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Q15365 (PCBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PCBP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

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

Tissue specificity

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.

Post-translational modification

Phosphorylated; lowers poly(rC)-binding activity.

Sequence similarities

Contains 3 KH domains.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Poly(rC)-binding protein 1
PRO_0000050087

Regions

Domain13 – 7563KH 1
Domain97 – 16266KH 2
Domain279 – 34365KH 3

Amino acid modifications

Modified residue11N-acetylmethionine Ref.17
Modified residue1731Phosphoserine Ref.7 Ref.10 Ref.13 Ref.14 Ref.16
Modified residue1901Phosphoserine Ref.10 Ref.13

Experimental info

Sequence conflict2051A → V in CAA55016. Ref.1
Sequence conflict299 – 3002Missing in CAA82631. Ref.3

Secondary structure

.......................... 356
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15365 [UniParc].

Last modified February 16, 2004. Version 2.
Checksum: 6D1A261276CA206D

FASTA35637,498
        10         20         30         40         50         60 
MDAGVTESGL NVTLTIRLLM HGKEVGSIIG KKGESVKRIR EESGARINIS EGNCPERIIT 

        70         80         90        100        110        120 
LTGPTNAIFK AFAMIIDKLE EDINSSMTNS TAASRPPVTL RLVVPATQCG SLIGKGGCKI 

       130        140        150        160        170        180 
KEIRESTGAQ VQVAGDMLPN STERAITIAG VPQSVTECVK QICLVMLETL SQSPQGRVMT 

       190        200        210        220        230        240 
IPYQPMPASS PVICAGGQDR CSDAAGYPHA THDLEGPPLD AYSIQGQHTI SPLDLAKLNQ 

       250        260        270        280        290        300 
VARQQSHFAM MHGGTGFAGI DSSSPEVKGY WASLDASTQT THELTIPNNL IGCIIGRQGA 

       310        320        330        340        350 
NINEIRQMSG AQIKIANPVE GSSGRQVTIT GSAASISLAQ YLINARLSSE KGMGCS 

« Hide

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78137 mRNA. Translation: CAA55016.1.
U24223 mRNA. Translation: AAA91317.1.
Z29505 mRNA. Translation: CAA82631.1. Frameshift.
BC039742 mRNA. Translation: AAH39742.1.
CCDSCCDS1898.1.
RefSeqNP_006187.2. NM_006196.3.
UniGeneHs.2853.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WVNX-ray2.10A279-356[»]
1ZTGX-ray3.00A/B/C/D14-85[»]
3VKEX-ray1.77A/B/C/D14-86[»]
ProteinModelPortalQ15365.
SMRQ15365. Positions 11-169, 278-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111126. 85 interactions.
DIPDIP-38136N.
IntActQ15365. 52 interactions.
MINTMINT-96267.
STRING9606.ENSP00000305556.

PTM databases

PhosphoSiteQ15365.

Polymorphism databases

DMDM42560548.

2D gel databases

OGPQ15365.
REPRODUCTION-2DPAGEIPI00016610.
UCD-2DPAGEQ15365.

Proteomic databases

MaxQBQ15365.
PaxDbQ15365.
PeptideAtlasQ15365.
PRIDEQ15365.

Protocols and materials databases

DNASU5093.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303577; ENSP00000305556; ENSG00000169564.
GeneID5093.
KEGGhsa:5093.
UCSCuc002sgf.3. human.

Organism-specific databases

CTD5093.
GeneCardsGC02P070314.
HGNCHGNC:8647. PCBP1.
HPACAB037113.
MIM601209. gene.
neXtProtNX_Q15365.
PharmGKBPA32986.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG315872.
HOGENOMHOG000182823.
HOVERGENHBG053520.
InParanoidQ15365.
KOK12889.
OMAQDRCGDA.
OrthoDBEOG7P02J4.
PhylomeDBQ15365.
TreeFamTF318292.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ15365.
BgeeQ15365.
CleanExHS_PCBP1.
GenevestigatorQ15365.

Family and domain databases

Gene3D3.30.1370.10. 3 hits.
InterProIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamPF00013. KH_1. 3 hits.
[Graphical view]
SMARTSM00322. KH. 3 hits.
[Graphical view]
SUPFAMSSF54791. SSF54791. 3 hits.
PROSITEPS50084. KH_TYPE_1. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPCBP1. human.
EvolutionaryTraceQ15365.
GeneWikiPCBP1.
GenomeRNAi5093.
NextBio19644.
PROQ15365.
SOURCESearch...

Entry information

Entry namePCBP1_HUMAN
AccessionPrimary (citable) accession number: Q15365
Secondary accession number(s): Q13157, Q14975
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 16, 2004
Last modified: July 9, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM