CHERP_HUMAN
ID CHERP_HUMAN Reviewed; 916 AA.
AC Q8IWX8; O00302; Q4G0Y5; Q8WU30; Q99492;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Calcium homeostasis endoplasmic reticulum protein;
DE AltName: Full=ERPROT 213-21;
DE AltName: Full=SR-related CTD-associated factor 6;
GN Name=CHERP {ECO:0000312|HGNC:HGNC:16930};
GN Synonyms=DAN26 {ECO:0000312|EMBL:CAA69591.1},
GN SCAF6 {ECO:0000312|EMBL:AAN77183.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAN77183.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-199.
RA Sampson N.D., Hewitt J.E.;
RT "Functional characterization of the novel SR-related CTD associated factor,
RT SCAF6.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH21294.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus {ECO:0000312|EMBL:AAH21294.1};
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] {ECO:0000305, ECO:0000312|EMBL:CAA69591.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-607.
RC TISSUE=Lymphoblast {ECO:0000312|EMBL:CAA69591.1};
RX PubMed=8896557; DOI=10.1038/ng1196-285;
RA Imbert G., Saudou F., Yvert G., Devys D., Trottier Y., Garnier J.-M.,
RA Weber C., Mandel J.-L., Cancel G., Abbas N., Duerr A., Didierjean O.,
RA Stevanin G., Agid Y., Brice A.;
RT "Cloning of the gene for spinocerebellar ataxia 2 reveals a locus with high
RT sensitivity to expanded CAG/glutamine repeats.";
RL Nat. Genet. 14:285-291(1996).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAB53327.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-916, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND VARIANT HIS-199.
RX PubMed=10794731; DOI=10.1042/bj3480189;
RA LaPlante J.M., O'Rourke F., Lu X., Fein A., Olsen A., Feinstein M.B.;
RT "Cloning of human Ca2+ homoeostasis endoplasmic reticulum protein (CHERP):
RT regulated expression of antisense cDNA depletes CHERP, inhibits
RT intracellular Ca2+ mobilization and decreases cell proliferation.";
RL Biochem. J. 348:189-199(2000).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=8010949; DOI=10.1042/bj3000673;
RA O'Rourke F., Soons K., Flaumenhauft R., Watras J., Baio-Larue C.,
RA Matthews E., Feinstein M.B.;
RT "Ca2+ release by inositol 1,4,5-trisphosphate is blocked by the K(+)-
RT channel blockers apamin and tetrapentylammonium ion, and a monoclonal
RT antibody to a 63 kDa membrane protein: reversal of blockade by K+
RT ionophores nigericin and valinomycin and purification of the 63 kDa
RT antibody-binding protein.";
RL Biochem. J. 300:673-683(1994).
RN [7] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12656674; DOI=10.1042/bj20030013;
RA O'Rourke F.A., LaPlante J.M., Feinstein M.B.;
RT "Antisense-mediated loss of calcium homoeostasis endoplasmic reticulum
RT protein (CHERP; ERPROT213-21) impairs Ca2+ mobilization, nuclear factor of
RT activated T-cells (NFAT) activation and cell proliferation in Jurkat T-
RT lymphocytes.";
RL Biochem. J. 373:133-143(2003).
RN [8]
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-813; SER-815; SER-817;
RP THR-819; SER-828 AND SER-904, 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815 AND SER-817, 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18 AND LYS-879, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813; SER-815; SER-817 AND
RP THR-819, 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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813; SER-815; SER-817;
RP THR-819; SER-855 AND SER-857, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-844 AND LYS-872, AND
RP IDENTIFICATION BY MASS 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: Involved in calcium homeostasis, growth and proliferation.
CC {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674}.
