Rnf111
entrez
93836
canonical
uniprot
Q99ML9
canonical
ensembl
ENSMUSG00000032217
resolver
ensp
ENSMUSP00000034739
resolver
ensp
ENSMUSP00000149445
resolver
ensp
ENSMUSP00000149501
resolver
ensp
ENSMUSP00000224443
resolver
ensp
ENSMUSP00000224444
resolver
ensp
ENSMUSP00000224445
resolver
ensp
ENSMUSP00000224447
resolver
ensp
ENSMUSP00000224448
resolver
ensp
ENSMUSP00000224449
resolver
ensp
ENSMUSP00000224451
resolver
ensp
ENSMUSP00000224455
resolver
ensp
ENSMUSP00000332611
resolver
ensp
ENSMUSP00000332615
resolver
enst
ENSMUST00000213647
resolver
genesymbol
Rnf111
resolver
uniprot
A0A1L1SRK3
resolver
uniprot
Q3UVL7
resolver
uniprot
Q6NSW2
resolver
uniprot
Q7TMR3
resolver
uniprot
Q8C881
resolver
uniprot
Q8CBC0
resolver
uniprot_entry
A0A1L1SRK3_MOUSE
resolver
uniprot_entry
RN111_MOUSE
resolver
uniprot_sec
Q3UVL7
resolver
uniprot_sec
Q6NSW2
resolver
uniprot_sec
Q7TMR3
resolver
uniprot_sec
Q8C881
resolver
uniprot_sec
Q8CBC0
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
MSQWTPEFNELYTLKVAMKSGTPDAPTTQESLKAVLLHPQPLGATKSFPAEVEMINSKVGNEFSHLCDDSQKQEKDMTGNQQEQEKSGVVRKKRKSQQAGPSYVQNCVKENQEILGRRQQLETPSDEDNDSSLSECLSSPSSSLHFGGSDTVTSDEDKEVSVRHTQPVLSAKSRSHSARSHKWPRTEADPVPSLLMKRPCFHGSALRRVTCRKRLVKSSSSQRTQKQKERMLVQRKKREALAQRKYALLSSSSSSSENDLSSDSSSSSSTDGEEDLCASASENPSNPAAPSGSIDEDVVVIEASFTPQVTANEEINVTSTDSEVEIVTVGESYRSRSTLGHSRSHWSQGSSSHTGRPQESRNRSRISTVIQPLRQNAAEVVDLTVDEDEPTIVPTTSARMDSQTTSASINNSNPSTSEQASDTTSTVASSQPSTVSETEATLTSNSATGSSVGDDVRRTASSAVPESGPPAMPRLPSCCPQHSPCGGTSQSHHALAHPHSSCFQQHGHHFQHHHHHHHTPHPAVPVSPSFSDPACPVERPQVQAPCGANSSSGSSYHDQQALPVDLSNSALRTHGSGGFHGASAFDPCCPVTSSRAAVFGHQAAAAPTQPLSIDGYGSSMVAQPQPQPPPQPSLSSCRHYMPPPYASLTRPLHHQASACHHSHGNAPPQTQPPPQVDYVIPHPVHAFHSQISSHAASHPVAPPPPTHLGSTAAPIPQHLPPAHQPISHHIPAPAPSAQRLHPHEVMQRMEVQRRRMMQHPTRAHERPPPHPHRMHPNYGHGHHIHVPQTMSSHPRQAPERTAWELGIEAGVTAATYTPGALHPHLAHYHAPPRLHHLQLGALPLMVPDMAGYPHIRYISSGLDGASFRGPFRGNFEELIHLEERLGNVNRGASQGTIERCTYPHKYKKVTTDWFSQRKLHCKQDGEEGTEEDTEEKCTICLSILEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVDIEAQLPSES
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase required for mesoderm patterning during embryonic development (PubMed:11298452). Acts as an enhancer of the transcriptional responses of the SMAD2/SMAD3 effectors, which are activated downstream of BMP (PubMed:14657019). 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). 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 (By similarity). Associates with UBE2D2 as an E2 enzyme (By similarity). Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates (PubMed:23530056). Catalyzes 'Lys-63'-linked ubiquitination of sumoylated XPC in response to UV irradiation, promoting nucleotide excision repair (By similarity). Mediates ubiquitination and degradation of sumoylated PML (PubMed:23530056). The regulation of the BMP-SMAD signaling is however independent of sumoylation and is not dependent of SUMO interaction motifs (SIMs) (PubMed:23530056). {ECO:0000250|UniProtKB:Q6ZNA4, ECO:0000269|PubMed:11298452, ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:17341133, ECO:0000269|PubMed:23530056}.
uniprot
proteins
mass_dalton
107896
uniprot
proteins
mutagenesis
MUTAGEN 298..301; /note="VVVI->AVAA: Abolishes binding to sumoylated proteins and ubiquitination and degradation of PML; when associated with 326-A--A-329 and 382-A--A-385."; /evidence="ECO:0000269|PubMed:23530056"; MUTAGEN 324..327; /note="VEIV->AEAA: Abolishes binding to sumoylated proteins and ubiquitination and degradation of PML; when associated with 300-A--A-303 and 382-A--A-385."; /evidence="ECO:0000269|PubMed:23530056"; MUTAGEN 380..383; /note="VVDL->AADA: Abolishes binding to sumoylated proteins and ubiquitination and degradation of PML; when associated with 300-A--A-303 and 326-A--A-329."; /evidence="ECO:0000269|PubMed:23530056"; MUTAGEN 937; /note="C->A: No effect on TGF-beta and BMP signaling."; /evidence="ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:23530056
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
protein_family
Arkadia family
uniprot
proteins
pubmed
11298452
uniprot
proteins
pubmed
14657019
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17341133
uniprot
proteins
pubmed
23530056
uniprot
proteins
sequence_length
989
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14657019}. Cytoplasm {ECO:0000250|UniProtKB:Q6ZNA4}. Nucleus, PML body {ECO:0000269|PubMed:23530056}. Note=Upon TGF-beta treatment, translocates from nucleus to cytosol. {ECO:0000250|UniProtKB:Q6ZNA4}.
uniprot
proteins