Full text data of PCBP2
PCBP2
[Confidence: low (only semi-automatic identification from reviews)]
Poly(rC)-binding protein 2 (Alpha-CP2; Heterogeneous nuclear ribonucleoprotein E2; hnRNP E2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Poly(rC)-binding protein 2 (Alpha-CP2; Heterogeneous nuclear ribonucleoprotein E2; hnRNP E2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15366
ID PCBP2_HUMAN Reviewed; 365 AA.
AC Q15366; A8K7X6; F8VYL7; I6L8F9; Q32Q82; Q59HD4; Q68Y55; Q6IPF4;
read moreAC Q6PKG5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Poly(rC)-binding protein 2;
DE AltName: Full=Alpha-CP2;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein E2;
DE Short=hnRNP E2;
GN Name=PCBP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7607214; DOI=10.1111/j.1432-1033.1995.tb20581.x;
RA Leffers H., Dejgaard K., Celis J.E.;
RT "Characterisation of two major cellular poly(rC)-binding human
RT proteins, each containing three K-homologous (KH) domains.";
RL Eur. J. Biochem. 230:447-453(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA Sugiyama A., Inoue H., Oka M.;
RT "Homo sapiens mRNA.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 5).
RC TISSUE=Eye, Lung, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 47-70; 102-115; 145-160 AND 323-354, AND MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP FUNCTION, AND INTERACTION WITH IFIH1; RNF135; MAVS AND ITCH.
RX PubMed=19881509; DOI=10.1038/ni.1815;
RA You F., Sun H., Zhou X., Sun W., Liang S., Zhai Z., Jiang Z.;
RT "PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin
RT ligase AIP4.";
RL Nat. Immunol. 10:1300-1308(2009).
RN [15]
RP IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M.,
RA Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic
RT RNPs.";
RL RNA 15:104-115(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-189 AND
RP SER-364, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-364 AND
RP SER-365, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 11-82 IN COMPLEX WITH DNA.
RX PubMed=16186123; DOI=10.1074/jbc.M508183200;
RA Du Z., Lee J.K., Tjhen R., Li S., Pan H., Stroud R.M., James T.L.;
RT "Crystal structure of the first KH domain of human poly(C)-binding
RT protein-2 in complex with a C-rich strand of human telomeric DNA at
RT 1.7 A.";
RL J. Biol. Chem. 280:38823-38830(2005).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 285-359 IN COMPLEX WITH DNA.
RX PubMed=17426136; DOI=10.1093/nar/gkm139;
RA Fenn S., Du Z., Lee J.K., Tjhen R., Stroud R.M., James T.L.;
RT "Crystal structure of the third KH domain of human poly(C)-binding
RT protein-2 in complex with a C-rich strand of human telomeric DNA at
RT 1.6 A resolution.";
RL Nucleic Acids Res. 35:2651-2660(2007).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 11-82 IN COMPLEX WITH DNA.
RX PubMed=17526645; DOI=10.1261/rna.410107;
RA Du Z., Lee J.K., Fenn S., Tjhen R., Stroud R.M., James T.L.;
RT "X-ray crystallographic and NMR studies of protein-protein and
RT protein-nucleic acid interactions involving the KH domains from human
RT poly(C)-binding protein-2.";
RL RNA 13:1043-1051(2007).
RN [23]
RP STRUCTURE BY NMR OF 11-169.
RX PubMed=18701464; DOI=10.1074/jbc.M803046200;
RA Du Z., Fenn S., Tjhen R., James T.L.;
RT "Structure of a construct of a human poly(C)-binding protein
RT containing the first and second KH domains reveals insights into its
RT regulatory mechanisms.";
RL J. Biol. Chem. 283:28757-28766(2008).
CC -!- FUNCTION: Single-stranded nucleic acid binding protein that binds
CC preferentially to oligo dC. Major cellular poly(rC)-binding
CC protein. Binds also poly(rU). Negatively regulates cellular
CC antiviral responses mediated by MAVS signaling. It acts as an
CC adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore
CC triggering MAVS ubiquitinationa and degradation.
CC -!- SUBUNIT: Identified in a mRNP complex, at least composed of DHX9,
CC DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1,
CC STAU2, SYNCRIP and YBX1. Interacts with IFIH1 and RNF135.
CC Interacts with MAVS (via C-terminus) and ITCH (via WW domains).
CC -!- INTERACTION:
CC Q15365:PCBP1; NbExp=2; IntAct=EBI-945799, EBI-946095;
CC P84103:SRSF3; NbExp=3; IntAct=EBI-945799, EBI-372557;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Loosely bound in
CC the nucleus. May shuttle between the nucleus and the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q15366-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15366-2; Sequence=VSP_042833;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q15366-3; Sequence=VSP_043161, VSP_042833;
CC Name=4;
CC IsoId=Q15366-4; Sequence=VSP_043161, VSP_043362, VSP_042833;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q15366-5; Sequence=VSP_043362, VSP_042833;
CC Note=No experimental confirmation available;
CC Name=6;
CC IsoId=Q15366-6; Sequence=VSP_043161;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Detected in all tissues examined.
CC -!- DOMAIN: The KH domains mediates poly(C) binding.
CC -!- PTM: Phosphorylated. The non-phosphorylated form(s) exhibited the
CC strongest poly(rC)-binding activity.
CC -!- SIMILARITY: Contains 3 KH domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92062.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; X78136; CAA55015.1; -; mRNA.
DR EMBL; AB188306; BAD36897.1; -; mRNA.
DR EMBL; AK292141; BAF84830.1; -; mRNA.
DR EMBL; AB208825; BAD92062.1; ALT_INIT; mRNA.
DR EMBL; AC023509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96706.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96707.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96709.1; -; Genomic_DNA.
DR EMBL; BC001155; AAH01155.1; -; mRNA.
DR EMBL; BC071942; AAH71942.1; -; mRNA.
DR EMBL; BC107688; AAI07689.1; -; mRNA.
DR PIR; S65679; S42471.
DR RefSeq; NP_001092090.1; NM_001098620.2.
DR RefSeq; NP_001122383.1; NM_001128911.1.
DR RefSeq; NP_001122384.1; NM_001128912.1.
DR RefSeq; NP_001122385.1; NM_001128913.1.
DR RefSeq; NP_001122386.1; NM_001128914.1.
DR RefSeq; NP_005007.2; NM_005016.5.
DR RefSeq; NP_114366.1; NM_031989.4.
DR UniGene; Hs.546271; -.
DR PDB; 2AXY; X-ray; 1.70 A; A/B/C/D=11-82.
DR PDB; 2JZX; NMR; -; A=11-169.
DR PDB; 2P2R; X-ray; 1.60 A; A=285-359.
DR PDB; 2PQU; X-ray; 2.12 A; A/B/C/D=11-82.
DR PDB; 2PY9; X-ray; 2.56 A; A/B/C/D=11-82.
DR PDBsum; 2AXY; -.
DR PDBsum; 2JZX; -.
DR PDBsum; 2P2R; -.
DR PDBsum; 2PQU; -.
DR PDBsum; 2PY9; -.
DR ProteinModelPortal; Q15366; -.
DR SMR; Q15366; 11-169, 286-358.
DR DIP; DIP-58934N; -.
DR IntAct; Q15366; 34.
DR MINT; MINT-96192; -.
DR STRING; 9606.ENSP00000352438; -.
DR PhosphoSite; Q15366; -.
DR DMDM; 6707736; -.
DR PaxDb; Q15366; -.
DR PeptideAtlas; Q15366; -.
DR PRIDE; Q15366; -.
DR DNASU; 5094; -.
DR Ensembl; ENST00000359282; ENSP00000352228; ENSG00000197111.
DR Ensembl; ENST00000359462; ENSP00000352438; ENSG00000197111.
DR Ensembl; ENST00000439930; ENSP00000408949; ENSG00000197111.
DR Ensembl; ENST00000447282; ENSP00000394116; ENSG00000197111.
DR Ensembl; ENST00000546463; ENSP00000448762; ENSG00000197111.
DR Ensembl; ENST00000548933; ENSP00000449062; ENSG00000197111.
DR Ensembl; ENST00000552296; ENSP00000448927; ENSG00000197111.
DR Ensembl; ENST00000603815; ENSP00000475032; ENSG00000197111.
DR GeneID; 5094; -.
DR KEGG; hsa:5094; -.
DR UCSC; uc001sde.4; human.
DR CTD; 5094; -.
DR GeneCards; GC12P053844; -.
DR HGNC; HGNC:8648; PCBP2.
DR HPA; HPA038356; -.
DR MIM; 601210; gene.
DR neXtProt; NX_Q15366; -.
DR PharmGKB; PA32987; -.
DR eggNOG; NOG315872; -.
DR HOGENOM; HOG000182823; -.
DR HOVERGEN; HBG053520; -.
DR InParanoid; Q15366; -.
DR KO; K13162; -.
DR OMA; GPTTSIF; -.
DR OrthoDB; EOG7P02J4; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PCBP2; human.
DR EvolutionaryTrace; Q15366; -.
DR GeneWiki; PCBP2; -.
DR GenomeRNAi; 5094; -.
DR NextBio; 19648; -.
DR PRO; PR:Q15366; -.
DR ArrayExpress; Q15366; -.
DR Bgee; Q15366; -.
DR CleanEx; HS_PCBP2; -.
DR Genevestigator; Q15366; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IMP:UniProtKB.
DR GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR Pfam; PF00013; KH_1; 3.
DR SMART; SM00322; KH; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense;
KW Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Immunity; Innate immunity; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding.
FT CHAIN 1 365 Poly(rC)-binding protein 2.
FT /FTId=PRO_0000050090.
FT DOMAIN 13 75 KH 1.
FT DOMAIN 97 162 KH 2.
FT DOMAIN 287 351 KH 3.
FT MOD_RES 173 173 Phosphoserine.
FT MOD_RES 189 189 Phosphoserine.
FT MOD_RES 272 272 Phosphoserine.
FT MOD_RES 364 364 Phosphoserine.
FT MOD_RES 365 365 Phosphoserine.
FT VAR_SEQ 169 172 Missing (in isoform 3, isoform 4 and
FT isoform 6).
FT /FTId=VSP_043161.
FT VAR_SEQ 198 228 Missing (in isoform 4 and isoform 5).
FT /FTId=VSP_043362.
FT VAR_SEQ 279 279 W -> WA (in isoform 2, isoform 3, isoform
FT 4 and isoform 5).
FT /FTId=VSP_042833.
FT STRAND 14 21
FT HELIX 22 29
FT HELIX 31 33
FT HELIX 34 43
FT STRAND 46 49
FT STRAND 55 63
FT HELIX 65 80
FT STRAND 89 91
FT STRAND 97 105
FT HELIX 106 113
FT HELIX 115 117
FT HELIX 118 127
FT STRAND 128 131
FT STRAND 143 150
FT HELIX 152 168
FT STRAND 288 295
FT HELIX 296 303
FT HELIX 305 307
FT HELIX 308 317
FT STRAND 320 323
FT STRAND 331 339
FT HELIX 341 355
SQ SEQUENCE 365 AA; 38580 MW; 43F035D76FDC2C63 CRC64;
MDTGVIEGGL NVTLTIRLLM HGKEVGSIIG KKGESVKKMR EESGARINIS EGNCPERIIT
LAGPTNAIFK AFAMIIDKLE EDISSSMTNS TAASRPPVTL RLVVPASQCG SLIGKGGCKI
KEIRESTGAQ VQVAGDMLPN STERAITIAG IPQSIIECVK QICVVMLETL SQSPPKGVTI
PYRPKPSSSP VIFAGGQDRY STGSDSASFP HTTPSMCLNP DLEGPPLEAY TIQGQYAIPQ
PDLTKLHQLA MQQSHFPMTH GNTGFSGIES SSPEVKGYWG LDASAQTTSH ELTIPNDLIG
CIIGRQGAKI NEIRQMSGAQ IKIANPVEGS TDRQVTITGS AASISLAQYL INVRLSSETG
GMGSS
//
ID PCBP2_HUMAN Reviewed; 365 AA.
AC Q15366; A8K7X6; F8VYL7; I6L8F9; Q32Q82; Q59HD4; Q68Y55; Q6IPF4;
read moreAC Q6PKG5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Poly(rC)-binding protein 2;
DE AltName: Full=Alpha-CP2;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein E2;
DE Short=hnRNP E2;
GN Name=PCBP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7607214; DOI=10.1111/j.1432-1033.1995.tb20581.x;
RA Leffers H., Dejgaard K., Celis J.E.;
RT "Characterisation of two major cellular poly(rC)-binding human
RT proteins, each containing three K-homologous (KH) domains.";
RL Eur. J. Biochem. 230:447-453(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA Sugiyama A., Inoue H., Oka M.;
RT "Homo sapiens mRNA.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 5).
RC TISSUE=Eye, Lung, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 47-70; 102-115; 145-160 AND 323-354, AND MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP FUNCTION, AND INTERACTION WITH IFIH1; RNF135; MAVS AND ITCH.
RX PubMed=19881509; DOI=10.1038/ni.1815;
RA You F., Sun H., Zhou X., Sun W., Liang S., Zhai Z., Jiang Z.;
RT "PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin
RT ligase AIP4.";
RL Nat. Immunol. 10:1300-1308(2009).
RN [15]
RP IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19029303; DOI=10.1261/rna.1175909;
RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M.,
RA Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.;
RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic
RT RNPs.";
RL RNA 15:104-115(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-189 AND
RP SER-364, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-364 AND
RP SER-365, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 11-82 IN COMPLEX WITH DNA.
RX PubMed=16186123; DOI=10.1074/jbc.M508183200;
RA Du Z., Lee J.K., Tjhen R., Li S., Pan H., Stroud R.M., James T.L.;
RT "Crystal structure of the first KH domain of human poly(C)-binding
RT protein-2 in complex with a C-rich strand of human telomeric DNA at
RT 1.7 A.";
RL J. Biol. Chem. 280:38823-38830(2005).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 285-359 IN COMPLEX WITH DNA.
RX PubMed=17426136; DOI=10.1093/nar/gkm139;
RA Fenn S., Du Z., Lee J.K., Tjhen R., Stroud R.M., James T.L.;
RT "Crystal structure of the third KH domain of human poly(C)-binding
RT protein-2 in complex with a C-rich strand of human telomeric DNA at
RT 1.6 A resolution.";
RL Nucleic Acids Res. 35:2651-2660(2007).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 11-82 IN COMPLEX WITH DNA.
RX PubMed=17526645; DOI=10.1261/rna.410107;
RA Du Z., Lee J.K., Fenn S., Tjhen R., Stroud R.M., James T.L.;
RT "X-ray crystallographic and NMR studies of protein-protein and
RT protein-nucleic acid interactions involving the KH domains from human
RT poly(C)-binding protein-2.";
RL RNA 13:1043-1051(2007).
RN [23]
RP STRUCTURE BY NMR OF 11-169.
RX PubMed=18701464; DOI=10.1074/jbc.M803046200;
RA Du Z., Fenn S., Tjhen R., James T.L.;
RT "Structure of a construct of a human poly(C)-binding protein
RT containing the first and second KH domains reveals insights into its
RT regulatory mechanisms.";
RL J. Biol. Chem. 283:28757-28766(2008).
CC -!- FUNCTION: Single-stranded nucleic acid binding protein that binds
CC preferentially to oligo dC. Major cellular poly(rC)-binding
CC protein. Binds also poly(rU). Negatively regulates cellular
CC antiviral responses mediated by MAVS signaling. It acts as an
CC adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore
CC triggering MAVS ubiquitinationa and degradation.
CC -!- SUBUNIT: Identified in a mRNP complex, at least composed of DHX9,
CC DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1,
CC STAU2, SYNCRIP and YBX1. Interacts with IFIH1 and RNF135.
CC Interacts with MAVS (via C-terminus) and ITCH (via WW domains).
CC -!- INTERACTION:
CC Q15365:PCBP1; NbExp=2; IntAct=EBI-945799, EBI-946095;
CC P84103:SRSF3; NbExp=3; IntAct=EBI-945799, EBI-372557;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Loosely bound in
CC the nucleus. May shuttle between the nucleus and the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q15366-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15366-2; Sequence=VSP_042833;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q15366-3; Sequence=VSP_043161, VSP_042833;
CC Name=4;
CC IsoId=Q15366-4; Sequence=VSP_043161, VSP_043362, VSP_042833;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q15366-5; Sequence=VSP_043362, VSP_042833;
CC Note=No experimental confirmation available;
CC Name=6;
CC IsoId=Q15366-6; Sequence=VSP_043161;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Detected in all tissues examined.
CC -!- DOMAIN: The KH domains mediates poly(C) binding.
CC -!- PTM: Phosphorylated. The non-phosphorylated form(s) exhibited the
CC strongest poly(rC)-binding activity.
CC -!- SIMILARITY: Contains 3 KH domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92062.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; X78136; CAA55015.1; -; mRNA.
DR EMBL; AB188306; BAD36897.1; -; mRNA.
DR EMBL; AK292141; BAF84830.1; -; mRNA.
DR EMBL; AB208825; BAD92062.1; ALT_INIT; mRNA.
DR EMBL; AC023509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96706.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96707.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96709.1; -; Genomic_DNA.
DR EMBL; BC001155; AAH01155.1; -; mRNA.
DR EMBL; BC071942; AAH71942.1; -; mRNA.
DR EMBL; BC107688; AAI07689.1; -; mRNA.
DR PIR; S65679; S42471.
DR RefSeq; NP_001092090.1; NM_001098620.2.
DR RefSeq; NP_001122383.1; NM_001128911.1.
DR RefSeq; NP_001122384.1; NM_001128912.1.
DR RefSeq; NP_001122385.1; NM_001128913.1.
DR RefSeq; NP_001122386.1; NM_001128914.1.
DR RefSeq; NP_005007.2; NM_005016.5.
DR RefSeq; NP_114366.1; NM_031989.4.
DR UniGene; Hs.546271; -.
DR PDB; 2AXY; X-ray; 1.70 A; A/B/C/D=11-82.
DR PDB; 2JZX; NMR; -; A=11-169.
DR PDB; 2P2R; X-ray; 1.60 A; A=285-359.
DR PDB; 2PQU; X-ray; 2.12 A; A/B/C/D=11-82.
DR PDB; 2PY9; X-ray; 2.56 A; A/B/C/D=11-82.
DR PDBsum; 2AXY; -.
DR PDBsum; 2JZX; -.
DR PDBsum; 2P2R; -.
DR PDBsum; 2PQU; -.
DR PDBsum; 2PY9; -.
DR ProteinModelPortal; Q15366; -.
DR SMR; Q15366; 11-169, 286-358.
DR DIP; DIP-58934N; -.
DR IntAct; Q15366; 34.
DR MINT; MINT-96192; -.
DR STRING; 9606.ENSP00000352438; -.
DR PhosphoSite; Q15366; -.
DR DMDM; 6707736; -.
DR PaxDb; Q15366; -.
DR PeptideAtlas; Q15366; -.
DR PRIDE; Q15366; -.
DR DNASU; 5094; -.
DR Ensembl; ENST00000359282; ENSP00000352228; ENSG00000197111.
DR Ensembl; ENST00000359462; ENSP00000352438; ENSG00000197111.
DR Ensembl; ENST00000439930; ENSP00000408949; ENSG00000197111.
DR Ensembl; ENST00000447282; ENSP00000394116; ENSG00000197111.
DR Ensembl; ENST00000546463; ENSP00000448762; ENSG00000197111.
DR Ensembl; ENST00000548933; ENSP00000449062; ENSG00000197111.
DR Ensembl; ENST00000552296; ENSP00000448927; ENSG00000197111.
DR Ensembl; ENST00000603815; ENSP00000475032; ENSG00000197111.
DR GeneID; 5094; -.
DR KEGG; hsa:5094; -.
DR UCSC; uc001sde.4; human.
DR CTD; 5094; -.
DR GeneCards; GC12P053844; -.
DR HGNC; HGNC:8648; PCBP2.
DR HPA; HPA038356; -.
DR MIM; 601210; gene.
DR neXtProt; NX_Q15366; -.
DR PharmGKB; PA32987; -.
DR eggNOG; NOG315872; -.
DR HOGENOM; HOG000182823; -.
