ZMYM3_HUMAN
ID ZMYM3_HUMAN Reviewed; 1370 AA.
AC Q14202; D3DVV3; O15089; Q96E26;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Zinc finger MYM-type protein 3;
DE AltName: Full=Zinc finger protein 261;
GN Name=ZMYM3; Synonyms=DXS6673E, KIAA0385, ZNF261;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RX PubMed=8817323; DOI=10.1093/hmg/5.7.887;
RA van der Maarel S.M., Scholten I.H.G.M., Huber I., Phillippe C.,
RA Suijkerbuijk R.F., Gilgenkrantz S., Kere J., Cremers F.P.M., Ropers H.-H.;
RT "Cloning and characterization of DXS6673E, a candidate gene for X-linked
RT mental retardation in Xq13.1.";
RL Hum. Mol. Genet. 5:887-897(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Lymph, and Muscle;
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 [7]
RP IDENTIFICATION IN THE BHC COMPLEX WITH GSE1; GTF2I; HDAC1; HDAC2; HMG20B;
RP KDM1A; RCOR1; PHF21A; ZNF217 AND ZMYM2.
RX PubMed=12493763; DOI=10.1074/jbc.m208992200;
RA Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
RT "A candidate X-linked mental retardation gene is a component of a new
RT family of histone deacetylase-containing complexes.";
RL J. Biol. Chem. 278:7234-7239(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-267 AND SER-464, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP FUNCTION.
RX PubMed=21834987; DOI=10.1186/1741-7007-9-54;
RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V.,
RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.;
RT "Identification and characterization of a set of conserved and new
RT regulators of cytoskeletal organisation, cell morphology and migration.";
RL BMC Biol. 9:54-54(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; THR-795; THR-817 AND
RP THR-826, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-817, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-308; LYS-320; LYS-328; LYS-778;
RP LYS-786; LYS-804; LYS-847; LYS-861; LYS-920 AND LYS-1275, SUMOYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-786 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. {ECO:0000269|PubMed:21834987}.
CC -!- SUBUNIT: May be a component of a BHC histone deacetylase complex that
CC contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST,
CC PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I.
CC {ECO:0000269|PubMed:12493763}.
CC -!- INTERACTION:
CC Q14202; Q92993: KAT5; NbExp=3; IntAct=EBI-2556139, EBI-399080;
CC Q14202; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-2556139, EBI-11742507;
CC Q14202; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-2556139, EBI-9090795;
CC Q14202; P61981: YWHAG; NbExp=3; IntAct=EBI-2556139, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q14202-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14202-2; Sequence=VSP_004492;
CC Name=3;
CC IsoId=Q14202-3; Sequence=VSP_043262, VSP_043263;
CC -!- TISSUE SPECIFICITY: Most abundant in brain, moderate in muscle and
CC heart, low in other tissues except placenta.
CC -!- DISEASE: Note=A chromosomal aberration involving ZMYM3 may be a cause
CC of X-linked intellectual disability in Xq13.1. Translocation
CC t(X;13)(q13.1;?). {ECO:0000269|PubMed:8817323}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20839.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X95808; CAA65075.1; -; mRNA.
DR EMBL; AB002383; BAA20839.2; ALT_INIT; mRNA.
DR EMBL; BT007095; AAP35759.1; -; mRNA.
DR EMBL; AL590762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471132; EAX05302.1; -; Genomic_DNA.
DR EMBL; CH471132; EAX05303.1; -; Genomic_DNA.
DR EMBL; BC069057; AAH69057.1; -; mRNA.
DR EMBL; BC013009; AAH13009.1; -; mRNA.
DR CCDS; CCDS14409.1; -. [Q14202-1]
DR CCDS; CCDS55443.1; -. [Q14202-3]
DR CCDS; CCDS55444.1; -. [Q14202-2]
DR RefSeq; NP_001164633.1; NM_001171162.1. [Q14202-2]
DR RefSeq; NP_001164634.1; NM_001171163.1. [Q14202-3]
DR RefSeq; NP_005087.1; NM_005096.3. [Q14202-1]
DR RefSeq; NP_963893.1; NM_201599.2. [Q14202-1]
DR RefSeq; XP_005262366.1; XM_005262309.3. [Q14202-1]
DR RefSeq; XP_005262367.1; XM_005262310.2. [Q14202-2]
DR RefSeq; XP_011529364.1; XM_011531062.2. [Q14202-1]
DR AlphaFoldDB; Q14202; -.
DR SMR; Q14202; -.
DR BioGRID; 114637; 107.
DR CORUM; Q14202; -.
DR IntAct; Q14202; 50.
DR MINT; Q14202; -.
DR STRING; 9606.ENSP00000322845; -.
DR iPTMnet; Q14202; -.
DR PhosphoSitePlus; Q14202; -.
DR BioMuta; ZMYM3; -.
DR DMDM; 12644413; -.
DR EPD; Q14202; -.
DR jPOST; Q14202; -.
DR MassIVE; Q14202; -.
DR MaxQB; Q14202; -.
DR PaxDb; Q14202; -.
DR PeptideAtlas; Q14202; -.
DR PRIDE; Q14202; -.
DR ProteomicsDB; 59922; -. [Q14202-1]
DR ProteomicsDB; 59923; -. [Q14202-2]
DR ProteomicsDB; 59924; -. [Q14202-3]
DR Antibodypedia; 524; 180 antibodies from 24 providers.
DR DNASU; 9203; -.
DR Ensembl; ENST00000314425.9; ENSP00000322845.5; ENSG00000147130.14. [Q14202-1]
DR Ensembl; ENST00000373981.5; ENSP00000363093.1; ENSG00000147130.14. [Q14202-3]
DR Ensembl; ENST00000373998.5; ENSP00000363110.1; ENSG00000147130.14. [Q14202-2]
DR GeneID; 9203; -.
DR KEGG; hsa:9203; -.
DR MANE-Select; ENST00000314425.9; ENSP00000322845.5; NM_201599.3; NP_963893.1.
DR UCSC; uc004dzh.3; human. [Q14202-1]
DR CTD; 9203; -.
DR DisGeNET; 9203; -.
DR GeneCards; ZMYM3; -.
DR HGNC; HGNC:13054; ZMYM3.
DR HPA; ENSG00000147130; Low tissue specificity.
DR MIM; 300061; gene.
DR neXtProt; NX_Q14202; -.
DR OpenTargets; ENSG00000147130; -.
DR PharmGKB; PA37632; -.
DR VEuPathDB; HostDB:ENSG00000147130; -.
DR eggNOG; ENOG502QQQ9; Eukaryota.
DR GeneTree; ENSGT00940000160693; -.
DR HOGENOM; CLU_004099_1_0_1; -.
DR InParanoid; Q14202; -.
DR OMA; QKRFCNA; -.
DR OrthoDB; 587724at2759; -.
DR PhylomeDB; Q14202; -.
DR TreeFam; TF336988; -.
DR PathwayCommons; Q14202; -.
DR SignaLink; Q14202; -.
DR BioGRID-ORCS; 9203; 26 hits in 715 CRISPR screens.
DR ChiTaRS; ZMYM3; human.
DR GeneWiki; ZMYM3; -.
DR GenomeRNAi; 9203; -.
DR Pharos; Q14202; Tbio.
DR PRO; PR:Q14202; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q14202; protein.
DR Bgee; ENSG00000147130; Expressed in right adrenal gland and 205 other tissues.
DR ExpressionAtlas; Q14202; baseline and differential.
DR Genevisible; Q14202; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
DR InterPro; IPR021893; DUF3504.
DR InterPro; IPR011017; TRASH_dom.
DR InterPro; IPR010507; Znf_MYM.
DR Pfam; PF12012; DUF3504; 1.
DR Pfam; PF06467; zf-FCS; 8.
