[1]
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NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 180-184; 193-197 AND 200-230.
DOI=10.1074/jbc.270.48.28780; PubMed=7499401 [NCBI, ExPASy, EBI, Israel, Japan]
Honore B.,
Rasmussen H.H.,
Vorum H.,
Dejgaard K.,
Liu X.,
Gromov P.,
Madsen P.,
Gesser B.,
Tommerup N.,
Celis J.E.;
"Heterogeneous nuclear ribonucleoproteins H, H', and F are members of a ubiquitously expressed subfamily of related but distinct proteins encoded by genes mapping to different chromosomes.";
J. Biol. Chem. 270:28780-28789(1995).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L.,
Schick M.,
Neubert P.,
Schatten R.,
Henze S.,
Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[4]
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PROTEIN SEQUENCE OF 1-14; 17-44; 50-68; 82-114; 151-167; 180-185; 300-347 AND 356-375, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND MET-2, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma, Cervix carcinoma, Hepatoma, Lung carcinoma, and Mammary carcinoma;
Bienvenut W.V.,
Boldt K.,
von Kriegsheim A.F.,
Matallanas D.,
Cooper W.N.,
Calvo F.,
Kolch W.,
Vousden K.H.,
Lukashchuk N.;
Submitted (MAR-2008) to UniProtKB.
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[5]
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PROTEIN SEQUENCE OF 99-114; 151-167; 300-316 AND 356-375, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G.,
Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
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[6]
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PROTEIN SEQUENCE OF 127-135 AND 153-163.
DOI=10.1093/nar/22.6.1059; PubMed=7512260 [NCBI, ExPASy, EBI, Israel, Japan]
Matunis M.J.,
Xing J.,
Dreyfuss G.;
"The hnRNP F protein: unique primary structure, nucleic acid-binding properties, and subcellular localization.";
Nucleic Acids Res. 22:1059-1067(1994).
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[7]
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PROTEIN SEQUENCE OF 200-230.
TISSUE=Keratinocyte;
DOI=10.1002/elps.11501301199; PubMed=1286667 [NCBI, ExPASy, EBI, Israel, Japan]
Rasmussen H.H.,
van Damme J.,
Puype M.,
Gesser B.,
Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
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[8]
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FUNCTION, AND INTERACTION WITH PTBP1; PTBP2 AND FUBP2.
DOI=10.1128/MCB.20.20.7463-7479.2000; PubMed=11003644 [NCBI, ExPASy, EBI, Israel, Japan]
Markovtsov V.,
Nikolic J.M.,
Goldman J.A.,
Turck C.W.,
Chou M.-Y.,
Black D.L.;
"Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein.";
Mol. Cell. Biol. 20:7463-7479(2000).
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[9]
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IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPICEOSOMAL C COMPLEX.
DOI=10.1017/S1355838202021088; PubMed=11991638 [NCBI, ExPASy, EBI, Israel, Japan]
Jurica M.S.,
Licklider L.J.,
Gygi S.P.,
Grigorieff N.,
Moore M.J.;
"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.";
RNA 8:426-439(2002).
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[10]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100, AND MASS SPECTROMETRY.
TISSUE=T-cell;
DOI=10.1021/ac035352d; PubMed=15144186 [NCBI, ExPASy, EBI, Israel, Japan]
Brill L.M.,
Salomon A.R.,
Ficarro S.B.,
Mukherji M.,
Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
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[11]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A.,
Jedrychowski M.,
Schwartz D.,
Elias J.E.,
Villen J.,
Li J.,
Cohn M.A.,
Cantley L.C.,
Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
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[12]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-246 AND TYR-306, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J.,
Moritz A.,
Lee K.A.,
Guo A.,
Goss V.L.,
Spek E.J.,
Zhang H.,
Zha X.-M.,
Polakiewicz R.D.,
Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
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[13]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V.,
Blagoev B.,
Gnad F.,
Macek B.,
Kumar C.,
Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
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[14]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-310, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R.,
Zhu Z.,
Chan K.C.,
Issaq H.J.,
Dimitrov D.S.,
Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
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[15]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K.,
Sugiyama N.,
Kyono Y.,
Tomita M.,
Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
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[16]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-104 AND THR-107, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N.,
Zhou C.,
Villen J.,
Beausoleil S.A.,
Bakalarski C.E.,
Elledge S.J.,
Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
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- FUNCTION: This protein is a component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Binds poly(RG).
- SUBUNIT: Part of a ternary complex containing FUBP2, PTBP1, PTBP2 and HNRNPH1. Identified in the spliceosome C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRNPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8.
- INTERACTION:
Q92597:NDRG1; NbExp=1; IntAct=EBI-351590, EBI-716486;
- SUBCELLULAR LOCATION: Nucleus, nucleoplasm.
- TISSUE SPECIFICITY: Expressed ubiquitously.
- DOMAIN: Each quasi-RRM repeat bound poly(RG), while only the N-terminal QRRM bound poly(RC) and poly(RU). None of the repeats bound detectable amounts of poly(RA).
- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
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