DR HOVERGEN; HBG053520; -.
DR InParanoid; Q15366; -.
DR KO; K13162; -.
DR OMA; GPTTSIF; -.
DR OrthoDB; EOG7P02J4; -.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_6900; Immune System.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PCBP2; human.
DR EvolutionaryTrace; Q15366; -.
DR GeneWiki; PCBP2; -.
DR GenomeRNAi; 5094; -.
DR NextBio; 19648; -.
DR PRO; PR:Q15366; -.
DR ArrayExpress; Q15366; -.
DR Bgee; Q15366; -.
DR CleanEx; HS_PCBP2; -.
DR Genevestigator; Q15366; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IMP:UniProtKB.
DR GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR Pfam; PF00013; KH_1; 3.
DR SMART; SM00322; KH; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense;
KW Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Immunity; Innate immunity; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; RNA-binding.
FT CHAIN 1 365 Poly(rC)-binding protein 2.
FT /FTId=PRO_0000050090.
FT DOMAIN 13 75 KH 1.
FT DOMAIN 97 162 KH 2.
FT DOMAIN 287 351 KH 3.
FT MOD_RES 173 173 Phosphoserine.
FT MOD_RES 189 189 Phosphoserine.
FT MOD_RES 272 272 Phosphoserine.
FT MOD_RES 364 364 Phosphoserine.
FT MOD_RES 365 365 Phosphoserine.
FT VAR_SEQ 169 172 Missing (in isoform 3, isoform 4 and
FT isoform 6).
FT /FTId=VSP_043161.
FT VAR_SEQ 198 228 Missing (in isoform 4 and isoform 5).
FT /FTId=VSP_043362.
FT VAR_SEQ 279 279 W -> WA (in isoform 2, isoform 3, isoform
FT 4 and isoform 5).
FT /FTId=VSP_042833.
FT STRAND 14 21
FT HELIX 22 29
FT HELIX 31 33
FT HELIX 34 43
FT STRAND 46 49
FT STRAND 55 63
FT HELIX 65 80
FT STRAND 89 91
FT STRAND 97 105
FT HELIX 106 113
FT HELIX 115 117
FT HELIX 118 127
FT STRAND 128 131
FT STRAND 143 150
FT HELIX 152 168
FT STRAND 288 295
FT HELIX 296 303
FT HELIX 305 307
FT HELIX 308 317
FT STRAND 320 323
FT STRAND 331 339
FT HELIX 341 355
SQ SEQUENCE 365 AA; 38580 MW; 43F035D76FDC2C63 CRC64;
MDTGVIEGGL NVTLTIRLLM HGKEVGSIIG KKGESVKKMR EESGARINIS EGNCPERIIT
LAGPTNAIFK AFAMIIDKLE EDISSSMTNS TAASRPPVTL RLVVPASQCG SLIGKGGCKI
KEIRESTGAQ VQVAGDMLPN STERAITIAG IPQSIIECVK QICVVMLETL SQSPPKGVTI
PYRPKPSSSP VIFAGGQDRY STGSDSASFP HTTPSMCLNP DLEGPPLEAY TIQGQYAIPQ
PDLTKLHQLA MQQSHFPMTH GNTGFSGIES SSPEVKGYWG LDASAQTTSH ELTIPNDLIG
CIIGRQGAKI NEIRQMSGAQ IKIANPVEGS TDRQVTITGS AASISLAQYL INVRLSSETG
GMGSS
//
MIM
601210
*RECORD*
*FIELD* NO
601210
*FIELD* TI
*601210 POLY(rC)-BINDING PROTEIN 2; PCBP2
;;HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN E2; HNRNPE2;;
read moreHNRPE2
*FIELD* TX
DESCRIPTION
Heterogeneous nuclear riboprotein E2 is a poly(rC)-binding protein with
translational regulatory functions (Ostareck-Lederer et al., 1998).
CLONING
Leffers et al. (1995) described the cloning and characterization of 2
cDNAs for poly(rC)-binding proteins, called PCBP1 (601209) and PCBP2 by
them. The authors analyzed an EST database for sequences that were
predicted to encode a protein with K-homologous (KH) domains. The 60- to
70-amino acid KH motifs are found in several putative nucleic acid
binding proteins such as FMR1 (309550) and HNRNPK (600712) and are
thought to be involved in RNA binding. Using primers from 1 EST the
authors produced a probe that was used to screen a cDNA library of
transformed human amnion cells. The cDNA they isolated for PCBP1 encodes
a putative 356-amino acid protein that contains 3 KH domains. It is 83%
identical to PCBP2 at the DNA level and 90% homologous at the amino acid
level. The PCBP2 protein is about 99% similar to the mouse hnRNP-X/mCTBP
protein (Hahm et al., 1993) and is a probable homolog.
Chkheidze and Liebhaber (2003) determined that endogenous HeLa cell
PCBP2 localized to the nucleus in a particulate and diffuse staining
pattern that differed from the speckled pattern observed with PCBP1.
They identified 2 nuclear localization signals within PCBP2, within a
9-amino acid segment between KH2 and KH3, and within a 12-amino acid
segment of KH3. Mutation analysis revealed that both signals were
required for nuclear localization. A splice variant of PCBP2 that
contains a 31-amino acid segment between KH2 and KH3 showed both nuclear
and cytoplasmic distribution.
