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 27-MAR-2024, entry version 221. DE RecName: Full=Poly(rC)-binding protein 1 {ECO:0000303|PubMed:7607214}; DE AltName: Full=Alpha-CP1 {ECO:0000303|PubMed:7556077}; DE AltName: Full=Heterogeneous nuclear ribonucleoprotein E1; DE Short=hnRNP E1; DE AltName: Full=Nucleic acid-binding protein SUB2.3; GN Name=PCBP1 {ECO:0000303|PubMed:7607214, ECO:0000312|HGNC:HGNC:8647}; 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], FUNCTION, SUBCELLULAR LOCATION, RP PHOSPHORYLATION, AND TISSUE SPECIFICITY. RX PubMed=7607214; DOI=10.1111/j.1432-1033.1995.tb20581.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], AND FUNCTION. 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], FUNCTION, AND TISSUE SPECIFICITY. 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 (MICROBIAL INFECTION). 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, FUNCTION, AND RP 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 (PubMed:7607214, PubMed:7556077, CC PubMed:8152927, PubMed:15731341). Together with PCBP2, required for CC erythropoiesis, possibly by regulating mRNA splicing (By similarity). CC {ECO:0000250|UniProtKB:P60335, ECO:0000269|PubMed:15731341, CC ECO:0000269|PubMed:7556077, ECO:0000269|PubMed:7607214, CC ECO:0000269|PubMed:8152927}. CC -!- FUNCTION: (Microbial infection) In case of infection by poliovirus, CC plays a role in initiation of viral RNA replication in concert with the CC viral protein 3CD. {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 {ECO:0000269|PubMed:7607214}. Cytoplasm CC {ECO:0000269|PubMed:7607214}. Note=Loosely bound in the nucleus CC (PubMed:7607214). May shuttle between the nucleus and the cytoplasm CC (PubMed:7607214). {ECO:0000269|PubMed:7607214}. 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. {ECO:0000269|PubMed:7607214, CC ECO:0000269|PubMed:8152927}. CC -!- PTM: Phosphorylated; lowers poly(rC)-binding activity. CC {ECO:0000269|PubMed:7607214}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA82631.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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; 632. DR DIP; DIP-38136N; -. DR IntAct; Q15365; 149. DR MINT; Q15365; -. DR STRING; 9606.ENSP00000305556; -. DR ChEMBL; CHEMBL4295825; -. DR GlyCosmos; Q15365; 2 sites, 1 glycan. DR GlyGen; Q15365; 5 sites, 1 O-linked glycan (5 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 CPTAC; CPTAC-417; -. DR CPTAC; CPTAC-418; -. DR EPD; Q15365; -. DR jPOST; Q15365; -. DR MassIVE; Q15365; -. DR PaxDb; 9606-ENSP00000305556; -. DR PeptideAtlas; Q15365; -. DR ProteomicsDB; 60541; -. DR Pumba; Q15365; -. DR TopDownProteomics; Q15365; -. DR Antibodypedia; 16295; 494 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 AGR; HGNC:8647; -. 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; LTIRMVM; -. DR OrthoDB; 378620at2759; -. 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; 811 hits in 1165 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 209 other cell types or tissues. DR ExpressionAtlas; Q15365; baseline and differential. 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:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW. 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:0039694; P:viral RNA genome replication; IDA:UniProtKB. DR CDD; cd22515; KH-I_PCBP1_2_rpt1; 1. DR CDD; cd22518; KH-I_PCBP1_2_rpt2; 1. DR CDD; cd22521; KH-I_PCBP1_2_rpt3; 1. DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 3. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR036612; KH_dom_type_1_sf. DR PANTHER; PTHR10288; KH DOMAIN CONTAINING RNA BINDING PROTEIN; 1. DR PANTHER; PTHR10288:SF96; POLY(RC)-BINDING PROTEIN 1; 1. DR Pfam; PF00013; KH_1; 3. DR SMART; SM00322; KH; 3. DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 3. DR PROSITE; PS50084; KH_TYPE_1; 3. DR UCD-2DPAGE; Q15365; -. DR Genevisible; Q15365; HS. 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 //