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UniProtKB/Swiss-Prot entry Q15365


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PCBP1_HUMAN
Primary accession number Q15365
Secondary accession numbers Q13157 Q14975
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on February 16, 2004 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 83)
Name and origin of the protein
Protein name Poly(rC)-binding protein 1
Synonyms Alpha-CP1
hnRNP-E1
Nucleic acid-binding protein SUB2.3
Gene name
Name: PCBP1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7607214 [NCBI, ExPASy, EBI, Israel, Japan]
Leffers H., Dejgaard K., Celis J.E.;
"Characterisation of two major cellular poly(rC)-binding human proteins, each containing three K-homologous (KH) domains.";
Eur. J. Biochem. 230:447-453(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7556077 [NCBI, ExPASy, EBI, Israel, Japan]
Kiledjian M., Wang X., Liebhaber S.A.;
"Identification of two KH domain proteins in the alpha-globin mRNP stability complex.";
EMBO J. 14:4357-4364(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lymphocyte;
DOI=10.1093/nar/22.6.959; PubMed=8152927 [NCBI, ExPASy, EBI, Israel, Japan]
Aasheim H.-C., Loukianova T., Deggerdal A., Smeland E.B.;
"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.";
Nucleic Acids Res. 22:959-964(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 326-346, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-246; SER-262; SER-263 AND SER-264, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"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.";
J. Proteome Res. 6:4150-4162(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X78137; CAA55016.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U24223; AAA91317.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z29505; CAA82631.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC039742; AAH39742.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_006187.1; -.
UniGene Hs.2853
3D structure databases
PDB
1WVN; X-ray; 2.10 A; A=279-356.[ExPASy / RCSB / EBI]
1ZTG; X-ray; 3.00 A; A/B/C/D=14-85.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1WVN; -.
1ZTG; -.
ModBase Q15365.
Protein-protein interaction databases
IntAct Q15365; -.
PTM databases
PhosphoSite Q15365; -.
Enzyme and pathway databases
Reactome REACT_1675; mRNA Processing.
REACT_6167; Influenza Infection.
REACT_71; Gene Expression.
2D gel databases
OGP Q15365; -.
REPRODUCTION-2DPAGE IPI00016610; -.
Organism-specific databases
H-InvDB HIX0023976; -.
HGNC HGNC:8647; PCBP1.
GenAtlas PCBP1.
MIM 601209; gene. [NCBI / EBI]
PharmGKB PA32986; -.
GeneCards Q15365.
Gene expression databases
ArrayExpress Q15365; -.
CleanEx HS_PCBP1; -.
GermOnline ENSG00000169564; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (non-traceable author statement from UniProtKB).
GO:0005634; Cellular component: nucleus (non-traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003723; Molecular function: RNA binding (inferred from direct assay from UniProtKB).
GO:0003697; Molecular function: single-stranded DNA binding (inferred from direct assay from UniProtKB).
GO:0000398; Biological process: nuclear mRNA splicing, via spliceosome (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR004087; KH.
IPR004088; KH_type_1.
Graphical view of domain structure.
Pfam PF00013; KH_1; 3.
Pfam graphical view of domain structure.
SMART SM00322; KH; 3.
SMART graphical view of domain structure.
PROSITE PS50084; KH_TYPE_1; 3.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q15365.
Proteomic databases
PeptideAtlas Q15365; -.
Genome annotation databases
Ensembl ENSG00000169564; Homo sapiens. [Contig view]
GeneID 5093; -.
KEGG hsa:5093; -.
Phylogenomic databases
HOGENOM Q15365; -.
HOVERGEN Q15365; -.
Other
LinkHub Q15365; -.
SOURCE PCBP1; Homo sapiens.
ProtoNet Q15365.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Repeat; Ribonucleoprotein; RNA-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   356  356     Poly(rC)-binding protein 1. PRO_0000050087
DOMAIN   13    75  63     KH 1. 
DOMAIN   97   162  66     KH 2. 
DOMAIN   279   343  65     KH 3. 
MOD_RES   173   173        Phosphoserine. 
MOD_RES   190   190        Phosphoserine. 
MOD_RES   246   246        Phosphoserine. 
MOD_RES   262   262        Phosphoserine. 
MOD_RES   263   263        Phosphoserine. 
MOD_RES   264   264        Phosphoserine. 
CONFLICT   205   205        A -> V (in Ref. 1; CAA55016). 
CONFLICT   299   300        Missing (in Ref. 3; CAA82631). 
STRAND   14    21  8      
HELIX   22    28  7      
HELIX   34    43  10      
STRAND   46    49  4      
STRAND   55    64  10      
HELIX   65    80  16      
STRAND   280   287  8      
HELIX   288   290  3      
HELIX   291   295  5      
HELIX   297   299  3      
HELIX   300   309  10      
STRAND   312   315  4      
STRAND   323   331  9      
HELIX   333   346  14      
Sequence information
Length: 356 AA [This is the length of the unprocessed precursor] Molecular weight: 37498 Da [This is the MW of the unprocessed precursor] CRC64: 6D1A261276CA206D [This is a checksum on the sequence]
        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 

Q15365 in FASTA format

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View entry in raw text format (no links)
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