RNF7
entrez
9616
canonical
uniprot
Q9UBF6
canonical
ensembl
ENSG00000114125
resolver
ensp
ENSP00000273480
resolver
ensp
ENSP00000376725
resolver
ensp
ENSP00000419084
resolver
genesymbol
RNF7
resolver
genesymbol_syn
RBX2
resolver
genesymbol_syn
ROC2
resolver
genesymbol_syn
SAG
resolver
hgnc
HGNC:10070
resolver
uniprot
A8K1H9
resolver
uniprot
A8MTB5
resolver
uniprot
C9JYL3
resolver
uniprot
D3DNF7
resolver
uniprot
D3DNF8
resolver
uniprot
Q9BXN8
resolver
uniprot
Q9Y5M7
resolver
uniprot_entry
RBX2_HUMAN
resolver
uniprot_sec
A8K1H9
resolver
uniprot_sec
A8MTB5
resolver
uniprot_sec
C9JYL3
resolver
uniprot_sec
D3DNF7
resolver
uniprot_sec
D3DNF8
resolver
uniprot_sec
Q9BXN8
resolver
uniprot_sec
Q9Y5M7
resolver
amino_acid_sequence
MADVEDGEETCALASHSGSSGSKSGGDKMFSLKKWNAVAMWSWDVECDTCAICRVQVMDACLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCPLCQQDWVVQRIGK
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
ec_number
2.3.2.32
uniprot
proteins
function
FUNCTION: Catalytic component of multiple cullin-5-RING E3 ubiquitin-protein ligase complexes (ECS complexes), which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:21980433, PubMed:33268465, PubMed:38418882, PubMed:38574733, PubMed:35512830, PubMed:40440427, PubMed:40963025). It is thereby involved in various biological processes, such as cell cycle progression, signal transduction and transcription (PubMed:21980433, PubMed:33268465, PubMed:38418882, PubMed:38574733). The functional specificity of the E3 ubiquitin-protein ligase ECS complexes depend on the variable SOCS box-containing substrate recognition component (PubMed:21980433, PubMed:33268465). Within ECS complexes, RNF7/RBX2 recruits the E2 ubiquitination enzyme to the complex via its RING-type and brings it into close proximity to the substrate (PubMed:34518685). Catalytic subunit of various SOCS-containing ECS complexes, such as the ECS(SOCS7) complex, that regulate reelin signaling by mediating ubiquitination and degradation of DAB1 (By similarity). The ECS(SOCS2) complex mediates the ubiquitination and subsequent proteasomal degradation of phosphorylated EPOR and GHR (PubMed:21980433, PubMed:25505247). Promotes ubiquitination and degradation of NF1, thereby regulating Ras protein signal transduction (By similarity). As part of the ECS(ASB9) complex, catalyzes ubiquitination and degradation of CKB (PubMed:33268465). The ECS(SPSB3) complex catalyzes ubiquitination of nuclear CGAS (PubMed:38418882). As part of the ECS(RAB40C) complex, mediates ANKRD28 ubiquitination and degradation, thereby inhibiting protein phosphatase 6 (PP6) complex activity and focal adhesion assembly during cell migration (PubMed:35512830). The ECS(ASB7) complex acts a negative regulator of H3K9me3 histone mark by mediating ubiquitination and degradation of SUV39H1 (PubMed:40440427). As part of some ECS complex, catalyzes 'Lys-11'-linked ubiquitination and degradation of BTRC (PubMed:27910872). ECS complexes and ARIH2 collaborate in tandem to mediate ubiquitination of target proteins; ARIH2 mediating addition of the first ubiquitin on CRLs targets (PubMed:34518685, PubMed:38418882). As part of the ECS(LRRC58) complex, mediates CDO1 ubiquitination and degradation, regulating cysteine catabolism (PubMed:40963025). Specifically catalyzes the neddylation of CUL5 via its interaction with UBE2F (PubMed:19250909). Does not catalyze neddylation of other cullins (CUL1, CUL2, CUL3, CUL4A or CUL4B) (PubMed:19250909). May play a role in protecting cells from apoptosis induced by redox agents (PubMed:10082581). {ECO:0000250|UniProtKB:Q9WTZ1, ECO:0000269|PubMed:10082581, ECO:0000269|PubMed:19250909, ECO:0000269|PubMed:21980433, ECO:0000269|PubMed:25505247, ECO:0000269|PubMed:27910872, ECO:0000269|PubMed:33268465, ECO:0000269|PubMed:34518685, ECO:0000269|PubMed:35512830, ECO:0000269|PubMed:38418882, ECO:0000269|PubMed:38574733, ECO:0000269|PubMed:40440427, ECO:0000269|PubMed:40963025}.; FUNCTION: [Isoform 2]: Inactive. {ECO:0000269|PubMed:11506706}.; FUNCTION: (Microbial infection) Following infection by HIV-1 virus, catalytic component of a cullin-5-RING E3 ubiquitin-protein ligase complex (ECS complex) hijacked by the HIV-1 Vif protein, which catalyzes ubiquitination and degradation of APOBEC3F and APOBEC3G. {ECO:0000269|PubMed:22190037, ECO:0000269|PubMed:23300442}.
uniprot
proteins
mass_dalton
12683
uniprot
proteins
mutagenesis
MUTAGEN 10; /note="T->A: Abolished phosphorylation by CK2, leading to increased protein stability. Does not affect its subcellular location of E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:16874460"; MUTAGEN 10; /note="T->E: Mimics phosphorylation; leading to decreased protein stability."; /evidence="ECO:0000269|PubMed:16874460
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:21980433, ECO:0000269|PubMed:25505247, ECO:0000269|PubMed:27910872, ECO:0000269|PubMed:33268465, ECO:0000269|PubMed:38418882, ECO:0000269|PubMed:38574733, ECO:0000269|PubMed:40440427}.; PATHWAY: Protein modification; protein neddylation. {ECO:0000269|PubMed:19250909, ECO:0000269|PubMed:23300442, ECO:0000269|PubMed:40963025}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-10 by CK2 promotes its degradation by the proteasome. {ECO:0000269|PubMed:10512750, ECO:0000269|PubMed:12748192, ECO:0000269|PubMed:16874460}.
uniprot
proteins
protein_family
RING-box family
uniprot
proteins
pubmed
10082581
uniprot
proteins
pubmed
10230407
uniprot
proteins
pubmed
10512750
uniprot
proteins
pubmed
10851089
uniprot
proteins
pubmed
11506706
uniprot
proteins
pubmed
12748192
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16874460
uniprot
proteins
pubmed
19250909
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
21980433
uniprot
proteins
pubmed
22190037
uniprot
proteins
pubmed
23300442
uniprot
proteins
pubmed
24337577
uniprot
proteins
pubmed
25505247
uniprot
proteins
pubmed
26906416
uniprot
proteins
pubmed
27910872
uniprot
proteins
pubmed
31387940
uniprot
proteins
pubmed
33268465
uniprot
proteins
pubmed
34518685
uniprot
proteins
pubmed
35512830
uniprot
proteins
pubmed
38418882
uniprot
proteins
pubmed
38574733
uniprot
proteins
pubmed
40440427
uniprot
proteins
pubmed
40963025
uniprot
proteins
sequence_length
113
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10082581, ECO:0000269|PubMed:16874460}. Nucleus {ECO:0000269|PubMed:10082581, ECO:0000269|PubMed:16874460}.
uniprot
proteins