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   27-MAR-2024, entry version 178.
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   GlyGen; Q99ML9; 1 site, 1 O-linked glycan (1 site).
DR   PhosphoSitePlus; Q99ML9; -.
DR   EPD; Q99ML9; -.
DR   PaxDb; 10090-ENSMUSP00000034739; -.
DR   ProteomicsDB; 299914; -. [Q99ML9-1]
DR   ProteomicsDB; 299915; -. [Q99ML9-2]
DR   Antibodypedia; 25360; 158 antibodies from 26 providers.
DR   DNASU; 93836; -.
DR   Ensembl; ENSMUST00000034739.12; ENSMUSP00000034739.6; ENSMUSG00000032217.14. [Q99ML9-1]
DR   Ensembl; ENSMUST00000113595.2; ENSMUSP00000109225.2; ENSMUSG00000032217.14. [Q99ML9-1]
DR   Ensembl; ENSMUST00000215848.2; ENSMUSP00000149445.2; ENSMUSG00000032217.14. [Q99ML9-2]
DR   GeneID; 93836; -.
DR   KEGG; mmu:93836; -.
DR   UCSC; uc009qoa.1; mouse. [Q99ML9-2]
DR   UCSC; uc009qoe.1; mouse. [Q99ML9-1]
DR   AGR; MGI:1934919; -.
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; FGHQATA; -.
DR   OrthoDB; 5474929at2759; -.
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 77 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 254 other cell types or tissues.
DR   ExpressionAtlas; Q99ML9; baseline and differential.
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:0045893; P:positive regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI.
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; IDA:MGI.
DR   CDD; cd16681; RING-H2_RNF111; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR029306; RNF111_N.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR16200:SF1; E3 UBIQUITIN-PROTEIN LIGASE PLR-1-RELATED; 1.
DR   PANTHER; PTHR16200; RING ZINC FINGER; 1.
DR   Pfam; PF15303; RNF111_N; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   Genevisible; Q99ML9; MM.
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
//