GENE FUNCTION
When expressed with a vaccinia virus system in transformed amnion cells,
Leffers et al. (1995) found that both PCBP1 and PCBP2 bound poly(rC)
when not phosphorylated; phosphorylated protein bound with much lower
affinity. Transcripts of both PCBPs were detected in all the human
tissues analyzed.
Studying the arrest of differentiation, which is a feature of chronic
myelogenous leukemia cells with the fusion BCR-ABL gene (151410),
Perrotti et al. (2002) found that BCR-ABL regulates the expression of
C/EBP-alpha (CEBPA; 116897), the principal regulator of granulocytic
differentiation, inducing HNRNPE2, which inhibits the translation of
CEBPA mRNA.
Using mouse and human myelogenous leukemia cell lines, Eiring et al.
(2010) showed that microRNA-328 (MIR328; 613701) inhibited HNRNPE2
activity. A C-rich region of the mature MIR328 sequence interacted with
the poly(rC)-binding region HNRNPE2. This interaction prevented binding
between HNRNPE2 and a C-rich 5-prime upstream region of CEBPA, releasing
CEBPA from translational inhibition by HNRNPE2. Mir328 with a mutated
seed sequence bound Hnrnpe2 and restored Cebpa expression in mouse
myeloid precursors, indicating that the effects of MIR328 on HNRNPE2 and
CEBPA were independent of its seed sequence.
EVOLUTION
One of the most evolutionarily constrained regions in mammalian genomes
is the ultraconserved element uc.338, a mammal-specific 223-basepair
region perfectly conserved between human, mouse, and rat, overlapping a
short protein-coding exon of PCBP2. Bejerano et al. (2006) showed that a
class of conserved primarily noncoding regions in tetrapods originated
from a previously unknown short interspersed repetitive element (SINE)
retroposon family that was active in the Sarcopterygii (lobe-finned
fishes and terrestrial vertebrates) in the Silurian period at least 410
million years ago, and seems to be recently active in the 'living
fossil' Indonesian coelacanth, Latimeria menadoensis. Using a mouse
enhancer assay, Bejerano et al. (2006) showed that one copy, 0.5 million
bases from the neurodevelopmental gene ISL1 (600366), is an enhancer
that recapitulates multiple aspects of Isl1 expression patterns. Several
other copies represent new, possibly regulatory, alternatively spliced
exons in the middle of preexisting Sarcopterygian genes. One of these, a
more than 200-basepair ultraconserved region, 100% identical in mammals,
and 80% identical to the coelacanth SINE, contains a 31-amino-acid
residue alternatively spliced exon of the mRNA processing gene PCBP2.
Bejerano et al. (2006) concluded that this SINE element adds to a
growing list of examples in which relics of transposable elements have
acquired a function that serves their host, a process termed
'exaptation', and provide an origin for at least some of the many highly
conserved vertebrate-specific genomic sequences.
MAPPING
Tommerup and Leffers (1996) mapped PCBP2 distal to FRA12A (136630) at
12q13.12-q13.13 by fluorescence in situ hybridization.
Makeyev and Liebhaber (2000) identified 2 processed PCBP2 pseudogenes
that mapped to chromosome 21q22.3 and chromosome 8q21-q22.
GENE STRUCTURE
Makeyev and Liebhaber (2000) determined that the human and mouse PCBP2
genes contain 15 exons and span more than 19 kb.
*FIELD* RF
1. Bejerano, G.; Lowe, C. B.; Ahituv, N.; King, B.; Siepel, A.; Salama,
S. R.; Rubin, E. M.; Kent, W. J.; Haussler, D.: A distal enhancer
and an ultraconserved exon are derived from a novel retroposon. Nature 441:
87-90, 2006.
2. Chkheidze, A. N.; Liebhaber, S. A.: A novel set of nuclear localization
signals determine distributions of the alpha-CP RNA-binding proteins. Molec.
Cell. Biol. 23: 8405-8415, 2003.
3. Eiring, A. M.; Harb, J. G.; Neviani, P.; Garton, C.; Oaks, J. J.;
Spizzo, R.; Liu, S.; Schwind, S.; Santhanam, R.; Hickey, C. J.; Becker,
H.; Chandler, J. C.; and 13 others: miR-328 functions as an RNA
decoy to modulate hnRNP E2 regulation of mRNA translation in leukemic
blasts. Cell 140: 652-665, 2010.
4. Hahm, K.; Kim, G.; Turck, C.; Smale, S. T.: Isolation of a murine
gene encoding a nucleic acid-binding protein with homology to hnRNP
K. Nucleic Acids Res. 21: 21-26, 1993.
5. Leffers, H.; Dejgaard, K.; Celis, J. E.: Characterisation of two
major cellular poly(rC)-binding human proteins, each containing three
K-homologous (KH) domains. Europ. J. Biochem. 230: 447-453, 1995.
6. Makeyev, A. V.; Liebhaber, S. A.: Identification of two novel
mammalian genes establishes a subfamily of KH-domain RNA-binding proteins. Genomics 67:
301-316, 2000.
