PCBP1_HUMAN
ID PCBP1_HUMAN Reviewed; 356 AA.
AC Q15365; Q13157; Q14975;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Poly(rC)-binding protein 1;
DE AltName: Full=Alpha-CP1;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein E1;
DE Short=hnRNP E1;
DE AltName: Full=Nucleic acid-binding protein SUB2.3;
GN Name=PCBP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7607214; DOI=10.1111/j.1432-1033.1995.0447h.x;
RA Leffers H., Dejgaard K., Celis J.E.;
RT "Characterisation of two major cellular poly(rC)-binding human proteins,
RT each containing three K-homologous (KH) domains.";
RL Eur. J. Biochem. 230:447-453(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7556077; DOI=10.1002/j.1460-2075.1995.tb00110.x;
RA Kiledjian M., Wang X., Liebhaber S.A.;
RT "Identification of two KH domain proteins in the alpha-globin mRNP
RT stability complex.";
RL EMBO J. 14:4357-4364(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphocyte;
RX PubMed=8152927; DOI=10.1093/nar/22.6.959;
RA Aasheim H.-C., Loukianova T., Deggerdal A., Smeland E.B.;
RT "Tissue specific expression and cDNA structure of a human transcript
RT encoding a nucleic acid binding [oligo(dC)] protein related to the pre-mRNA
RT binding protein K.";
RL Nucleic Acids Res. 22:959-964(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP PROTEIN SEQUENCE OF 47-70; 79-115; 125-160; 178-200; 298-306 AND 315-346,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP FUNCTION.
RX PubMed=12414943; DOI=10.1128/jvi.76.23.12008-12022.2002;
RA Walter B.L., Parsley T.B., Ehrenfeld E., Semler B.L.;
RT "Distinct poly(rC) binding protein KH domain determinants for poliovirus
RT translation initiation and viral RNA replication.";
RL J. Virol. 76:12008-12022(2002).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-190, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-190, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP 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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-246 AND SER-264, 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-273, 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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-115, 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).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 279-356, AND RNA-BINDING.
RX PubMed=15731341; DOI=10.1093/nar/gki265;
RA Sidiqi M., Wilce J.A., Vivian J.P., Porter C.J., Barker A., Leedman P.J.,
RA Wilce M.C.;
RT "Structure and RNA binding of the third KH domain of poly(C)-binding
RT protein 1.";
RL Nucleic Acids Res. 33:1213-1221(2005).
CC -!- FUNCTION: Single-stranded nucleic acid binding protein that binds
CC preferentially to oligo dC. In case of infection by poliovirus, plays a
CC role in initiation of viral RNA replication in concert with the viral
CC protein 3CD (PubMed:12414943). {ECO:0000269|PubMed:12414943}.
CC -!- INTERACTION:
CC Q15365; A0A024R5S0: hCG_2003792; NbExp=3; IntAct=EBI-946095, EBI-10188461;
CC Q15365; O00425: IGF2BP3; NbExp=3; IntAct=EBI-946095, EBI-1058566;
CC Q15365; Q13351: KLF1; NbExp=3; IntAct=EBI-946095, EBI-8284732;
CC Q15365; Q13153: PAK1; NbExp=2; IntAct=EBI-946095, EBI-1307;
