Full text data of PCBP1
PCBP1
[Confidence: low (only semi-automatic identification from reviews)]
Poly(rC)-binding protein 1 (Alpha-CP1; Heterogeneous nuclear ribonucleoprotein E1; hnRNP E1; Nucleic acid-binding protein SUB2.3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Poly(rC)-binding protein 1 (Alpha-CP1; Heterogeneous nuclear ribonucleoprotein E1; hnRNP E1; Nucleic acid-binding protein SUB2.3)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15365
ID PCBP1_HUMAN Reviewed; 356 AA.
AC Q15365; Q13157; Q14975;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-FEB-2004, sequence version 2.
DT 22-JAN-2014, entry version 138.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT proteins, each containing three K-homologous (KH) domains.";
RL Eur. J. Biochem. 230:447-453(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7556077;
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
RT pre-mRNA 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
RT project: 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
RP 315-346, AND 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 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
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
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [9]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-190, AND
RP MASS SPECTROMETRY.
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 [11]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-190, AND
RP MASS SPECTROMETRY.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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.,
RA Buerckstuemmer T., 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
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.,
RA Leedman P.J., 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.
CC -!- INTERACTION:
CC Q15366:PCBP2; NbExp=2; IntAct=EBI-946095, EBI-945799;
CC Q13427:PPIG; NbExp=2; IntAct=EBI-946095, EBI-396072;
CC Q6P2Q9:PRPF8; NbExp=2; IntAct=EBI-946095, EBI-538479;
CC P26599:PTBP1; NbExp=2; IntAct=EBI-946095, EBI-350540;
CC Q9UHX1:PUF60; NbExp=2; IntAct=EBI-946095, EBI-1053259;
CC Q96PU8:QKI; NbExp=2; IntAct=EBI-946095, EBI-945792;
CC Q96EK4:THAP11; NbExp=4; IntAct=EBI-946095, EBI-1790529;
CC Q9Y3Q8:TSC22D4; NbExp=2; IntAct=EBI-946095, EBI-739485;
CC Q9Y2W2:WBP11; NbExp=2; IntAct=EBI-946095, EBI-714455;
CC Q96NB3:ZNF830; NbExp=2; IntAct=EBI-946095, EBI-3920997;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Loosely bound in
CC the nucleus. May shuttle between the nucleus and the cytoplasm.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in skeletal muscle,
CC thymus and peripheral blood leukocytes while a lower expression is
CC observed in prostate, spleen, testis, ovary, small intestine,
CC heart, liver, adrenal and thyroid glands.
CC -!- PTM: Phosphorylated; lowers poly(rC)-binding activity.
CC -!- SIMILARITY: Contains 3 KH domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA82631.1; Type=Frameshift; Positions=301;
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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 RefSeq; NP_006187.2; NM_006196.3.
DR RefSeq; XP_005264398.1; XM_005264341.1.
DR UniGene; Hs.2853; -.
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 ProteinModelPortal; Q15365; -.
DR SMR; Q15365; 11-169, 278-348.
DR DIP; DIP-38136N; -.
DR IntAct; Q15365; 51.
DR MINT; MINT-96267; -.
DR STRING; 9606.ENSP00000305556; -.
DR PhosphoSite; Q15365; -.
DR DMDM; 42560548; -.
DR OGP; Q15365; -.
DR REPRODUCTION-2DPAGE; IPI00016610; -.
DR UCD-2DPAGE; Q15365; -.
DR PaxDb; Q15365; -.
DR PeptideAtlas; Q15365; -.
DR PRIDE; Q15365; -.
DR DNASU; 5093; -.
DR Ensembl; ENST00000303577; ENSP00000305556; ENSG00000169564.
DR GeneID; 5093; -.
DR KEGG; hsa:5093; -.
DR UCSC; uc002sgf.3; human.
DR CTD; 5093; -.
DR GeneCards; GC02P070314; -.
DR HGNC; HGNC:8647; PCBP1.
DR HPA; CAB037113; -.
DR MIM; 601209; gene.
DR neXtProt; NX_Q15365; -.
DR PharmGKB; PA32986; -.
DR eggNOG; NOG315872; -.
DR HOGENOM; HOG000182823; -.
DR HOVERGEN; HBG053520; -.
DR InParanoid; Q15365; -.
DR KO; K12889; -.
DR OMA; NINGVME; -.
DR OrthoDB; EOG7P02J4; -.
DR PhylomeDB; Q15365; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PCBP1; human.
DR EvolutionaryTrace; Q15365; -.
DR GeneWiki; PCBP1; -.
DR GenomeRNAi; 5093; -.
DR NextBio; 19644; -.
DR PRO; PR:Q15365; -.
DR ArrayExpress; Q15365; -.
DR Bgee; Q15365; -.
DR CleanEx; HS_PCBP1; -.
DR Genevestigator; Q15365; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR Pfam; PF00013; KH_1; 3.
DR SMART; SM00322; KH; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding.
FT CHAIN 1 356 Poly(rC)-binding protein 1.
FT /FTId=PRO_0000050087.
FT DOMAIN 13 75 KH 1.
FT DOMAIN 97 162 KH 2.
FT DOMAIN 279 343 KH 3.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 173 173 Phosphoserine.
FT MOD_RES 190 190 Phosphoserine.
FT CONFLICT 205 205 A -> V (in Ref. 1; CAA55016).
FT CONFLICT 299 300 Missing (in Ref. 3; CAA82631).
FT STRAND 14 21
FT HELIX 22 29
FT HELIX 31 33
FT HELIX 34 43
FT STRAND 46 49
FT STRAND 55 64
FT HELIX 65 81
FT TURN 82 84
FT STRAND 280 287
FT HELIX 288 290
FT HELIX 291 295
FT HELIX 297 299
FT HELIX 300 309
FT STRAND 312 315
FT STRAND 323 331
FT HELIX 333 346
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
//
ID PCBP1_HUMAN Reviewed; 356 AA.
AC Q15365; Q13157; Q14975;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-FEB-2004, sequence version 2.
DT 22-JAN-2014, entry version 138.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT proteins, each containing three K-homologous (KH) domains.";
RL Eur. J. Biochem. 230:447-453(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7556077;
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
RT pre-mRNA 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
RT project: 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
RP 315-346, AND 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 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
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
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [9]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-190, AND
RP MASS SPECTROMETRY.
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 [11]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-190, AND
RP MASS SPECTROMETRY.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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.,
RA Buerckstuemmer T., 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
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.,
RA Leedman P.J., 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.
CC -!- INTERACTION:
CC Q15366:PCBP2; NbExp=2; IntAct=EBI-946095, EBI-945799;
CC Q13427:PPIG; NbExp=2; IntAct=EBI-946095, EBI-396072;
CC Q6P2Q9:PRPF8; NbExp=2; IntAct=EBI-946095, EBI-538479;
CC P26599:PTBP1; NbExp=2; IntAct=EBI-946095, EBI-350540;
CC Q9UHX1:PUF60; NbExp=2; IntAct=EBI-946095, EBI-1053259;
CC Q96PU8:QKI; NbExp=2; IntAct=EBI-946095, EBI-945792;
CC Q96EK4:THAP11; NbExp=4; IntAct=EBI-946095, EBI-1790529;
CC Q9Y3Q8:TSC22D4; NbExp=2; IntAct=EBI-946095, EBI-739485;
CC Q9Y2W2:WBP11; NbExp=2; IntAct=EBI-946095, EBI-714455;
CC Q96NB3:ZNF830; NbExp=2; IntAct=EBI-946095, EBI-3920997;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Loosely bound in
CC the nucleus. May shuttle between the nucleus and the cytoplasm.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in skeletal muscle,
CC thymus and peripheral blood leukocytes while a lower expression is
CC observed in prostate, spleen, testis, ovary, small intestine,
CC heart, liver, adrenal and thyroid glands.
CC -!- PTM: Phosphorylated; lowers poly(rC)-binding activity.
CC -!- SIMILARITY: Contains 3 KH domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA82631.1; Type=Frameshift; Positions=301;
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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 RefSeq; NP_006187.2; NM_006196.3.
DR RefSeq; XP_005264398.1; XM_005264341.1.
DR UniGene; Hs.2853; -.
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 ProteinModelPortal; Q15365; -.
DR SMR; Q15365; 11-169, 278-348.
DR DIP; DIP-38136N; -.
DR IntAct; Q15365; 51.
DR MINT; MINT-96267; -.
DR STRING; 9606.ENSP00000305556; -.
DR PhosphoSite; Q15365; -.
DR DMDM; 42560548; -.
DR OGP; Q15365; -.
DR REPRODUCTION-2DPAGE; IPI00016610; -.
DR UCD-2DPAGE; Q15365; -.
DR PaxDb; Q15365; -.
DR PeptideAtlas; Q15365; -.
