RNF11
entrez
26994
canonical
uniprot
Q9Y3C5
canonical
ensembl
ENSG00000123091
resolver
ensp
ENSP00000242719
resolver
ensp
ENSP00000526586
resolver
ensp
ENSP00000526587
resolver
enst
ENST00000242719
resolver
enst
ENST00000856527
resolver
enst
ENST00000856528
resolver
genesymbol
RNF11
resolver
hgnc
HGNC:10056
resolver
uniprot
A8KAI2
resolver
uniprot
Q5T7R8
resolver
uniprot_entry
RNF11_HUMAN
resolver
uniprot_sec
A8KAI2
resolver
uniprot_sec
Q5T7R8
resolver
amino_acid_sequence
MGNCLKSPTSDDISLLHESQSDRASFGEGTEPDQEPPPPYQEQVPVPVYHPTPSQTRLATQLTEEEQIRIAQRIGLIQHLPKGVYDPGRDGSEKKIRECVICMMDFVYGDPIRFLPCMHIYHLDCIDDWLMRSFTCPSCMEPVDAALLSSYETN
uniprot
proteins
function
FUNCTION: Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, leading to its degradation by the 26S proteasome. {ECO:0000269|PubMed:14755250}.
uniprot
proteins
mass_dalton
17444
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="G->A: Loss of myristoylation. Change in subcellular location: Becomes diffused throughout the cytosol. Strong reduction of ubiquitination. Reduced efficiency of ITCH-binding."; /evidence="ECO:0000269|PubMed:20676133"; MUTAGEN 4; /note="C->S: Change in subcellular location: Becomes partially cytosolic and retained in association with the Golgi apparatus. Partial reduction of ubiquitination."; /evidence="ECO:0000269|PubMed:20676133"; MUTAGEN 12; /note="D->A: Loss of GGA1-binding."; /evidence="ECO:0000269|PubMed:20676133"; MUTAGEN 15; /note="L->A: Loss of GGA1-binding."; /evidence="ECO:0000269|PubMed:20676133"; MUTAGEN 16; /note="L->A: Loss of GGA1-binding."; /evidence="ECO:0000269|PubMed:20676133"; MUTAGEN 40; /note="Y->A: Loss of ITCH-, SMURF2- and WWP1-binding. Partial loss of ubiquitination by ITCH. No effect on STAMBP-binding; when associated with S-99 and S-102. Persistent TNF-mediated NFKBIA phosphorylation. Loss of stimulus-dependent complex formation with TAX1BP1, TNFAIP3 and RIPK1."; /evidence="ECO:0000269|PubMed:14559117, ECO:0000269|PubMed:14562029, ECO:0000269|PubMed:14755250, ECO:0000269|PubMed:18724389, ECO:0000269|PubMed:19131965"; MUTAGEN 99; /note="C->S: No effect on STAMBP- and SMURF2-binding; when associated with S-102. Persistent TNF-mediated NFKBIA phosphorylation. No effect on STAMBP-binding; when associated with A-40 and S-102. No effect on ubiquitination by ITCH; when associated with S-102. Loss of stimulus-dependent complex formation with TAX1BP1, TNFAIP3 and RIPK1."; /evidence="ECO:0000269|PubMed:14562029, ECO:0000269|PubMed:14755250, ECO:0000269|PubMed:19131965, ECO:0000269|PubMed:20676133"; MUTAGEN 102; /note="C->S: No effect on STAMBP- and SMURF2-binding; when associated with S-99. No effect on ubiquitination by ITCH; when associated with S-102. No effect on STAMBP-binding; when associated with A-40 and S-99."; /evidence="ECO:0000269|PubMed:14562029, ECO:0000269|PubMed:14755250, ECO:0000269|PubMed:20676133"; MUTAGEN 103; /note="M->A,G: Loss of UBE2N-binding. No gain of UBE2L3-binding."; /evidence="ECO:0000269|PubMed:18615712"; MUTAGEN 103; /note="M->L: No effect on UBE2N-binding. No gain of UBE2L3-binding; when associated with L-127 and L-128."; /evidence="ECO:0000269|PubMed:18615712"; MUTAGEN 103; /note="M->V: No effect on UBE2N-binding. Gain of UBE2L3-binding."; /evidence="ECO:0000269|PubMed:18615712"; MUTAGEN 127; /note="D->L: No effect on UBE2N-binding. No gain of UBE2L3-binding; when associated with L-128."; /evidence="ECO:0000269|PubMed:18615712"; MUTAGEN 128; /note="D->L: No effect on UBE2N-binding. No gain of UBE2L3-binding."; /evidence="ECO:0000269|PubMed:18615712"; MUTAGEN 135; /note="T->E: Loss of phosphorylation and of 14-3-3-binding."; /evidence="ECO:0000269|PubMed:16123141
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated in the presence of ITCH, or SMURF2, and UBE2D1, as well as WWP1. {ECO:0000269|PubMed:14562029, ECO:0000269|PubMed:20676133}.; PTM: Phosphorylation by PKB/AKT1 may accelerate degradation by the proteasome. {ECO:0000269|PubMed:16123141}.; PTM: Acylation at both Gly-2 and Cys-4 is required for proper localization to the endosomes. {ECO:0000269|PubMed:20676133}.
uniprot
proteins
pubmed
10673045
uniprot
proteins
pubmed
10810093
uniprot
proteins
pubmed
14559117
uniprot
proteins
pubmed
14562029
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14755250
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16123141
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17917589
uniprot
proteins
pubmed
18615712
uniprot
proteins
pubmed
18724389
uniprot
proteins
pubmed
19131965
uniprot
proteins
pubmed
20213681
uniprot
proteins
pubmed
20676133
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
sequence_length
154
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Early endosome. Recycling endosome. Cytoplasm. Nucleus. Note=Predominantly cytoplasmic, when unphosphorylated, and nuclear, when phosphorylated by PKB/AKT1. {ECO:0000269|PubMed:16123141}.
uniprot
proteins