CC Q15365; Q13153-1: PAK1; NbExp=5; IntAct=EBI-946095, EBI-15628682;
CC Q15365; Q15366: PCBP2; NbExp=2; IntAct=EBI-946095, EBI-945799;
CC Q15365; Q13427: PPIG; NbExp=2; IntAct=EBI-946095, EBI-396072;
CC Q15365; Q6P2Q9: PRPF8; NbExp=2; IntAct=EBI-946095, EBI-538479;
CC Q15365; P26599: PTBP1; NbExp=2; IntAct=EBI-946095, EBI-350540;
CC Q15365; Q9UHX1: PUF60; NbExp=2; IntAct=EBI-946095, EBI-1053259;
CC Q15365; Q96PU8: QKI; NbExp=2; IntAct=EBI-946095, EBI-945792;
CC Q15365; O43251-10: RBFOX2; NbExp=3; IntAct=EBI-946095, EBI-11963050;
CC Q15365; P98179: RBM3; NbExp=3; IntAct=EBI-946095, EBI-2949699;
CC Q15365; Q14498: RBM39; NbExp=2; IntAct=EBI-946095, EBI-395290;
CC Q15365; Q14498-2: RBM39; NbExp=2; IntAct=EBI-946095, EBI-11032687;
CC Q15365; Q6ZRY4: RBPMS2; NbExp=4; IntAct=EBI-946095, EBI-11987469;
CC Q15365; P09012: SNRPA; NbExp=9; IntAct=EBI-946095, EBI-607085;
CC Q15365; Q96EK4: THAP11; NbExp=4; IntAct=EBI-946095, EBI-1790529;
CC Q15365; Q08117-2: TLE5; NbExp=3; IntAct=EBI-946095, EBI-11741437;
CC Q15365; Q9Y3Q8: TSC22D4; NbExp=2; IntAct=EBI-946095, EBI-739485;
CC Q15365; Q9Y2W2: WBP11; NbExp=2; IntAct=EBI-946095, EBI-714455;
CC Q15365; Q96NB3: ZNF830; NbExp=2; IntAct=EBI-946095, EBI-3920997;
CC Q15365; O41951: GAMMAHV.ORF34; Xeno; NbExp=4; IntAct=EBI-946095, EBI-9640556;
CC Q15365; Q67020: PA; Xeno; NbExp=2; IntAct=EBI-946095, EBI-11514477;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Loosely bound in the
CC nucleus. May shuttle between the nucleus and the cytoplasm.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in skeletal muscle, thymus and
CC peripheral blood leukocytes while a lower expression is observed in
CC prostate, spleen, testis, ovary, small intestine, heart, liver, adrenal
CC and thyroid glands.
CC -!- PTM: Phosphorylated; lowers poly(rC)-binding activity.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA82631.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X78137; CAA55016.1; -; mRNA.
DR EMBL; U24223; AAA91317.1; -; mRNA.
DR EMBL; Z29505; CAA82631.1; ALT_FRAME; mRNA.
DR EMBL; BC039742; AAH39742.1; -; mRNA.
DR CCDS; CCDS1898.1; -.
DR RefSeq; NP_006187.2; NM_006196.3.
DR PDB; 1WVN; X-ray; 2.10 A; A=279-356.
DR PDB; 1ZTG; X-ray; 3.00 A; A/B/C/D=14-85.
DR PDB; 3VKE; X-ray; 1.77 A; A/B/C/D=14-86.
DR PDBsum; 1WVN; -.
DR PDBsum; 1ZTG; -.
DR PDBsum; 3VKE; -.
DR AlphaFoldDB; Q15365; -.
DR SMR; Q15365; -.
DR BioGRID; 111126; 513.
DR DIP; DIP-38136N; -.
DR IntAct; Q15365; 145.
DR MINT; Q15365; -.
DR STRING; 9606.ENSP00000305556; -.
DR ChEMBL; CHEMBL4295825; -.
DR GlyGen; Q15365; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q15365; -.
DR MetOSite; Q15365; -.
DR PhosphoSitePlus; Q15365; -.
DR SwissPalm; Q15365; -.
DR BioMuta; PCBP1; -.
DR DMDM; 42560548; -.
DR OGP; Q15365; -.
DR REPRODUCTION-2DPAGE; IPI00016610; -.
DR UCD-2DPAGE; Q15365; -.
DR CPTAC; CPTAC-417; -.
DR CPTAC; CPTAC-418; -.
DR EPD; Q15365; -.
DR jPOST; Q15365; -.
DR MassIVE; Q15365; -.
DR PaxDb; Q15365; -.
DR PeptideAtlas; Q15365; -.
DR PRIDE; Q15365; -.
DR ProteomicsDB; 60541; -.
DR TopDownProteomics; Q15365; -.
DR Antibodypedia; 16295; 449 antibodies from 37 providers.
DR DNASU; 5093; -.
DR Ensembl; ENST00000303577.7; ENSP00000305556.5; ENSG00000169564.7.
