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

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Q15365 (PCBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 133. History...

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

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

PCBP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

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

Binary interactions

With	Entry	#Exp.	IntAct
PCBP2	Q15366	2	EBI-946095,EBI-945799
PTBP1	P26599	2	EBI-946095,EBI-350540
PUF60	Q9UHX1	2	EBI-946095,EBI-1053259
QKI	Q96PU8	2	EBI-946095,EBI-945792
TSC22D4	Q9Y3Q8	2	EBI-946095,EBI-739485
WBP11	Q9Y2W2	2	EBI-946095,EBI-714455

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 Ref.7 Ref.10 Ref.12 Ref.13 Ref.15

Modified residue

190

Phosphoserine Ref.10 Ref.12

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...

Sequences

Sequence

Length

Mass (Da)

Tools

Q15365 [UniParc].

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

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] [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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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].
[12]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"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, MASS SPECTROMETRY.
[16]	"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.

IPI

IPI00016610.

RefSeq

NP_006187.2. NM_006196.3.

UniGene

Hs.2853.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q15365.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38136N.

IntAct

Q15365. 37 interactions.

MINT

MINT-96267.

STRING

9606.ENSP00000305556.

PTM databases

PhosphoSite

Q15365.

Polymorphism databases

DMDM

42560548.

2D gel databases

OGP

Q15365.

REPRODUCTION-2DPAGE

IPI00016610.

UCD-2DPAGE

Q15365.

Proteomic databases

PaxDb

Q15365.

PeptideAtlas

Q15365.

PRIDE

Q15365.

Protocols and materials databases

DNASU

5093.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000303577; ENSP00000305556; ENSG00000169564.

GeneID

5093.

KEGG

hsa:5093.

UCSC

uc002sgf.3. human.

Organism-specific databases

CTD

5093.

GeneCards

GC02P070314.

HGNC

HGNC:8647. PCBP1.

HPA

CAB037113.

MIM

601209. gene.

neXtProt

NX_Q15365.

PharmGKB

PA32986.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG315872.

HOGENOM

HOG000182823.

HOVERGEN

HBG053520.

InParanoid

Q15365.

K12889.

OMA

RNISERN.

OrthoDB

EOG46WZ8K.

PhylomeDB

Q15365.

Enzyme and pathway databases

Reactome

REACT_1675. mRNA Processing.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q15365.

Bgee

Q15365.

CleanEx

HS_PCBP1.

Genevestigator

Q15365.

GermOnline

ENSG00000169564. Homo sapiens.

Family and domain databases

InterPro

IPR004087. KH_dom.
IPR004088. KH_dom_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

ChiTaRS

PCBP1. human.

EvolutionaryTrace

Q15365.

GenomeRNAi

5093.

NextBio

19644.

SOURCE

Search...

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:	May 1, 2013
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

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

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

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

Polymorphism databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents