NEST_HUMAN
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 03-AUG-2022, entry version 175.
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=3; 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_006617.1.
DR AlphaFoldDB; P48681; -.
DR SMR; P48681; -.
DR BioGRID; 115983; 129.
DR IntAct; P48681; 71.
DR MINT; P48681; -.
DR STRING; 9606.ENSP00000357206; -.
DR GlyGen; P48681; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P48681; -.
DR MetOSite; P48681; -.
DR PhosphoSitePlus; P48681; -.
DR SwissPalm; P48681; -.
DR BioMuta; NES; -.
DR DMDM; 146345464; -.
DR EPD; P48681; -.
DR jPOST; P48681; -.
DR MassIVE; P48681; -.
DR MaxQB; P48681; -.
DR PaxDb; P48681; -.
DR PeptideAtlas; P48681; -.
DR PRIDE; P48681; -.
DR ProteomicsDB; 55923; -.
DR Antibodypedia; 1658; 1113 antibodies from 49 providers.
DR DNASU; 10763; -.
DR Ensembl; ENST00000368223.4; ENSP00000357206.3; ENSG00000132688.11.
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 CTD; 10763; -.
DR DisGeNET; 10763; -.
DR GeneCards; NES; -.
DR HGNC; HGNC:7756; NES.
DR HPA; ENSG00000132688; Tissue enhanced (heart).
DR MIM; 600915; gene.
DR neXtProt; NX_P48681; -.
DR OpenTargets; ENSG00000132688; -.
DR PharmGKB; PA31556; -.
DR VEuPathDB; HostDB:ENSG00000132688; -.
DR eggNOG; ENOG502RYFK; Eukaryota.
DR GeneTree; ENSGT00940000162240; -.
DR HOGENOM; CLU_003317_0_0_1; -.
DR InParanoid; P48681; -.
DR OMA; RKEGWDP; -.
DR OrthoDB; 127811at2759; -.
DR PhylomeDB; P48681; -.
DR TreeFam; TF336633; -.
DR PathwayCommons; P48681; -.
DR SignaLink; P48681; -.
DR SIGNOR; P48681; -.
DR BioGRID-ORCS; 10763; 13 hits in 1078 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 175 other tissues.
DR Genevisible; P48681; HS.
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:0048858; P:cell projection morphogenesis; IEA:Ensembl.
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:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
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 InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR031211; Nestin.
DR PANTHER; PTHR47051; PTHR47051; 1.
DR Pfam; PF00038; Filament; 2.
DR SMART; SM01391; Filament; 1.
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; Reference proteome;
KW 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 675..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1294
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1371
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 1443..1460
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