DR GeneID; 5093; -.
DR KEGG; hsa:5093; -.
DR MANE-Select; ENST00000303577.7; ENSP00000305556.5; NM_006196.4; NP_006187.2.
DR CTD; 5093; -.
DR DisGeNET; 5093; -.
DR GeneCards; PCBP1; -.
DR HGNC; HGNC:8647; PCBP1.
DR HPA; ENSG00000169564; Low tissue specificity.
DR MIM; 601209; gene.
DR neXtProt; NX_Q15365; -.
DR OpenTargets; ENSG00000169564; -.
DR PharmGKB; PA32986; -.
DR VEuPathDB; HostDB:ENSG00000169564; -.
DR eggNOG; KOG2190; Eukaryota.
DR GeneTree; ENSGT00940000161582; -.
DR HOGENOM; CLU_022670_0_1_1; -.
DR InParanoid; Q15365; -.
DR OMA; GQDRCGD; -.
DR OrthoDB; 954970at2759; -.
DR PhylomeDB; Q15365; -.
DR TreeFam; TF318292; -.
DR PathwayCommons; Q15365; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR SignaLink; Q15365; -.
DR SIGNOR; Q15365; -.
DR BioGRID-ORCS; 5093; 777 hits in 1086 CRISPR screens.
DR ChiTaRS; PCBP1; human.
DR EvolutionaryTrace; Q15365; -.
DR GeneWiki; PCBP1; -.
DR GenomeRNAi; 5093; -.
DR Pharos; Q15365; Tbio.
DR PRO; PR:Q15365; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q15365; protein.
DR Bgee; ENSG00000169564; Expressed in oocyte and 207 other tissues.
DR ExpressionAtlas; Q15365; baseline and differential.
DR Genevisible; Q15365; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0098847; F:sequence-specific single stranded DNA binding; IEA:Ensembl.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0051252; P:regulation of RNA metabolic process; IBA:GO_Central.
DR GO; GO:0039694; P:viral RNA genome replication; IDA:UniProtKB.
DR Gene3D; 3.30.1370.10; -; 3.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF00013; KH_1; 3.
DR SMART; SM00322; KH; 3.
DR SUPFAM; SSF54791; SSF54791; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ribonucleoprotein; RNA-binding; Ubl conjugation;
KW Viral RNA replication.
FT CHAIN 1..356
FT /note="Poly(rC)-binding protein 1"
FT /id="PRO_0000050087"
FT DOMAIN 13..75
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 97..162
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 279..343
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60335"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 205
FT /note="A -> V (in Ref. 1; CAA55016)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..300
FT /note="Missing (in Ref. 3; CAA82631)"
FT /evidence="ECO:0000305"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:3VKE"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:3VKE"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:3VKE"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:3VKE"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:3VKE"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:3VKE"
FT HELIX 65..81
FT /evidence="ECO:0007829|PDB:3VKE"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:3VKE"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:1WVN"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:1WVN"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:1WVN"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1WVN"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:1WVN"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:1WVN"
FT STRAND 323..331
FT /evidence="ECO:0007829|PDB:1WVN"
FT HELIX 333..346
FT /evidence="ECO:0007829|PDB:1WVN"
SQ SEQUENCE 356 AA; 37498 MW; 6D1A261276CA206D CRC64;
MDAGVTESGL NVTLTIRLLM HGKEVGSIIG KKGESVKRIR EESGARINIS EGNCPERIIT
LTGPTNAIFK AFAMIIDKLE EDINSSMTNS TAASRPPVTL RLVVPATQCG SLIGKGGCKI
KEIRESTGAQ VQVAGDMLPN STERAITIAG VPQSVTECVK QICLVMLETL SQSPQGRVMT
IPYQPMPASS PVICAGGQDR CSDAAGYPHA THDLEGPPLD AYSIQGQHTI SPLDLAKLNQ
VARQQSHFAM MHGGTGFAGI DSSSPEVKGY WASLDASTQT THELTIPNNL IGCIIGRQGA
NINEIRQMSG AQIKIANPVE GSSGRQVTIT GSAASISLAQ YLINARLSSE KGMGCS
