q9Y3V1
resolver
uniprot_entry
RN167_HUMAN
resolver
uniprot_sec
D3DTK8
resolver
uniprot_sec
I3L0L6
resolver
uniprot_sec
Q6XYE0
resolver
uniprot_sec
Q8NDC1
resolver
uniprot_sec
Q9Y3V1
resolver
amino_acid_sequence
MHPAAFPLPVVVAAVLWGAAPTRGLIRATSDHNASMDFADLPALFGATLSQEGLQGFLVEAHPDNACSPIAPPPPAPVNGSVFIALLRRFDCNFDLKVLNAQKAGYGAAVVHNVNSNELLNMVWNSEEIQQQIWIPSVFIGERSSEYLRALFVYEKGARVLLVPDNTFPLGYYLIPFTGIVGLLVLAMGAVMIARCIQHRKRLQRNRLTKEQLKQIPTHDYQKGDQYDVCAICLDEYEDGDKLRVLPCAHAYHSRCVDPWLTQTRKTCPICKQPVHRGPGDEDQEEETQGQEEGDEGEPRDHPASERTPLLGSSPTLPTSFGSLAPAPLVFPGPSTDPPLSPPSSPVILV
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase that acts as a regulator of the TORC1 signaling pathway (PubMed:33594058, PubMed:35114100). Positively regulates the TORC1 signaling pathway independently of arginine levels: acts by catalyzing 'Lys-29'-polyubiquitination and degradation of CASTOR1, releasing the GATOR2 complex from CASTOR1 (PubMed:33594058). Also negatively regulates the TORC1 signaling pathway in response to leucine deprivation: acts by mediating 'Lys-63'-linked polyubiquitination of SESN2, promoting SESN2-interaction with the GATOR2 complex (PubMed:35114100). Also involved in protein trafficking and localization (PubMed:23129617, PubMed:23353890, PubMed:24387786, PubMed:27808481, PubMed:32409562). Acts as a regulator of synaptic transmission by mediating ubiquitination and degradation of AMPAR receptor GluA2/GRIA2 (PubMed:23129617, PubMed:33650289). Does not catalyze ubiquitination of GluA1/GRIA1 (PubMed:23129617). Also acts as a regulator of the recycling endosome pathway by mediating ubiquitination of VAMP3 (PubMed:23353890). Regulates lysosome positioning by catalyzing ubiquitination and degradation of ARL8B (PubMed:27808481). Plays a role in growth regulation involved in G1/S transition by mediating, possibly by mediating ubiquitination of SLC22A18 (PubMed:16314844). Acts with a limited set of E2 enzymes, such as UBE2D1 and UBE2N (PubMed:33650289). {ECO:0000269|PubMed:16314844, ECO:0000269|PubMed:23129617, ECO:0000269|PubMed:23353890, ECO:0000269|PubMed:24387786, ECO:0000269|PubMed:27808481, ECO:0000269|PubMed:32409562, ECO:0000269|PubMed:33594058, ECO:0000269|PubMed:33650289, ECO:0000269|PubMed:35114100}.
uniprot
proteins
mass_dalton
38299
uniprot
proteins
mutagenesis
MUTAGEN 33; /note="N->Q: Reduced N-glycosylation. Abolished N-glycosylation; when associated with Q-79."; /evidence="ECO:0000269|PubMed:23129617"; MUTAGEN 79; /note="N->Q: Reduced N-glycosylation. Abolished N-glycosylation; when associated with Q-33."; /evidence="ECO:0000269|PubMed:23129617"; MUTAGEN 232; /note="I->A: Drastically increased stability; reduction in auto-ubiquitination activity; loss of cell delay/arrest in G1."; /evidence="ECO:0000269|PubMed:16314844"; MUTAGEN 233; /note="C->S: Abolished E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:27808481, ECO:0000269|PubMed:32409562"; MUTAGEN 250..253; /note="HAYH->WAYW: Abolished E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:23129617, ECO:0000269|PubMed:33650289"; MUTAGEN 260; /note="W->A: Drastically increased stability; reduction in auto-ubiquitination activity; loss of cell delay/arrest in G1."; /evidence="ECO:0000269|PubMed:16314844
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23129617, ECO:0000269|PubMed:23353890, ECO:0000269|PubMed:27808481, ECO:0000269|PubMed:33594058, ECO:0000269|PubMed:33650289, ECO:0000269|PubMed:35114100}.
uniprot
proteins
post_translational_modification
PTM: Autoubiquitinated in vitro in the presence of UBE2D1 and UBE2E1. {ECO:0000269|PubMed:16314844, ECO:0000269|PubMed:33650289}.
uniprot
proteins
protein_family
Godzilla family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15498874
uniprot
proteins
pubmed
16314844
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
23129617
uniprot
proteins
pubmed
23353890
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24387786
uniprot
proteins
pubmed
27808481
uniprot
proteins
pubmed
32409562
uniprot
proteins
pubmed
33594058
uniprot
proteins
pubmed
33650289
uniprot
proteins
pubmed
35114100
uniprot
proteins
sequence_length
350
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:16314844, ECO:0000269|PubMed:27808481, ECO:0000269|PubMed:35114100}; Single-pass type I membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:24387786}; Single-pass type I membrane protein {ECO:0000255}. Endomembrane system {ECO:0000269|PubMed:16314844}; Single-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:23129617}; Single-pass type I membrane protein {ECO:0000255}. Note=Targeted to cytoplasmic membranes; mainly localizes to lysosomal membrane (PubMed:16314844, PubMed:23129617). A subpopulation localizes to the cell membrane of neurons (PubMed:23129617). {ECO:0000269|PubMed:16314844, ECO:0000269|PubMed:23129617}.; SUBCELLULAR LOCATION: [Isoform 1]: Lysosome membrane {ECO:0000269|PubMed:32409562}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol {ECO:0000269|PubMed:32409562}.
uniprot
proteins
transmembrane_region
TRANSMEM 174..194; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins