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 |
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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 |
| ||
| Organism | Homo sapiens (Human) | ||
| 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. |
| Sequence processing | The displayed sequence is not processed. |
| 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 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. |
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 nucleusNon-traceable author statement. Source: UniProtKB ribonucleoprotein complexInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | RNA binding Ref.1 Ref.2 Ref.3 Inferred from direct assay. Source: UniProtKB protein bindingInferred from physical interaction. Source: IntAct single-stranded DNA binding Ref.3Inferred from direct assay. Source: UniProtKB |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| 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 |
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 | 63 | KH 1 | |||||||||||||||||||||||||||||
| Domain | 97 – 162 | 66 | KH 2 | |||||||||||||||||||||||||||||
| Domain | 279 – 343 | 65 | KH 3 | |||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||
| Modified residue | 173 | 1 | Phosphoserine | |||||||||||||||||||||||||||||
| Modified residue | 190 | 1 | Phosphoserine | |||||||||||||||||||||||||||||
| Modified residue | 246 | 1 | Phosphoserine | |||||||||||||||||||||||||||||
| Modified residue | 262 | 1 | Phosphoserine | |||||||||||||||||||||||||||||
| Modified residue | 263 | 1 | Phosphoserine | |||||||||||||||||||||||||||||
| Modified residue | 264 | 1 | Phosphoserine | |||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||
| Sequence conflict | 205 | 1 | A → V in CAA55016. Ref.1 | |||||||||||||||||||||||||||||
| Sequence conflict | 299 – 300 | 2 | Missing in CAA82631. Ref.3 | |||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||
| Beta strand | 14 – 21 | 8 | ||||||||||||||||||||||||||||||
| Helix | 22 – 28 | 7 | ||||||||||||||||||||||||||||||
| Helix | 34 – 43 | 10 | ||||||||||||||||||||||||||||||
| Beta strand | 46 – 49 | 4 | ||||||||||||||||||||||||||||||
| Beta strand | 55 – 64 | 10 | ||||||||||||||||||||||||||||||
| Helix | 65 – 80 | 16 | ||||||||||||||||||||||||||||||
| Beta strand | 280 – 287 | 8 | ||||||||||||||||||||||||||||||
| Helix | 288 – 290 | 3 | ||||||||||||||||||||||||||||||
| Helix | 291 – 295 | 5 | ||||||||||||||||||||||||||||||
| Helix | 297 – 299 | 3 | ||||||||||||||||||||||||||||||
| Helix | 300 – 309 | 10 | ||||||||||||||||||||||||||||||
| Beta strand | 312 – 315 | 4 | ||||||||||||||||||||||||||||||
| Beta strand | 323 – 331 | 9 | ||||||||||||||||||||||||||||||
| Helix | 333 – 346 | 14 | ||||||||||||||||||||||||||||||
Sequences
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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: 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. |
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 | |||||||||||||||||||
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| 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... | ||||||||||||||||||
Entry information
| Entry name | PCBP1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q15365 Secondary accession number(s): Q13157, Q14975 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
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 |

Clusters with


