RNF111
entrez
54778
canonical
uniprot
Q6ZNA4
canonical
ensembl
ENSG00000157450
resolver
ensp
ENSP00000288199
resolver
ensp
ENSP00000452732
resolver
ensp
ENSP00000453015
resolver
ensp
ENSP00000453872
resolver
ensp
ENSP00000565841
resolver
genesymbol
RNF111
resolver
hgnc
HGNC:17384
resolver
uniprot
C9JUS4
resolver
uniprot
H0YN55
resolver
uniprot
Q6P9A4
resolver
uniprot
Q6ZMU2
resolver
uniprot
Q7L428
resolver
uniprot
Q7Z346
resolver
uniprot
Q8N1P9
resolver
uniprot
Q8WUA3
resolver
uniprot
Q9NSR1
resolver
uniprot_entry
RN111_HUMAN
resolver
uniprot_sec
C9JUS4
resolver
uniprot_sec
H0YN55
resolver
uniprot_sec
Q6P9A4
resolver
uniprot_sec
Q6ZMU2
resolver
uniprot_sec
Q7L428
resolver
uniprot_sec
Q7Z346
resolver
uniprot_sec
Q8N1P9
resolver
uniprot_sec
Q8WUA3
resolver
uniprot_sec
Q9NSR1
resolver
activity_regulation
ACTIVITY REGULATION: Binds free ubiquitin non-covalently via its RING-type zinc finger. Ubiquitin-binding leads to enhance the E3 ubiquitin-protein ligase activity by stabilizing the ubiquitin-conjugating enzyme E2 (donor ubiquitin) in the 'closed' conformation and activating ubiquitin transfer. {ECO:0000250|UniProtKB:Q6ZSG1}.
uniprot
proteins
amino_acid_sequence
MSQWTPEYNELYTLKVDMKSEIPSDAPKTQESLKGILLHPEPIGAAKSFPAGVEMINSKVGNEFSHLCDDSQKQEKEMNGNQQEQEKSLVVRKKRKSQQAGPSYVQNCVKENQGILGLRQHLGTPSDEDNDSSFSDCLSSPSSSLHFGDSDTVTSDEDKEVSVRHSQTILNAKSRSHSARSHKWPRTETESVSGLLMKRPCLHGSSLRRLPCRKRFVKNNSSQRTQKQKERILMQRKKREVLARRKYALLPSSSSSSENDLSSESSSSSSTEGEEDLFVSASENHQNNPAVPSGSIDEDVVVIEASSTPQVTANEEINVTSTDSEVEIVTVGESYRSRSTLGHSRSHWSQGSSSHASRPQEPRNRSRISTVIQPLRQNAAEVVDLTVDEDEPTVVPTTSARMESQATSASINNSNPSTSEQASDTASAVTSSQPSTVSETSATLTSNSTTGTSIGDDSRRTTSSAVTETGPPAMPRLPSCCPQHSPCGGSSQNHHALGHPHTSCFQQHGHHFQHHHHHHHTPHPAVPVSPSFSDPACPVERPPQVQAPCGANSSSGTSYHEQQALPVDLSNSGIRSHGSGSFHGASAFDPCCPVSSSRAAIFGHQAAAAAPSQPLSSIDGYGSSMVAQPQPQPPPQPSLSSCRHYMPPPYASLTRPLHHQASACPHSHGNPPPQTQPPPQVDYVIPHPVHAFHSQISSHATSHPVAPPPPTHLASTAAPIPQHLPPTHQPISHHIPATAPPAQRLHPHEVMQRMEVQRRRMMQHPTRAHERPPPHPHRMHPNYGHGHHIHVPQTMSSHPRQAPERSAWELGIEAGVTAATYTPGALHPHLAHYHAPPRLHHLQLGALPLMVPDMAGYPHIRYISSGLDGTSFRGPFRGNFEELIHLEERLGNVNRGASQGTIERCTYPHKYKKVTTDWFSQRKLHCKQDGEEGTEEDTEEKCTICLSILEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVDIEAQLPSES
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase (PubMed:26656854). Required for mesoderm patterning during embryonic development (By similarity). Acts as an enhancer of the transcriptional responses of the SMAD2/SMAD3 effectors, which are activated downstream of BMP (PubMed:14657019, PubMed:16601693). Acts by mediating ubiquitination and degradation of SMAD inhibitors such as SMAD7, inducing their proteasomal degradation and thereby enhancing the transcriptional activity of TGF-beta and BMP (PubMed:14657019, PubMed:16601693). In addition to enhance transcription of SMAD2/SMAD3 effectors, also regulates their turnover by mediating their ubiquitination and subsequent degradation, coupling their activation with degradation, thereby ensuring that only effectors 'in use' are degraded (By similarity). Activates SMAD3/SMAD4-dependent transcription by triggering signal-induced degradation of SNON isoform of SKIL (PubMed:17591695). Associates with UBE2D2 as an E2 enzyme (PubMed:22411132). Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates (PubMed:23751493). Catalyzes 'Lys-63'-linked ubiquitination of sumoylated XPC in response to UV irradiation, promoting nucleotide excision repair (PubMed:23751493). Mediates ubiquitination and degradation of sumoylated PML (By similarity). The regulation of the BMP-SMAD signaling is however independent of sumoylation and is not dependent of SUMO interaction motifs (SIMs) (By similarity). {ECO:0000250|UniProtKB:Q99ML9, ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17591695, ECO:0000269|PubMed:22411132, ECO:0000269|PubMed:23751493, ECO:0000269|PubMed:26656854}.
uniprot
proteins
mass_dalton
108862
uniprot
proteins
mutagenesis
MUTAGEN 300..303; /note="VVVI->AAAA,AVAA: Abolishes binding to sumoylated proteins and ubiquitination and degradation of XPC; when associated with 326-A--A-329 and 382-A--A-385."; /evidence="ECO:0000269|PubMed:23751493"; MUTAGEN 326..329; /note="VEIV->AAAA,AEAA: Abolishes binding to sumoylated proteins and ubiquitination and degradation of XPC; when associated with 300-A--A-303 and 382-A--A-385."; /evidence="ECO:0000269|PubMed:23751493"; MUTAGEN 382..385; /note="VVDL->AAAA,AADA: Abolishes binding to sumoylated proteins and ubiquitination and degradation of XPC; when associated with 300-A--A-303 and 326-A--A-329."; /evidence="ECO:0000269|PubMed:23751493"; MUTAGEN 382; /note="V->A: Abolishes SUMO binding."; /evidence="ECO:0000269|PubMed:23086935"; MUTAGEN 382; /note="V->L: Loss of affinity to SUMO1 and SUMO2."; /evidence="ECO:0000269|PubMed:23086935"; MUTAGEN 382; /note="V->Y: No loss of affinity toward SUMO1 and SUMO2."; /evidence="ECO:0000269|PubMed:23086935"; MUTAGEN 383; /note="V->A: Abolishes SUMO binding."; /evidence="ECO:0000269|PubMed:23086935"; MUTAGEN 383; /note="V->I: No loss of affinity toward SUMO1 and SUMO2."; /evidence="ECO:0000269|PubMed:23086935"; MUTAGEN 384; /note="D->A: Abolishes SUMO binding."; /evidence="ECO:0000269|PubMed:23086935"; MUTAGEN 384; /note="D->E: Loss of affinity to SUMO1 and SUMO2."; /evidence="ECO:0000269|PubMed:23086935"; MUTAGEN 384; /note="D->N: Loss of affinity to SUMO1 and SUMO2."; /evidence="ECO:0000269|PubMed:23086935"; MUTAGEN 385; /note="L->A: Abolishes SUMO binding."; /evidence="ECO:0000269|PubMed:23086935"; MUTAGEN 385; /note="L->I: Loss of affinity to SUMO1 and SUMO2."; /evidence="ECO:0000269|PubMed:23086935"; MUTAGEN 386; /note="T->A: Abolishes SUMO binding."; /evidence="ECO:0000269|PubMed:23086935"; MUTAGEN 386; /note="T->S: Loss of affinity to SUMO1 and SUMO2."; /evidence="ECO:0000269|PubMed:23086935"; MUTAGEN 386; /note="T->V: Loss of affinity to SUMO1 and SUMO2."; /evidence="ECO:0000269|PubMed:23086935
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:17591695, ECO:0000269|PubMed:22411132, ECO:0000269|PubMed:23751493, ECO:0000269|PubMed:26656854}.
uniprot
proteins
protein_family
Arkadia family
uniprot
proteins
pubmed
14657019
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
16601693
uniprot
proteins
pubmed
17591695
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
22411132
uniprot
proteins
pubmed
23086935
uniprot
proteins
pubmed
23751493
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
26656854
uniprot
proteins
pubmed
28112733
uniprot
proteins
sequence_length
994
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16601693, ECO:0000269|PubMed:23751493}. Cytoplasm {ECO:0000269|PubMed:16601693}. Nucleus, PML body {ECO:0000250|UniProtKB:Q99ML9}. Note=Upon TGF-beta treatment, translocates from nucleus to cytosol. {ECO:0000269|PubMed:16601693}.
uniprot
proteins