The relative expression of human histone H2A genes is similar in different types of proliferating cells.Mannironi C., Orr A., Hatch C., Pilch D., Ivanova V., Bonner W.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCDNA Cell Biol. 13:161-170 (1994)Cited in2
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
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.[...], Sugano S.View abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]TissueTongueCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Genet. 36:40-45 (2004)Cited in99+99+
Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B.[...], LaBaer J.Cited forNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (JUN-2004)Cited in99+99+
The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K.[...], Bentley D.R.View abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 441:315-321 (2006)Cited in99+99+
No title available.Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H.[...], Venter J.C.Cited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (JUL-2005)Cited in99+
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]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCGenome Res. 14:2121-2127 (2004)Cited in99+99+
Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo.Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N., Takio K., Kaneko M., Takeshima Y.[...], Ito T.View abstractCited forPHOSPHORYLATION AT THR-121CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCGenes Dev. 18:877-888 (2004)Cited in13Mapped to4
Phosphorylation of histone H2A inhibits transcription on chromatin templates.Zhang Y., Griffin K., Mondal N., Parvin J.D.View abstractCited forPHOSPHORYLATION AT SER-2, MUTAGENESIS OF SER-2CategoriesPTM / Processing, Disease & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 279:21866-21872 (2004)Cited in12Mapped to1
Role of histone H2A ubiquitination in Polycomb silencing.Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S., Zhang Y.View abstractCited forUBIQUITINATION AT LYS-120CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 431:873-878 (2004)Cited in17Mapped to3
Deimination of histone H2A and H4 at arginine 3 in HL-60 granulocytes.Hagiwara T., Hidaka Y., Yamada M.View abstractCited forACETYLATION AT SER-2, CITRULLINATION AT ARG-4, IDENTIFICATION BY MASS SPECTROMETRYCategoriesPTM / Processing, SequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochemistry 44:5827-5834 (2005)Cited in11
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
DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2A.Bergink S., Salomons F.A., Hoogstraten D., Groothuis T.A.M., de Waard H., Wu J., Yuan L., Citterio E., Houtsmuller A.B.[...], Dantuma N.P.View abstractCited forUBIQUITINATION AT LYS-120CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCGenes Dev. 20:1343-1352 (2006)Cited in11
Precise characterization of human histones in the H2A gene family by top down mass spectrometry.Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.View abstractCited forMASS SPECTROMETRY, ACETYLATION AT SER-2 AND LYS-6, UBIQUITINATION AT LYS-120CategoriesPTM / Processing, SequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Proteome Res. 5:248-253 (2006)Cited in9
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
The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage.Stewart G.S., Panier S., Townsend K., Al-Hakim A.K., Kolas N.K., Miller E.S., Nakada S., Ylanko J., Olivarius S.[...], Durocher D.View abstractCited forUBIQUITINATIONCategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell 136:420-434 (2009)Cited in15Mapped to32
RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins.Doil C., Mailand N., Bekker-Jensen S., Menard P., Larsen D.H., Pepperkok R., Ellenberg J., Panier S., Durocher D.[...], Lukas C.View abstractCited forUBIQUITINATIONCategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell 136:435-446 (2009)Cited in14Mapped to33
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-126CategoriesPTM / 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
A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase.Gatti M., Pinato S., Maspero E., Soffientini P., Polo S., Penengo L.View abstractCited forUBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell Cycle 11:2538-2544 (2012)Cited in12
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
VprBP has intrinsic kinase activity targeting histone H2A and represses gene transcription.Kim K., Kim J.M., Kim J.S., Choi J., Lee Y.S., Neamati N., Song J.S., Heo K., An W.View abstractCited forPHOSPHORYLATION AT THR-121CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell 52:459-467 (2013)Cited in12Mapped to1
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
Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification.Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J., Nielsen M.L., Kouzarides T.View abstractCited forMETHYLATION AT GLN-105CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 505:564-568 (2014)Cited in33