7. Ostareck-Lederer, A.; Ostareck, D. H.; Hentze, M. W.: Cytoplasmic
regulatory functions of the KH-domain proteins hnRNPs K and E1/E2. Trends
Biochem. Sci. 23: 409-411, 1998.
8. Perrotti, D.; Cesi, V.; Trotta, R.; Guerzoni, C.; Santilli, G.;
Campbell, K.; Iervolino, A.; Condorelli, F.; Gambacorti-Passerini,
C.; Caligiuri, M. A.; Calabretta, B.: BCR-ABL suppresses C/EBP-alpha
expression through inhibitory action of hnRNP E2. Nature Genet. 30:
48-58, 2002.
9. Tommerup, N.; Leffers, H.: Assignment of human KH-box-containing
genes by in situ hybridization: HNRNPK maps to 9q21.32-q21.33, PCBP1
to 2p12-p13, and PCBP2 to 12q13.12-q13.13, distal to FRA12A. Genomics 32:
297-298, 1996.
*FIELD* CN
Patricia A. Hartz - updated: 1/19/2011
Ada Hamosh - updated: 6/1/2006
Patricia A. Hartz - updated: 2/11/2004
Victor A. McKusick - updated: 1/14/2002
*FIELD* CD
Alan F. Scott: 4/17/1996
*FIELD* ED
mgross: 11/18/2011
terry: 11/11/2011
mgross: 1/19/2011
wwang: 8/27/2008
alopez: 6/3/2006
terry: 6/1/2006
cwells: 3/2/2004
terry: 2/11/2004
terry: 3/6/2002
alopez: 1/14/2002
mark: 6/7/1996
terry: 5/2/1996
mark: 4/17/1996
terry: 4/17/1996
mark: 4/17/1996
*RECORD*
*FIELD* NO
601210
*FIELD* TI
*601210 POLY(rC)-BINDING PROTEIN 2; PCBP2
;;HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN E2; HNRNPE2;;
read moreHNRPE2
*FIELD* TX
DESCRIPTION
Heterogeneous nuclear riboprotein E2 is a poly(rC)-binding protein with
translational regulatory functions (Ostareck-Lederer et al., 1998).
CLONING
Leffers et al. (1995) described the cloning and characterization of 2
cDNAs for poly(rC)-binding proteins, called PCBP1 (601209) and PCBP2 by
them. The authors analyzed an EST database for sequences that were
predicted to encode a protein with K-homologous (KH) domains. The 60- to
70-amino acid KH motifs are found in several putative nucleic acid
binding proteins such as FMR1 (309550) and HNRNPK (600712) and are
thought to be involved in RNA binding. Using primers from 1 EST the
authors produced a probe that was used to screen a cDNA library of
transformed human amnion cells. The cDNA they isolated for PCBP1 encodes
a putative 356-amino acid protein that contains 3 KH domains. It is 83%
identical to PCBP2 at the DNA level and 90% homologous at the amino acid
level. The PCBP2 protein is about 99% similar to the mouse hnRNP-X/mCTBP
protein (Hahm et al., 1993) and is a probable homolog.
Chkheidze and Liebhaber (2003) determined that endogenous HeLa cell
PCBP2 localized to the nucleus in a particulate and diffuse staining
pattern that differed from the speckled pattern observed with PCBP1.
They identified 2 nuclear localization signals within PCBP2, within a
9-amino acid segment between KH2 and KH3, and within a 12-amino acid
segment of KH3. Mutation analysis revealed that both signals were
required for nuclear localization. A splice variant of PCBP2 that
contains a 31-amino acid segment between KH2 and KH3 showed both nuclear
and cytoplasmic distribution.
GENE FUNCTION
When expressed with a vaccinia virus system in transformed amnion cells,
Leffers et al. (1995) found that both PCBP1 and PCBP2 bound poly(rC)
when not phosphorylated; phosphorylated protein bound with much lower
affinity. Transcripts of both PCBPs were detected in all the human
tissues analyzed.
Studying the arrest of differentiation, which is a feature of chronic
myelogenous leukemia cells with the fusion BCR-ABL gene (151410),
Perrotti et al. (2002) found that BCR-ABL regulates the expression of
C/EBP-alpha (CEBPA; 116897), the principal regulator of granulocytic
differentiation, inducing HNRNPE2, which inhibits the translation of
CEBPA mRNA.
Using mouse and human myelogenous leukemia cell lines, Eiring et al.
(2010) showed that microRNA-328 (MIR328; 613701) inhibited HNRNPE2
activity. A C-rich region of the mature MIR328 sequence interacted with
the poly(rC)-binding region HNRNPE2. This interaction prevented binding
between HNRNPE2 and a C-rich 5-prime upstream region of CEBPA, releasing
CEBPA from translational inhibition by HNRNPE2. Mir328 with a mutated
seed sequence bound Hnrnpe2 and restored Cebpa expression in mouse
myeloid precursors, indicating that the effects of MIR328 on HNRNPE2 and
CEBPA were independent of its seed sequence.
