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Q15365

- PCBP1_HUMAN

UniProt

Q15365 - PCBP1_HUMAN

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Protein

Poly(rC)-binding protein 1

Gene

PCBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. RNA binding Source: UniProtKB
  3. single-stranded DNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA splicing, via spliceosome Source: Reactome
  3. RNA splicing Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PCBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:8647. PCBP1.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: UniProtKB
  3. membrane Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. ribonucleoprotein complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32986.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Poly(rC)-binding protein 1PRO_0000050087Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei173 – 1731Phosphoserine5 Publications
Modified residuei190 – 1901Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated; lowers poly(rC)-binding activity.5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15365.
PaxDbiQ15365.
PeptideAtlasiQ15365.
PRIDEiQ15365.

2D gel databases

OGPiQ15365.
REPRODUCTION-2DPAGEIPI00016610.
UCD-2DPAGEQ15365.

PTM databases

PhosphoSiteiQ15365.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiQ15365.
CleanExiHS_PCBP1.
ExpressionAtlasiQ15365. baseline and differential.
GenevestigatoriQ15365.

Organism-specific databases

HPAiCAB037113.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
GAMMAHV.ORF34O419514EBI-946095,EBI-9640556From a different organism.
PCBP2Q153662EBI-946095,EBI-945799
PPIGQ134272EBI-946095,EBI-396072
PRPF8Q6P2Q92EBI-946095,EBI-538479
PTBP1P265992EBI-946095,EBI-350540
PUF60Q9UHX12EBI-946095,EBI-1053259
QKIQ96PU82EBI-946095,EBI-945792
THAP11Q96EK44EBI-946095,EBI-1790529
TSC22D4Q9Y3Q82EBI-946095,EBI-739485
WBP11Q9Y2W22EBI-946095,EBI-714455
ZNF830Q96NB32EBI-946095,EBI-3920997

Protein-protein interaction databases

BioGridi111126. 98 interactions.
DIPiDIP-38136N.
IntActiQ15365. 54 interactions.
MINTiMINT-96267.
STRINGi9606.ENSP00000305556.

Structurei

Secondary structure

1
356
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 218Combined sources
Helixi22 – 298Combined sources
Helixi31 – 333Combined sources
Helixi34 – 4310Combined sources
Beta strandi46 – 494Combined sources
Beta strandi55 – 6410Combined sources
Helixi65 – 8117Combined sources
Turni82 – 843Combined sources
Beta strandi280 – 2878Combined sources
Helixi288 – 2903Combined sources
Helixi291 – 2955Combined sources
Helixi297 – 2993Combined sources
Helixi300 – 30910Combined sources
Beta strandi312 – 3154Combined sources
Beta strandi323 – 3319Combined sources
Helixi333 – 34614Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WVNX-ray2.10A279-356[»]
1ZTGX-ray3.00A/B/C/D14-85[»]
3VKEX-ray1.77A/B/C/D14-86[»]
ProteinModelPortaliQ15365.
SMRiQ15365. Positions 11-169, 278-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15365.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 7563KH 1PROSITE-ProRule annotationAdd
BLAST
Domaini97 – 16266KH 2PROSITE-ProRule annotationAdd
BLAST
Domaini279 – 34365KH 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 KH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG315872.
HOGENOMiHOG000182823.
HOVERGENiHBG053520.
InParanoidiQ15365.
KOiK12889.
OMAiQDRCGDA.
OrthoDBiEOG7P02J4.
PhylomeDBiQ15365.
TreeFamiTF318292.

Family and domain databases

Gene3Di3.30.1370.10. 3 hits.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamiPF00013. KH_1. 3 hits.
[Graphical view]
SMARTiSM00322. KH. 3 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 3 hits.
PROSITEiPS50084. KH_TYPE_1. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15365-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDAGVTESGL NVTLTIRLLM HGKEVGSIIG KKGESVKRIR EESGARINIS
60 70 80 90 100
EGNCPERIIT LTGPTNAIFK AFAMIIDKLE EDINSSMTNS TAASRPPVTL
110 120 130 140 150
RLVVPATQCG SLIGKGGCKI KEIRESTGAQ VQVAGDMLPN STERAITIAG
160 170 180 190 200
VPQSVTECVK QICLVMLETL SQSPQGRVMT IPYQPMPASS PVICAGGQDR
210 220 230 240 250
CSDAAGYPHA THDLEGPPLD AYSIQGQHTI SPLDLAKLNQ VARQQSHFAM
260 270 280 290 300
MHGGTGFAGI DSSSPEVKGY WASLDASTQT THELTIPNNL IGCIIGRQGA
310 320 330 340 350
NINEIRQMSG AQIKIANPVE GSSGRQVTIT GSAASISLAQ YLINARLSSE

KGMGCS
Length:356
Mass (Da):37,498
Last modified:February 16, 2004 - v2
Checksum:i6D1A261276CA206D
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti205 – 2051A → V in CAA55016. (PubMed:7607214)Curated
Sequence conflicti299 – 3002Missing in CAA82631. (PubMed:8152927)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78137 mRNA. Translation: CAA55016.1.
U24223 mRNA. Translation: AAA91317.1.
Z29505 mRNA. Translation: CAA82631.1. Frameshift.
BC039742 mRNA. Translation: AAH39742.1.
CCDSiCCDS1898.1.
RefSeqiNP_006187.2. NM_006196.3.
UniGeneiHs.2853.

Genome annotation databases

EnsembliENST00000303577; ENSP00000305556; ENSG00000169564.
GeneIDi5093.
KEGGihsa:5093.
UCSCiuc002sgf.3. human.

Polymorphism databases

DMDMi42560548.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78137 mRNA. Translation: CAA55016.1 .
U24223 mRNA. Translation: AAA91317.1 .
Z29505 mRNA. Translation: CAA82631.1 . Frameshift.
BC039742 mRNA. Translation: AAH39742.1 .
CCDSi CCDS1898.1.
RefSeqi NP_006187.2. NM_006196.3.
UniGenei Hs.2853.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali Q15365.
SMRi Q15365. Positions 11-169, 278-348.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111126. 98 interactions.
DIPi DIP-38136N.
IntActi Q15365. 54 interactions.
MINTi MINT-96267.
STRINGi 9606.ENSP00000305556.

PTM databases

PhosphoSitei Q15365.

Polymorphism databases

DMDMi 42560548.

2D gel databases

OGPi Q15365.
REPRODUCTION-2DPAGE IPI00016610.
UCD-2DPAGE Q15365.

Proteomic databases

MaxQBi Q15365.
PaxDbi Q15365.
PeptideAtlasi Q15365.
PRIDEi Q15365.

Protocols and materials databases

DNASUi 5093.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000303577 ; ENSP00000305556 ; ENSG00000169564 .
GeneIDi 5093.
KEGGi hsa:5093.
UCSCi uc002sgf.3. human.

Organism-specific databases

CTDi 5093.
GeneCardsi GC02P070314.
HGNCi HGNC:8647. PCBP1.
HPAi CAB037113.
MIMi 601209. gene.
neXtProti NX_Q15365.
PharmGKBi PA32986.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG315872.
HOGENOMi HOG000182823.
HOVERGENi HBG053520.
InParanoidi Q15365.
KOi K12889.
OMAi QDRCGDA.
OrthoDBi EOG7P02J4.
PhylomeDBi Q15365.
TreeFami TF318292.

Enzyme and pathway databases

Reactomei REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi PCBP1. human.
EvolutionaryTracei Q15365.
GeneWikii PCBP1.
GenomeRNAii 5093.
NextBioi 19644.
PROi Q15365.
SOURCEi Search...

Gene expression databases

Bgeei Q15365.
CleanExi HS_PCBP1.
ExpressionAtlasi Q15365. baseline and differential.
Genevestigatori Q15365.

Family and domain databases

Gene3Di 3.30.1370.10. 3 hits.
InterProi IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view ]
Pfami PF00013. KH_1. 3 hits.
[Graphical view ]
SMARTi SM00322. KH. 3 hits.
[Graphical view ]
SUPFAMi SSF54791. SSF54791. 3 hits.
PROSITEi PS50084. KH_TYPE_1. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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.

Entry informationi

Entry nameiPCBP1_HUMAN
AccessioniPrimary (citable) accession number: Q15365
Secondary accession number(s): Q13157, Q14975
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 16, 2004
Last modified: November 26, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3