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Histone H4

 H4_HUMAN                Reviewed;         103 AA.
P62805; A2VCL0; P02304; P02305; Q6DRA9; Q6FGB8; Q6NWP7;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 175.
RecName: Full=Histone H4;
Name=HIST1H4A; Synonyms=H4/A, H4FA;
and
Name=HIST1H4B; Synonyms=H4/I, H4FI;
and
Name=HIST1H4C; Synonyms=H4/G, H4FG;
and
Name=HIST1H4D; Synonyms=H4/B, H4FB;
and
Name=HIST1H4E; Synonyms=H4/J, H4FJ;
and
Name=HIST1H4F; Synonyms=H4/C, H4FC;
and
Name=HIST1H4H; Synonyms=H4/H, H4FH;
and
Name=HIST1H4I; Synonyms=H4/M, H4FM;
and
Name=HIST1H4J; Synonyms=H4/E, H4FE;
and
Name=HIST1H4K; Synonyms=H4/D, H4FD;
and
Name=HIST1H4L; Synonyms=H4/K, H4FK;
and
Name=HIST2H4A; Synonyms=H4/N, H4F2, H4FN, HIST2H4;
and
Name=HIST2H4B; Synonyms=H4/O, H4FO;
and
Name=HIST4H4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6314274; DOI=10.1093/nar/11.20.7069;
Sierra F., Stein G., Stein J.;
"Structure and in vitro transcription of a human H4 histone gene.";
Nucleic Acids Res. 11:7069-7086(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3035717; DOI=10.1126/science.3035717;
Pauli U., Chrysogelos S., Stein G., Stein J., Nick H.;
"Protein-DNA interactions in vivo upstream of a cell cycle-regulated
human H4 histone gene.";
Science 236:1308-1311(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=1916825; DOI=10.1016/0888-7543(91)90183-F;
Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.;
"Isolation and characterization of two human H1 histone genes within
clusters of core histone genes.";
Genomics 10:940-948(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7626218; DOI=10.1089/dna.1995.14.591;
Drabent B., Kardalinou E., Bode C., Doenecke D.;
"Association of histone H4 genes with the mammalian testis-specific
H1t histone gene.";
DNA Cell Biol. 14:591-597(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9031620; DOI=10.1016/S0378-1119(96)00582-3;
Albig W., Meergans T., Doenecke D.;
"Characterization of the H1.5 gene completes the set of human H1
subtype genes.";
Gene 184:141-148(1997).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9439656; DOI=10.1007/s004390050630;
Albig W., Doenecke D.;
"The human histone gene cluster at the D6S105 locus.";
Hum. Genet. 101:284-294(1997).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9119399; DOI=10.1006/geno.1996.4592;
Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D.;
"Human histone gene organization: nonregular arrangement within a
large cluster.";
Genomics 40:314-322(1997).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H4A; HIST1H4B; HIST1H4C;
HIST1H4D; HIST1H4E; HIST1H4F; HIST1H4H; HIST1H4I; HIST1H4J; HIST1H4K;
HIST1H4L; HIST2H4A AND HIST4H4).
PubMed=12408966; DOI=10.1006/geno.2002.6850;
Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
"The human and mouse replication-dependent histone genes.";
Genomics 80:487-498(2002).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8988030;
Akasaka T., Miura I., Takahashi N., Akasaka H., Yonetani N., Ohno H.,
Fukuhara S., Okuma M.;
"A recurring translocation, t(3;6)(q27;p21), in non-Hodgkin's lymphoma
results in replacement of the 5' regulatory region of BCL6 with a
novel H4 histone gene.";
Cancer Res. 57:7-12(1997).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=15527963; DOI=10.1016/j.gene.2004.07.036;
Braastad C.D., Hovhannisyan H., van Wijnen A.J., Stein J.L.,
Stein G.S.;
"Functional characterization of a human histone gene cluster
duplication.";
Gene 342:35-40(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HIST1H4F; HIST1H4H AND
HIST2H4A).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIST1H4A; HIST1H4B;
HIST1H4C; HIST1H4D; HIST1H4E; HIST1H4F; HIST1H4H; HIST1H4I; HIST1H4J;
HIST1H4K AND HIST1H4L).
PubMed=14574404; DOI=10.1038/nature02055;
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., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum, Eye, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[15]
PROTEIN SEQUENCE OF 25-36; 47-56; 61-78 AND 81-93, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (MAR-2005) to UniProtKB.
[16]
ACETYLATION AT LYS-6; LYS-9; LYS-13 AND LYS-17.
PubMed=7664735;
O'Neill L.P., Turner B.M.;
"Histone H4 acetylation distinguishes coding regions of the human
genome from heterochromatin in a differentiation-dependent but
transcription-independent manner.";
EMBO J. 14:3946-3957(1995).
[17]
DNA-BINDING REGION.
PubMed=3340182; DOI=10.1038/331365a0;
Ebralidse K.K., Grachev S.A., Mirzabekov A.D.;
"A highly basic histone H4 domain bound to the sharply bent region of
nucleosomal DNA.";
Nature 331:365-367(1988).
[18]
ACETYLATION AT LYS-6; LYS-9; LYS-13 AND LYS-17.
PubMed=2474456; DOI=10.1016/0014-5793(89)80947-0;
Turner B.M., O'Neill L.P., Allan I.M.;
"Histone H4 acetylation in human cells. Frequency of acetylation at
different sites defined by immunolabeling with site-specific
antibodies.";
FEBS Lett. 253:141-145(1989).
[19]
METHYLATION AT ARG-4.
PubMed=11448779; DOI=10.1016/S0960-9822(01)00294-9;
Strahl B.D., Briggs S.D., Brame C.J., Caldwell J.A., Koh S.S., Ma H.,
Cook R.G., Shabanowitz J., Hunt D.F., Stallcup M.R., Allis C.D.;
"Methylation of histone H4 at arginine 3 occurs in vivo and is
mediated by the nuclear receptor coactivator PRMT1.";
Curr. Biol. 11:996-1000(2001).
[20]
METHYLATION AT ARG-4.
PubMed=11387442; DOI=10.1126/science.1060781;
Wang H., Huang Z.-Q., Xia L., Feng Q., Erdjument-Bromage H.,
Strahl B.D., Briggs S.D., Allis C.D., Wong J., Tempst P., Zhang Y.;
"Methylation of histone H4 at arginine 3 facilitating transcriptional
activation by nuclear hormone receptor.";
Science 293:853-857(2001).
[21]
INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, AND CHROMOSOMAL
TRANSLOCATION WITH BCL6.
PubMed=12414651;
Kurata M., Maesako Y., Ueda C., Nishikori M., Akasaka T., Uchiyama T.,
Ohno H.;
"Characterization of t(3;6)(q27;p21) breakpoints in B-cell non-
Hodgkin's lymphoma and construction of the histone H4/BCL6 fusion
gene, leading to altered expression of Bcl-6.";
Cancer Res. 62:6224-6230(2002).
[22]
METHYLATION AT LYS-21.
PubMed=12086618; DOI=10.1016/S1097-2765(02)00548-8;
Nishioka K., Rice J.C., Sarma K., Erdjument-Bromage H., Werner J.,
Wang Y., Chuikov S., Valenzuela P., Tempst P., Steward R., Lis J.T.,
Allis C.D., Reinberg D.;
"PR-Set7 is a nucleosome-specific methyltransferase that modifies
lysine 20 of histone H4 and is associated with silent chromatin.";
Mol. Cell 9:1201-1213(2002).
[23]
SUMOYLATION.
