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Protein

Poly(rC)-binding protein 2

Gene

PCBP2

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

Functioni

Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. Major cellular poly(rC)-binding protein. Binds also poly(rU). Negatively regulates cellular antiviral responses mediated by MAVS signaling (PubMed:19881509). It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation (PubMed:19881509). In case of infection by poliovirus, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation (PubMed:12414943). Also plays a role in initiation of viral RNA replication in concert with the viral protein 3CD (PubMed:12414943).2 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • enzyme binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • defense response to virus Source: UniProtKB-KW
  • gene expression Source: Reactome
  • innate immune response Source: Reactome
  • mRNA metabolic process Source: UniProtKB
  • mRNA splicing, via spliceosome Source: Reactome
  • negative regulation of defense response to virus Source: UniProtKB
  • negative regulation of type I interferon production Source: Reactome
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • RNA splicing Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity, Viral RNA replication

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(rC)-binding protein 2
Alternative name(s):
Alpha-CP2
Heterogeneous nuclear ribonucleoprotein E2
Short name:
hnRNP E2
Gene namesi
Name:PCBP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:8648. PCBP2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32987.

Polymorphism and mutation databases

BioMutaiPCBP2.
DMDMi6707736.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 365365Poly(rC)-binding protein 2PRO_0000050090Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei173 – 1731PhosphoserineCombined sources
Modified residuei189 – 1891PhosphoserineCombined sources
Modified residuei272 – 2721PhosphoserineCombined sources
Modified residuei364 – 3641PhosphoserineCombined sources
Modified residuei365 – 3651PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated. The non-phosphorylated form(s) exhibited the strongest poly(rC)-binding activity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ15366.
MaxQBiQ15366.
PaxDbiQ15366.
PeptideAtlasiQ15366.
PRIDEiQ15366.

PTM databases

iPTMnetiQ15366.
PhosphoSiteiQ15366.
SwissPalmiQ15366.

Expressioni

Tissue specificityi

Detected in all tissues examined.

Gene expression databases

BgeeiQ15366.
CleanExiHS_PCBP2.
ExpressionAtlasiQ15366. baseline and differential.
GenevisibleiQ15366. HS.

Organism-specific databases

HPAiHPA038356.

Interactioni

Subunit structurei

Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Interacts with IFIH1 and RNF135. Interacts with MAVS (via C-terminus) and ITCH (via WW domains).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PCBP1Q153652EBI-945799,EBI-946095
SNRPAP090123EBI-945799,EBI-607085
SRSF3P841033EBI-945799,EBI-372557

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111127. 90 interactions.
DIPiDIP-58934N.
IntActiQ15366. 44 interactions.
MINTiMINT-96192.
STRINGi9606.ENSP00000352438.

Structurei

Secondary structure

1
365
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 – 639Combined sources
Helixi65 – 8016Combined sources
Beta strandi89 – 913Combined sources
Beta strandi97 – 1059Combined sources
Helixi106 – 1138Combined sources
Helixi115 – 1173Combined sources
Helixi118 – 12710Combined sources
Beta strandi128 – 1314Combined sources
Beta strandi143 – 1508Combined sources
Helixi152 – 16817Combined sources
Beta strandi288 – 2958Combined sources
Helixi296 – 3038Combined sources
Helixi305 – 3073Combined sources
Helixi308 – 31710Combined sources
Beta strandi320 – 3234Combined sources
Beta strandi331 – 3399Combined sources
Helixi341 – 35515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AXYX-ray1.70A/B/C/D11-82[»]
2JZXNMR-A11-169[»]
2P2RX-ray1.60A285-359[»]
2PQUX-ray2.12A/B/C/D11-82[»]
2PY9X-ray2.56A/B/C/D11-82[»]
ProteinModelPortaliQ15366.
SMRiQ15366. Positions 11-169, 286-358.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15366.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 7563KH 1PROSITE-ProRule annotationAdd
BLAST
Domaini97 – 16266KH 2PROSITE-ProRule annotationAdd
BLAST
Domaini287 – 35165KH 3PROSITE-ProRule annotationAdd
BLAST

Domaini

The KH domains mediates poly(C) binding.

Sequence similaritiesi

Contains 3 KH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2190. Eukaryota.
ENOG410XNN8. LUCA.
GeneTreeiENSGT00760000119144.
HOGENOMiHOG000182823.
HOVERGENiHBG053520.
InParanoidiQ15366.
KOiK13162.
OMAiPIAPGNQ.
OrthoDBiEOG7P02J4.
PhylomeDBiQ15366.
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]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15366-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDTGVIEGGL NVTLTIRLLM HGKEVGSIIG KKGESVKKMR EESGARINIS
60 70 80 90 100
EGNCPERIIT LAGPTNAIFK AFAMIIDKLE EDISSSMTNS TAASRPPVTL
110 120 130 140 150
RLVVPASQCG SLIGKGGCKI KEIRESTGAQ VQVAGDMLPN STERAITIAG
160 170 180 190 200
IPQSIIECVK QICVVMLETL SQSPPKGVTI PYRPKPSSSP VIFAGGQDRY
210 220 230 240 250
STGSDSASFP HTTPSMCLNP DLEGPPLEAY TIQGQYAIPQ PDLTKLHQLA
260 270 280 290 300
MQQSHFPMTH GNTGFSGIES SSPEVKGYWG LDASAQTTSH ELTIPNDLIG
310 320 330 340 350
CIIGRQGAKI NEIRQMSGAQ IKIANPVEGS TDRQVTITGS AASISLAQYL
360
INVRLSSETG GMGSS
Length:365
Mass (Da):38,580
Last modified:November 1, 1996 - v1
Checksum:i43F035D76FDC2C63
GO
Isoform 2 (identifier: Q15366-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     279-279: W → WA

Note: No experimental confirmation available.
Show »
Length:366
Mass (Da):38,651
Checksum:i3464C973504D90DE
GO
Isoform 3 (identifier: Q15366-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     169-172: Missing.
     279-279: W → WA

Show »
Length:362
Mass (Da):38,222
Checksum:i70C8AF710E3BF3C0
GO
Isoform 4 (identifier: Q15366-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     169-172: Missing.
     198-228: Missing.
     279-279: W → WA

Note: No experimental confirmation available.
Show »
Length:331
Mass (Da):34,917
Checksum:iE831D4BF718C26E3
GO
Isoform 5 (identifier: Q15366-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     198-228: Missing.
     279-279: W → WA

Note: No experimental confirmation available.
Show »
Length:335
Mass (Da):35,347
Checksum:iBD1A8AA65EABF0BF
GO
Isoform 6 (identifier: Q15366-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     169-172: Missing.

Note: No experimental confirmation available.
Show »
Length:361
Mass (Da):38,151
Checksum:i4F96378919BF3215
GO
Isoform 7 (identifier: Q15366-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     169-172: Missing.
     198-228: Missing.
     267-279: GIESSSPEVKGYW → A

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:318
Mass (Da):33,497
Checksum:iB5B41191CFD1B171
GO
Isoform 8 (identifier: Q15366-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     198-228: Missing.
     267-279: GIESSSPEVKGYW → A

Note: No experimental confirmation available.
Show »
Length:322
Mass (Da):33,926
Checksum:i7DDD51D4F8BEB977
GO

Sequence cautioni

The sequence BAD92062.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei169 – 1724Missing in isoform 3, isoform 4, isoform 6 and isoform 7. 4 PublicationsVSP_043161
Alternative sequencei198 – 22831Missing in isoform 4, isoform 5, isoform 7 and isoform 8. 3 PublicationsVSP_043362Add
BLAST
Alternative sequencei267 – 27913GIESS…VKGYW → A in isoform 7 and isoform 8. 1 PublicationVSP_054045Add
BLAST
Alternative sequencei279 – 2791W → WA in isoform 2, isoform 3, isoform 4 and isoform 5. 3 PublicationsVSP_042833

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78136 mRNA. Translation: CAA55015.1.
AB188306 mRNA. Translation: BAD36897.1.
AK292141 mRNA. Translation: BAF84830.1.
AK302067 mRNA. Translation: BAG63457.1.
AB208825 mRNA. Translation: BAD92062.1. Different initiation.
AC023509 Genomic DNA. No translation available.
AC068889 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96706.1.
CH471054 Genomic DNA. Translation: EAW96707.1.
CH471054 Genomic DNA. Translation: EAW96709.1.
CH471054 Genomic DNA. Translation: EAW96711.1.
BC001155 mRNA. Translation: AAH01155.1.
BC071942 mRNA. Translation: AAH71942.1.
BC107688 mRNA. Translation: AAI07689.1.
CCDSiCCDS44900.1. [Q15366-2]
CCDS44901.1. [Q15366-1]
CCDS44902.1. [Q15366-5]
CCDS44903.1. [Q15366-4]
CCDS44904.1. [Q15366-7]
CCDS55830.1. [Q15366-6]
CCDS8859.1. [Q15366-3]
PIRiS65679. S42471.
RefSeqiNP_001092090.1. NM_001098620.2. [Q15366-4]
NP_001122383.1. NM_001128911.1. [Q15366-1]
NP_001122384.1. NM_001128912.1. [Q15366-6]
NP_001122385.1. NM_001128913.1. [Q15366-5]
NP_001122386.1. NM_001128914.1. [Q15366-7]
NP_005007.2. NM_005016.5. [Q15366-2]
NP_114366.1. NM_031989.4. [Q15366-3]
UniGeneiHs.546271.

Genome annotation databases

EnsembliENST00000359282; ENSP00000352228; ENSG00000197111. [Q15366-4]
ENST00000359462; ENSP00000352438; ENSG00000197111. [Q15366-2]
ENST00000437231; ENSP00000390304; ENSG00000197111. [Q15366-7]
ENST00000439930; ENSP00000408949; ENSG00000197111. [Q15366-1]
ENST00000447282; ENSP00000394116; ENSG00000197111. [Q15366-5]
ENST00000455667; ENSP00000388008; ENSG00000197111. [Q15366-7]
ENST00000546463; ENSP00000448762; ENSG00000197111. [Q15366-3]
ENST00000548933; ENSP00000449062; ENSG00000197111. [Q15366-5]
ENST00000552296; ENSP00000448927; ENSG00000197111. [Q15366-6]
ENST00000552819; ENSP00000449070; ENSG00000197111. [Q15366-8]
GeneIDi5094.
KEGGihsa:5094.
UCSCiuc001sdb.5. human. [Q15366-1]
uc058oqk.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78136 mRNA. Translation: CAA55015.1.
AB188306 mRNA. Translation: BAD36897.1.
AK292141 mRNA. Translation: BAF84830.1.
AK302067 mRNA. Translation: BAG63457.1.
AB208825 mRNA. Translation: BAD92062.1. Different initiation.
AC023509 Genomic DNA. No translation available.
AC068889 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96706.1.
CH471054 Genomic DNA. Translation: EAW96707.1.
CH471054 Genomic DNA. Translation: EAW96709.1.
CH471054 Genomic DNA. Translation: EAW96711.1.
BC001155 mRNA. Translation: AAH01155.1.
BC071942 mRNA. Translation: AAH71942.1.
BC107688 mRNA. Translation: AAI07689.1.
CCDSiCCDS44900.1. [Q15366-2]
CCDS44901.1. [Q15366-1]
CCDS44902.1. [Q15366-5]
CCDS44903.1. [Q15366-4]
CCDS44904.1. [Q15366-7]
CCDS55830.1. [Q15366-6]
CCDS8859.1. [Q15366-3]
PIRiS65679. S42471.
RefSeqiNP_001092090.1. NM_001098620.2. [Q15366-4]
NP_001122383.1. NM_001128911.1. [Q15366-1]
NP_001122384.1. NM_001128912.1. [Q15366-6]
NP_001122385.1. NM_001128913.1. [Q15366-5]
NP_001122386.1. NM_001128914.1. [Q15366-7]
NP_005007.2. NM_005016.5. [Q15366-2]
NP_114366.1. NM_031989.4. [Q15366-3]
UniGeneiHs.546271.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AXYX-ray1.70A/B/C/D11-82[»]
2JZXNMR-A11-169[»]
2P2RX-ray1.60A285-359[»]
2PQUX-ray2.12A/B/C/D11-82[»]
2PY9X-ray2.56A/B/C/D11-82[»]
ProteinModelPortaliQ15366.
SMRiQ15366. Positions 11-169, 286-358.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111127. 90 interactions.
DIPiDIP-58934N.
IntActiQ15366. 44 interactions.
MINTiMINT-96192.
STRINGi9606.ENSP00000352438.

PTM databases

iPTMnetiQ15366.
PhosphoSiteiQ15366.
SwissPalmiQ15366.

Polymorphism and mutation databases

BioMutaiPCBP2.
DMDMi6707736.

Proteomic databases

EPDiQ15366.
MaxQBiQ15366.
PaxDbiQ15366.
PeptideAtlasiQ15366.
PRIDEiQ15366.

Protocols and materials databases

DNASUi5094.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359282; ENSP00000352228; ENSG00000197111. [Q15366-4]
ENST00000359462; ENSP00000352438; ENSG00000197111. [Q15366-2]
ENST00000437231; ENSP00000390304; ENSG00000197111. [Q15366-7]
ENST00000439930; ENSP00000408949; ENSG00000197111. [Q15366-1]
ENST00000447282; ENSP00000394116; ENSG00000197111. [Q15366-5]
ENST00000455667; ENSP00000388008; ENSG00000197111. [Q15366-7]
ENST00000546463; ENSP00000448762; ENSG00000197111. [Q15366-3]
ENST00000548933; ENSP00000449062; ENSG00000197111. [Q15366-5]
ENST00000552296; ENSP00000448927; ENSG00000197111. [Q15366-6]
ENST00000552819; ENSP00000449070; ENSG00000197111. [Q15366-8]
GeneIDi5094.
KEGGihsa:5094.
UCSCiuc001sdb.5. human. [Q15366-1]
uc058oqk.1. human.

Organism-specific databases

CTDi5094.
GeneCardsiPCBP2.
HGNCiHGNC:8648. PCBP2.
HPAiHPA038356.
MIMi601210. gene.
neXtProtiNX_Q15366.
PharmGKBiPA32987.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2190. Eukaryota.
ENOG410XNN8. LUCA.
GeneTreeiENSGT00760000119144.
HOGENOMiHOG000182823.
HOVERGENiHBG053520.
InParanoidiQ15366.
KOiK13162.
OMAiPIAPGNQ.
OrthoDBiEOG7P02J4.
PhylomeDBiQ15366.
TreeFamiTF318292.

Enzyme and pathway databases

ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.

Miscellaneous databases

ChiTaRSiPCBP2. human.
EvolutionaryTraceiQ15366.
GeneWikiiPCBP2.
GenomeRNAii5094.
NextBioi19648.
PROiQ15366.
SOURCEiSearch...

Gene expression databases

BgeeiQ15366.
CleanExiHS_PCBP2.
ExpressionAtlasiQ15366. baseline and differential.
GenevisibleiQ15366. HS.

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]
ProtoNetiSearch...

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] (ISOFORM 1).
  2. "Homo sapiens mRNA."
    Sugiyama A., Inoue H., Oka M.
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 8).
    Tissue: Synovium and Testis.
  4. "Homo sapiens protein coding cDNA."
    Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
    Tissue: Brain.
  5. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORMS 1; 3 AND 5).
    Tissue: Eye, Lung and Mammary gland.
  8. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 47-70; 102-115; 145-160 AND 323-354, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  9. "Distinct poly(rC) binding protein KH domain determinants for poliovirus translation initiation and viral RNA replication."
    Walter B.L., Parsley T.B., Ehrenfeld E., Semler B.L.
    J. Virol. 76:12008-12022(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "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.
  11. "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.
  12. "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.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4."
    You F., Sun H., Zhou X., Sun W., Liang S., Zhai Z., Jiang Z.
    Nat. Immunol. 10:1300-1308(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IFIH1; RNF135; MAVS AND ITCH.
  16. "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
    Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
    RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "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-189, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "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; SER-189 AND SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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; SER-364 AND SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Crystal structure of the first KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.7 A."
    Du Z., Lee J.K., Tjhen R., Li S., Pan H., Stroud R.M., James T.L.
    J. Biol. Chem. 280:38823-38830(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 11-82 IN COMPLEX WITH DNA.
  24. "Crystal structure of the third KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.6 A resolution."
    Fenn S., Du Z., Lee J.K., Tjhen R., Stroud R.M., James T.L.
    Nucleic Acids Res. 35:2651-2660(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 285-359 IN COMPLEX WITH DNA.
  25. "X-ray crystallographic and NMR studies of protein-protein and protein-nucleic acid interactions involving the KH domains from human poly(C)-binding protein-2."
    Du Z., Lee J.K., Fenn S., Tjhen R., Stroud R.M., James T.L.
    RNA 13:1043-1051(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 11-82 IN COMPLEX WITH DNA.
  26. "Structure of a construct of a human poly(C)-binding protein containing the first and second KH domains reveals insights into its regulatory mechanisms."
    Du Z., Fenn S., Tjhen R., James T.L.
    J. Biol. Chem. 283:28757-28766(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 11-169.

Entry informationi

Entry nameiPCBP2_HUMAN
AccessioniPrimary (citable) accession number: Q15366
Secondary accession number(s): A8K7X6
, B4DXP5, F8VYL7, G3V0E8, I6L8F9, Q32Q82, Q59HD4, Q68Y55, Q6IPF4, Q6PKG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 164 of the entry and version 1 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 12
    Human chromosome 12: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.