DR PRIDE; Q15365; -.
DR DNASU; 5093; -.
DR Ensembl; ENST00000303577; ENSP00000305556; ENSG00000169564.
DR GeneID; 5093; -.
DR KEGG; hsa:5093; -.
DR UCSC; uc002sgf.3; human.
DR CTD; 5093; -.
DR GeneCards; GC02P070314; -.
DR HGNC; HGNC:8647; PCBP1.
DR HPA; CAB037113; -.
DR MIM; 601209; gene.
DR neXtProt; NX_Q15365; -.
DR PharmGKB; PA32986; -.
DR eggNOG; NOG315872; -.
DR HOGENOM; HOG000182823; -.
DR HOVERGEN; HBG053520; -.
DR InParanoid; Q15365; -.
DR KO; K12889; -.
DR OMA; NINGVME; -.
DR OrthoDB; EOG7P02J4; -.
DR PhylomeDB; Q15365; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PCBP1; human.
DR EvolutionaryTrace; Q15365; -.
DR GeneWiki; PCBP1; -.
DR GenomeRNAi; 5093; -.
DR NextBio; 19644; -.
DR PRO; PR:Q15365; -.
DR ArrayExpress; Q15365; -.
DR Bgee; Q15365; -.
DR CleanEx; HS_PCBP1; -.
DR Genevestigator; Q15365; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR Pfam; PF00013; KH_1; 3.
DR SMART; SM00322; KH; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding.
FT CHAIN 1 356 Poly(rC)-binding protein 1.
FT /FTId=PRO_0000050087.
FT DOMAIN 13 75 KH 1.
FT DOMAIN 97 162 KH 2.
FT DOMAIN 279 343 KH 3.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 173 173 Phosphoserine.
FT MOD_RES 190 190 Phosphoserine.
FT CONFLICT 205 205 A -> V (in Ref. 1; CAA55016).
FT CONFLICT 299 300 Missing (in Ref. 3; CAA82631).
FT STRAND 14 21
FT HELIX 22 29
FT HELIX 31 33
FT HELIX 34 43
FT STRAND 46 49
FT STRAND 55 64
FT HELIX 65 81
FT TURN 82 84
FT STRAND 280 287
FT HELIX 288 290
FT HELIX 291 295
FT HELIX 297 299
FT HELIX 300 309
FT STRAND 312 315
FT STRAND 323 331
FT HELIX 333 346
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
//
MIM
601209
*RECORD*
*FIELD* NO
601209
*FIELD* TI
*601209 POLY(rC)-BINDING PROTEIN 1; PCBP1
*FIELD* TX
CLONING
Leffers et al. (1995) described the cloning and characterization of 2
read morecDNAs for poly(rC)-binding proteins, called PCBP1 and PCBP2 (601210) by
them. The authors analyzed an EST database for sequences that were
predicted to encode a protein with K-homologous (KH) domains. The 60- to
70-amino acid KH motifs are found in several putative nucleic acid
binding proteins such as FMR1 (309550) and HNRNPK (600712) and are
thought to be involved in RNA binding. Using primers from 1 EST the
authors produced a probe that was used to screen a cDNA library of
transformed human amnion cells. The cDNA they isolated for PCBP1 encodes
a putative 356-amino acid protein that contains 3 KH domains. It is 83%
identical to PCBP2 at the DNA level and 90% homologous at the amino acid
level. The PCBP1 protein is about 85% similar to the mouse hnRNP-X/mCTBP
protein (Hahm et al., 1993).
Chkheidze and Liebhaber (2003) determined that endogenous HeLa cell
PCBP1 colocalized to nuclear speckles with SC35 (600813). They
identified a nuclear localization signal within a 9-amino acid segment
between KH2 and KH3. Deletion of this segment blocked nuclear
accumulation of PCBP1.
GENE FUNCTION
When expressed with a vaccinia virus system in transformed amnion cells,
Leffers et al. (1995) found that both PCBP1 and PCBP2 bound poly(rC)
when not phosphorylated; phosphorylated protein bound with much lower
affinity.
By yeast 2-hybrid analysis of a human brain cDNA library, Kosturko et
al. (2006) found that mouse Hnrnpa2 (600124) interacted with human
HNRNPE1. They confirmed the interaction with in vivo and in vitro
protein interaction assays. Hnrnpe1 colocalized with Hnrnpa2 and A2RE
mRNA in granules in dendrites of rat oligodendrocytes. Overexpression of
HNRNPE1 or microinjection of exogenous HNRNPE1 in rat neural cells
inhibited translation of A2RE mRNA, but not translation of mutated A2RE
mRNA. Excess HNRNPE1 added to an in vitro translation system reduced
translation efficiency of A2RE mRNA in an Hnrnpa2-dependent manner.