PubMed=14578449; DOI=10.1073/pnas.1735528100;
Shiio Y., Eisenman R.N.;
"Histone sumoylation is associated with transcriptional repression.";
Proc. Natl. Acad. Sci. U.S.A. 100:13225-13230(2003).
[24]
CITRULLINATION AT ARG-4, AND METHYLATION AT ARG-4.
PubMed=15345777; DOI=10.1126/science.1101400;
Wang Y., Wysocka J., Sayegh J., Lee Y.-H., Perlin J.R., Leonelli L.,
Sonbuchner L.S., McDonald C.H., Cook R.G., Dou Y., Roeder R.G.,
Clarke S., Stallcup M.R., Allis C.D., Coonrod S.A.;
"Human PAD4 regulates histone arginine methylation levels via
demethylimination.";
Science 306:279-283(2004).
[25]
METHYLATION AT LYS-21.
PubMed=15964846; DOI=10.1074/jbc.M501691200;
Yin Y., Liu C., Tsai S.N., Zhou B., Ngai S.M., Zhu G.;
"SET8 recognizes the sequence RHRK20VLRDN within the N terminus of
histone H4 and mono-methylates lysine 20.";
J. Biol. Chem. 280:30025-30031(2005).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
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).
[28]
UBIQUITINATION.
PubMed=16678110; DOI=10.1016/j.molcel.2006.03.035;
Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H.,
Tempst P., Xiong Y., Zhang Y.;
"Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin
ligase facilitates cellular response to DNA damage.";
Mol. Cell 22:383-394(2006).
[29]
CITRULLINATION AT ARG-4.
PubMed=16567635; DOI=10.1073/pnas.0509639103;
Arita K., Shimizu T., Hashimoto H., Hidaka Y., Yamada M., Sato M.;
"Structural basis for histone N-terminal recognition by human
peptidylarginine deiminase 4.";
Proc. Natl. Acad. Sci. U.S.A. 103:5291-5296(2006).
[30]
ACETYLATION AT SER-2; LYS-13 AND LYS-17, PHOSPHORYLATION AT SER-2, AND
METHYLATION AT LYS-21.
PubMed=17967882; DOI=10.1128/MCB.01517-07;
Pesavento J.J., Yang H., Kelleher N.L., Mizzen C.A.;
"Certain and progressive methylation of histone H4 at lysine 20 during
the cell cycle.";
Mol. Cell. Biol. 28:468-486(2008).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
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).
[32]
ACETYLATION AT LYS-92, AND UBIQUITINATION AT LYS-92.
PubMed=19818714; DOI=10.1016/j.molcel.2009.08.019;
Yan Q., Dutt S., Xu R., Graves K., Juszczynski P., Manis J.P.,
Shipp M.A.;
"BBAP monoubiquitylates histone H4 at lysine 91 and selectively
modulates the DNA damage response.";
Mol. Cell 36:110-120(2009).
[33]
PROPIONYLATION AT LYS-9; LYS-17; LYS-32; LYS-45; LYS-78; LYS-80 AND
LYS-92, AND BUTYRYLATION AT LYS-9; LYS-17; LYS-32; LYS-45; LYS-78;
LYS-80 AND LYS-92.
PubMed=17267393; DOI=10.1074/mcp.M700021-MCP200;
Chen Y., Sprung R., Tang Y., Ball H., Sangras B., Kim S.C.,
Falck J.R., Peng J., Gu W., Zhao Y.;
"Lysine propionylation and butyrylation are novel post-translational
modifications in histones.";
Mol. Cell. Proteomics 6:812-819(2007).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[35]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13; LYS-17 AND
LYS-32, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND TYR-52, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[37]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[38]
CROTONYLATION AT LYS-6; LYS-9 AND LYS-13.
PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q.,
Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.;
"Identification of 67 histone marks and histone lysine crotonylation
as a new type of histone modification.";
Cell 146:1016-1028(2011).
[39]
PHOSPHORYLATION AT SER-48.
PubMed=21724829; DOI=10.1101/gad.2055511;
Kang B., Pu M., Hu G., Wen W., Dong Z., Zhao K., Stillman B.,
Zhang Z.;
"Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome
assembly.";
Genes Dev. 25:1359-1364(2011).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[41]
SUCCINYLATION AT LYS-13; LYS-32; LYS-78 AND LYS-92.
PubMed=22389435; DOI=10.1074/mcp.M111.015875;
Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
"Lysine succinylation and lysine malonylation in histones.";
Mol. Cell. Proteomics 11:100-107(2012).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND TYR-89, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[44]
HYDROXYBUTYRYLATION AT LYS-6; LYS-9; LYS-13; LYS-17; LYS-32; LYS-45;
LYS-60; LYS-78; LYS-80 AND LYS-92.
PubMed=24681537; DOI=10.1038/nchembio.1497;
Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H.,
Debernardi A., Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z.,
Allis C.D., Ren B., Khochbin S., Zhao Y.;
"Lysine 2-hydroxyisobutyrylation is a widely distributed active
histone mark.";
Nat. Chem. Biol. 10:365-370(2014).
[45]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[46]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[47]
BUTYRYLATION AT LYS-6; LYS-9; LYS-13 AND LYS-17.
PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014;
Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z.,
Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J.,
Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C.,
Panne D., Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.;
"Dynamic competing histone H4 K5K8 acetylation and butyrylation are
hallmarks of highly active gene promoters.";
Mol. Cell 62:169-180(2016).
[48]
HYDROXYBUTYRYLATION AT LYS-9; LYS-13; LYS-32; LYS-78 AND LYS-92.
PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
"Metabolic regulation of gene expression by histone lysine beta-
hydroxybutyrylation.";
Mol. Cell 62:194-206(2016).
[49]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-21; LYS-32; LYS-60; LYS-80
AND LYS-92, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[50]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=15951514; DOI=10.1093/nar/gki663;
Tsunaka Y., Kajimura N., Tate S., Morikawa K.;
"Alteration of the nucleosomal DNA path in the crystal structure of a
human nucleosome core particle.";
Nucleic Acids Res. 33:3424-3434(2005).
[51]
VARIANT [LARGE SCALE ANALYSIS] GLN-64.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
compact DNA into chromatin, limiting DNA accessibility to the
cellular machineries which require DNA as a template. Histones
thereby play a central role in transcription regulation, DNA
repair, DNA replication and chromosomal stability. DNA
accessibility is regulated via a complex set of post-translational
modifications of histones, also called histone code, and
nucleosome remodeling.
-!- SUBUNIT: The nucleosome is a histone octamer containing two
molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
heterotetramer and two H2A-H2B heterodimers. The octamer wraps
approximately 147 bp of DNA.
-!- INTERACTION:
P35609:ACTN2; NbExp=3; IntAct=EBI-302023, EBI-77797;
Q9Y294:ASF1A; NbExp=19; IntAct=EBI-302023, EBI-749553;
Q12830:BPTF; NbExp=3; IntAct=EBI-302023, EBI-1560273;
Q12830-4:BPTF; NbExp=16; IntAct=EBI-302023, EBI-4288838;
P25440:BRD2; NbExp=5; IntAct=EBI-302023, EBI-2874802;
O60885-1:BRD4; NbExp=10; IntAct=EBI-302023, EBI-9345088;
P55201:BRPF1; NbExp=8; IntAct=EBI-302023, EBI-2837428;
P49450:CENPA; NbExp=6; IntAct=EBI-302023, EBI-1751979;
P49450-1:CENPA; NbExp=2; IntAct=EBI-302023, EBI-15826012;
Q96DZ9-2:CMTM5; NbExp=4; IntAct=EBI-302023, EBI-11522780;
Q9NQ92:COPRS; NbExp=3; IntAct=EBI-302023, EBI-1642558;
Q92793:CREBBP; NbExp=6; IntAct=EBI-302023, EBI-81215;
P45481:Crebbp (xeno); NbExp=2; IntAct=EBI-302023, EBI-296306;
P84243:H3F3B; NbExp=12; IntAct=EBI-302023, EBI-120658;
O14929:HAT1; NbExp=7; IntAct=EBI-302023, EBI-2339359;
Q13547:HDAC1; NbExp=3; IntAct=EBI-302023, EBI-301834;
P68431:HIST1H3D; NbExp=6; IntAct=EBI-302023, EBI-79722;
Q71DI3:HIST2H3A; NbExp=3; IntAct=EBI-302023, EBI-750650;
Q16695:HIST3H3; NbExp=2; IntAct=EBI-302023, EBI-358900;
Q9H9V9:JMJD4; NbExp=3; IntAct=EBI-302023, EBI-2866290;
O75164:KDM4A; NbExp=7; IntAct=EBI-302023, EBI-936709;
Q9NQR1:KMT5A; NbExp=5; IntAct=EBI-302023, EBI-1268946;
Q9Y468:L3MBTL1; NbExp=4; IntAct=EBI-302023, EBI-1265089;
P49736:MCM2; NbExp=8; IntAct=EBI-302023, EBI-374819;
P25205:MCM3; NbExp=2; IntAct=EBI-302023, EBI-355153;
P33992:MCM5; NbExp=2; IntAct=EBI-302023, EBI-359410;
Q86UY6-1:NAA40; NbExp=3; IntAct=EBI-302023, EBI-16140302;
Q9BVI0:PHF20; NbExp=3; IntAct=EBI-302023, EBI-2560802;
A8MW92:PHF20L1; NbExp=2; IntAct=EBI-302023, EBI-2560834;
Q99873:PRMT1; NbExp=2; IntAct=EBI-302023, EBI-78738;
O14744:PRMT5; NbExp=6; IntAct=EBI-302023, EBI-351098;
Q582G4:PRMT7 (xeno); NbExp=4; IntAct=EBI-302023, EBI-16101095;
Q16576:RBBP7; NbExp=8; IntAct=EBI-302023, EBI-352227;
P38890:SET5 (xeno); NbExp=2; IntAct=EBI-302023, EBI-24263;
Q9VK33:Sfmbt (xeno); NbExp=10; IntAct=EBI-302023, EBI-117801;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-302023, EBI-747107;
O60264:SMARCA5; NbExp=2; IntAct=EBI-302023, EBI-352588;
Q04724:TLE1; NbExp=6; IntAct=EBI-302023, EBI-711424;
Q12888:TP53BP1; NbExp=11; IntAct=EBI-302023, EBI-396540;
Q12888-1:TP53BP1; NbExp=3; IntAct=EBI-302023, EBI-8022649;
P63104:YWHAZ; NbExp=3; IntAct=EBI-302023, EBI-347088;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- PTM: Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13
(H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the
genome but not in heterochromatin. {ECO:0000269|PubMed:17967882,
ECO:0000269|PubMed:2474456, ECO:0000269|PubMed:7664735}.
-!- PTM: Citrullination at Arg-4 (H4R3ci) by PADI4 impairs
methylation. {ECO:0000269|PubMed:11387442,
ECO:0000269|PubMed:11448779, ECO:0000269|PubMed:15345777,
ECO:0000269|PubMed:16567635}.
-!- PTM: Monomethylation and asymmetric dimethylation at Arg-4
(H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation
at Lys-9 (H4K8ac) and Lys-13 (H4K12ac). Demethylation is performed
by JMJD6. Symmetric dimethylation on Arg-4 (H4R3me2s) by the
PRDM1/PRMT5 complex may play a crucial role in the germ-cell
lineage. {ECO:0000269|PubMed:11387442,
ECO:0000269|PubMed:11448779, ECO:0000269|PubMed:15345777}.
-!- PTM: Monomethylated, dimethylated or trimethylated at Lys-21
(H4K20me1, H4K20me2, H4K20me3). Monomethylation is performed by
SET8. Trimethylation is performed by KMT5B and KMT5C and induces
gene silencing. {ECO:0000269|PubMed:12086618,
ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882}.
-!- PTM: Phosphorylated by PAK2 at Ser-48 (H4S47ph). This
phosphorylation increases the association of H3.3-H4 with the
histone chaperone HIRA, thus promoting nucleosome assembly of
H3.3-H4 and inhibiting nucleosome assembly of H3.1-H4.
{ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:21724829}.
-!- PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to
ultraviolet irradiation. This may weaken the interaction between
histones and DNA and facilitate DNA accessibility to repair
proteins. Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in
response to DNA damage. The exact role of H4K91ub1 in DNA damage
response is still unclear but it may function as a licensing
signal for additional histone H4 post-translational modifications
such as H4 Lys-21 methylation (H4K20me).
{ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:15964846,
ECO:0000269|PubMed:16678110, ECO:0000269|PubMed:17967882,
ECO:0000269|PubMed:19818714}.
-!- PTM: Sumoylated, which is associated with transcriptional
repression. {ECO:0000269|PubMed:14578449}.
-!- PTM: Crotonylation (Kcr) is specifically present in male germ
cells and marks testis-specific genes in post-meiotic cells,
including X-linked genes that escape sex chromosome inactivation
in haploid cells. Crotonylation marks active promoters and
enhancers and confers resistance to transcriptional repressors. It
is also associated with post-meiotically activated genes on
autosomes. {ECO:0000269|PubMed:21925322}.
-!- PTM: Butyrylation of histones marks active promoters and competes
with histone acetylation. {ECO:0000250|UniProtKB:P62806}.
-!- DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a
cause of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation
t(3;6)(q27;p21), with BCL6. {ECO:0000269|PubMed:12414651}.
-!- SIMILARITY: Belongs to the histone H4 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAI28106.1; Type=Frameshift; Positions=3; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X00038; CAA24918.1; ALT_SEQ; Genomic_DNA.
EMBL; M16707; AAA52652.1; -; Genomic_DNA.
EMBL; M60749; AAA63188.1; -; Genomic_DNA.
EMBL; X60481; CAA43011.1; -; Genomic_DNA.
EMBL; X60482; CAA43012.1; -; Genomic_DNA.
EMBL; X60483; CAA43013.1; -; Genomic_DNA.
EMBL; X60484; CAA43014.1; -; Genomic_DNA.
EMBL; X60486; CAA43016.1; -; Genomic_DNA.
EMBL; X60487; CAA43017.1; -; Genomic_DNA.
EMBL; X67081; CAA47464.1; -; Genomic_DNA.
EMBL; Z80787; CAB02549.1; -; Genomic_DNA.
EMBL; X83548; CAA58538.1; -; Genomic_DNA.
EMBL; AF525682; AAM83108.1; -; Genomic_DNA.
EMBL; AY128653; AAN01438.1; -; Genomic_DNA.
EMBL; AY128654; AAN01439.1; -; Genomic_DNA.
EMBL; AY128655; AAN01440.1; -; Genomic_DNA.
EMBL; AY128656; AAN01441.1; -; Genomic_DNA.
EMBL; AY128657; AAN01442.1; -; Genomic_DNA.
EMBL; AY128658; AAN01443.1; -; Genomic_DNA.
EMBL; AY128659; AAN01444.1; -; Genomic_DNA.
EMBL; AY128661; AAN01446.1; -; Genomic_DNA.
EMBL; AY128662; AAN01447.1; -; Genomic_DNA.
EMBL; AY128663; AAN01448.1; -; Genomic_DNA.
EMBL; AY128664; AAN01449.1; -; Genomic_DNA.
EMBL; AY128665; AAN01450.1; -; Genomic_DNA.
EMBL; AB000905; BAA19208.1; -; Genomic_DNA.
EMBL; AY648850; AAT68253.1; -; Genomic_DNA.
EMBL; CR542169; CAG46966.1; -; mRNA.
EMBL; CR542172; CAG46969.1; -; mRNA.
EMBL; CR542180; CAG46977.1; -; mRNA.
EMBL; CR542187; CAG46984.1; -; mRNA.
EMBL; CR542189; CAG46986.1; -; mRNA.
EMBL; AL021807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL021917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL031777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL049822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL353759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z98744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL591493; CAI12560.1; -; Genomic_DNA.
EMBL; AL591493; CAI12567.1; -; Genomic_DNA.
EMBL; CH471087; EAW55509.1; -; Genomic_DNA.
EMBL; CH471087; EAW55510.1; -; Genomic_DNA.
EMBL; CH471087; EAW55538.1; -; Genomic_DNA.
EMBL; CH471087; EAW55549.1; -; Genomic_DNA.
EMBL; CH471087; EAW55555.1; -; Genomic_DNA.
EMBL; CH471094; EAW96325.1; -; Genomic_DNA.
EMBL; CH471081; EAX03086.1; -; Genomic_DNA.
EMBL; CH471081; EAX03111.1; -; Genomic_DNA.
EMBL; CH471081; EAX03112.1; -; Genomic_DNA.
EMBL; CH471081; EAX03121.1; -; Genomic_DNA.
EMBL; BC017361; AAH17361.1; -; mRNA.
EMBL; BC054014; AAH54014.1; -; mRNA.
EMBL; BC066248; AAH66248.1; -; mRNA.
EMBL; BC066249; AAH66249.1; -; mRNA.
EMBL; BC066250; AAH66250.1; -; mRNA.
EMBL; BC067495; AAH67495.1; -; mRNA.
EMBL; BC067496; AAH67496.1; -; mRNA.
EMBL; BC067497; AAH67497.1; -; mRNA.
EMBL; BC069288; AAH69288.1; -; mRNA.
EMBL; BC069392; AAH69392.1; -; mRNA.
EMBL; BC069467; AAH69467.1; -; mRNA.
EMBL; BC069654; AAH69654.1; -; mRNA.
EMBL; BC093763; AAH93763.1; -; mRNA.
EMBL; BC093765; AAH93765.1; -; mRNA.
EMBL; BC093969; AAH93969.1; -; mRNA.
EMBL; BC111093; AAI11094.1; -; mRNA.
EMBL; BC111434; AAI11435.1; -; mRNA.
EMBL; BC112193; AAI12194.1; -; mRNA.
EMBL; BC120939; AAI20940.1; -; mRNA.
EMBL; BC128104; AAI28105.1; -; mRNA.
EMBL; BC128105; AAI28106.1; ALT_FRAME; mRNA.
EMBL; BC130558; AAI30559.1; -; mRNA.
EMBL; BC130560; AAI30561.1; -; mRNA.
EMBL; BC143045; AAI43046.1; -; mRNA.
CCDS; CCDS30847.1; -.
CCDS; CCDS30851.1; -.
CCDS; CCDS4571.1; -.
CCDS; CCDS4572.1; -.
CCDS; CCDS4583.1; -.
CCDS; CCDS4589.1; -.
CCDS; CCDS4593.1; -.
CCDS; CCDS4598.1; -.
CCDS; CCDS4604.1; -.
CCDS; CCDS4620.1; -.
CCDS; CCDS4630.1; -.
CCDS; CCDS4631.1; -.
CCDS; CCDS4637.1; -.
CCDS; CCDS8665.1; -.
PIR; D40335; HSHU4.
RefSeq; NP_001029249.1; NM_001034077.4.
RefSeq; NP_003486.1; NM_003495.2.
RefSeq; NP_003529.1; NM_003538.3.
RefSeq; NP_003530.1; NM_003539.3.
RefSeq; NP_003531.1; NM_003540.3.
RefSeq; NP_003532.1; NM_003541.2.
RefSeq; NP_003533.1; NM_003542.3.
RefSeq; NP_003534.1; NM_003543.3.
RefSeq; NP_003535.1; NM_003544.2.
RefSeq; NP_003536.1; NM_003545.3.
RefSeq; NP_003537.1; NM_003546.2.
RefSeq; NP_003539.1; NM_003548.2.
RefSeq; NP_068803.1; NM_021968.3.
RefSeq; NP_778224.1; NM_175054.2.
UniGene; Hs.143080; -.
UniGene; Hs.247816; -.
UniGene; Hs.248172; -.
UniGene; Hs.248178; -.
UniGene; Hs.248179; -.
UniGene; Hs.278483; -.
UniGene; Hs.46423; -.
UniGene; Hs.528055; -.
UniGene; Hs.533295; -.
UniGene; Hs.55468; -.
UniGene; Hs.591790; -.
UniGene; Hs.655235; -.
UniGene; Hs.662174; -.
UniGene; Hs.706635; -.
UniGene; Hs.745457; -.
PDB; 1ZKK; X-ray; 1.45 A; E/F/G/H=16-25.
PDB; 2BQZ; X-ray; 1.50 A; B/F=18-26.
PDB; 2CV5; X-ray; 2.50 A; B/F=1-103.
PDB; 2IG0; X-ray; 1.70 A; B=17-26.
PDB; 2KWN; NMR; -; B=10-24.
PDB; 2KWO; NMR; -; B=2-21.
PDB; 2LVM; NMR; -; B=15-28.
PDB; 2QQS; X-ray; 2.82 A; C/D=17-26.
PDB; 2RJE; X-ray; 1.86 A; P/Q=16-26.
PDB; 2RNY; NMR; -; B=14-28.
PDB; 2RS9; NMR; -; A=2-11.
PDB; 3A6N; X-ray; 2.70 A; B/F=1-103.
PDB; 3AFA; X-ray; 2.50 A; B/F=1-103.
PDB; 3AN2; X-ray; 3.60 A; B/F=1-103.
PDB; 3AV1; X-ray; 2.50 A; B/F=1-103.
PDB; 3AV2; X-ray; 2.80 A; B/F=1-103.
PDB; 3AYW; X-ray; 2.90 A; B/F=1-103.
PDB; 3AZE; X-ray; 3.00 A; B/F=1-103.
PDB; 3AZF; X-ray; 2.70 A; B/F=1-103.
PDB; 3AZG; X-ray; 2.40 A; B/F=1-103.
PDB; 3AZH; X-ray; 3.49 A; B/F=1-103.
PDB; 3AZI; X-ray; 2.70 A; B/F=1-103.
PDB; 3AZJ; X-ray; 2.89 A; B/F=1-103.
PDB; 3AZK; X-ray; 3.20 A; B/F=1-103.
PDB; 3AZL; X-ray; 2.70 A; B/F=1-103.
PDB; 3AZM; X-ray; 2.89 A; B/F=1-103.
PDB; 3AZN; X-ray; 3.00 A; B/F=1-103.
PDB; 3CFS; X-ray; 2.40 A; E=28-42.
PDB; 3CFV; X-ray; 2.60 A; E/F=25-42.
PDB; 3F9W; X-ray; 1.60 A; E/F/G/H=16-25.
PDB; 3F9X; X-ray; 1.25 A; E/F/G/H=16-25.
PDB; 3F9Y; X-ray; 1.50 A; E/F=16-25.
PDB; 3F9Z; X-ray; 1.60 A; E/F/G/H=16-25.
PDB; 3IJ1; X-ray; 2.10 A; B=16-26.
PDB; 3JPX; X-ray; 2.05 A; B=14-28.
PDB; 3NQJ; X-ray; 2.10 A; B=21-103.
PDB; 3NQU; X-ray; 2.50 A; B=1-103.
PDB; 3O36; X-ray; 1.70 A; D/E=15-20.
PDB; 3QBY; X-ray; 1.95 A; H=16-26.
PDB; 3QZS; X-ray; 1.80 A; C/D=13-22.
PDB; 3QZT; X-ray; 1.50 A; B=13-22.
PDB; 3QZV; X-ray; 2.00 A; C=8-18.
PDB; 3R45; X-ray; 2.60 A; B=1-103.
PDB; 3UVW; X-ray; 1.37 A; B=2-12.
PDB; 3UVX; X-ray; 1.91 A; B=12-22.
PDB; 3UVY; X-ray; 2.02 A; B=16-26.
PDB; 3UW9; X-ray; 2.30 A; E/F=8-18.
PDB; 3W96; X-ray; 3.00 A; B/F=1-103.
PDB; 3W97; X-ray; 3.20 A; B/F=1-103.
PDB; 3W98; X-ray; 3.42 A; B/F=1-103.
PDB; 3W99; X-ray; 3.00 A; B/F=17-103.
PDB; 3WA9; X-ray; 3.07 A; B/F=1-103.
PDB; 3WAA; X-ray; 3.20 A; B/F=1-103.
PDB; 3WKJ; X-ray; 2.80 A; B/F=1-103.
PDB; 3WTP; X-ray; 2.67 A; B/F=1-103.
PDB; 3X1S; X-ray; 2.81 A; B/F=2-103.
PDB; 3X1T; X-ray; 2.81 A; B/F=2-103.
PDB; 3X1U; X-ray; 3.25 A; B/F=2-103.
PDB; 3X1V; X-ray; 2.92 A; B/F=2-103.
PDB; 4GQB; X-ray; 2.06 A; C=2-22.
PDB; 4H9N; X-ray; 1.95 A; B=2-103.
PDB; 4H9O; X-ray; 2.05 A; B=2-103.
PDB; 4H9P; X-ray; 2.20 A; B=2-103.
PDB; 4H9Q; X-ray; 1.95 A; B=2-103.
PDB; 4H9R; X-ray; 2.20 A; B=2-103.
PDB; 4H9S; X-ray; 2.60 A; C/D=21-103.
PDB; 4HGA; X-ray; 2.80 A; C=1-103.
PDB; 4M38; X-ray; 2.20 A; E/F=2-22.
PDB; 4N3W; X-ray; 1.90 A; C=14-28.
PDB; 4N4F; X-ray; 1.83 A; C=6-26.
PDB; 4QUT; X-ray; 1.70 A; B=10-16.
PDB; 4QUU; X-ray; 1.80 A; B=4-16.
PDB; 4QYD; X-ray; 1.94 A; B=5-18.
PDB; 4U9W; X-ray; 2.49 A; E/F/G/H=2-6.
PDB; 4YM5; X-ray; 4.00 A; B/F=1-103.
PDB; 4YM6; X-ray; 3.51 A; B/F=1-103.
PDB; 4YY6; X-ray; 1.45 A; Z=2-12.
PDB; 4YYD; X-ray; 1.52 A; Z=2-12.
PDB; 4YYG; X-ray; 2.10 A; B=2-12.
PDB; 4YYH; X-ray; 1.74 A; Y/Z=2-12.
PDB; 4YYI; X-ray; 1.50 A; C/F=2-12.
PDB; 4YYJ; X-ray; 1.85 A; C/F=2-12.
PDB; 4YYK; X-ray; 1.79 A; C/F=2-12.
PDB; 4YYM; X-ray; 1.50 A; Z=2-12.
PDB; 4YYN; X-ray; 1.85 A; Z=2-12.
PDB; 4Z2M; X-ray; 2.98 A; H/J=1-103.
PDB; 4Z5T; X-ray; 2.80 A; B/F=1-103.
PDB; 5AV5; X-ray; 2.40 A; B/F=1-103.
PDB; 5AV6; X-ray; 2.20 A; B/F=1-103.
PDB; 5AV8; X-ray; 2.20 A; B/F=1-103.
PDB; 5AV9; X-ray; 2.20 A; B/F=1-103.
PDB; 5AVB; X-ray; 2.40 A; B/F=1-103.
PDB; 5AVC; X-ray; 2.40 A; B/F=1-103.
PDB; 5AY8; X-ray; 2.80 A; B/F=1-103.
PDB; 5B0Y; X-ray; 2.56 A; B/F=1-103.
PDB; 5B0Z; X-ray; 1.99 A; B/F=1-103.
PDB; 5B24; X-ray; 3.60 A; B/F=1-103.
PDB; 5B2I; X-ray; 3.00 A; B/F=1-103.
PDB; 5B2J; X-ray; 2.60 A; B/F=1-103.
PDB; 5B31; X-ray; 2.20 A; B/F=1-103.
PDB; 5B32; X-ray; 2.35 A; B/F=1-103.
PDB; 5B33; X-ray; 2.92 A; B/F=1-103.
PDB; 5B40; X-ray; 3.33 A; B/F=1-103.
PDB; 5BNV; X-ray; 2.79 A; B/E=2-103.
PDB; 5BNX; X-ray; 2.31 A; B=2-103.
PDB; 5BO0; X-ray; 2.91 A; B=2-103.
PDB; 5C3I; X-ray; 3.50 A; C/G/K/O/S/W=1-103.
PDB; 5CPI; X-ray; 2.90 A; B/F=1-103.
PDB; 5CPJ; X-ray; 3.15 A; B/F=1-103.
PDB; 5CPK; X-ray; 2.63 A; B/F=1-103.
PDB; 5FA5; X-ray; 2.34 A; C=2-21.
PDB; 5FFW; X-ray; 1.50 A; C=2-11.
PDB; 5FWE; X-ray; 2.05 A; C/D=2-16.
PDB; 5GSE; X-ray; 3.14 A; B/F/L/P=1-103.
PDB; 5GSU; X-ray; 3.10 A; B/F=2-103.
PDB; 5GT0; X-ray; 2.82 A; B/F=2-103.
PDB; 5GT3; X-ray; 2.91 A; B/F=2-103.
PDB; 5GTC; X-ray; 2.70 A; B/F=1-103.
PDB; 5GXQ; X-ray; 2.85 A; B/F=1-103.
PDB; 5JA4; X-ray; 2.42 A; B=2-103.
PDB; 5JRG; X-ray; 2.50 A; B/F=1-103.
PDB; 5KDM; X-ray; 3.50 A; B=2-103.
PDB; 5TEG; X-ray; 1.30 A; D/E=17-24.
PDB; 5X7X; X-ray; 2.18 A; B/F=1-103.
PDB; 5XF3; X-ray; 2.60 A; B/F=1-103.
PDB; 5XF4; X-ray; 2.87 A; B/F=1-103.
PDB; 5XF5; X-ray; 2.82 A; B/F=1-103.
PDBsum; 1ZKK; -.
PDBsum; 2BQZ; -.
PDBsum; 2CV5; -.
PDBsum; 2IG0; -.
PDBsum; 2KWN; -.
PDBsum; 2KWO; -.
PDBsum; 2LVM; -.
PDBsum; 2QQS; -.
PDBsum; 2RJE; -.
PDBsum; 2RNY; -.
PDBsum; 2RS9; -.
PDBsum; 3A6N; -.
PDBsum; 3AFA; -.
PDBsum; 3AN2; -.
PDBsum; 3AV1; -.
PDBsum; 3AV2; -.
PDBsum; 3AYW; -.
PDBsum; 3AZE; -.
PDBsum; 3AZF; -.
PDBsum; 3AZG; -.
PDBsum; 3AZH; -.
PDBsum; 3AZI; -.
PDBsum; 3AZJ; -.
PDBsum; 3AZK; -.
PDBsum; 3AZL; -.
PDBsum; 3AZM; -.
PDBsum; 3AZN; -.
PDBsum; 3CFS; -.
PDBsum; 3CFV; -.
PDBsum; 3F9W; -.
PDBsum; 3F9X; -.
PDBsum; 3F9Y; -.
PDBsum; 3F9Z; -.
PDBsum; 3IJ1; -.
PDBsum; 3JPX; -.
PDBsum; 3NQJ; -.
PDBsum; 3NQU; -.
PDBsum; 3O36; -.
PDBsum; 3QBY; -.
PDBsum; 3QZS; -.
PDBsum; 3QZT; -.
PDBsum; 3QZV; -.
PDBsum; 3R45; -.
PDBsum; 3UVW; -.
PDBsum; 3UVX; -.
PDBsum; 3UVY; -.
PDBsum; 3UW9; -.
PDBsum; 3W96; -.
PDBsum; 3W97; -.
PDBsum; 3W98; -.
PDBsum; 3W99; -.
PDBsum; 3WA9; -.
PDBsum; 3WAA; -.
PDBsum; 3WKJ; -.
PDBsum; 3WTP; -.
PDBsum; 3X1S; -.
PDBsum; 3X1T; -.
PDBsum; 3X1U; -.
PDBsum; 3X1V; -.
PDBsum; 4GQB; -.
PDBsum; 4H9N; -.
PDBsum; 4H9O; -.
PDBsum; 4H9P; -.
PDBsum; 4H9Q; -.
PDBsum; 4H9R; -.
PDBsum; 4H9S; -.
PDBsum; 4HGA; -.
PDBsum; 4M38; -.
PDBsum; 4N3W; -.
PDBsum; 4N4F; -.
PDBsum; 4QUT; -.
PDBsum; 4QUU; -.
PDBsum; 4QYD; -.
PDBsum; 4U9W; -.
PDBsum; 4YM5; -.
PDBsum; 4YM6; -.
PDBsum; 4YY6; -.
PDBsum; 4YYD; -.
PDBsum; 4YYG; -.
PDBsum; 4YYH; -.
PDBsum; 4YYI; -.
PDBsum; 4YYJ; -.
PDBsum; 4YYK; -.
PDBsum; 4YYM; -.
PDBsum; 4YYN; -.
PDBsum; 4Z2M; -.
PDBsum; 4Z5T; -.
PDBsum; 5AV5; -.
PDBsum; 5AV6; -.
PDBsum; 5AV8; -.
PDBsum; 5AV9; -.
PDBsum; 5AVB; -.
PDBsum; 5AVC; -.
PDBsum; 5AY8; -.
PDBsum; 5B0Y; -.
PDBsum; 5B0Z; -.
PDBsum; 5B24; -.
PDBsum; 5B2I; -.
PDBsum; 5B2J; -.
PDBsum; 5B31; -.
PDBsum; 5B32; -.
PDBsum; 5B33; -.
PDBsum; 5B40; -.
PDBsum; 5BNV; -.
PDBsum; 5BNX; -.
PDBsum; 5BO0; -.
PDBsum; 5C3I; -.
PDBsum; 5CPI; -.
PDBsum; 5CPJ; -.
PDBsum; 5CPK; -.
PDBsum; 5FA5; -.
PDBsum; 5FFW; -.
PDBsum; 5FWE; -.
PDBsum; 5GSE; -.
PDBsum; 5GSU; -.
PDBsum; 5GT0; -.
PDBsum; 5GT3; -.
PDBsum; 5GTC; -.
PDBsum; 5GXQ; -.
PDBsum; 5JA4; -.
PDBsum; 5JRG; -.
PDBsum; 5KDM; -.
PDBsum; 5TEG; -.
PDBsum; 5X7X; -.
PDBsum; 5XF3; -.
PDBsum; 5XF4; -.
PDBsum; 5XF5; -.
ProteinModelPortal; P62805; -.
SMR; P62805; -.
BioGrid; 113899; 24.
BioGrid; 113955; 177.
BioGrid; 113956; 17.
BioGrid; 113957; 30.
BioGrid; 113958; 16.
BioGrid; 113959; 20.
BioGrid; 113960; 16.
BioGrid; 113961; 20.
BioGrid; 113962; 16.
BioGrid; 113963; 21.
BioGrid; 113964; 18.
BioGrid; 113966; 49.
BioGrid; 125732; 88.
BioGrid; 299853; 18.
CORUM; P62805; -.
DIP; DIP-33079N; -.
IntAct; P62805; 130.
MINT; MINT-276350; -.
STRING; 9606.ENSP00000367034; -.
BindingDB; P62805; -.
ChEMBL; CHEMBL5876; -.
iPTMnet; P62805; -.
PhosphoSitePlus; P62805; -.
SwissPalm; P62805; -.
BioMuta; HIST1H4A; -.
DMDM; 51317339; -.
SWISS-2DPAGE; P62805; -.
EPD; P62805; -.
MaxQB; P62805; -.
PaxDb; P62805; -.
PeptideAtlas; P62805; -.
PRIDE; P62805; -.
TopDownProteomics; P62805; -.
DNASU; 8294; -.
DNASU; 8360; -.
DNASU; 8362; -.
DNASU; 8363; -.
DNASU; 8364; -.
DNASU; 8365; -.
DNASU; 8366; -.
DNASU; 8367; -.
DNASU; 8368; -.
DNASU; 8370; -.
Ensembl; ENST00000244537; ENSP00000244537; ENSG00000274618.
Ensembl; ENST00000355057; ENSP00000347168; ENSG00000197238.
Ensembl; ENST00000358064; ENSP00000350767; ENSG00000197837.
Ensembl; ENST00000377727; ENSP00000366956; ENSG00000158406.
Ensembl; ENST00000377745; ENSP00000366974; ENSG00000278705.
Ensembl; ENST00000377803; ENSP00000367034; ENSG00000197061.
Ensembl; ENST00000539745; ENSP00000443017; ENSG00000197837.
Ensembl; ENST00000578186; ENSP00000462667; ENSG00000270882.
Ensembl; ENST00000579512; ENSP00000462355; ENSG00000270276.
Ensembl; ENST00000611927; ENSP00000479794; ENSG00000273542.
Ensembl; ENST00000612061; ENSP00000482412; ENSG00000270276.
Ensembl; ENST00000613412; ENSP00000481343; ENSG00000270882.
Ensembl; ENST00000614247; ENSP00000479461; ENSG00000277157.
Ensembl; ENST00000614272; ENSP00000478519; ENSG00000270882.
Ensembl; ENST00000615164; ENSP00000484789; ENSG00000276966.
Ensembl; ENST00000615353; ENSP00000481486; ENSG00000276180.
Ensembl; ENST00000617569; ENSP00000479106; ENSG00000278637.
Ensembl; ENST00000618193; ENSP00000478786; ENSG00000270882.
Ensembl; ENST00000618305; ENSP00000480960; ENSG00000275126.
Ensembl; ENST00000621520; ENSP00000481507; ENSG00000270276.
Ensembl; ENST00000634560; ENSP00000489319; ENSG00000158406.
Ensembl; ENST00000634956; ENSP00000489567; ENSG00000158406.
Ensembl; ENST00000635491; ENSP00000489236; ENSG00000158406.
GeneID; 121504; -.
GeneID; 554313; -.
GeneID; 8294; -.
GeneID; 8359; -.
GeneID; 8360; -.
GeneID; 8361; -.
GeneID; 8362; -.
GeneID; 8363; -.
GeneID; 8364; -.
GeneID; 8365; -.
GeneID; 8366; -.
GeneID; 8367; -.
GeneID; 8368; -.
GeneID; 8370; -.
KEGG; hsa:121504; -.
KEGG; hsa:554313; -.
KEGG; hsa:8294; -.
KEGG; hsa:8359; -.
KEGG; hsa:8360; -.
KEGG; hsa:8361; -.
KEGG; hsa:8362; -.
KEGG; hsa:8363; -.
KEGG; hsa:8364; -.
KEGG; hsa:8365; -.
KEGG; hsa:8366; -.
KEGG; hsa:8367; -.
KEGG; hsa:8368; -.
KEGG; hsa:8370; -.
UCSC; uc001ess.4; human.
CTD; 121504; -.
CTD; 554313; -.
CTD; 8294; -.
CTD; 8359; -.
CTD; 8360; -.
CTD; 8361; -.
CTD; 8362; -.
CTD; 8363; -.
CTD; 8364; -.
CTD; 8365; -.
CTD; 8366; -.
CTD; 8367; -.
CTD; 8368; -.
CTD; 8370; -.
DisGeNET; 121504; -.
DisGeNET; 554313; -.
DisGeNET; 8294; -.
DisGeNET; 8359; -.
DisGeNET; 8360; -.
DisGeNET; 8361; -.
DisGeNET; 8362; -.
DisGeNET; 8363; -.
DisGeNET; 8364; -.
DisGeNET; 8365; -.
DisGeNET; 8366; -.
DisGeNET; 8367; -.
DisGeNET; 8368; -.
DisGeNET; 8370; -.
EuPathDB; HostDB:ENSG00000158406.4; -.
EuPathDB; HostDB:ENSG00000197061.4; -.
EuPathDB; HostDB:ENSG00000197238.4; -.
EuPathDB; HostDB:ENSG00000197837.3; -.
EuPathDB; HostDB:ENSG00000270276.2; -.
EuPathDB; HostDB:ENSG00000270882.2; -.
EuPathDB; HostDB:ENSG00000273542.1; -.
EuPathDB; HostDB:ENSG00000274618.1; -.
EuPathDB; HostDB:ENSG00000275126.1; -.
EuPathDB; HostDB:ENSG00000276180.1; -.
EuPathDB; HostDB:ENSG00000276966.2; -.
EuPathDB; HostDB:ENSG00000277157.1; -.
EuPathDB; HostDB:ENSG00000278637.1; -.
EuPathDB; HostDB:ENSG00000278705.1; -.
GeneCards; HIST1H4A; -.
GeneCards; HIST1H4B; -.
GeneCards; HIST1H4C; -.
GeneCards; HIST1H4D; -.
GeneCards; HIST1H4E; -.
GeneCards; HIST1H4F; -.
GeneCards; HIST1H4H; -.
GeneCards; HIST1H4I; -.
GeneCards; HIST1H4J; -.
GeneCards; HIST1H4K; -.
GeneCards; HIST1H4L; -.
GeneCards; HIST2H4A; -.
GeneCards; HIST2H4B; -.
GeneCards; HIST4H4; -.
HGNC; HGNC:4781; HIST1H4A.
HGNC; HGNC:4789; HIST1H4B.
HGNC; HGNC:4787; HIST1H4C.
HGNC; HGNC:4782; HIST1H4D.
HGNC; HGNC:4790; HIST1H4E.
HGNC; HGNC:4783; HIST1H4F.
HGNC; HGNC:4788; HIST1H4H.
HGNC; HGNC:4793; HIST1H4I.
HGNC; HGNC:4785; HIST1H4J.
HGNC; HGNC:4784; HIST1H4K.
HGNC; HGNC:4791; HIST1H4L.
HGNC; HGNC:4794; HIST2H4A.
HGNC; HGNC:29607; HIST2H4B.
HGNC; HGNC:20510; HIST4H4.
HPA; CAB011503; -.
HPA; CAB021887; -.
HPA; CAB037279; -.
HPA; HPA042201; -.
MIM; 142750; gene.
MIM; 602822; gene.
MIM; 602823; gene.
MIM; 602824; gene.
MIM; 602825; gene.
MIM; 602826; gene.
MIM; 602827; gene.
MIM; 602828; gene.
MIM; 602829; gene.
MIM; 602830; gene.
MIM; 602831; gene.
MIM; 602833; gene.
MIM; 615069; gene.
neXtProt; NX_P62805; -.
OpenTargets; ENSG00000158406; -.
OpenTargets; ENSG00000197061; -.
OpenTargets; ENSG00000197238; -.
OpenTargets; ENSG00000197837; -.
OpenTargets; ENSG00000270276; -.
OpenTargets; ENSG00000270882; -.
OpenTargets; ENSG00000273542; -.
OpenTargets; ENSG00000274618; -.
OpenTargets; ENSG00000275126; -.
OpenTargets; ENSG00000276180; -.
OpenTargets; ENSG00000276966; -.
OpenTargets; ENSG00000277157; -.
OpenTargets; ENSG00000278637; -.
OpenTargets; ENSG00000278705; -.
PharmGKB; PA29169; -.
eggNOG; KOG3467; Eukaryota.
eggNOG; COG2036; LUCA.
GeneTree; ENSGT00760000119019; -.
HOGENOM; HOG000234654; -.
HOVERGEN; HBG051878; -.
InParanoid; P62805; -.
KO; K11254; -.
OMA; YEEVRVV; -.
OrthoDB; EOG09370I2I; -.
PhylomeDB; P62805; -.
Reactome; R-HSA-1221632; Meiotic synapsis.
Reactome; R-HSA-171306; Packaging Of Telomere Ends.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-3214842; HDMs demethylate histones.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression.
Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-HSA-5334118; DNA methylation.
Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
Reactome; R-HSA-73777; RNA Polymerase I Chain Elongation.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-912446; Meiotic recombination.
Reactome; R-HSA-977225; Amyloid fiber formation.
SIGNOR; P62805; -.
ChiTaRS; HIST1H4A; human.
EvolutionaryTrace; P62805; -.
GeneWiki; HIST1H4A; -.
GeneWiki; HIST1H4B; -.
GeneWiki; HIST1H4C; -.
GeneWiki; HIST1H4D; -.
GeneWiki; HIST1H4E; -.
GeneWiki; HIST1H4F; -.
GeneWiki; HIST1H4H; -.
GeneWiki; HIST1H4I; -.
GeneWiki; HIST1H4J; -.
GeneWiki; HIST1H4K; -.
GeneWiki; HIST1H4L; -.
GeneWiki; HIST2H4A; -.
GeneWiki; HIST4H4; -.
Proteomes; UP000005640; Chromosome 1.
Proteomes; UP000005640; Chromosome 12.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000158406; -.
CleanEx; HS_HIST1H4A; -.
CleanEx; HS_HIST1H4B; -.
CleanEx; HS_HIST1H4C; -.
CleanEx; HS_HIST1H4D; -.
CleanEx; HS_HIST1H4E; -.
CleanEx; HS_HIST1H4F; -.
CleanEx; HS_HIST1H4H; -.
CleanEx; HS_HIST1H4I; -.
CleanEx; HS_HIST1H4L; -.
CleanEx; HS_HIST2H4A; -.
CleanEx; HS_HIST2H4B; -.
CleanEx; HS_HIST4H4; -.
ExpressionAtlas; P62805; baseline and differential.
Genevisible; P62805; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0000788; C:nuclear nucleosome; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000786; C:nucleosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IBA:GO_Central.
GO; GO:0042393; F:histone binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0034080; P:CENP-A containing nucleosome assembly; TAS:Reactome.
GO; GO:0000183; P:chromatin silencing at rDNA; TAS:Reactome.
GO; GO:0006335; P:DNA replication-dependent nucleosome assembly; IDA:UniProtKB.
GO; GO:0006336; P:DNA replication-independent nucleosome assembly; IDA:UniProtKB.
GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; IDA:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
GO; GO:0045815; P:positive regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
GO; GO:0060964; P:regulation of gene silencing by miRNA; TAS:Reactome.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0016233; P:telomere capping; TAS:Reactome.
GO; GO:0032200; P:telomere organization; TAS:BHF-UCL.
CDD; cd00076; H4; 1.
InterPro; IPR035425; CENP-T/H4_C.
InterPro; IPR009072; Histone-fold.
InterPro; IPR001951; Histone_H4.
InterPro; IPR019809; Histone_H4_CS.
InterPro; IPR004823; TAF_TATA-bd.
Pfam; PF15511; CENP-T_C; 1.
PRINTS; PR00623; HISTONEH4.
SMART; SM00417; H4; 1.
SMART; SM00803; TAF; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00047; HISTONE_H4; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromosomal rearrangement; Chromosome;
Citrullination; Complete proteome; Direct protein sequencing;
DNA-binding; Hydroxylation; Isopeptide bond; Methylation;
Nucleosome core; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:17967882}.
CHAIN 2 103 Histone H4.
/FTId=PRO_0000158320.
DNA_BIND 17 21
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:17967882}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000269|PubMed:17967882}.
MOD_RES 4 4 Asymmetric dimethylarginine; by PRMT1;
alternate. {ECO:0000269|PubMed:11387442,
ECO:0000269|PubMed:11448779,
ECO:0000269|PubMed:15345777}.
MOD_RES 4 4 Citrulline; alternate.
{ECO:0000269|PubMed:15345777,
ECO:0000269|PubMed:16567635}.
MOD_RES 4 4 Omega-N-methylarginine; by PRMT1;
alternate. {ECO:0000269|PubMed:11387442,
ECO:0000269|PubMed:11448779,
ECO:0000269|PubMed:15345777}.
MOD_RES 4 4 Symmetric dimethylarginine; by PRMT5 and
PRMT7; alternate.
{ECO:0000250|UniProtKB:P62806}.
MOD_RES 6 6 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 6 6 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:2474456,
ECO:0000269|PubMed:7664735}.
MOD_RES 6 6 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 6 6 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 9 9 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 9 9 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 9 9 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:2474456,
ECO:0000269|PubMed:7664735}.
MOD_RES 9 9 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:17267393,
ECO:0000269|PubMed:27105113}.
MOD_RES 9 9 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 9 9 N6-propionyllysine; alternate.
{ECO:0000269|PubMed:17267393}.
MOD_RES 13 13 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 13 13 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 13 13 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:17967882,
ECO:0000269|PubMed:2474456,
ECO:0000269|PubMed:7664735}.
MOD_RES 13 13 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 13 13 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 13 13 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MOD_RES 17 17 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 17 17 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:17967882,
ECO:0000269|PubMed:2474456,
ECO:0000269|PubMed:7664735}.
MOD_RES 17 17 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:17267393,
ECO:0000269|PubMed:27105113}.
MOD_RES 17 17 N6-crotonyllysine; alternate.
{ECO:0000250|UniProtKB:P62806}.
MOD_RES 17 17 N6-propionyllysine; alternate.
{ECO:0000269|PubMed:17267393}.
MOD_RES 21 21 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:12086618,
ECO:0000269|PubMed:15964846,
ECO:0000269|PubMed:17967882}.
MOD_RES 21 21 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:12086618,
ECO:0000269|PubMed:15964846,
ECO:0000269|PubMed:17967882}.
MOD_RES 21 21 N6-methyllysine; alternate.
{ECO:0000269|PubMed:12086618,
ECO:0000269|PubMed:15964846,
ECO:0000269|PubMed:17967882}.
MOD_RES 32 32 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 32 32 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 32 32 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 32 32 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:17267393}.
MOD_RES 32 32 N6-propionyllysine; alternate.
{ECO:0000269|PubMed:17267393}.
MOD_RES 32 32 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MOD_RES 45 45 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 45 45 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:17267393}.
MOD_RES 45 45 N6-propionyllysine; alternate.
{ECO:0000269|PubMed:17267393}.
MOD_RES 48 48 Phosphoserine; by PAK2.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:21724829}.
MOD_RES 52 52 Phosphotyrosine.
{ECO:0000244|PubMed:15592455,
ECO:0000244|PubMed:20068231}.
MOD_RES 60 60 N6-(2-hydroxyisobutyryl)lysine.
{ECO:0000269|PubMed:24681537}.
MOD_RES 78 78 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 78 78 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 78 78 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:17267393}.
MOD_RES 78 78 N6-propionyllysine; alternate.
{ECO:0000269|PubMed:17267393}.
MOD_RES 78 78 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MOD_RES 80 80 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 80 80 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:17267393}.
MOD_RES 80 80 N6-propionyllysine; alternate.
{ECO:0000269|PubMed:17267393}.
MOD_RES 81 81 Phosphothreonine.
{ECO:0000250|UniProtKB:P62806}.
MOD_RES 89 89 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 92 92 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 92 92 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 92 92 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:19818714}.
MOD_RES 92 92 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:17267393}.
MOD_RES 92 92 N6-propionyllysine; alternate.
{ECO:0000269|PubMed:17267393}.
MOD_RES 92 92 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
CROSSLNK 13 13 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447}.
CROSSLNK 21 21 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 60 60 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 80 80 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 92 92 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 92 92 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:19818714}.
VARIANT 64 64 E -> Q (in a breast cancer sample;
somatic mutation; dbSNP:rs747622981).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036206.
CONFLICT 71 71 V -> A (in Ref. 14; AAH67496).
{ECO:0000305}.
CONFLICT 77 77 A -> P (in Ref. 11; CAG46986).
{ECO:0000305}.
TURN 7 10 {ECO:0000244|PDB:4YYM}.
STRAND 21 23 {ECO:0000244|PDB:3F9X}.
STRAND 28 30 {ECO:0000244|PDB:4H9N}.
HELIX 32 41 {ECO:0000244|PDB:4H9N}.
STRAND 45 47 {ECO:0000244|PDB:5CPK}.
HELIX 49 76 {ECO:0000244|PDB:4H9N}.
STRAND 80 82 {ECO:0000244|PDB:4H9N}.
HELIX 84 91 {ECO:0000244|PDB:4H9N}.
STRAND 94 96 {ECO:0000244|PDB:4H9N}.
TURN 97 102 {ECO:0000244|PDB:4H9N}.
SEQUENCE 103 AA; 11367 MW; A9E5DFD3F8B97598 CRC64;
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG


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