ZN609_HUMAN
ID ZN609_HUMAN Reviewed; 1411 AA.
AC O15014; Q0D2I2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Zinc finger protein 609 {ECO:0000312|HGNC:HGNC:29003};
GN Name=ZNF609 {ECO:0000312|HGNC:HGNC:29003};
GN Synonyms=KIAA0295 {ECO:0000303|PubMed:9205841};
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 431-1411.
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] OF 1341-1411.
RC TISSUE=Skin;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-849, AND IDENTIFICATION BY
RP 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-576; SER-578;
RP SER-846; SER-849 AND SER-1055, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-842 AND SER-849, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576; SER-578 AND SER-804, AND
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576; SER-578; THR-746 AND
RP SER-1055, AND 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-379; THR-381;
RP SER-413; SER-433; SER-446; SER-452; SER-467; SER-470; SER-576; SER-578;
RP SER-743; THR-746; SER-758; SER-804; THR-823; SER-842; SER-849 AND SER-1055,
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-1055, AND
RP IDENTIFICATION BY 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 [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-789, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [14]
RP INDUCTION.
RX PubMed=25921068; DOI=10.1016/j.molcel.2015.03.027;
RA Rybak-Wolf A., Stottmeister C., Glazar P., Jens M., Pino N., Giusti S.,
RA Hanan M., Behm M., Bartok O., Ashwal-Fluss R., Herzog M., Schreyer L.,
RA Papavasileiou P., Ivanov A., Oehman M., Refojo D., Kadener S., Rajewsky N.;
RT "Circular RNAs in the mammalian brain are highly abundant, conserved, and
RT dynamically expressed.";
RL Mol. Cell 58:870-885(2015).
RN [15]
RP FUNCTION (ISOFORM 2), TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION
RP (ISOFORM 2), AND IDENTIFICATION (ISOFORM 2).
RX PubMed=28344082; DOI=10.1016/j.molcel.2017.02.017;
RA Legnini I., Di Timoteo G., Rossi F., Morlando M., Briganti F.,
RA Sthandier O., Fatica A., Santini T., Andronache A., Wade M., Laneve P.,
RA Rajewsky N., Bozzoni I.;
RT "Circ-ZNF609 is a circular RNA that can be translated and functions in
RT myogenesis.";
RL Mol. Cell 0:0-0(2017).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-479; LYS-789; LYS-1061; LYS-1153
RP AND LYS-1297, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Transcription factor, which activates RAG1, and possibly
CC RAG2, transcription. Through the regulation of RAG1/2 expression, may
CC regulate thymocyte maturation. Along with NIPBL and the multiprotein
CC complex Integrator, promotes cortical neuron migration during brain
CC development by regulating the transcription of crucial genes in this
CC process. Preferentially binds promoters containing paused RNA
CC polymerase II. Up-regulates the expression of SEMA3A, NRP1, PLXND1 and
CC GABBR2 genes, among others. {ECO:0000250|UniProtKB:Q8BZ47}.
CC -!- FUNCTION: [Isoform 2]: Involved in the regulation of myoblast
CC proliferation during myogenesis. {ECO:0000269|PubMed:28344082}.
CC -!- SUBUNIT: Interacts (via N-terminus) with NIPBL. Interacts with the
CC multiprotein complex Integrator. {ECO:0000250|UniProtKB:Q8BZ47}.
CC -!- INTERACTION:
CC O15014; Q93009: USP7; NbExp=2; IntAct=EBI-948874, EBI-302474;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:28344082}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15014-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15014-2; Sequence=VSP_059082, VSP_059083;
CC -!- TISSUE SPECIFICITY: Isoform 1: Expressed in myoblasts and myotubes.
CC Isoform 2: Expressed in myoblasts and myotubes, with a preference in
CC undifferentiated myoblasts. {ECO:0000269|PubMed:28344082}.
CC -!- INDUCTION: Isoform 1: Up-regulated during neuronal differentiation in
CC retinoic acid-treated SH-SY5Y cells (PubMed:25921068). Isoform 2: Down-
CC regulated during myogenesis (PubMed:28344082).
CC {ECO:0000269|PubMed:25921068, ECO:0000269|PubMed:28344082}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by a back-splicing reaction which
CC joins the 5'-splice site of the first coding exon with the 3'-splice
CC site of the upstream intron resulting in a circular RNA, called circ-
CC ZNF609. The translation starts with the same initiator methionine as
CC that of the linear transcript encoding isoform 1. The stop codon is
CC created upon circularization. {ECO:0000269|PubMed:28344082}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Round in circles - Issue 199
CC of January 2018;
CC URL="https://web.expasy.org/spotlight/back_issues/199/";
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; AC090543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB002293; BAA20755.1; -; mRNA.
DR EMBL; BC110401; AAI10402.1; -; mRNA.
DR CCDS; CCDS32270.1; -. [O15014-1]
DR RefSeq; NP_055857.1; NM_015042.1. [O15014-1]
DR RefSeq; XP_011519688.1; XM_011521386.2.
DR RefSeq; XP_016877510.1; XM_017022021.1. [O15014-1]
DR AlphaFoldDB; O15014; -.
DR BioGRID; 116695; 121.
DR DIP; DIP-50012N; -.
DR IntAct; O15014; 75.
DR MINT; O15014; -.
DR STRING; 9606.ENSP00000316527; -.
DR GlyGen; O15014; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O15014; -.
DR PhosphoSitePlus; O15014; -.
DR BioMuta; ZNF609; -.
DR EPD; O15014; -.
DR jPOST; O15014; -.
DR MassIVE; O15014; -.
DR MaxQB; O15014; -.
DR PaxDb; O15014; -.
DR PeptideAtlas; O15014; -.
DR PRIDE; O15014; -.
DR ProteomicsDB; 48369; -.
DR Antibodypedia; 25830; 36 antibodies from 13 providers.
DR DNASU; 23060; -.
DR Ensembl; ENST00000326648.5; ENSP00000316527.3; ENSG00000180357.10. [O15014-1]
DR GeneID; 23060; -.
DR KEGG; hsa:23060; -.
DR MANE-Select; ENST00000326648.5; ENSP00000316527.3; NM_015042.2; NP_055857.1.
DR UCSC; uc002ann.4; human. [O15014-1]
DR CTD; 23060; -.
DR DisGeNET; 23060; -.
DR GeneCards; ZNF609; -.
DR HGNC; HGNC:29003; ZNF609.
DR HPA; ENSG00000180357; Low tissue specificity.
DR MIM; 617474; gene.
DR neXtProt; NX_O15014; -.
DR OpenTargets; ENSG00000180357; -.
DR PharmGKB; PA134952302; -.
DR VEuPathDB; HostDB:ENSG00000180357; -.
DR eggNOG; ENOG502RCUP; Eukaryota.
DR GeneTree; ENSGT00390000008748; -.
DR HOGENOM; CLU_004142_0_0_1; -.
DR InParanoid; O15014; -.
DR OMA; VDRNCPS; -.
DR OrthoDB; 60503at2759; -.
DR PhylomeDB; O15014; -.
DR TreeFam; TF329775; -.
DR PathwayCommons; O15014; -.
DR SignaLink; O15014; -.
DR BioGRID-ORCS; 23060; 16 hits in 1077 CRISPR screens.
DR ChiTaRS; ZNF609; human.
DR GenomeRNAi; 23060; -.
DR Pharos; O15014; Tdark.
DR PRO; PR:O15014; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O15014; protein.
DR Bgee; ENSG00000180357; Expressed in ventricular zone and 152 other tissues.
DR ExpressionAtlas; O15014; baseline and differential.
DR Genevisible; O15014; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:ARUK-UCL.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:2001224; P:positive regulation of neuron migration; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:2000291; P:regulation of myoblast proliferation; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR InterPro; IPR040010; ZN608/ZN609.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR21564; PTHR21564; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Developmental protein; Isopeptide bond;
KW Metal-binding; Myogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1411
FT /note="Zinc finger protein 609"
FT /id="PRO_0000280422"
FT ZN_FING 495..520
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1153..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1040
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZ47"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 381
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BZ47"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 743
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 746
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 804
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 823
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 842
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 849
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1055
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 479
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 789
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1061
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1153
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 250
FT /note="M -> Q (in isoform 2)"
FT /id="VSP_059082"
FT VAR_SEQ 251..1411
FT /note="Missing (in isoform 2)"
FT /id="VSP_059083"
FT CONFLICT 766
FT /note="D -> N (in Ref. 2; BAA20755)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1411 AA; 151191 MW; 63A32348BB5C678E CRC64;
MSLSSGASGG KGVDANPVET YDSGDEWDIG VGNLIIDLDA DLEKDQQKLE MSGSKEVGIP
APNAVATLPD NIKFVTPVPG PQGKEGKSKS KRSKSGKDTS KPTPGTSLFT PSEGAASKKE
VQGRSGDGAN AGGLVAAIAP KGSEKAAKAS RSVAGSKKEK ENSSSKSKKE RSEGVGTCSE
KDPGVLQPVP LGGRGGQYDG SAGVDTGAVE PLGSIAIEPG AALNPLGTKP EPEEGENECR
LLKKVKSEKM ESPVSTPAVL PIHLLVPVVN NDISSPCEQI MVRTRSVGVN TCDVALATEP
ECLGPCEPGT SVNLEGIVWQ ETEDGMLVVN VTWRNKTYVG TLLDCTRHDW APPRFCDSPT
SDLEMRNGRG RGKRMRPNSN TPVNETATAS DSKGTSNSSK TRAGANSKGR RGSQNSSEHR
PPASSTSEDV KASPSSANKR KNKPLSDMEL NSSSEDSKGS KRVRTNSMGS ATGPLPGTKV
EPTVLDRNCP SPVLIDCPHP NCNKKYKHIN GLKYHQAHAH TDDDSKPEAD GDSEYGEEPI
LHADLGSCNG ASVSQKGSLS PARSATPKVR LVEPHSPSPS SKFSTKGLCK KKLSGEGDTD
LGALSNDGSD DGPSVMDETS NDAFDSLERK CMEKEKCKKP SSLKPEKIPS KSLKSARPIA
PAIPPQQIYT FQTATFTAAS PGSSSGLTAT VAQAMPNSPQ LKPIQPKPTV MGEPFTVNPA
LTPAKDKKKK DKKKKESSKE LESPLTPGKV CRAEEGKSPF RESSGDGMKM EGLLNGSSDP
HQSRLASIKA EADKIYSFTD NAPSPSIGGS SRLENTTPTQ PLTPLHVVTQ NGAEASSVKT
NSPAYSDISD AGEDGEGKVD SVKSKDAEQL VKEGAKKTLF PPQPQSKDSP YYQGFESYYS
PSYAQSSPGA LNPSSQAGVE SQALKTKRDE EPESIEGKVK NDICEEKKPE LSSSSQQPSV
IQQRPNMYMQ SLYYNQYAYV PPYGYSDQSY HTHLLSTNTA YRQQYEEQQK RQSLEQQQRG
VDKKAEMGLK EREAALKEEW KQKPSIPPTL TKAPSLTDLV KSGPGKAKEP GADPAKSVII
PKLDDSSKLP GQAPEGLKVK LSDASHLSKE ASEAKTGAEC GRQAEMDPIL WYRQEAEPRM
WTYVYPAKYS DIKSEDERWK EERDRKLKEE RSRSKDSVPK EDGKESTSSD CKLPTSEESR
LGSKEPRPSV HVPVSSPLTQ HQSYIPYMHG YSYSQSYDPN HPSYRSMPAV MMQNYPGSYL
PSSYSFSPYG SKVSGGEDAD KARASPSVTC KSSSESKALD ILQQHASHYK SKSPTISDKT
SQERDRGGCG VVGGGGSCSS VGGASGGERS VDRPRTSPSQ RLMSTHHHHH HLGYSLLPAQ
YNLPYAAGLS STAIVASQQG STPSLYPPPR R
