RN111_MOUSE
ID RN111_MOUSE Reviewed; 989 AA.
AC Q99ML9; Q3UVL7; Q6NSW2; Q7TMR3; Q8C881; Q8CBC0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=E3 ubiquitin-protein ligase Arkadia {ECO:0000305|PubMed:11298452};
DE EC=2.3.2.27 {ECO:0000269|PubMed:23530056};
DE AltName: Full=RING finger protein 111 {ECO:0000312|MGI:MGI:1934919};
DE AltName: Full=RING-type E3 ubiquitin transferase Arkadia {ECO:0000305};
GN Name=Rnf111 {ECO:0000312|MGI:MGI:1934919};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=129/Sv;
RX PubMed=11298452; DOI=10.1038/35071095;
RA Episkopou V., Arkell R., Timmons P.M., Walsh J.J., Andrew R.L., Swan D.;
RT "Induction of the mammalian node requires Arkadia function in the
RT extraembryonic lineages.";
RL Nature 410:825-830(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 805-989 (ISOFORM 1).
RC STRAIN=CD-1, and FVB/N-3; TISSUE=Mammary tumor, and Neural stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, MUTAGENESIS OF CYS-937, INTERACTION WITH SMAD6 AND SMAD7, AND
RP SUBCELLULAR LOCATION.
RX PubMed=14657019; DOI=10.1093/emboj/cdg632;
RA Koinuma D., Shinozaki M., Komuro A., Goto K., Saitoh M., Hanyu A.,
RA Ebina M., Nukiwa T., Miyazawa K., Imamura T., Miyazono K.;
RT "Arkadia amplifies TGF-beta superfamily signaling through degradation of
RT Smad7.";
RL EMBO J. 22:6458-6470(2003).
RN [5]
RP FUNCTION, AND INTERACTION WITH SMAD2 AND SMAD3.
RX PubMed=17341133; DOI=10.1371/journal.pbio.0050067;
RA Mavrakis K.J., Andrew R.L., Lee K.L., Petropoulou C., Dixon J.E.,
RA Navaratnam N., Norris D.P., Episkopou V.;
RT "Arkadia enhances Nodal/TGF-beta signaling by coupling phospho-Smad2/3
RT activity and turnover.";
RL PLoS Biol. 5:E67-E67(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF
RP 298-VAL--ILE-301; 324-VAL--VAL-327; 380-VAL--LEU-383 AND CYS-937.
RX PubMed=23530056; DOI=10.1128/mcb.01019-12;
RA Erker Y., Neyret-Kahn H., Seeler J.S., Dejean A., Atfi A., Levy L.;
RT "Arkadia, a novel SUMO-targeted ubiquitin ligase involved in PML
RT degradation.";
RL Mol. Cell. Biol. 33:2163-2177(2013).
CC -!- FUNCTION: E3 ubiquitin-protein ligase required for mesoderm patterning
CC during embryonic development (PubMed:11298452). Acts as an enhancer of
CC the transcriptional responses of the SMAD2/SMAD3 effectors, which are
CC activated downstream of BMP (PubMed:14657019). Acts by mediating
CC ubiquitination and degradation of SMAD inhibitors such as SMAD7,
CC inducing their proteasomal degradation and thereby enhancing the
CC transcriptional activity of TGF-beta and BMP (PubMed:14657019). In
CC addition to enhance transcription of SMAD2/SMAD3 effectors, also
CC regulates their turnover by mediating their ubiquitination and
CC subsequent degradation, coupling their activation with degradation,
CC thereby ensuring that only effectors 'in use' are degraded (By
CC similarity). Activates SMAD3/SMAD4-dependent transcription by
CC triggering signal-induced degradation of SNON isoform of SKIL (By
CC similarity). Associates with UBE2D2 as an E2 enzyme (By similarity).
CC Specifically binds polysumoylated chains via SUMO interaction motifs
CC (SIMs) and mediates ubiquitination of sumoylated substrates
CC (PubMed:23530056). Catalyzes 'Lys-63'-linked ubiquitination of
CC sumoylated XPC in response to UV irradiation, promoting nucleotide
CC excision repair (By similarity). Mediates ubiquitination and
CC degradation of sumoylated PML (PubMed:23530056). The regulation of the
CC BMP-SMAD signaling is however independent of sumoylation and is not
CC dependent of SUMO interaction motifs (SIMs) (PubMed:23530056).
CC {ECO:0000250|UniProtKB:Q6ZNA4, ECO:0000269|PubMed:11298452,
CC ECO:0000269|PubMed:14657019, ECO:0000269|PubMed:17341133,
CC ECO:0000269|PubMed:23530056}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:23530056};
CC -!- ACTIVITY REGULATION: Binds free ubiquitin non-covalently via its RING-
CC type zinc finger. Ubiquitin-binding leads to enhance the E3 ubiquitin-
CC protein ligase activity by stabilizing the ubiquitin-conjugating enzyme
CC E2 (donor ubiquitin) in the 'closed' conformation and activating
CC ubiquitin transfer. {ECO:0000250|UniProtKB:Q6ZSG1}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with SMAD6, SMAD7, AXIN1,
CC AXIN2 and SKIL isoform SNON (PubMed:14657019). Interacts with
CC (phosphorylated) SMAD2 and SMAD3 (PubMed:17341133). Part of a complex
CC containing RNF111, AXIN1 and SMAD7 (By similarity). Interacts (via SIM
CC domains) with SUMO1 and SUMO2 (PubMed:23530056).
CC {ECO:0000250|UniProtKB:Q6ZNA4, ECO:0000269|PubMed:14657019,
CC ECO:0000269|PubMed:17341133, ECO:0000269|PubMed:23530056}.
CC -!- INTERACTION:
CC Q99ML9; O35625: Axin1; NbExp=4; IntAct=EBI-646015, EBI-2365912;
CC Q99ML9; O15169: AXIN1; Xeno; NbExp=5; IntAct=EBI-646015, EBI-710484;
CC Q99ML9; O15105: SMAD7; Xeno; NbExp=2; IntAct=EBI-646015, EBI-3861591;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14657019}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q6ZNA4}. Nucleus, PML body
CC {ECO:0000269|PubMed:23530056}. Note=Upon TGF-beta treatment,
CC translocates from nucleus to cytosol. {ECO:0000250|UniProtKB:Q6ZNA4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99ML9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99ML9-2; Sequence=VSP_023842;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11298452}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed from ES cells to
CC midgestation. {ECO:0000269|PubMed:11298452}.
CC -!- DOMAIN: The SUMO interaction motifs (SIMs) mediates the binding to
CC polysumoylated substrate. {ECO:0000269|PubMed:23530056}.
CC -!- DOMAIN: The RING-type zinc finger mediates the E3 ubiquitin-protein
CC ligase activity and binds directly to free ubiquitin. Non-covalent
CC ubiquitin-binding stabilizes the ubiquitin-conjugating enzyme E2 (donor
CC ubiquitin) in the 'closed' conformation and stimulates ubiquitin
CC transfer. {ECO:0000250|UniProtKB:Q6ZSG1}.
CC -!- DISRUPTION PHENOTYPE: Mice rarely develop beyond 15 somites, have a
CC reduced head, fail to undergo turning and die at midgestation.
CC {ECO:0000269|PubMed:11298452}.
CC -!- SIMILARITY: Belongs to the Arkadia family. {ECO:0000305}.
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DR EMBL; AF330197; AAK38272.1; -; mRNA.
DR EMBL; AK048110; BAC33245.1; -; mRNA.
DR EMBL; AK036351; BAC29394.1; -; mRNA.
DR EMBL; AK137148; BAE23252.1; -; mRNA.
DR EMBL; BC054842; AAH54842.1; -; mRNA.
DR EMBL; BC069835; AAH69835.1; -; mRNA.
DR CCDS; CCDS23321.1; -. [Q99ML9-1]
DR CCDS; CCDS90614.1; -. [Q99ML9-2]
DR RefSeq; NP_291082.1; NM_033604.2. [Q99ML9-1]
DR RefSeq; XP_006511649.1; XM_006511586.2.
DR AlphaFoldDB; Q99ML9; -.
DR BMRB; Q99ML9; -.
DR SMR; Q99ML9; -.
DR BioGRID; 220311; 13.
DR IntAct; Q99ML9; 7.
DR MINT; Q99ML9; -.
DR STRING; 10090.ENSMUSP00000034739; -.
DR PhosphoSitePlus; Q99ML9; -.
DR EPD; Q99ML9; -.
DR PaxDb; Q99ML9; -.
DR PRIDE; Q99ML9; -.
DR ProteomicsDB; 299914; -. [Q99ML9-1]
DR ProteomicsDB; 299915; -. [Q99ML9-2]
DR Antibodypedia; 25360; 132 antibodies from 26 providers.
DR DNASU; 93836; -.
DR Ensembl; ENSMUST00000034739; ENSMUSP00000034739; ENSMUSG00000032217. [Q99ML9-1]
DR Ensembl; ENSMUST00000113595; ENSMUSP00000109225; ENSMUSG00000032217. [Q99ML9-1]
DR Ensembl; ENSMUST00000215848; ENSMUSP00000149445; ENSMUSG00000032217. [Q99ML9-2]
DR GeneID; 93836; -.
DR KEGG; mmu:93836; -.
DR UCSC; uc009qoa.1; mouse. [Q99ML9-2]
DR UCSC; uc009qoe.1; mouse. [Q99ML9-1]
DR CTD; 54778; -.
DR MGI; MGI:1934919; Rnf111.
DR VEuPathDB; HostDB:ENSMUSG00000032217; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000157691; -.
DR HOGENOM; CLU_309031_0_0_1; -.
DR InParanoid; Q99ML9; -.
DR OMA; EPGPPAM; -.
DR OrthoDB; 1098052at2759; -.
DR PhylomeDB; Q99ML9; -.
DR TreeFam; TF331862; -.
DR Reactome; R-MMU-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 93836; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Rnf111; mouse.
DR PRO; PR:Q99ML9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q99ML9; protein.
DR Bgee; ENSMUSG00000032217; Expressed in animal zygote and 251 other tissues.
DR ExpressionAtlas; Q99ML9; baseline and differential.
DR Genevisible; Q99ML9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0032184; F:SUMO polymer binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:BHF-UCL.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:Reactome.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0030579; P:ubiquitin-dependent SMAD protein catabolic process; IDA:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR029306; RNF111_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF15303; RNF111_N; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; DNA damage;
KW DNA repair; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..989
FT /note="E3 ubiquitin-protein ligase Arkadia"
FT /id="PRO_0000280691"
FT ZN_FING 937..978
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 63..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..402
FT /note="Interaction with AXIN1"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT REGION 335..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..904
FT /note="Ubiquitin binding"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT REGION 952..956
FT /note="Ubiquitin binding"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT MOTIF 298..302
FT /note="SUMO interaction motif 1 (SIM)"
FT /evidence="ECO:0000269|PubMed:23530056"
FT MOTIF 323..329
FT /note="SUMO interaction motif 2 (SIM)"
FT /evidence="ECO:0000269|PubMed:23530056"
FT MOTIF 380..384
FT /note="SUMO interaction motif 3 (SIM)"
FT /evidence="ECO:0000269|PubMed:23530056"
FT COMPBIAS 65..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..521
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 937
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT BINDING 940
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT BINDING 960
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT BINDING 963
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q6ZSG1"
FT CROSSLNK 19
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT CROSSLNK 72
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT CROSSLNK 95
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT CROSSLNK 172
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT CROSSLNK 217
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT CROSSLNK 918
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT CROSSLNK 922
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6ZNA4"
FT VAR_SEQ 909..916
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023842"
FT MUTAGEN 298..301
FT /note="VVVI->AVAA: Abolishes binding to sumoylated proteins
FT and ubiquitination and degradation of PML; when associated
FT with 326-A--A-329 and 382-A--A-385."