EVOLUTION
One of the most evolutionarily constrained regions in mammalian genomes
is the ultraconserved element uc.338, a mammal-specific 223-basepair
region perfectly conserved between human, mouse, and rat, overlapping a
short protein-coding exon of PCBP2. Bejerano et al. (2006) showed that a
class of conserved primarily noncoding regions in tetrapods originated
from a previously unknown short interspersed repetitive element (SINE)
retroposon family that was active in the Sarcopterygii (lobe-finned
fishes and terrestrial vertebrates) in the Silurian period at least 410
million years ago, and seems to be recently active in the 'living
fossil' Indonesian coelacanth, Latimeria menadoensis. Using a mouse
enhancer assay, Bejerano et al. (2006) showed that one copy, 0.5 million
bases from the neurodevelopmental gene ISL1 (600366), is an enhancer
that recapitulates multiple aspects of Isl1 expression patterns. Several
other copies represent new, possibly regulatory, alternatively spliced
exons in the middle of preexisting Sarcopterygian genes. One of these, a
more than 200-basepair ultraconserved region, 100% identical in mammals,
and 80% identical to the coelacanth SINE, contains a 31-amino-acid
residue alternatively spliced exon of the mRNA processing gene PCBP2.
Bejerano et al. (2006) concluded that this SINE element adds to a
growing list of examples in which relics of transposable elements have
acquired a function that serves their host, a process termed
'exaptation', and provide an origin for at least some of the many highly
conserved vertebrate-specific genomic sequences.
MAPPING
Tommerup and Leffers (1996) mapped PCBP2 distal to FRA12A (136630) at
12q13.12-q13.13 by fluorescence in situ hybridization.
Makeyev and Liebhaber (2000) identified 2 processed PCBP2 pseudogenes
that mapped to chromosome 21q22.3 and chromosome 8q21-q22.
GENE STRUCTURE
Makeyev and Liebhaber (2000) determined that the human and mouse PCBP2
genes contain 15 exons and span more than 19 kb.
*FIELD* RF
1. Bejerano, G.; Lowe, C. B.; Ahituv, N.; King, B.; Siepel, A.; Salama,
S. R.; Rubin, E. M.; Kent, W. J.; Haussler, D.: A distal enhancer
and an ultraconserved exon are derived from a novel retroposon. Nature 441:
87-90, 2006.
2. Chkheidze, A. N.; Liebhaber, S. A.: A novel set of nuclear localization
signals determine distributions of the alpha-CP RNA-binding proteins. Molec.
Cell. Biol. 23: 8405-8415, 2003.
3. Eiring, A. M.; Harb, J. G.; Neviani, P.; Garton, C.; Oaks, J. J.;
Spizzo, R.; Liu, S.; Schwind, S.; Santhanam, R.; Hickey, C. J.; Becker,
H.; Chandler, J. C.; and 13 others: miR-328 functions as an RNA
decoy to modulate hnRNP E2 regulation of mRNA translation in leukemic
blasts. Cell 140: 652-665, 2010.
4. Hahm, K.; Kim, G.; Turck, C.; Smale, S. T.: Isolation of a murine
gene encoding a nucleic acid-binding protein with homology to hnRNP
K. Nucleic Acids Res. 21: 21-26, 1993.
5. Leffers, H.; Dejgaard, K.; Celis, J. E.: Characterisation of two
major cellular poly(rC)-binding human proteins, each containing three
K-homologous (KH) domains. Europ. J. Biochem. 230: 447-453, 1995.
6. Makeyev, A. V.; Liebhaber, S. A.: Identification of two novel
mammalian genes establishes a subfamily of KH-domain RNA-binding proteins. Genomics 67:
301-316, 2000.
7. Ostareck-Lederer, A.; Ostareck, D. H.; Hentze, M. W.: Cytoplasmic
regulatory functions of the KH-domain proteins hnRNPs K and E1/E2. Trends
Biochem. Sci. 23: 409-411, 1998.
8. Perrotti, D.; Cesi, V.; Trotta, R.; Guerzoni, C.; Santilli, G.;
Campbell, K.; Iervolino, A.; Condorelli, F.; Gambacorti-Passerini,
C.; Caligiuri, M. A.; Calabretta, B.: BCR-ABL suppresses C/EBP-alpha
expression through inhibitory action of hnRNP E2. Nature Genet. 30:
48-58, 2002.
9. Tommerup, N.; Leffers, H.: Assignment of human KH-box-containing
genes by in situ hybridization: HNRNPK maps to 9q21.32-q21.33, PCBP1
to 2p12-p13, and PCBP2 to 12q13.12-q13.13, distal to FRA12A. Genomics 32:
297-298, 1996.
*FIELD* CN
Patricia A. Hartz - updated: 1/19/2011
Ada Hamosh - updated: 6/1/2006
Patricia A. Hartz - updated: 2/11/2004
Victor A. McKusick - updated: 1/14/2002
*FIELD* CD
Alan F. Scott: 4/17/1996
*FIELD* ED
mgross: 11/18/2011
terry: 11/11/2011
mgross: 1/19/2011
wwang: 8/27/2008
alopez: 6/3/2006
terry: 6/1/2006
cwells: 3/2/2004
terry: 2/11/2004
terry: 3/6/2002
alopez: 1/14/2002
mark: 6/7/1996
terry: 5/2/1996
mark: 4/17/1996
terry: 4/17/1996
mark: 4/17/1996