CC -!- INTERACTION:
CC Q8IWX8; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-2555370, EBI-10173507;
CC Q8IWX8; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-2555370, EBI-946029;
CC Q8IWX8; P49761: CLK3; NbExp=3; IntAct=EBI-2555370, EBI-745579;
CC Q8IWX8; Q14562: DHX8; NbExp=2; IntAct=EBI-2555370, EBI-2511477;
CC Q8IWX8; Q14296: FASTK; NbExp=3; IntAct=EBI-2555370, EBI-1754067;
CC Q8IWX8; Q5HY92: FIGN; NbExp=3; IntAct=EBI-2555370, EBI-12297985;
CC Q8IWX8; Q70Z53: FRA10AC1; NbExp=2; IntAct=EBI-2555370, EBI-710176;
CC Q8IWX8; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-2555370, EBI-1052037;
CC Q8IWX8; Q14847-2: LASP1; NbExp=3; IntAct=EBI-2555370, EBI-9088686;
CC Q8IWX8; Q9NQ29: LUC7L; NbExp=2; IntAct=EBI-2555370, EBI-473747;
CC Q8IWX8; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-2555370, EBI-716006;
CC Q8IWX8; O43251-10: RBFOX2; NbExp=3; IntAct=EBI-2555370, EBI-11963050;
CC Q8IWX8; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-2555370, EBI-3957636;
CC Q8IWX8; Q15637: SF1; NbExp=6; IntAct=EBI-2555370, EBI-744603;
CC Q8IWX8; Q8WVK2: SNRNP27; NbExp=2; IntAct=EBI-2555370, EBI-2512550;
CC Q8IWX8; O60504: SORBS3; NbExp=3; IntAct=EBI-2555370, EBI-741237;
CC Q8IWX8; Q04726-4: TLE3; NbExp=3; IntAct=EBI-2555370, EBI-12014388;
CC Q8IWX8; P26368: U2AF2; NbExp=2; IntAct=EBI-2555370, EBI-742339;
CC Q8IWX8; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-2555370, EBI-11975223;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10794731,
CC ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:10794731,
CC ECO:0000269|PubMed:12656674, ECO:0000269|PubMed:8010949}. Endoplasmic
CC reticulum {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674,
CC ECO:0000269|PubMed:8010949}. Note=Distributed throughout the cytoplasm
CC and also localizes to the perinuclear region of both human
CC erythroleukemia (HEL) cells and Jurkat cells. Colocalizes with ITPR1.
CC {ECO:0000269|PubMed:10794731, ECO:0000269|PubMed:12656674,
CC ECO:0000269|PubMed:8010949}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, placenta, lung, liver, kidney,
CC pancreas, cardiac and skeletal muscle, and in cultured HEL and Dami
CC cells. {ECO:0000269|PubMed:10794731}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB53327.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH21294.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA69591.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA69591.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF536542; AAN77183.1; -; mRNA.
DR EMBL; AC008764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021294; AAH21294.1; ALT_INIT; mRNA.
DR EMBL; Y08265; CAA69591.1; ALT_SEQ; mRNA.
DR EMBL; U94836; AAB53327.1; ALT_INIT; mRNA.
DR CCDS; CCDS42518.1; -.
DR RefSeq; NP_006378.3; NM_006387.5.
DR AlphaFoldDB; Q8IWX8; -.
DR SMR; Q8IWX8; -.
DR BioGRID; 115778; 225.
DR CORUM; Q8IWX8; -.
DR IntAct; Q8IWX8; 86.
DR MINT; Q8IWX8; -.
DR STRING; 9606.ENSP00000439856; -.
DR MoonDB; Q8IWX8; Predicted.
DR GlyGen; Q8IWX8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IWX8; -.
DR MetOSite; Q8IWX8; -.
DR PhosphoSitePlus; Q8IWX8; -.
DR BioMuta; CHERP; -.
DR DMDM; 296439404; -.
DR EPD; Q8IWX8; -.
DR jPOST; Q8IWX8; -.
DR MassIVE; Q8IWX8; -.
DR MaxQB; Q8IWX8; -.
DR PaxDb; Q8IWX8; -.
DR PeptideAtlas; Q8IWX8; -.
DR PRIDE; Q8IWX8; -.
DR ProteomicsDB; 70925; -.
DR Antibodypedia; 27406; 220 antibodies from 30 providers.
DR DNASU; 10523; -.
DR Ensembl; ENST00000546361.7; ENSP00000439856.2; ENSG00000085872.15.
DR GeneID; 10523; -.
DR KEGG; hsa:10523; -.
DR MANE-Select; ENST00000546361.7; ENSP00000439856.2; NM_006387.6; NP_006378.3.
DR UCSC; uc002nei.2; human.
DR CTD; 10523; -.
DR DisGeNET; 10523; -.
DR GeneCards; CHERP; -.
DR HGNC; HGNC:16930; CHERP.
DR HPA; ENSG00000085872; Low tissue specificity.
DR MIM; 618539; gene.
DR neXtProt; NX_Q8IWX8; -.
DR OpenTargets; ENSG00000085872; -.
DR PharmGKB; PA26459; -.
DR VEuPathDB; HostDB:ENSG00000085872; -.
DR eggNOG; KOG4368; Eukaryota.
DR GeneTree; ENSGT00730000111147; -.
DR HOGENOM; CLU_009446_0_0_1; -.
DR InParanoid; Q8IWX8; -.
DR OMA; QNTHHDI; -.
DR OrthoDB; 1256232at2759; -.
DR PhylomeDB; Q8IWX8; -.
DR TreeFam; TF318512; -.
DR PathwayCommons; Q8IWX8; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q8IWX8; -.
DR BioGRID-ORCS; 10523; 748 hits in 1083 CRISPR screens.
DR ChiTaRS; CHERP; human.
DR GenomeRNAi; 10523; -.
DR Pharos; Q8IWX8; Tbio.
DR PRO; PR:Q8IWX8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8IWX8; protein.
DR Bgee; ENSG00000085872; Expressed in secondary oocyte and 198 other tissues.
DR ExpressionAtlas; Q8IWX8; baseline and differential.
DR Genevisible; Q8IWX8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IMP:UniProtKB.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:UniProtKB.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 1.10.10.790; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR039037; CHERP.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR035967; SWAP/Surp_sf.
DR PANTHER; PTHR12323; PTHR12323; 3.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF01805; Surp; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00648; SWAP; 1.
DR SUPFAM; SSF109905; SSF109905; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS51391; CID; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50128; SURP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Endoplasmic reticulum; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..916
FT /note="Calcium homeostasis endoplasmic reticulum protein"
FT /id="PRO_0000299492"
FT REPEAT 15..57
FT /note="SURP motif"
FT /evidence="ECO:0000255"
FT DOMAIN 149..289
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT DOMAIN 841..891
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT REGION 336..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..379
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..450
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..535
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..621
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..816
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 18
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 714
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGZ0"
FT MOD_RES 813
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 819
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 879
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 844
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 872
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 199
FT /note="N -> H (in dbSNP:rs1043448)"
FT /evidence="ECO:0000269|PubMed:10794731, ECO:0000269|Ref.1"
FT /id="VAR_034833"
FT CONFLICT 99
FT /note="A -> D (in Ref. 4; CAA69591)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="A -> G (in Ref. 4; CAA69591)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="K -> T (in Ref. 4; CAA69591)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="H -> Y (in Ref. 4; CAA69591)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="A -> V (in Ref. 4; CAA69591)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="K -> N (in Ref. 4; CAA69591)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="S -> N (in Ref. 4; CAA69591)"
FT /evidence="ECO:0000305"
FT CONFLICT 776
FT /note="Y -> S (in Ref. 1; AAN77183)"
FT /evidence="ECO:0000305"
FT CONFLICT 778
FT /note="R -> C (in Ref. 1; AAN77183)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 916 AA; 103702 MW; 0C5D56F4DE4C5B9B CRC64;
MEMPLPPDDQ ELRNVIDKLA QFVARNGPEF EKMTMEKQKD NPKFSFLFGG EFYSYYKCKL
ALEQQQLICK QQTPELEPAA TMPPLPQPPL APAAPIPPAQ GAPSMDELIQ QSQWNLQQQE
QHLLALRQEQ VTAAVAHAVE QQMQKLLEET QLDMNEFDNL LQPIIDTCTK DAISAGKNWM
FSNAKSPPHC ELMAGHLRNR ITADGAHFEL RLHLIYLIND VLHHCQRKQA RELLAALQKV
VVPIYCTSFL AVEEDKQQKI ARLLQLWEKN GYFDDSIIQQ LQSPALGLGQ YQATLINEYS
SVVQPVQLAF QQQIQTLKTQ HEEFVTSLAQ QQQQQQQQQQ QLQMPQMEAE VKATPPPPAP
PPAPAPAPAI PPTTQPDDSK PPIQMPGSSE YEAPGGVQDP AAAGPRGPGP HDQIPPNKPP
WFDQPHPVAP WGQQQPPEQP PYPHHQGGPP HCPPWNNSHE GMWGEQRGDP GWNGQRDAPW
NNQPDAAWNS QFEGPWNSQH EQPPWGGGQR EPPFRMQRPP HFRGPFPPHQ QHPQFNQPPH
PHNFNRFPPR FMQDDFPPRH PFERPPYPHR FDYPQGDFPA EMGPPHHHPG HRMPHPGINE
HPPWAGPQHP DFGPPPHGFN GQPPHMRRQG PPHINHDDPS LVPNVPYFDL PAGLMAPLVK
LEDHEYKPLD PKDIRLPPPM PPSERLLAAV EAFYSPPSHD RPRNSEGWEQ NGLYEFFRAK
MRARRRKGQE KRNSGPSRSR SRSKSRGRSS SRSNSRSSKS SGSYSRSRSR SCSRSYSRSR
SRSRSRSRSS RSRSRSQSRS RSKSYSPGRR RRSRSRSPTP PSSAGLGSNS APPIPDSRLG
EENKGHQMLV KMGWSGSGGL GAKEQGIQDP IKGGDVRDKW DQYKGVGVAL DDPYENYRRN
KSYSFIARMK ARDECK