FT /evidence="ECO:0000269|PubMed:23530056"
FT MUTAGEN 324..327
FT /note="VEIV->AEAA: Abolishes binding to sumoylated proteins
FT and ubiquitination and degradation of PML; when associated
FT with 300-A--A-303 and 382-A--A-385."
FT /evidence="ECO:0000269|PubMed:23530056"
FT MUTAGEN 380..383
FT /note="VVDL->AADA: Abolishes binding to sumoylated proteins
FT and ubiquitination and degradation of PML; when associated
FT with 300-A--A-303 and 326-A--A-329."
FT /evidence="ECO:0000269|PubMed:23530056"
FT MUTAGEN 937
FT /note="C->A: No effect on TGF-beta and BMP signaling."
FT /evidence="ECO:0000269|PubMed:14657019,
FT ECO:0000269|PubMed:23530056"
FT CONFLICT 121
FT /note="L -> V (in Ref. 2; BAC29394)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="S -> G (in Ref. 2; BAC33245)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="S -> N (in Ref. 2; BAC33245)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="L -> V (in Ref. 3; AAH54842)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 989 AA; 107896 MW; 212E3C37BC70DCB5 CRC64;
MSQWTPEFNE LYTLKVAMKS GTPDAPTTQE SLKAVLLHPQ PLGATKSFPA EVEMINSKVG
NEFSHLCDDS QKQEKDMTGN QQEQEKSGVV RKKRKSQQAG PSYVQNCVKE NQEILGRRQQ
LETPSDEDND SSLSECLSSP SSSLHFGGSD TVTSDEDKEV SVRHTQPVLS AKSRSHSARS
HKWPRTEADP VPSLLMKRPC FHGSALRRVT CRKRLVKSSS SQRTQKQKER MLVQRKKREA
LAQRKYALLS SSSSSSENDL SSDSSSSSST DGEEDLCASA SENPSNPAAP SGSIDEDVVV
IEASFTPQVT ANEEINVTST DSEVEIVTVG ESYRSRSTLG HSRSHWSQGS SSHTGRPQES
RNRSRISTVI QPLRQNAAEV VDLTVDEDEP TIVPTTSARM DSQTTSASIN NSNPSTSEQA
SDTTSTVASS QPSTVSETEA TLTSNSATGS SVGDDVRRTA SSAVPESGPP AMPRLPSCCP
QHSPCGGTSQ SHHALAHPHS SCFQQHGHHF QHHHHHHHTP HPAVPVSPSF SDPACPVERP
QVQAPCGANS SSGSSYHDQQ ALPVDLSNSA LRTHGSGGFH GASAFDPCCP VTSSRAAVFG
HQAAAAPTQP LSIDGYGSSM VAQPQPQPPP QPSLSSCRHY MPPPYASLTR PLHHQASACH
HSHGNAPPQT QPPPQVDYVI PHPVHAFHSQ ISSHAASHPV APPPPTHLGS TAAPIPQHLP
PAHQPISHHI PAPAPSAQRL HPHEVMQRME VQRRRMMQHP TRAHERPPPH PHRMHPNYGH
GHHIHVPQTM SSHPRQAPER TAWELGIEAG VTAATYTPGA LHPHLAHYHA PPRLHHLQLG
ALPLMVPDMA GYPHIRYISS GLDGASFRGP FRGNFEELIH LEERLGNVNR GASQGTIERC
TYPHKYKKVT TDWFSQRKLH CKQDGEEGTE EDTEEKCTIC LSILEEGEDV RRLPCMHLFH
QVCVDQWLIT NKKCPICRVD IEAQLPSES
