The human and mouse replication-dependent histone genes.Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCGenomics 80:487-498 (2002)Cited in712Mapped to16
The DNA sequence and analysis of human chromosome 6.Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E.[...], Beck S.View abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 425:805-811 (2003)Cited in99+99+
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]TissueTestisCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCGenome Res. 14:2121-2127 (2004)Cited in99+99+
Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing.Cao R., Tsukada Y., Zhang Y.View abstractCited forUBIQUITINATION AT LYS-120CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell 20:845-854 (2005)Cited in17Mapped to27
RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins.Mailand N., Bekker-Jensen S., Faustrup H., Melander F., Bartek J., Lukas C., Lukas J.View abstractCited forUBIQUITINATIONCategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell 131:887-900 (2007)Cited in13Mapped to58
RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly.Huen M.S.Y., Grant R., Manke I., Minn K., Yu X., Yaffe M.B., Chen J.View abstractCited forUBIQUITINATIONCategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell 131:901-914 (2007)Cited in13Mapped to61
Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification.Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S.[...], Zhao Y.View abstractCited forCROTONYLATION AT LYS-37; LYS-119; LYS-120 AND LYS-127CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell 146:1016-1028 (2011)Cited in65
RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage signaling.Mattiroli F., Vissers J.H., van Dijk W.J., Ikpa P., Citterio E., Vermeulen W., Marteijn J.A., Sixma T.K.View abstractCited forUBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell 150:1182-1195 (2012)Cited in14Mapped to34
Lysine succinylation and lysine malonylation in histones.Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.View abstractCited forSUCCINYLATION AT LYS-10 AND LYS-96CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell. Proteomics 11:100-107 (2012)Cited in58
Lysine 2-hydroxyisobutyrylation is a widely distributed active histone mark.Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H., Debernardi A., Buchou T., Rousseaux S.[...], Zhao Y.View abstractCited forHYDROXYBUTYRYLATION AT LYS-6; LYS-10; LYS-37; LYS-75; LYS-76; LYS-96 AND LYS-119SourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Chem. Biol. 10:365-370 (2014)Cited in64
Metabolic regulation of gene expression by histone lysine beta- hydroxybutyrylation.Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J., Colak G.[...], Zhao Y.View abstractCited forHYDROXYBUTYRYLATION AT LYS-10; LYS-14; LYS-37; LYS-96 AND LYS-119SourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell 62:194-206 (2016)Cited in64
Overlapping but distinct patterns of histone acetylation by the human coactivators p300 and PCAF within nucleosomal substrates.Schiltz R.L., Mizzen C.A., Vassilev A., Cook R.G., Allis C.D., Nakatani Y.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-4549203, Reactome: R-HSA-4568583PubMedEurope PMCJ Biol Chem 274:1189-1192 (1999)Mapped to68
The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities.Zhang Y., LeRoy G., Seelig H.-P., Lane W.S., Reinberg D.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-4549203, Reactome: R-HSA-4551321PubMedEurope PMCCell 95:279-289 (1998)Cited in2Mapped to50
SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex.Zhang Y., Sun Z.-W., Iratni R., Erdjument-Bromage H., Tempst P., Hampsey M., Reinberg D.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-4549203, Reactome: R-HSA-4551321PubMedEurope PMCMol. Cell 1:1021-1031 (1998)Cited in4Mapped to99+
Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex.Zhang Y., Iratni R., Erdjument-Bromage H., Tempst P., Reinberg D.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-4549203, Reactome: R-HSA-4551321PubMedEurope PMCCell 89:357-364 (1997)Cited in3Mapped to49
Proteomic analyses reveal distinct chromatin-associated and soluble transcription factor complexes.Li X., Wang W., Wang J., Malovannaya A., Xi Y., Li W., Guerra R., Hawke D.H., Qin J., Chen J.View abstractCategoriesInteractionSourceIntAct: Q96QV6PubMedEurope PMCMol Syst Biol 11:775-775 (2015)Mapped to99+
Perturbation of the mutated EGFR interactome identifies vulnerabilities and resistance mechanisms.Li J., Bennett K., Stukalov A., Fang B., Zhang G., Yoshida T., Okamoto I., Kim J.Y., Song L.[...], Haura E.B.View abstractCategoriesInteractionSourceIntAct: Q96QV6PubMedEurope PMCMol Syst Biol 9:705-705 (2013)Mapped to99+
The cellular EJC interactome reveals higher-order mRNP structure and an EJC-SR protein nexus.Singh G., Kucukural A., Cenik C., Leszyk J.D., Shaffer S.A., Weng Z., Moore M.J.View abstractCategoriesInteractionSourceIntAct: Q96QV6PubMedEurope PMCCell 151:750-764 (2012)Mapped to99+
Histone H2A deubiquitinase activity of the Polycomb repressive complex PR- DUB.Scheuermann J.C., de Ayala Alonso A.G., Oktaba K., Ly-Hartig N., McGinty R.K., Fraterman S., Wilm M., Muir T.W., Muller J.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-4549203, Reactome: R-HSA-6782493PubMedEurope PMCNature 465:243-247 (2010)Cited in5Mapped to71
Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6.Humphries J.D., Byron A., Bass M.D., Craig S.E., Pinney J.W., Knight D., Humphries M.J.View abstractCategoriesInteractionSourceIntAct: Q96QV6PubMedEurope PMCSci Signal 2:ra51-ra51 (2009)Mapped to99+
Altered histone monoubiquitylation mediated by mutant huntingtin induces transcriptional dysregulation.Kim M.O., Chawla P., Overland R.P., Xia E., Sadri-Vakili G., Cha J.H.View abstractCategoriesPTM / ProcessingSourcePRO: PR:000044902PubMedEurope PMCJ Neurosci 28:3947-3957 (2008)Mapped to55
Identification and characterization of three new components of the mSin3A corepressor complex.Fleischer T.C., Yun U.J., Ayer D.E.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-4549203, Reactome: R-HSA-4551321PubMedEurope PMCMol. Cell. Biol. 23:3456-3467 (2003)Cited in6Mapped to49
A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes.Hakimi M.-A., Bochar D.A., Chenoweth J., Lane W.S., Mandel G., Shiekhattar R.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-4549203, Reactome: R-HSA-4551321PubMedEurope PMCProc. Natl. Acad. Sci. U.S.A. 99:7420-7425 (2002)Cited in4Mapped to51
Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex.Alland L., David G., Shen-Li H., Potes J., Muhle R., Lee H.-C., Hou H. Jr., Chen K., DePinho R.A.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-4549203, Reactome: R-HSA-4551321PubMedEurope PMCMol. Cell. Biol. 22:2743-2750 (2002)Cited in4Mapped to62
NuRD and SIN3 histone deacetylase complexes in development.Ahringer J.View abstractAnnotationPathwayCategoriesFunctionSourceReactome: R-HSA-4549203, Reactome: R-HSA-4551321PubMedEurope PMCTrends Genet. 16:351-356 (2000)Cited in2Mapped to77