A cyclin associated with the CDK-activating kinase MO15.Maekelae T.P., Tassan J.-P., Nigg E.A., Frutiger S., Hughes G.J., Weinberg R.A.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-20; 106-133 AND 256-279TissueLiverCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 371:254-257 (1994)Cited in1Mapped to1
A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase.Fisher R.P., Morgan D.O.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 10-21; 90-102 AND 190-197CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell 78:713-724 (1994)Cited in2
Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.Cited forNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-270CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (MAY-2004)Cited in99+47
No title available.NIEHS SNPs programCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-28; VAL-54; ARG-138 AND ALA-270CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (JAN-2002)Cited in2
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project TeamView abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-270TissueBone marrow, Brain, Embryonic brain, Urinary bladderCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCGenome Res. 14:2121-2127 (2004)Cited in99+99+
Cdk-activating kinase complex is a component of human transcription factor TFIIH.Shiekhattar R., Mermelstein F., Fisher R.P., Drapkin R., Dynlacht B., Wessling H.C., Morgan D.O., Reinberg D.View abstractCited forFUNCTIONCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 374:283-287 (1995)Cited in1
Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes.Kershnar E., Wu S.-Y., Chiang C.-M.View abstractCited forIDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTORSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 273:34444-34453 (1998)Cited in20
Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7.Tirode F., Busso D., Coin F., Egly J.-M.View abstractCited forFUNCTIONCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell 3:87-95 (1999)Cited in10Mapped to37
TFIIH is negatively regulated by cdk8-containing mediator complexes.Akoulitchev S., Chuikov S., Reinberg D.View abstractCited forPHOSPHORYLATION AT SER-5 AND SER-304, MUTAGENESIS OF SER-5 AND SER-304CategoriesPTM / Processing, Disease & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 407:102-106 (2000)Cited in6Mapped to2
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.View abstractCited forPHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]TissueCervix carcinomaCategoriesPTM / Processing, SequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell 127:635-648 (2006)Cited in99+99+Mapped to1
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.View abstractCited forPHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; THR-315 AND SER-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]TissueCervix carcinomaCategoriesPTM / Processing, SequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell 31:438-448 (2008)Cited in99+99+
A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.View abstractCited forIDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]TissueCervix carcinomaCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProc. Natl. Acad. Sci. U.S.A. 105:10762-10767 (2008)Cited in99+99+
Large-scale proteomics analysis of the human kinome.Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.View abstractCited forPHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]CategoriesPTM / Processing, SequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell. Proteomics 8:1751-1764 (2009)Cited in99+99+
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.View abstractCited forPHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]TissueLeukemic T-cellCategoriesPTM / Processing, SequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCSci. Signal. 2:RA46-RA46 (2009)Cited in99+99+
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.[...], Mann M.View abstractCited forPHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315 AND SER-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]TissueCervix carcinomaCategoriesPTM / Processing, SequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCSci. Signal. 3:RA3-RA3 (2010)Cited in99+99+Mapped to4
Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.View abstractCited forIDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBMC Syst. Biol. 5:17-17 (2011)Cited in99+99+
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.View abstractCited forPHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]CategoriesPTM / Processing, SequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCSci. Signal. 4:RS3-RS3 (2011)Cited in99+99+
Toward a comprehensive characterization of a human cancer cell phosphoproteome.Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.View abstractCited forPHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND THR-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]TissueCervix carcinoma, ErythroleukemiaCategoriesPTM / Processing, SequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Proteome Res. 12:260-271 (2013)Cited in99+99+
Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase.Kim K.K., Chamberlin H.M., Morgan D.O., Kim S.-H.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Struct. Biol. 3:849-855 (1996)Cited in1
The structure of cyclin H: common mode of kinase activation and specific features.Andersen G., Busso D., Poterszman A., Hwang J.R., Wurtz J.-M., Ripp R., Thierry J.-C., Egly J.-M., Moras D.View abstractCited forX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 11-287CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEMBO J. 16:958-967 (1997)Cited in1
Efficient PCNA complex formation is dependent upon both transcription coupled repair and genome overall repair.Balajee A.S., May A., Dianova I., Bohr V.A.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-69220PubMedEurope PMCMutat Res 409:135-146 (1998)Mapped to59
Cyclin E2, a novel human G1 cyclin and activating partner of CDK2 and CDK3, is induced by viral oncoproteins.Zariwala M., Liu J., Xiong Y.View abstractCategoriesInteractionSourceIntAct: P51946PubMedEurope PMCOncogene 17:2787-2798 (1998)Cited in2Mapped to11
Cloning and characterization of three human cDNAs encoding mRNA (guanine- 7-)methyltransferase, an mRNA cap methylase.Tsukamoto T., Shibagaki Y., Niikura Y., Kiyohisa M.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-69220PubMedEurope PMCBiochem. Biophys. Res. Commun. 251:27-34 (1998)Cited in11Mapped to26
Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIH.Coin F., Marinoni J.-C., Rodolfo C., Fribourg S., Pedrini A.M., Egly J.-M.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-69220PubMedEurope PMCNat. Genet. 20:184-188 (1998)Cited in1Mapped to25
FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO.Archambault J., Pan G., Dahmus G.K., Cartier M., Marshall N., Zhang S., Dahmus M.E., Greenblatt J.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-69220PubMedEurope PMCJ. Biol. Chem. 273:27593-27601 (1998)Cited in1Mapped to77