DR SMART; SM00746; TRASH; 10.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosomal rearrangement; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1370
FT /note="Zinc finger MYM-type protein 3"
FT /id="PRO_0000191378"
FT ZN_FING 332..366
FT /note="MYM-type 1"
FT ZN_FING 378..422
FT /note="MYM-type 2"
FT ZN_FING 429..464
FT /note="MYM-type 3"
FT ZN_FING 477..511
FT /note="MYM-type 4"
FT ZN_FING 521..559
FT /note="MYM-type 5"
FT ZN_FING 567..604
FT /note="MYM-type 6"
FT ZN_FING 612..646
FT /note="MYM-type 7"
FT ZN_FING 653..692
FT /note="MYM-type 8"
FT ZN_FING 699..733
FT /note="MYM-type 9"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..275
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..828
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 795
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 817
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 826
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 308
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 320
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 328
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 778
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 786
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 804
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 847
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 861
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 920
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 491..495
FT /note="KNTRV -> VGPRE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_043262"
FT VAR_SEQ 496..1370
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_043263"
FT VAR_SEQ 793..804
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8817323"
FT /id="VSP_004492"
FT CROSSLNK Q14202-2:786
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 1370 AA; 152379 MW; 088B5E01E7EE9C30 CRC64;
MDPSDFPSPF DPLTLPEKPL AGDLPVDMEF GEDLLESQTA PTRGWAPPGP SPSSGALDLL
DTPAGLEKDP GVLDGATELL GLGGLLYKAP SPPEVDHGPE GTLAWDAGDQ TLEPGPGGQT
PEVVPPDPGA GANSCSPEGL LEPLAPDSPI TLQSPHIEEE ETTSIATARR GSPGQEEELP
QGQPQSPNAP PSPSVGETLG DGINSSQTKP GGSSPPAHPS LPGDGLTAKA SEKPPERKRS
ERVRRAEPPK PEVVDSTESI PVSDEDSDAM VDDPNDEDFV PFRPRRSPRM SLRSSVSQRA
GRSAVGTKMT CAHCRTPLQK GQTAYQRKGL PQLFCSSSCL TTFSKKPSGK KTCTFCKKEI
WNTKDSVVAQ TGSGGSFHEF CTSVCLSLYE AQQQRPIPQS GDPADATRCS ICQKTGEVLH
EVSNGSVVHR LCSDSCFSKF RANKGLKTNC CDQCGAYIYT KTGSPGPELL FHEGQQKRFC
NTTCLGAYKK KNTRVYPCVW CKTLCKNFEM LSHVDRNGKT SLFCSLCCTT SYKVKQAGLT
GPPRPCSFCR RSLSDPCYYN KVDRTVYQFC SPSCWTKFQR TSPEGGIHLS CHYCHSLFSG
KPEVLDWQDQ VFQFCCRDCC EDFKRLRGVV SQCEHCRQEK LLHEKLRFSG VEKSFCSEGC
VLLYKQDFTK KLGLCCITCT YCSQTCQRGV TEQLDGSTWD FCSEDCKSKY LLWYCKAARC
HACKRQGKLL ETIHWRGQIR HFCNQQCLLR FYSQQNQPNL DTQSGPESLL NSQSPESKPQ
TPSQTKVENS NTVRTPEENG NLGKIPVKTR SAPTAPTPPP PPPPATPRKN KAAMCKPLMQ
NRGVSCKVEM KSKGSQTEEW KPQVIVLPIP VPIFVPVPMH LYCQKVPVPF SMPIPVPVPM
FLPTTLESTD KIVETIEELK VKIPSNPLEA DILAMAEMIA EAEELDKASS DLCDLVSNQS
AEGLLEDCDL FGPARDDVLA MAVKMANVLD EPGQDLEADF PKNPLDINPS VDFLFDCGLV
GPEDVSTEQD LPRTMRKGQK RLVLSESCSR DSMSSQPSCT GLNYSYGVNA WKCWVQSKYA
NGETSKGDEL RFGPKPMRIK EDILACSAAE LNYGLAQFVR EITRPNGERY EPDSIYYLCL
GIQQYLLENN RMVNIFTDLY YLTFVQELNK SLSTWQPTLL PNNTVFSRVE EEHLWECKQL
GVYSPFVLLN TLMFFNTKFF GLQTAEEHMQ LSFTNVVRQS RKCTTPRGTT KVVSIRYYAP
VRQRKGRDTG PGKRKREDEA PILEQRENRM NPLRCPVKFY EFYLSKCPES LRTRNDVFYL
QPERSCIAES PLWYSVIPMD RSMLESMLNR ILAVREIYEE LGRPGEEDLD