Kosturko et al. (2006) hypothesized that binding of HNRNPE1 to HNRNPA2
inhibits A2RE mRNA translation during granule transport.
Shi et al. (2008) identified PCBP1 in a genetic screen to identify human
genes that, when expressed in yeast, could increase the amount of iron
loaded into ferritin (see 134790). PCBP1 bound to ferritin in vivo, and
bound iron and facilitated iron loading into ferritin in vitro.
Depletion of PCBP1 in human cells inhibited ferritin iron loading and
increased cytosolic iron pools. Thus, Shi et al. (2008) concluded that
PCBP1 can function as a cytosolic iron chaperone in the delivery of iron
to ferritin.
MAPPING
Transcripts of both PCBPs were detected in all the human tissues
analyzed. Tommerup and Leffers (1996) mapped PCBP1 to 2p13-p12 by
fluorescence in situ hybridization.
*FIELD* RF
1. Chkheidze, A. N.; Liebhaber, S. A.: A novel set of nuclear localization
signals determine distributions of the alpha-CP RNA-binding proteins. Molec.
Cell. Biol. 23: 8405-8415, 2003.
2. Hahm, K.; Kim, G.; Turck, C. W.; Smale, S. T.: Isolation of a
murine gene encoding a nucleic acid-binding protein with homology
to hnRNP K. Nucleic Acids Res. 21: 3894 only, 1993.
3. Kosturko, L. D.; Maggipinto, M. J.; Korza, G.; Lee, J. W.; Carson,
J. H.; Barbarese, E.: Heterogeneous nuclear ribonucleoprotein (hnRNP)
E1 binds to hnRNP A2 and inhibits translation of A2 response element
mRNAs. Molec. Biol. Cell 17: 3521-3533, 2006.
4. Leffers, H.; Dejgaard, K.; Celis, J. E.: Characterisation of two
major cellular poly(rC)-binding human proteins, each containing three
K-homologous (KH) domains. Europ. J. Biochem. 230: 447-453, 1995.
5. Shi, H.; Bencze, K. Z.; Stemmler, T. L.; Philpott, C. C.: A cytosolic
iron chaperone that delivers iron to ferritin. Science 320: 1207-1210,
2008.
6. Tommerup, N.; Leffers, H.: Assignment of human KH-box-containing
genes by in situ hybridization: HNRNPK maps to 9q21.32-q21.33, PCBP1
to 2p12-p13, and PCBP2 to 12q13.12-q13.13, distal to FRA12A. Genomics 32:
297-298, 1996.
*FIELD* CN
Patricia A. Hartz - updated: 9/10/2009
Ada Hamosh - updated: 6/10/2008
Patricia A. Hartz - updated: 2/11/2004
*FIELD* CD
Alan F. Scott: 4/17/1996
*FIELD* ED
mgross: 09/17/2009
terry: 9/10/2009
alopez: 6/12/2008
terry: 6/10/2008
cwells: 3/2/2004
terry: 2/11/2004
mark: 9/4/1996
mark: 6/7/1996
terry: 5/2/1996
mark: 4/17/1996
terry: 4/17/1996
mark: 4/17/1996
*RECORD*
*FIELD* NO
601209
*FIELD* TI
*601209 POLY(rC)-BINDING PROTEIN 1; PCBP1
*FIELD* TX
CLONING
Leffers et al. (1995) described the cloning and characterization of 2
read morecDNAs for poly(rC)-binding proteins, called PCBP1 and PCBP2 (601210) by
them. The authors analyzed an EST database for sequences that were
predicted to encode a protein with K-homologous (KH) domains. The 60- to
70-amino acid KH motifs are found in several putative nucleic acid
binding proteins such as FMR1 (309550) and HNRNPK (600712) and are
thought to be involved in RNA binding. Using primers from 1 EST the
authors produced a probe that was used to screen a cDNA library of
transformed human amnion cells. The cDNA they isolated for PCBP1 encodes
a putative 356-amino acid protein that contains 3 KH domains. It is 83%
identical to PCBP2 at the DNA level and 90% homologous at the amino acid
level. The PCBP1 protein is about 85% similar to the mouse hnRNP-X/mCTBP
protein (Hahm et al., 1993).
Chkheidze and Liebhaber (2003) determined that endogenous HeLa cell
PCBP1 colocalized to nuclear speckles with SC35 (600813). They
identified a nuclear localization signal within a 9-amino acid segment
between KH2 and KH3. Deletion of this segment blocked nuclear
accumulation of PCBP1.
GENE FUNCTION
When expressed with a vaccinia virus system in transformed amnion cells,
Leffers et al. (1995) found that both PCBP1 and PCBP2 bound poly(rC)
when not phosphorylated; phosphorylated protein bound with much lower
affinity.
By yeast 2-hybrid analysis of a human brain cDNA library, Kosturko et
al. (2006) found that mouse Hnrnpa2 (600124) interacted with human
HNRNPE1. They confirmed the interaction with in vivo and in vitro
protein interaction assays. Hnrnpe1 colocalized with Hnrnpa2 and A2RE
mRNA in granules in dendrites of rat oligodendrocytes. Overexpression of
HNRNPE1 or microinjection of exogenous HNRNPE1 in rat neural cells
inhibited translation of A2RE mRNA, but not translation of mutated A2RE
mRNA. Excess HNRNPE1 added to an in vitro translation system reduced
translation efficiency of A2RE mRNA in an Hnrnpa2-dependent manner.
Kosturko et al. (2006) hypothesized that binding of HNRNPE1 to HNRNPA2
inhibits A2RE mRNA translation during granule transport.
Shi et al. (2008) identified PCBP1 in a genetic screen to identify human
genes that, when expressed in yeast, could increase the amount of iron
loaded into ferritin (see 134790). PCBP1 bound to ferritin in vivo, and
bound iron and facilitated iron loading into ferritin in vitro.
Depletion of PCBP1 in human cells inhibited ferritin iron loading and
increased cytosolic iron pools. Thus, Shi et al. (2008) concluded that
PCBP1 can function as a cytosolic iron chaperone in the delivery of iron
to ferritin.
MAPPING
Transcripts of both PCBPs were detected in all the human tissues
analyzed. Tommerup and Leffers (1996) mapped PCBP1 to 2p13-p12 by
fluorescence in situ hybridization.
*FIELD* RF
1. Chkheidze, A. N.; Liebhaber, S. A.: A novel set of nuclear localization
signals determine distributions of the alpha-CP RNA-binding proteins. Molec.
Cell. Biol. 23: 8405-8415, 2003.
2. Hahm, K.; Kim, G.; Turck, C. W.; Smale, S. T.: Isolation of a
murine gene encoding a nucleic acid-binding protein with homology
to hnRNP K. Nucleic Acids Res. 21: 3894 only, 1993.
3. Kosturko, L. D.; Maggipinto, M. J.; Korza, G.; Lee, J. W.; Carson,
J. H.; Barbarese, E.: Heterogeneous nuclear ribonucleoprotein (hnRNP)
E1 binds to hnRNP A2 and inhibits translation of A2 response element
mRNAs. Molec. Biol. Cell 17: 3521-3533, 2006.
4. Leffers, H.; Dejgaard, K.; Celis, J. E.: Characterisation of two
major cellular poly(rC)-binding human proteins, each containing three
K-homologous (KH) domains. Europ. J. Biochem. 230: 447-453, 1995.
5. Shi, H.; Bencze, K. Z.; Stemmler, T. L.; Philpott, C. C.: A cytosolic
iron chaperone that delivers iron to ferritin. Science 320: 1207-1210,
2008.
6. Tommerup, N.; Leffers, H.: Assignment of human KH-box-containing
genes by in situ hybridization: HNRNPK maps to 9q21.32-q21.33, PCBP1
to 2p12-p13, and PCBP2 to 12q13.12-q13.13, distal to FRA12A. Genomics 32:
297-298, 1996.
*FIELD* CN
Patricia A. Hartz - updated: 9/10/2009
Ada Hamosh - updated: 6/10/2008
Patricia A. Hartz - updated: 2/11/2004
*FIELD* CD
Alan F. Scott: 4/17/1996
*FIELD* ED
mgross: 09/17/2009
terry: 9/10/2009
alopez: 6/12/2008
terry: 6/10/2008
cwells: 3/2/2004
terry: 2/11/2004
mark: 9/4/1996
mark: 6/7/1996
terry: 5/2/1996
mark: 4/17/1996
terry: 4/17/1996
mark: 4/17/1996