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Q15365

- PCBP1_HUMAN

UniProt

Q15365 - PCBP1_HUMAN

Protein

Poly(rC)-binding protein 1

Gene

PCBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (16 Feb 2004)
      Previous versions | rss
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    Functioni

    Single-stranded nucleic acid binding protein that binds preferentially to oligo dC.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. RNA binding Source: UniProtKB
    4. single-stranded DNA binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA splicing, via spliceosome Source: Reactome
    3. RNA splicing Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Poly(rC)-binding protein 1
    Alternative name(s):
    Alpha-CP1
    Heterogeneous nuclear ribonucleoprotein E1
    Short name:
    hnRNP E1
    Nucleic acid-binding protein SUB2.3
    Gene namesi
    Name:PCBP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:8647. PCBP1.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Loosely bound in the nucleus. May shuttle between the nucleus and the cytoplasm.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. ribonucleoprotein complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA32986.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 356356Poly(rC)-binding protein 1PRO_0000050087Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei173 – 1731Phosphoserine5 Publications
    Modified residuei190 – 1901Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated; lowers poly(rC)-binding activity.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15365.
    PaxDbiQ15365.
    PeptideAtlasiQ15365.
    PRIDEiQ15365.

    2D gel databases

    OGPiQ15365.
    REPRODUCTION-2DPAGEIPI00016610.
    UCD-2DPAGEQ15365.

    PTM databases

    PhosphoSiteiQ15365.

    Expressioni

    Tissue specificityi

    Abundantly expressed in skeletal muscle, thymus and peripheral blood leukocytes while a lower expression is observed in prostate, spleen, testis, ovary, small intestine, heart, liver, adrenal and thyroid glands.

    Gene expression databases

    ArrayExpressiQ15365.
    BgeeiQ15365.
    CleanExiHS_PCBP1.
    GenevestigatoriQ15365.

    Organism-specific databases

    HPAiCAB037113.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GAMMAHV.ORF34O419514EBI-946095,EBI-9640556From a different organism.
    PCBP2Q153662EBI-946095,EBI-945799
    PPIGQ134272EBI-946095,EBI-396072
    PRPF8Q6P2Q92EBI-946095,EBI-538479
    PTBP1P265992EBI-946095,EBI-350540
    PUF60Q9UHX12EBI-946095,EBI-1053259
    QKIQ96PU82EBI-946095,EBI-945792
    THAP11Q96EK44EBI-946095,EBI-1790529
    TSC22D4Q9Y3Q82EBI-946095,EBI-739485
    WBP11Q9Y2W22EBI-946095,EBI-714455
    ZNF830Q96NB32EBI-946095,EBI-3920997

    Protein-protein interaction databases

    BioGridi111126. 85 interactions.
    DIPiDIP-38136N.
    IntActiQ15365. 53 interactions.
    MINTiMINT-96267.
    STRINGi9606.ENSP00000305556.

    Structurei

    Secondary structure

    1
    356
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi14 – 218
    Helixi22 – 298
    Helixi31 – 333
    Helixi34 – 4310
    Beta strandi46 – 494
    Beta strandi55 – 6410
    Helixi65 – 8117
    Turni82 – 843
    Beta strandi280 – 2878
    Helixi288 – 2903
    Helixi291 – 2955
    Helixi297 – 2993
    Helixi300 – 30910
    Beta strandi312 – 3154
    Beta strandi323 – 3319
    Helixi333 – 34614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WVNX-ray2.10A279-356[»]
    1ZTGX-ray3.00A/B/C/D14-85[»]
    3VKEX-ray1.77A/B/C/D14-86[»]
    ProteinModelPortaliQ15365.
    SMRiQ15365. Positions 11-169, 278-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15365.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 7563KH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini97 – 16266KH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini279 – 34365KH 3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 3 KH domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG315872.
    HOGENOMiHOG000182823.
    HOVERGENiHBG053520.
    InParanoidiQ15365.
    KOiK12889.
    OMAiQDRCGDA.
    OrthoDBiEOG7P02J4.
    PhylomeDBiQ15365.
    TreeFamiTF318292.

    Family and domain databases

    Gene3Di3.30.1370.10. 3 hits.
    InterProiIPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    [Graphical view]
    PfamiPF00013. KH_1. 3 hits.
    [Graphical view]
    SMARTiSM00322. KH. 3 hits.
    [Graphical view]
    SUPFAMiSSF54791. SSF54791. 3 hits.
    PROSITEiPS50084. KH_TYPE_1. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q15365-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDAGVTESGL NVTLTIRLLM HGKEVGSIIG KKGESVKRIR EESGARINIS    50
    EGNCPERIIT LTGPTNAIFK AFAMIIDKLE EDINSSMTNS TAASRPPVTL 100
    RLVVPATQCG SLIGKGGCKI KEIRESTGAQ VQVAGDMLPN STERAITIAG 150
    VPQSVTECVK QICLVMLETL SQSPQGRVMT IPYQPMPASS PVICAGGQDR 200
    CSDAAGYPHA THDLEGPPLD AYSIQGQHTI SPLDLAKLNQ VARQQSHFAM 250
    MHGGTGFAGI DSSSPEVKGY WASLDASTQT THELTIPNNL IGCIIGRQGA 300
    NINEIRQMSG AQIKIANPVE GSSGRQVTIT GSAASISLAQ YLINARLSSE 350
    KGMGCS 356
    Length:356
    Mass (Da):37,498
    Last modified:February 16, 2004 - v2
    Checksum:i6D1A261276CA206D
    GO

    Sequence cautioni

    The sequence CAA82631.1 differs from that shown. Reason: Frameshift at position 301.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti205 – 2051A → V in CAA55016. (PubMed:7607214)Curated
    Sequence conflicti299 – 3002Missing in CAA82631. (PubMed:8152927)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78137 mRNA. Translation: CAA55016.1.
    U24223 mRNA. Translation: AAA91317.1.
    Z29505 mRNA. Translation: CAA82631.1. Frameshift.
    BC039742 mRNA. Translation: AAH39742.1.
    CCDSiCCDS1898.1.
    RefSeqiNP_006187.2. NM_006196.3.
    UniGeneiHs.2853.

    Genome annotation databases

    EnsembliENST00000303577; ENSP00000305556; ENSG00000169564.
    GeneIDi5093.
    KEGGihsa:5093.
    UCSCiuc002sgf.3. human.

    Polymorphism databases

    DMDMi42560548.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78137 mRNA. Translation: CAA55016.1 .
    U24223 mRNA. Translation: AAA91317.1 .
    Z29505 mRNA. Translation: CAA82631.1 . Frameshift.
    BC039742 mRNA. Translation: AAH39742.1 .
    CCDSi CCDS1898.1.
    RefSeqi NP_006187.2. NM_006196.3.
    UniGenei Hs.2853.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WVN X-ray 2.10 A 279-356 [» ]
    1ZTG X-ray 3.00 A/B/C/D 14-85 [» ]
    3VKE X-ray 1.77 A/B/C/D 14-86 [» ]
    ProteinModelPortali Q15365.
    SMRi Q15365. Positions 11-169, 278-348.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111126. 85 interactions.
    DIPi DIP-38136N.
    IntActi Q15365. 53 interactions.
    MINTi MINT-96267.
    STRINGi 9606.ENSP00000305556.

    PTM databases

    PhosphoSitei Q15365.

    Polymorphism databases

    DMDMi 42560548.

    2D gel databases

    OGPi Q15365.
    REPRODUCTION-2DPAGE IPI00016610.
    UCD-2DPAGE Q15365.

    Proteomic databases

    MaxQBi Q15365.
    PaxDbi Q15365.
    PeptideAtlasi Q15365.
    PRIDEi Q15365.

    Protocols and materials databases

    DNASUi 5093.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303577 ; ENSP00000305556 ; ENSG00000169564 .
    GeneIDi 5093.
    KEGGi hsa:5093.
    UCSCi uc002sgf.3. human.

    Organism-specific databases

    CTDi 5093.
    GeneCardsi GC02P070314.
    HGNCi HGNC:8647. PCBP1.
    HPAi CAB037113.
    MIMi 601209. gene.
    neXtProti NX_Q15365.
    PharmGKBi PA32986.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG315872.
    HOGENOMi HOG000182823.
    HOVERGENi HBG053520.
    InParanoidi Q15365.
    KOi K12889.
    OMAi QDRCGDA.
    OrthoDBi EOG7P02J4.
    PhylomeDBi Q15365.
    TreeFami TF318292.

    Enzyme and pathway databases

    Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi PCBP1. human.
    EvolutionaryTracei Q15365.
    GeneWikii PCBP1.
    GenomeRNAii 5093.
    NextBioi 19644.
    PROi Q15365.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15365.
    Bgeei Q15365.
    CleanExi HS_PCBP1.
    Genevestigatori Q15365.

    Family and domain databases

    Gene3Di 3.30.1370.10. 3 hits.
    InterProi IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    [Graphical view ]
    Pfami PF00013. KH_1. 3 hits.
    [Graphical view ]
    SMARTi SM00322. KH. 3 hits.
    [Graphical view ]
    SUPFAMi SSF54791. SSF54791. 3 hits.
    PROSITEi PS50084. KH_TYPE_1. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterisation of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains."
      Leffers H., Dejgaard K., Celis J.E.
      Eur. J. Biochem. 230:447-453(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Identification of two KH domain proteins in the alpha-globin mRNP stability complex."
      Kiledjian M., Wang X., Liebhaber S.A.
      EMBO J. 14:4357-4364(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Tissue specific expression and cDNA structure of a human transcript encoding a nucleic acid binding [oligo(dC)] protein related to the pre-mRNA binding protein K."
      Aasheim H.-C., Loukianova T., Deggerdal A., Smeland E.B.
      Nucleic Acids Res. 22:959-964(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lymphocyte.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skin.
    5. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 47-70; 79-115; 125-160; 178-200; 298-306 AND 315-346, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-190, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Structure and RNA binding of the third KH domain of poly(C)-binding protein 1."
      Sidiqi M., Wilce J.A., Vivian J.P., Porter C.J., Barker A., Leedman P.J., Wilce M.C.
      Nucleic Acids Res. 33:1213-1221(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 279-356, RNA-BINDING.

    Entry informationi

    Entry nameiPCBP1_HUMAN
    AccessioniPrimary (citable) accession number: Q15365
    Secondary accession number(s): Q13157, Q14975
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: February 16, 2004
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3