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RNF111

Gene
RNF111
Protein
E3 ubiquitin-protein ligase Arkadia
Organism
Homo sapiens
Length
994 amino acids
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).
Similarity
Belongs to the Arkadia family.
Mass
108.862 kDa
Sequence
MSQWTPEYNELYTLKVDMKSEIPSDAPKTQESLKGILLHPEPIGAAKSFPAGVEMINSKVGNEFSHLCDDSQKQEKEMNGNQQEQEKSLVVRKKRKSQQAGPSYVQNCVKENQGILGLRQHLGTPSDEDNDSSFSDCLSSPSSSLHFGDSDTVTSDEDKEVSVRHSQTILNAKSRSHSARSHKWPRTETESVSGLLMKRPCLHGSSLRRLPCRKRFVKNNSSQRTQKQKERILMQRKKREVLARRKYALLPSSSSSSENDLSSESSSSSSTEGEEDLFVSASENHQNNPAVPSGSIDEDVVVIEASSTPQVTANEEINVTSTDSEVEIVTVGESYRSRSTLGHSRSHWSQGSSSHASRPQEPRNRSRISTVIQPLRQNAAEVVDLTVDEDEPTVVPTTSARMESQATSASINNSNPSTSEQASDTASAVTSSQPSTVSETSATLTSNSTTGTSIGDDSRRTTSSAVTETGPPAMPRLPSCCPQHSPCGGSSQNHHALGHPHTSCFQQHGHHFQHHHHHHHTPHPAVPVSPSFSDPACPVERPPQVQAPCGANSSSGTSYHEQQALPVDLSNSGIRSHGSGSFHGASAFDPCCPVSSSRAAIFGHQAAAAAPSQPLSSIDGYGSSMVAQPQPQPPPQPSLSSCRHYMPPPYASLTRPLHHQASACPHSHGNPPPQTQPPPQVDYVIPHPVHAFHSQISSHATSHPVAPPPPTHLASTAAPIPQHLPPTHQPISHHIPATAPPAQRLHPHEVMQRMEVQRRRMMQHPTRAHERPPPHPHRMHPNYGHGHHIHVPQTMSSHPRQAPERSAWELGIEAGVTAATYTPGALHPHLAHYHAPPRLHHLQLGALPLMVPDMAGYPHIRYISSGLDGTSFRGPFRGNFEELIHLEERLGNVNRGASQGTIERCTYPHKYKKVTTDWFSQRKLHCKQDGEEGTEEDTEEKCTICLSILEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVDIEAQLPSES

Gene
Rnf111
Protein
E3 ubiquitin-protein ligase Arkadia
Organism
Mus musculus
Length
989 amino acids
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).
Similarity
Belongs to the Arkadia family.
Mass
107.896 kDa
Sequence
MSQWTPEFNELYTLKVAMKSGTPDAPTTQESLKAVLLHPQPLGATKSFPAEVEMINSKVGNEFSHLCDDSQKQEKDMTGNQQEQEKSGVVRKKRKSQQAGPSYVQNCVKENQEILGRRQQLETPSDEDNDSSLSECLSSPSSSLHFGGSDTVTSDEDKEVSVRHTQPVLSAKSRSHSARSHKWPRTEADPVPSLLMKRPCFHGSALRRVTCRKRLVKSSSSQRTQKQKERMLVQRKKREALAQRKYALLSSSSSSSENDLSSDSSSSSSTDGEEDLCASASENPSNPAAPSGSIDEDVVVIEASFTPQVTANEEINVTSTDSEVEIVTVGESYRSRSTLGHSRSHWSQGSSSHTGRPQESRNRSRISTVIQPLRQNAAEVVDLTVDEDEPTIVPTTSARMDSQTTSASINNSNPSTSEQASDTTSTVASSQPSTVSETEATLTSNSATGSSVGDDVRRTASSAVPESGPPAMPRLPSCCPQHSPCGGTSQSHHALAHPHSSCFQQHGHHFQHHHHHHHTPHPAVPVSPSFSDPACPVERPQVQAPCGANSSSGSSYHDQQALPVDLSNSALRTHGSGGFHGASAFDPCCPVTSSRAAVFGHQAAAAPTQPLSIDGYGSSMVAQPQPQPPPQPSLSSCRHYMPPPYASLTRPLHHQASACHHSHGNAPPQTQPPPQVDYVIPHPVHAFHSQISSHAASHPVAPPPPTHLGSTAAPIPQHLPPAHQPISHHIPAPAPSAQRLHPHEVMQRMEVQRRRMMQHPTRAHERPPPHPHRMHPNYGHGHHIHVPQTMSSHPRQAPERTAWELGIEAGVTAATYTPGALHPHLAHYHAPPRLHHLQLGALPLMVPDMAGYPHIRYISSGLDGASFRGPFRGNFEELIHLEERLGNVNRGASQGTIERCTYPHKYKKVTTDWFSQRKLHCKQDGEEGTEEDTEEKCTICLSILEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVDIEAQLPSES

Gene
RNF111
Protein
E3 ubiquitin-protein ligase Arkadia
Organism
Pongo abelii
Length
986 amino acids
Function
E3 ubiquitin-protein ligase (By similarity). 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. 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 (By similarity). 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. Associates with UBE2D2 as an E2 enzyme. Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates. 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 (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).
Similarity
Belongs to the Arkadia family.
Mass
107.942 kDa
Sequence
MSQWTPEYNELYTLKVDMKSEIPSDAPKTQESLKGILLHPEPIGAAKSFPAGVEMINSKVGNEFSHLCDDSQKQEKDMNGNQQEQEKSLVVRKKRKSQQAGPSYVQNCVKENQGILGLRQHLGTPSDEDNDSSFSDCLSSPSSSLHFGDSDTVTSDEDKEVSVRHSQTILNAKSRSHSARSHKWPRTETESVSGLLMKRPCLHGSSLRRLPCRKRFVKNNSSQRTQKQKERILMQRKKREVLARRKYALLPSSSSSSENDLSSESSSSSSTEGEEDLFVSASENHQNNPAVPSGSIDEDVVVIEASSTPQVTANEEINVTSTDSEVEIVTVGESYRSRSTLGHSRSHWSQGSSSHASRPQEPRNRSRISTVIQPLRQNAAEVVDLTVDEDEPTVVPTTSARMESQATSASINNSNPSTSEQASDTASAVTGSQPSTVSETSATLTSNSTTGTSIGDDSRRTTSSAVMETGPPAMPRLPSCCPQHSPCGGSSQNHHALGHPHTSCFQQHGHHFQHHHHHHHTPHPAVPVSPSFSDPACPVERPPQVQAPCGANSSSGTSYHEQQALPVDLSNNGIRSHGSGSFHGASAFDPCCPVSSSRAAIFGHQAAAAAPSQPLSSIDGYGSSMVAQPQPQPPPQPSLSSCRHYMPPTYASLTRPLHHQASACPHSHGNPPPQTQPPPQVDYVIPHPVHAFHSQISSHATSHPVAPPPPTHLASTAAPIPQHLPPTHQPISHHIPATAPPAQRLHPHEVMQRMEVRRRRMMQHPTRAHERPPPHPHRMHPNYGHGHHIHVPQTMSSHPRQAPERSAWELGIEAGVTAATYTPGALHPHLAHYHAPPRLHHLQLGALPLMVPDMAGYPHIRYISSGLDGTSFRGPFRGNFEELIHLEERLGNVNRGASQGTIERCTYPHKYKKRKLHCKQDGEEGTEEDTEEKCTICLSILEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVDIEAQLPSES

Gene
rnf111
Protein
E3 ubiquitin-protein ligase arkadia
Organism
Xenopus tropicalis
Length
954 amino acids
Function
E3 ubiquitin-protein ligase 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. 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. Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates (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).
Similarity
Belongs to the Arkadia family.
Mass
104.889 kDa
Sequence
MKSEVSSDAPKRQENLKGVLLNPEAIGASKSFPKEVEMIASKVSNEFSHLCSDTNKQQRDLNSNGTEQEKNLVVHKKRKNQQAGTSYAQSCEVKENQRLLRLQPQSDEDNDSSFSDCISSPSSSSHFGDSDTMTSDEDKDNPRRYSPAGVNATPRTQSARAQKWPRPHTDSVSSLVMKRPCYQVSSLRRPLHRKRFVKNVSSQRTQKQKERMMLQRKKREVLARQKYALLPSSSSSSENDLSSESSSSSSTEGEEDLFVSPGENHQDGTTLPSGGMDEDVVVIEASSTPQVTANEEINVTSTDSEVEIVTVGETYRSRTTLGHPRSHWGQNTQSGRTQEQRTRNRVSTVIQPLRQNTTEVVDLTVDEDDPTVVPTTSGRVESQPVSTVSSNTSTSEPASDSASGPLGSRGSAIPEIPPIPPNSNTVGTIADDSRTSTSGTNVDGGPPAMPRLPSCCPQHSPCGGSSQNHVLGHPHSSCFPPHSHHFPHHHHHHHQSSHPGVPLSPSFRDSHCPVERNAAVPPPCGATSSSGSTYHDPQALPVDLSNNGIRSHGSVSFHSTSAFDPCCPGSSSRSTVYGHQSTTSTAQTMAIDGYGSSMVAQAQPPPPTPLSSCRHYMHAPYTSLTRPLHHQTSSCPHSHSNVGDYVIAHQVPFISPLPSLAATHAVPPPPPSHHLSTAAAPQHLSTSHQSMSHHISATAPATQRLHTHEVIQRMEVQRRRMMQHPTRAHERPPPHPHRMHPNYGHGHHIHVPQTMSSHPRQGPERSAWEIAIETGVTAAPYQTGPLHTHLAHYHAPPRLHHLQIGALPLMVPDMAGYPHIRYISSGLDGRSFRVPFRGNFEELIHLEERLGNVNRGASQGTIERCTYPHKYEKVSTDWFSQRKLHSKQDGEEATEEDTEEKCTICLSILEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVDIDTQLPTES