ID   NEST_HUMAN              Reviewed;        1621 AA.
AC   P48681; O00552; Q3LIF5; Q5SYZ6;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   02-SEP-2026, entry version 194.
DE   RecName: Full=Nestin;
GN   Name=NES; ORFNames=Nbla00170;
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 [GENOMIC DNA], AND VARIANTS ASN-1016; LEU-1101 AND
RP   LEU-1275.
RC   TISSUE=Placenta;
RX   PubMed=1478958; DOI=10.1242/jcs.103.2.589;
RA   Dahlstrand J., McKay R.D.G., Zimmerman L.B., Lendahl U.;
RT   "Characterization of the human nestin gene reveals a close evolutionary
RT   relationship to neurofilaments.";
RL   J. Cell Sci. 103:589-597(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 297-310.
RX   PubMed=9917366; DOI=10.1006/dbio.1998.9035;
RA   Yaworsky P.J., Kappen C.;
RT   "Heterogeneity of neural progenitor cells revealed by enhancers in the
RT   nestin gene.";
RL   Dev. Biol. 205:309-321(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 604-1621, AND VARIANT ILE-815.
RC   TISSUE=Neuroblastoma;
RX   PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5;
RA   Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA   Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA   Hirato J., Nakagawara A.;
RT   "Neuroblastoma oligo-capping cDNA project: toward the understanding of the
RT   genesis and biology of neuroblastoma.";
RL   Cancer Lett. 197:63-68(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680; SER-1409 AND SER-1418,
RP   AND 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311; THR-315; SER-325;
RP   THR-388; SER-398; SER-471; SER-548; SER-564; SER-578; SER-588; SER-746;
RP   SER-768; THR-851; SER-905 AND SER-1418, VARIANT [LARGE SCALE ANALYSIS]
RP   LEU-1275, AND 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1418, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18318008; DOI=10.1002/pmic.200700884;
RA   Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA   Zou H., Gu J.;
RT   "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT   and fractionation of phosphopeptides with strong anion exchange
RT   chromatography.";
RL   Proteomics 8:1346-1361(2008).
RN   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-398; SER-548 AND
RP   SER-680, AND 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   [10]
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; SER-355; SER-358;
RP   SER-548; SER-578; SER-680; SER-746; SER-768; SER-790; SER-820; SER-831;
RP   SER-894; SER-905; SER-913; SER-934; SER-1261; SER-1282; SER-1286; SER-1347;
RP   SER-1418; SER-1452; SER-1496; SER-1498; SER-1577; SER-1617 AND SER-1618,
RP   VARIANT [LARGE SCALE ANALYSIS] LEU-1275, AND IDENTIFICATION BY MASS
RP   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   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; THR-338; SER-471;
RP   SER-548; SER-578; SER-680; SER-768; SER-905; SER-1409 AND SER-1418, AND
RP   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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471; SER-476; SER-768;
RP   SER-1016 AND SER-1577, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [15]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-811, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [16]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-811, 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: Required for brain and eye development. Promotes the
CC       disassembly of phosphorylated vimentin intermediate filaments (IF)
CC       during mitosis and may play a role in the trafficking and distribution
CC       of IF proteins and other cellular factors to daughter cells during
CC       progenitor cell division. Required for survival, renewal and mitogen-
CC       stimulated proliferation of neural progenitor cells (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Forms homodimers and homotetramers in vitro. In mixtures with
CC       other intermediate filament proteins such as vimentin and alpha-
CC       internexin, tis protein preferentially forms heterodimers which can
CC       assemble to form intermediate filaments if nestin does not exceed 25%.
CC       Interacts with FHOD3 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P48681; P08670: VIM; NbExp=5; IntAct=EBI-10966836, EBI-353844;
CC   -!- TISSUE SPECIFICITY: CNS stem cells.
CC   -!- DEVELOPMENTAL STAGE: Upon terminal neural differentiation, nestin is
CC       down-regulated and replaced by neurofilaments.
CC   -!- PTM: Constitutively phosphorylated. This increases during mitosis when
CC       the cytoplasmic intermediate filament network is reorganized (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; AL590666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X65964; CAA46780.1; -; Genomic_DNA.
DR   EMBL; AF004335; AAB64426.1; -; Genomic_DNA.
DR   EMBL; AB073350; BAE45713.1; -; mRNA.
DR   CCDS; CCDS1151.1; -.
DR   PIR; S21424; S21424.
DR   RefSeq; NP_006608.1; NM_006617.2.
DR   AlphaFoldDB; P48681; -.
DR   SMR; P48681; -.
DR   BioGRID; 115983; 344.
DR   FunCoup; P48681; 367.
DR   IntAct; P48681; 117.
DR   MINT; P48681; -.
DR   NDEx; IQUERY-CP-NES; 1 NDEx IQuery Curated Pathway.
DR   STRING; 9606.ENSP00000357206; -.
DR   BindingDB; P48681; -.
DR   ChEMBL; CHEMBL6066462; -.
DR   GlyGen; P48681; 3 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P48681; -.
DR   MetOSite; P48681; -.
DR   PhosphoSitePlus; P48681; -.
DR   SwissPalm; P48681; -.
DR   BioMuta; NES; -.
DR   DMDM; 146345464; -.
DR   jPOST; P48681; -.
DR   MassIVE; P48681; -.
DR   PaxDb; 9606-ENSP00000357206; -.
DR   PeptideAtlas; P48681; -.
DR   ProteomicsDB; 55923; -.
DR   Pumba; P48681; -.
DR   Antibodypedia; 1658; 1121 antibodies from 51 providers.
DR   DNASU; 10763; -.
DR   Ensembl; ENST00000368223.4; ENSP00000357206.3; ENSG00000132688.12.
DR   GeneID; 10763; -.
DR   KEGG; hsa:10763; -.
DR   MANE-Select; ENST00000368223.4; ENSP00000357206.3; NM_006617.2; NP_006608.1.
DR   UCSC; uc001fpq.4; human.
DR   AGR; HGNC:7756; -.
DR   ClinPGx; PA31556; -.
DR   CTD; 10763; -.
DR   DisGeNET; 10763; -.
DR   GeneCards; NES; -.
DR   HGNC; HGNC:7756; NES.
DR   HPA; ENSG00000132688; Tissue enhanced (heart).
DR   MIM; 600915; gene.
DR   OpenTargets; ENSG00000132688; -.
DR   VEuPathDB; HostDB:ENSG00000132688; -.
DR   eggNOG; ENOG502RYFK; Eukaryota.
DR   GeneTree; ENSGT00940000162240; -.
DR   HOGENOM; CLU_003317_0_0_1; -.
DR   InParanoid; P48681; -.
DR   OMA; CQEVENQ; -.
DR   OrthoDB; 8886319at2759; -.
DR   PAN-GO; P48681; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; P48681; -.
DR   PathwayCommons; P48681; -.
DR   SignaLink; P48681; -.
DR   SIGNOR; P48681; -.
DR   Agora; ENSG00000132688; -.
DR   BioGRID-ORCS; 10763; 17 hits in 1156 CRISPR screens.
DR   ChiTaRS; NES; human.
DR   GeneWiki; Nestin_(protein); -.
DR   GenomeRNAi; 10763; -.
DR   Pharos; P48681; Tbio.
DR   PRO; PR:P48681; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P48681; protein.
DR   Bgee; ENSG00000132688; Expressed in ventricular zone and 177 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:DFLAT.
DR   GO; GO:0005882; C:intermediate filament; IBA:GO_Central.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR   GO; GO:0031730; F:CCR5 chemokine receptor binding; IBA:GO_Central.
DR   GO; GO:0019215; F:intermediate filament binding; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR   GO; GO:0007417; P:central nervous system development; NAS:UniProtKB.
DR   GO; GO:0031076; P:embryonic camera-type eye development; ISS:UniProtKB.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:DFLAT.
DR   GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
DR   GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
DR   GO; GO:0030844; P:positive regulation of intermediate filament depolymerization; ISS:UniProtKB.
DR   GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISS:UniProtKB.
DR   GO; GO:0072089; P:stem cell proliferation; IMP:DFLAT.
DR   FunFam; 1.20.5.170:FF:000081; Nestin; 1.
DR   FunFam; 1.20.5.1160:FF:000018; nestin; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR031211; Nestin.
DR   PANTHER; PTHR47051; NESTIN; 1.
DR   PANTHER; PTHR47051:SF1; NESTIN; 1.
DR   Pfam; PF00038; Filament; 2.
DR   SMART; SM01391; Filament; 1.
DR   SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR   PROSITE; PS00226; IF_ROD_1; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Developmental protein; Intermediate filament;
KW   Isopeptide bond; Neurogenesis; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..1621
FT                   /note="Nestin"
FT                   /id="PRO_0000063853"
FT   DOMAIN          8..313
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..7
FT                   /note="Head"
FT   REGION          8..43
FT                   /note="Coil 1A"
FT   REGION          44..55
FT                   /note="Linker 1"
FT   REGION          56..151
FT                   /note="Coil 1B"
FT   REGION          152..173
FT                   /note="Linker 12"
FT   REGION          174..192
FT                   /note="Coil 2A"
FT   REGION          193..195
FT                   /note="Linker 2"
FT   REGION          196..313
FT                   /note="Coil 2B"
FT   REGION          314..1621
FT                   /note="Tail"
FT   REGION          439..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          670..788
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..1593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..725
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..770
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        779..788
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..936
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        949..960
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        980..994
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1012..1024
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1085..1098
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1099..1110
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1129..1145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1159..1184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1275..1292
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1409..1428
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1440..1453
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1460..1470
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1486..1495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         311
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         315
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         325
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         338
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         358
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         388
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         398
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         471
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         476
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         548
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         564
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         578
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         588
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         638
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P5H2"
FT   MOD_RES         680
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         702
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P5H2"
FT   MOD_RES         746
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         768
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         790
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         820
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         831
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         842
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21263"
FT   MOD_RES         851
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         894
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         905
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         913
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         934
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1016
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         1261
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1282
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1286
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1310
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P5H2"
FT   MOD_RES         1347
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1418
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1452
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1496
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1498
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1577
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         1617
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1618
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   CROSSLNK        811
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   CROSSLNK        811
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         130
FT                   /note="V -> A (in dbSNP:rs4278369)"
FT                   /id="VAR_061301"
FT   VARIANT         815
FT                   /note="V -> I (in dbSNP:rs951781)"
FT                   /evidence="ECO:0000269|PubMed:12880961"
FT                   /id="VAR_049814"
FT   VARIANT         1016
FT                   /note="S -> N (in dbSNP:rs2365718)"
FT                   /evidence="ECO:0000269|PubMed:1478958"
FT                   /id="VAR_049815"
FT   VARIANT         1101
FT                   /note="P -> L (in dbSNP:rs2886443)"
FT                   /evidence="ECO:0000269|PubMed:1478958"
FT                   /id="VAR_049816"
FT   VARIANT         1133
FT                   /note="R -> S (in dbSNP:rs17393797)"
FT                   /id="VAR_049817"
FT   VARIANT         1275
FT                   /note="P -> L (in dbSNP:rs3748570)"
FT                   /evidence="ECO:0000269|PubMed:1478958,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692"
FT                   /id="VAR_049818"
FT   CONFLICT        24
FT                   /note="A -> G (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="E -> G (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        45
FT                   /note="A -> R (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        96
FT                   /note="Q -> E (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="V -> G (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        161
FT                   /note="C -> L (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="Missing (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        205..207
FT                   /note="GQA -> DQT (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="G -> A (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        221
FT                   /note="G -> V (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        595..612
FT                   /note="ELLKDVEVVRPLEKEAVG -> RAIKGCGGSETSRKRGCR (in Ref. 1;
FT                   CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        857..908
FT                   /note="QGAMNPLEKEIQEPLESVEVNQETFRLLEEENQESLRSLGAWNLENLRSPEE
FT                   -> KSGGNESSRKGNSRTTGVCGSEPRDIQTPGRGESGIIEISGSMEPGEFEISRG
FT                   (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        975
FT                   /note="E -> K (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1008
FT                   /note="I -> F (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1050
FT                   /note="A -> T (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1235
FT                   /note="P -> L (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1256
FT                   /note="Missing (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1314..1325
FT                   /note="DPTGEQRPPPQG -> TPLESRGHPLK (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1344..1345
FT                   /note="AP -> E (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1472
FT                   /note="S -> N (in Ref. 4; BAE45713)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1542
FT                   /note="L -> M (in Ref. 4; BAE45713)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1563..1568
FT                   /note="VGQGMP -> SGARNA (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1589..1591
FT                   /note="TSW -> RSS (in Ref. 1; CAA46780)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1621 AA;  177439 MW;  0E4F967C11F44C13 CRC64;
     MEGCMGEESF QMWELNRRLE AYLARVKALE EQNELLSAEL GGLRAQSADT SWRAHADDEL
     AALRALVDQR WREKHAAEVA RDNLAEELEG VAGRCQQLRL ARERTTEEVA RNRRAVEAEK
     CARAWLSSQV AELERELEAL RVAHEEERVG LNAQAACAPR CPAPPRGPPA PAPEVEELAR
     RLGEAWRGAV RGYQERVAHM ETSLGQARER LGRAVQGARE GRLELQQLQA ERGGLLERRA
     ALEQRLEGRW QERLRATEKF QLAVEALEQE KQGLQSQIAQ VLEGRQQLAH LKMSLSLEVA
     TYRTLLEAEN SRLQTPGGGS KTSLSFQDPK LELQFPRTPE GRRLGSLLPV LSPTSLPSPL
     PATLETPVPA FLKNQEFLQA RTPTLASTPI PPTPQAPSPA VDAEIRAQDA PLSLLQTQGG
     RKQAPEPLRA EARVAIPASV LPGPEEPGGQ RQEASTGQSP EDHASLAPPL SPDHSSLEAK
     DGESGGSRVF SICRGEGEGQ IWGLVEKETA IEGKVVSSLQ QEIWEEEDLN RKEIQDSQVP
     LEKETLKSLG EEIQESLKTL ENQSHETLER ENQECPRSLE EDLETLKSLE KENKELLKDV
     EVVRPLEKEA VGQLKPTGKE DTQTLQSLQK ENQELMKSLE GNLETFLFPG TENQELVSSL
     QENLESLTAL EKENQEPLRS PEVGDEEALR PLTKENQEPL RSLEDENKEA FRSLEKENQE
     PLKTLEEEDQ SIVRPLETEN HKSLRSLEEQ DQETLRTLEK ETQQRRRSLG EQDQMTLRPP
     EKVDLEPLKS LDQEIARPLE NENQEFLKSL KEESVEAVKS LETEILESLK SAGQENLETL
     KSPETQAPLW TPEEINQGAM NPLEKEIQEP LESVEVNQET FRLLEEENQE SLRSLGAWNL
     ENLRSPEEVD KESQRNLEEE ENLGKGEYQE SLRSLEEEGQ ELPQSADVQR WEDTVEKDQE
     LAQESPPGMA GVENEDEAEL NLREQDGFTG KEEVVEQGEL NATEEVWIPG EGHPESPEPK
     EQRGLVEGAS VKGGAEGLQD PEGQSQQVGA PGLQAPQGLP EAIEPLVEDD VAPGGDQASP
     EVMLGSEPAM GESAAGAEPG PGQGVGGLGD PGHLTREEVM EPPLEEESLE AKRVQGLEGP
     RKDLEEAGGL GTEFSELPGK SRDPWEPPRE GREESEAEAP RGAEEAFPAE TLGHTGSDAP
     SPWPLGSEEA EEDVPPVLVS PSPTYTPILE DAPGPQPQAE GSQEASWGVQ GRAEALGKVE
     SEQEELGSGE IPEGPQEEGE ESREESEEDE LGETLPDSTP LGFYLRSPTS PRWDPTGEQR
     PPPQGETGKE GWDPAVLASE GLEAPPSEKE EGEEGEEECG RDSDLSEEFE DLGTEAPFLP
     GVPGEVAEPL GQVPQLLLDP AAWDRDGESD GFADEEESGE EGEEDQEEGR EPGAGRWGPG
     SSVGSLQALS SSQRGEFLES DSVSVSVPWD DSLRGAVAGA PKTALETESQ DSAEPSGSEE
     ESDPVSLERE DKVPGPLEIP SGMEDAGPGA DIIGVNGQGP NLEGKSQHVN GGVMNGLEQS
     EEVGQGMPLV SEGDRGSPFQ EEEGSALKTS WAGAPVHLGQ GQFLKFTQRE GDRESWSSGE
     D
//