Poly(rC)-binding protein 1 - Homo sapiens (Human)

Contribute

Send feedback

Reviewed, UniProtKB/Swiss-Prot Q15365 (PCBP1_HUMAN)

Last modified November 25, 2008. Version 85. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Poly(rC)-binding protein 1
Alternative name(s):
    Alpha-CP1
      Short name=hnRNP-E1
    Nucleic acid-binding protein SUB2.3

Gene names

Name:

PCBP1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

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 leucocytes 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.

Hide | Top

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	DNA-binding RNA-binding
Molecular function	Ribonucleoprotein
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	nuclear mRNA splicing, via spliceosome Inferred from Experiment. Source: Reactome
Cellular component	cytoplasm Non-traceable author statement. Source: UniProtKB nucleus Non-traceable author statement. Source: UniProtKB ribonucleoprotein complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	RNA binding Ref.1 Ref.2 Ref.3 Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct single-stranded DNA binding Ref.3 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct
PCBP2	Q15366	1	EBI-946095,EBI-945799
PTBP1	P26599	1	EBI-946095,EBI-350540
PUF60	Q9UHX1	1	EBI-946095,EBI-1053259
QKI	Q96PU8	1	EBI-946095,EBI-945792
TSC22D4	Q9Y3Q8	1	EBI-946095,EBI-739485
WBP11	Q9Y2W2	1	EBI-946095,EBI-714455

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 356

356

Poly(rC)-binding protein 1

PRO_0000050087

Regions

Domain

13 – 75

KH 1

Domain

97 – 162

KH 2

Domain

279 – 343

KH 3

Amino acid modifications

Modified residue

173

Phosphoserine

Modified residue

190

Phosphoserine

Modified residue

246

Phosphoserine

Modified residue

262

Phosphoserine

Modified residue

263

Phosphoserine

Modified residue

264

Phosphoserine

Experimental info

Sequence conflict

205

A → V in CAA55016. Ref.1

Sequence conflict

299 – 300

Missing in CAA82631. Ref.3

Secondary structure

356

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q15365-1 [UniParc].

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

FASTA

356

37,498

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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: 7607214] [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: 7556077] [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: 8152927] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[5]	Lubec G., Afjehi-Sadat L. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 326-346, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[6]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-246; SER-262; SER-263 AND SER-264, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, MASS SPECTROMETRY.
[11]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, MASS SPECTROMETRY.
[12]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-190, MASS SPECTROMETRY.
[13]	"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: 15731341] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 279-356, RNA-BINDING.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

X78137 mRNA. Translation: CAA55016.1.
U24223 mRNA. Translation: AAA91317.1.
Z29505 mRNA. Translation: CAA82631.1. Frameshift.
BC039742 mRNA. Translation: AAH39742.1.

RefSeq

NP_006187.1.

UniGene

Hs.2853

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15365.

PTM databases

PhosphoSite

Q15365.

2-D gel databases

OGP

Q15365.

REPRODUCTION-2DPAGE

IPI00016610.

Proteomic databases

PeptideAtlas

Q15365.

Genome annotation databases

Ensembl

ENSG00000169564. Homo sapiens. [Contig view]

GeneID

5093.

KEGG

hsa:5093.

Organism-specific databases

H-InvDB

HIX0023976.

HGNC

HGNC:8647. PCBP1.

MIM

601209. gene.

PharmGKB

PA32986.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

Q15365.

HOVERGEN

Q15365.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q15365.

CleanEx

HS_PCBP1.

GermOnline

ENSG00000169564. Homo sapiens.

Family and domain databases

InterPro

IPR004087. KH.
IPR004088. KH_type_1.
[Graphical view]

Pfam

PF00013. KH_1. 3 hits.
[Graphical view]

SMART

SM00322. KH. 3 hits.
[Graphical view]

PROSITE

PS50084. KH_TYPE_1. 3 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

Q15365.

NextBio

19644.

SOURCE

Search...

Hide | Top

Entry information

Entry name

PCBP1_HUMAN

Accession

Primary (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:	November 25, 2008
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Human chromosome 2

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents