H4_HUMAN
ID H4_HUMAN Reviewed; 103 AA.
AC P62805; A2VCL0; P02304; P02305; Q6DRA9; Q6FGB8; Q6NWP7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Histone H4;
GN Name=H4C1; Synonyms=H4/A, H4FA, HIST1H4A;
GN and
GN Name=H4C2; Synonyms=H4/I, H4FI, HIST1H4B;
GN and
GN Name=H4C3; Synonyms=H4/G, H4FG, HIST1H4C;
GN and
GN Name=H4C4; Synonyms=H4/B, H4FB, HIST1H4D;
GN and
GN Name=H4C5; Synonyms=H4/J, H4FJ, HIST1H4E;
GN and
GN Name=H4C6; Synonyms=H4/C, H4FC, HIST1H4F;
GN and
GN Name=H4C8; Synonyms=H4/H, H4FH, HIST1H4H;
GN and
GN Name=H4C9; Synonyms=H4/M, H4FM, HIST1H4I;
GN and
GN Name=H4C11; Synonyms=H4/E, H4FE, HIST1H4J;
GN and
GN Name=H4C12; Synonyms=H4/D, H4FD, HIST1H4K;
GN and
GN Name=H4C13; Synonyms=H4/K, H4FK, HIST1H4L;
GN and
GN Name=H4C14; Synonyms=H4/N, H4F2, H4FN, HIST2H4, HIST2H4A;
GN and
GN Name=H4C15; Synonyms=H4/O, H4FO, HIST2H4B;
GN and
GN Name=H4-16; Synonyms=HIST4H4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6314274; DOI=10.1093/nar/11.20.7069;
RA Sierra F., Stein G., Stein J.;
RT "Structure and in vitro transcription of a human H4 histone gene.";
RL Nucleic Acids Res. 11:7069-7086(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3035717; DOI=10.1126/science.3035717;
RA Pauli U., Chrysogelos S., Stein G., Stein J., Nick H.;
RT "Protein-DNA interactions in vivo upstream of a cell cycle-regulated human
RT H4 histone gene.";
RL Science 236:1308-1311(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=1916825; DOI=10.1016/0888-7543(91)90183-f;
RA Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.;
RT "Isolation and characterization of two human H1 histone genes within
RT clusters of core histone genes.";
RL Genomics 10:940-948(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7626218; DOI=10.1089/dna.1995.14.591;
RA Drabent B., Kardalinou E., Bode C., Doenecke D.;
RT "Association of histone H4 genes with the mammalian testis-specific H1t
RT histone gene.";
RL DNA Cell Biol. 14:591-597(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9031620; DOI=10.1016/s0378-1119(96)00582-3;
RA Albig W., Meergans T., Doenecke D.;
RT "Characterization of the H1.5 gene completes the set of human H1 subtype
RT genes.";
RL Gene 184:141-148(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9439656; DOI=10.1007/s004390050630;
RA Albig W., Doenecke D.;
RT "The human histone gene cluster at the D6S105 locus.";
RL Hum. Genet. 101:284-294(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9119399; DOI=10.1006/geno.1996.4592;
RA Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D.;
RT "Human histone gene organization: nonregular arrangement within a large
RT cluster.";
RL Genomics 40:314-322(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H4C1; H4C2; H4C3; H4C4; H4C5; H4C6;
RP H4C8; H4C9; H4C11; H4C12; H4C13; H4C14 AND H4-16).
RX PubMed=12408966; DOI=10.1006/geno.2002.6850;
RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT "The human and mouse replication-dependent histone genes.";
RL Genomics 80:487-498(2002).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8988030;
RA Akasaka T., Miura I., Takahashi N., Akasaka H., Yonetani N., Ohno H.,
RA Fukuhara S., Okuma M.;
RT "A recurring translocation, t(3;6)(q27;p21), in non-Hodgkin's lymphoma
RT results in replacement of the 5' regulatory region of BCL6 with a novel H4
RT histone gene.";
RL Cancer Res. 57:7-12(1997).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15527963; DOI=10.1016/j.gene.2004.07.036;
RA Braastad C.D., Hovhannisyan H., van Wijnen A.J., Stein J.L., Stein G.S.;
RT "Functional characterization of a human histone gene cluster duplication.";
RL Gene 342:35-40(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (H4C6; H4C8 AND H4C14).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (H4C1; H4C2; H4C3; H4C4;
RP H4C5; H4C6; H4C8; H4C9; H4C11; H4C12 AND H4C13).
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum, Eye, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [15]
RP PROTEIN SEQUENCE OF 25-36; 47-56; 61-78 AND 81-93, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [16]
RP ACETYLATION AT LYS-6; LYS-9; LYS-13 AND LYS-17.
RX PubMed=7664735; DOI=10.1002/j.1460-2075.1995.tb00066.x;
RA O'Neill L.P., Turner B.M.;
RT "Histone H4 acetylation distinguishes coding regions of the human genome
RT from heterochromatin in a differentiation-dependent but transcription-
RT independent manner.";
RL EMBO J. 14:3946-3957(1995).
RN [17]
RP DNA-BINDING REGION.
RX PubMed=3340182; DOI=10.1038/331365a0;
RA Ebralidse K.K., Grachev S.A., Mirzabekov A.D.;
RT "A highly basic histone H4 domain bound to the sharply bent region of
RT nucleosomal DNA.";
RL Nature 331:365-367(1988).
RN [18]
RP ACETYLATION AT LYS-6; LYS-9; LYS-13 AND LYS-17.
RX PubMed=2474456; DOI=10.1016/0014-5793(89)80947-0;
RA Turner B.M., O'Neill L.P., Allan I.M.;
RT "Histone H4 acetylation in human cells. Frequency of acetylation at
RT different sites defined by immunolabeling with site-specific antibodies.";
RL FEBS Lett. 253:141-145(1989).
RN [19]
RP METHYLATION AT ARG-4.
RX PubMed=11448779; DOI=10.1016/s0960-9822(01)00294-9;
RA Strahl B.D., Briggs S.D., Brame C.J., Caldwell J.A., Koh S.S., Ma H.,
RA Cook R.G., Shabanowitz J., Hunt D.F., Stallcup M.R., Allis C.D.;
RT "Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by
RT the nuclear receptor coactivator PRMT1.";
RL Curr. Biol. 11:996-1000(2001).
RN [20]
RP METHYLATION AT ARG-4.
RX PubMed=11387442; DOI=10.1126/science.1060781;
RA Wang H., Huang Z.-Q., Xia L., Feng Q., Erdjument-Bromage H., Strahl B.D.,
RA Briggs S.D., Allis C.D., Wong J., Tempst P., Zhang Y.;
RT "Methylation of histone H4 at arginine 3 facilitating transcriptional
RT activation by nuclear hormone receptor.";
RL Science 293:853-857(2001).
RN [21]
RP INVOLVEMENT IN B-CELL NON-HODGKIN LYMPHOMA, AND CHROMOSOMAL TRANSLOCATION
RP WITH BCL6.
RX PubMed=12414651;
RA Kurata M., Maesako Y., Ueda C., Nishikori M., Akasaka T., Uchiyama T.,
RA Ohno H.;
RT "Characterization of t(3;6)(q27;p21) breakpoints in B-cell non-Hodgkin's
RT lymphoma and construction of the histone H4/BCL6 fusion gene, leading to
RT altered expression of Bcl-6.";
RL Cancer Res. 62:6224-6230(2002).
RN [22]
RP METHYLATION AT LYS-21.
RX PubMed=12086618; DOI=10.1016/s1097-2765(02)00548-8;
RA Nishioka K., Rice J.C., Sarma K., Erdjument-Bromage H., Werner J., Wang Y.,
RA Chuikov S., Valenzuela P., Tempst P., Steward R., Lis J.T., Allis C.D.,
RA Reinberg D.;
RT "PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20
RT of histone H4 and is associated with silent chromatin.";
RL Mol. Cell 9:1201-1213(2002).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [24]
RP SUMOYLATION.
RX PubMed=14578449; DOI=10.1073/pnas.1735528100;
RA Shiio Y., Eisenman R.N.;
RT "Histone sumoylation is associated with transcriptional repression.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13225-13230(2003).
RN [25]
RP CITRULLINATION AT ARG-4, AND METHYLATION AT ARG-4.
RX PubMed=15345777; DOI=10.1126/science.1101400;
RA Wang Y., Wysocka J., Sayegh J., Lee Y.-H., Perlin J.R., Leonelli L.,
RA Sonbuchner L.S., McDonald C.H., Cook R.G., Dou Y., Roeder R.G., Clarke S.,
RA Stallcup M.R., Allis C.D., Coonrod S.A.;
RT "Human PAD4 regulates histone arginine methylation levels via
RT demethylimination.";
RL Science 306:279-283(2004).
RN [26]
RP METHYLATION AT LYS-21.
RX PubMed=15964846; DOI=10.1074/jbc.m501691200;
RA Yin Y., Liu C., Tsai S.N., Zhou B., Ngai S.M., Zhu G.;
RT "SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone
RT H4 and mono-methylates lysine 20.";
RL J. Biol. Chem. 280:30025-30031(2005).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [29]
RP UBIQUITINATION.
RX PubMed=16678110; DOI=10.1016/j.molcel.2006.03.035;
RA Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H.,
RA Tempst P., Xiong Y., Zhang Y.;
RT "Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase
RT facilitates cellular response to DNA damage.";
RL Mol. Cell 22:383-394(2006).
RN [30]
RP CITRULLINATION AT ARG-4.
RX PubMed=16567635; DOI=10.1073/pnas.0509639103;
RA Arita K., Shimizu T., Hashimoto H., Hidaka Y., Yamada M., Sato M.;
RT "Structural basis for histone N-terminal recognition by human
RT peptidylarginine deiminase 4.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5291-5296(2006).
RN [31]
RP ACETYLATION AT SER-2; LYS-13 AND LYS-17, PHOSPHORYLATION AT SER-2, AND
RP METHYLATION AT LYS-21.
RX PubMed=17967882; DOI=10.1128/mcb.01517-07;
RA Pesavento J.J., Yang H., Kelleher N.L., Mizzen C.A.;
RT "Certain and progressive methylation of histone H4 at lysine 20 during the
RT cell cycle.";
RL Mol. Cell. Biol. 28:468-486(2008).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [33]
RP ACETYLATION AT LYS-92, AND UBIQUITINATION AT LYS-92.
RX PubMed=19818714; DOI=10.1016/j.molcel.2009.08.019;
RA Yan Q., Dutt S., Xu R., Graves K., Juszczynski P., Manis J.P., Shipp M.A.;
RT "BBAP monoubiquitylates histone H4 at lysine 91 and selectively modulates
RT the DNA damage response.";
RL Mol. Cell 36:110-120(2009).
RN [34]
RP PROPIONYLATION AT LYS-9; LYS-17; LYS-32; LYS-45; LYS-78; LYS-80 AND LYS-92,
RP AND BUTYRYLATION AT LYS-9; LYS-17; LYS-32; LYS-45; LYS-78; LYS-80 AND
RP LYS-92.
RX PubMed=17267393; DOI=10.1074/mcp.m700021-mcp200;
RA Chen Y., Sprung R., Tang Y., Ball H., Sangras B., Kim S.C., Falck J.R.,
RA Peng J., Gu W., Zhao Y.;
RT "Lysine propionylation and butyrylation are novel post-translational
RT modifications in histones.";
RL Mol. Cell. Proteomics 6:812-819(2007).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [36]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13; LYS-17 AND
RP LYS-32, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND TYR-52, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [38]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [39]
RP CROTONYLATION AT LYS-6; LYS-9 AND LYS-13.
RX PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J.,
RA Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation as a
RT new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [40]
RP PHOSPHORYLATION AT SER-48.
RX PubMed=21724829; DOI=10.1101/gad.2055511;
RA Kang B., Pu M., Hu G., Wen W., Dong Z., Zhao K., Stillman B., Zhang Z.;
RT "Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosome assembly.";
RL Genes Dev. 25:1359-1364(2011).
RN [41]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [42]
RP SUCCINYLATION AT LYS-13; LYS-32; LYS-78 AND LYS-92.
RX PubMed=22389435; DOI=10.1074/mcp.m111.015875;
RA Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
RT "Lysine succinylation and lysine malonylation in histones.";
RL Mol. Cell. Proteomics 11:100-107(2012).
RN [43]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [44]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND TYR-89, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [45]
RP HYDROXYBUTYRYLATION AT LYS-6; LYS-9; LYS-13; LYS-17; LYS-32; LYS-45;
RP LYS-60; LYS-78; LYS-80 AND LYS-92.
RX PubMed=24681537; DOI=10.1038/nchembio.1497;
RA Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H., Debernardi A.,
RA Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z., Allis C.D., Ren B.,
RA Khochbin S., Zhao Y.;
RT "Lysine 2-hydroxyisobutyrylation is a widely distributed active histone
RT mark.";
RL Nat. Chem. Biol. 10:365-370(2014).
RN [46]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [47]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [48]
RP BUTYRYLATION AT LYS-6; LYS-9; LYS-13 AND LYS-17.
RX PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014;
RA Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z.,
RA Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J.,
RA Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C., Panne D.,
RA Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.;
RT "Dynamic competing histone H4 K5K8 acetylation and butyrylation are
RT hallmarks of highly active gene promoters.";
RL Mol. Cell 62:169-180(2016).
RN [49]
RP HYDROXYBUTYRYLATION AT LYS-9; LYS-13; LYS-32; LYS-78 AND LYS-92.
RX PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
RA Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
RA Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
RA Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
RA White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
RT "Metabolic regulation of gene expression by histone lysine beta-
RT hydroxybutyrylation.";
RL Mol. Cell 62:194-206(2016).
RN [50]
RP CROTONYLATION AT LYS-9 AND LYS-13.
RX PubMed=28497810; DOI=10.1038/cr.2017.68;
RA Wei W., Liu X., Chen J., Gao S., Lu L., Zhang H., Ding G., Wang Z.,
RA Chen Z., Shi T., Li J., Yu J., Wong J.;
RT "Class I histone deacetylases are major histone decrotonylases: evidence
RT for critical and broad function of histone crotonylation in
RT transcription.";
RL Cell Res. 27:898-915(2017).
RN [51]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-21; LYS-32; LYS-60; LYS-80 AND
RP LYS-92, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [52]
RP GLUTARYLATION AT LYS-6; LYS-13; LYS-32; LYS-60 LYS-78; LYS-80 AND LYS-92.
RX PubMed=31542297; DOI=10.1016/j.molcel.2019.08.018;
RA Bao X., Liu Z., Zhang W., Gladysz K., Fung Y.M.E., Tian G., Xiong Y.,
RA Wong J.W.H., Yuen K.W.Y., Li X.D.;
RT "Glutarylation of histone H4 lysine 91 regulates chromatin dynamics.";
RL Mol. Cell 0:0-0(2019).
RN [53]
RP UFMYLATION AT LYS-32, AND MUTAGENESIS OF LYS-32.
RX PubMed=30886146; DOI=10.1038/s41467-019-09175-0;
RA Qin B., Yu J., Nowsheen S., Wang M., Tu X., Liu T., Li H., Wang L., Lou Z.;
RT "UFL1 promotes histone H4 ufmylation and ATM activation.";
RL Nat. Commun. 10:1242-1242(2019).
RN [54]
RP LACTYLATION AT LYS-6; LYS-9; LYS-13; LYS-17; LYS-32; LYS-78 AND LYS-92.
RX PubMed=31645732; DOI=10.1038/s41586-019-1678-1;
RA Zhang D., Tang Z., Huang H., Zhou G., Cui C., Weng Y., Liu W., Kim S.,
RA Lee S., Perez-Neut M., Ding J., Czyz D., Hu R., Ye Z., He M., Zheng Y.G.,
RA Shuman H.A., Dai L., Ren B., Roeder R.G., Becker L., Zhao Y.;
RT "Metabolic regulation of gene expression by histone lactylation.";
RL Nature 574:575-580(2019).
RN [55]
RP METHYLATION AT LYS-13, AND MUTAGENESIS OF LYS-13.
RX PubMed=31061526; DOI=10.1038/s41594-019-0219-9;
RA Metzger E., Wang S., Urban S., Willmann D., Schmidt A., Offermann A.,
RA Allen A., Sum M., Obier N., Cottard F., Ulferts S., Preca B.T., Hermann B.,
RA Maurer J., Greschik H., Hornung V., Einsle O., Perner S., Imhof A.,
RA Jung M., Schule R.;
RT "KMT9 monomethylates histone H4 lysine 12 and controls proliferation of
RT prostate cancer cells.";
RL Nat. Struct. Mol. Biol. 26:361-371(2019).
RN [56]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=15951514; DOI=10.1093/nar/gki663;
RA Tsunaka Y., Kajimura N., Tate S., Morikawa K.;
RT "Alteration of the nucleosomal DNA path in the crystal structure of a human
RT nucleosome core particle.";
RL Nucleic Acids Res. 33:3424-3434(2005).
RN [57] {ECO:0007744|PDB:5AY8}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH H2A; H2B AND H3.Y.
RX PubMed=27016736; DOI=10.1093/nar/gkw202;
RA Kujirai T., Horikoshi N., Sato K., Maehara K., Machida S., Osakabe A.,
RA Kimura H., Ohkawa Y., Kurumizaka H.;
RT "Structure and function of human histone H3.Y nucleosome.";
RL Nucleic Acids Res. 44:6127-6141(2016).
RN [58] {ECO:0007744|PDB:5JA4}
RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 2-103 IN COMPLEX WITH TONSL, AND
RP METHYLATION AT LYS-21.
RX PubMed=27338793; DOI=10.1038/nature18312;
RA Saredi G., Huang H., Hammond C.M., Alabert C., Bekker-Jensen S., Forne I.,
RA Reveron-Gomez N., Foster B.M., Mlejnkova L., Bartke T., Cejka P.,
RA Mailand N., Imhof A., Patel D.J., Groth A.;
RT "H4K20me0 marks post-replicative chromatin and recruits the TONSL-MMS22L
RT DNA repair complex.";
RL Nature 534:714-718(2016).
RN [59] {ECO:0007744|PDB:7CCQ, ECO:0007744|PDB:7CCR}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 24-103 IN COMPLEX WITH
RP NUCLEOSOME CORE AND CGAS.
RX PubMed=33051594; DOI=10.1038/s41422-020-00422-4;
RA Cao D., Han X., Fan X., Xu R.M., Zhang X.;
RT "Structural basis for nucleosome-mediated inhibition of cGAS activity.";
RL Cell Res. 30:1088-1097(2020).
RN [60] {ECO:0007744|PDB:6Y5D}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS) IN COMPLEX WITH
RP NUCLEOSOME CORE AND CGAS.
RX PubMed=32911482; DOI=10.1038/s41586-020-2750-6;
RA Pathare G.R., Decout A., Glueck S., Cavadini S., Makasheva K., Hovius R.,
RA Kempf G., Weiss J., Kozicka Z., Guey B., Melenec P., Fierz B., Thomae N.H.,
RA Ablasser A.;
RT "Structural mechanism of cGAS inhibition by the nucleosome.";
RL Nature 587:668-672(2020).
RN [61] {ECO:0007744|PDB:6X59, ECO:0007744|PDB:6X5A, ECO:0007744|PDB:6XJD}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.98 ANGSTROMS) OF 2-103 IN COMPLEX WITH
RP NUCLEOSOME CORE AND CGAS.
RX PubMed=32911481; DOI=10.1038/s41586-020-2749-z;
RA Zhao B., Xu P., Rowlett C.M., Jing T., Shinde O., Lei Y., West A.P.,
RA Liu W.R., Li P.;
RT "The molecular basis of tight nuclear tethering and inactivation of cGAS.";
RL Nature 587:673-677(2020).
RN [62] {ECO:0007744|PDB:7A08}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.11 ANGSTROMS) OF 2-103 IN COMPLEX WITH
RP NUCLEOSOME CORE AND CGAS.
RX PubMed=32911480; DOI=10.1038/s41586-020-2748-0;
RA Michalski S., de Oliveira Mann C.C., Stafford C.A., Witte G., Bartho J.,
RA Lammens K., Hornung V., Hopfner K.P.;
RT "Structural basis for sequestration and autoinhibition of cGAS by
RT chromatin.";
RL Nature 587:678-682(2020).
RN [63] {ECO:0007744|PDB:6USJ}
RP STRUCTURE BY ELECTRON MICROSCOPY (10.50 ANGSTROMS) OF NUCLEOSOME CORE
RP COMPLEX IN COMPLEX WITH PARP2.
RX PubMed=33141820; DOI=10.1371/journal.pone.0240932;
RA Gaullier G., Roberts G., Muthurajan U.M., Bowerman S., Rudolph J.,
RA Mahadevan J., Jha A., Rae P.S., Luger K.;
RT "Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances
RT its interaction with HPF1.";
RL PLoS ONE 15:e0240932-e0240932(2020).
RN [64] {ECO:0007744|PDB:7JO9, ECO:0007744|PDB:7JOA}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) IN COMPLEX WITH
RP NUCLEOSOME CORE AND CGAS.
RX PubMed=32913000; DOI=10.1126/science.abd0609;
RA Boyer J.A., Spangler C.J., Strauss J.D., Cesmat A.P., Liu P., McGinty R.K.,
RA Zhang Q.;
RT "Structural basis of nucleosome-dependent cGAS inhibition.";
RL Science 370:450-454(2020).
RN [65] {ECO:0007744|PDB:7C0M}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 2-103 IN COMPLEX WITH
RP NUCLEOSOME CORE AND CGAS.
RX PubMed=32912999; DOI=10.1126/science.abd0237;
RA Kujirai T., Zierhut C., Takizawa Y., Kim R., Negishi L., Uruma N.,
RA Hirai S., Funabiki H., Kurumizaka H.;
RT "Structural basis for the inhibition of cGAS by nucleosomes.";
RL Science 370:455-458(2020).
RN [66] {ECO:0007744|PDB:7CIZ, ECO:0007744|PDB:7CJ0}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH DNJC9 171-249 MUTANT
RP CYS-243; MCM2 61-130 AND HISTONE H3.3, IDENTIFICATION IN A CO-CHAPERONE
RP COMPLEX WITH DNJC9; MCM2 AND HISTONE H3.3, AND INTERACTION WITH DNJC9.
RX PubMed=33857403; DOI=10.1016/j.molcel.2021.03.041;
RA Hammond C.M., Bao H., Hendriks I.A., Carraro M., Garcia-Nieto A., Liu Y.,
RA Reveron-Gomez N., Spanos C., Chen L., Rappsilber J., Nielsen M.L.,
RA Patel D.J., Huang H., Groth A.;
RT "DNAJC9 integrates heat shock molecular chaperones into the histone
RT chaperone network.";
RL Mol. Cell 0:0-0(2021).
RN [67]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-64.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC DNA into chromatin, limiting DNA accessibility to the cellular
CC machineries which require DNA as a template. Histones thereby play a
CC central role in transcription regulation, DNA repair, DNA replication
CC and chromosomal stability. DNA accessibility is regulated via a complex
CC set of post-translational modifications of histones, also called
CC histone code, and nucleosome remodeling.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA
CC (By similarity). Found in a co-chaperone complex with DNJC9, MCM2 and
CC histone H3.3-H4 dimers (PubMed:33857403). Within the complex, interacts
CC with DNJC9 (via C-terminus); the interaction is direct
CC (PubMed:33857403). {ECO:0000250|UniProtKB:P62806,
CC ECO:0000269|PubMed:33857403}.
CC -!- INTERACTION:
CC P62805; P35609: ACTN2; NbExp=3; IntAct=EBI-302023, EBI-77797;
CC P62805; Q9Y294: ASF1A; NbExp=15; IntAct=EBI-302023, EBI-749553;
CC P62805; Q12830: BPTF; NbExp=3; IntAct=EBI-302023, EBI-1560273;
CC P62805; Q12830-4: BPTF; NbExp=16; IntAct=EBI-302023, EBI-4288838;
CC P62805; P25440: BRD2; NbExp=5; IntAct=EBI-302023, EBI-2874802;
CC P62805; O60885-1: BRD4; NbExp=10; IntAct=EBI-302023, EBI-9345088;
CC P62805; P55201: BRPF1; NbExp=8; IntAct=EBI-302023, EBI-2837428;
CC P62805; P45973: CBX5; NbExp=3; IntAct=EBI-302023, EBI-78219;
CC P62805; P49450: CENPA; NbExp=6; IntAct=EBI-302023, EBI-1751979;
CC P62805; P49450-1: CENPA; NbExp=2; IntAct=EBI-302023, EBI-15826012;
CC P62805; Q9NQ92: COPRS; NbExp=3; IntAct=EBI-302023, EBI-1642558;
CC P62805; Q92793: CREBBP; NbExp=6; IntAct=EBI-302023, EBI-81215;
CC P62805; P04908: H2AC8; NbExp=11; IntAct=EBI-302023, EBI-358971;
CC P62805; P16104: H2AX; NbExp=5; IntAct=EBI-302023, EBI-494830;
CC P62805; P84243: H3-3B; NbExp=12; IntAct=EBI-302023, EBI-120658;
CC P62805; Q16695: H3-4; NbExp=3; IntAct=EBI-302023, EBI-358900;
CC P62805; P68431: H3C12; NbExp=7; IntAct=EBI-302023, EBI-79722;
CC P62805; Q71DI3: H3C15; NbExp=4; IntAct=EBI-302023, EBI-750650;
CC P62805; O14929: HAT1; NbExp=7; IntAct=EBI-302023, EBI-2339359;
CC P62805; Q13547: HDAC1; NbExp=3; IntAct=EBI-302023, EBI-301834;
CC P62805; P42858: HTT; NbExp=3; IntAct=EBI-302023, EBI-466029;
CC P62805; Q9H9V9: JMJD4; NbExp=3; IntAct=EBI-302023, EBI-2866290;
CC P62805; Q92993: KAT5; NbExp=4; IntAct=EBI-302023, EBI-399080;
CC P62805; O75164: KDM4A; NbExp=7; IntAct=EBI-302023, EBI-936709;
CC P62805; Q9NQR1: KMT5A; NbExp=6; IntAct=EBI-302023, EBI-1268946;
CC P62805; Q9Y468: L3MBTL1; NbExp=4; IntAct=EBI-302023, EBI-1265089;
CC P62805; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-302023, EBI-11742507;
CC P62805; Q05BQ5: MBTD1; NbExp=3; IntAct=EBI-302023, EBI-5666902;
CC P62805; P49736: MCM2; NbExp=9; IntAct=EBI-302023, EBI-374819;
CC P62805; P25205: MCM3; NbExp=2; IntAct=EBI-302023, EBI-355153;
CC P62805; P33992: MCM5; NbExp=2; IntAct=EBI-302023, EBI-359410;
CC P62805; Q86UY6-1: NAA40; NbExp=3; IntAct=EBI-302023, EBI-16140302;
CC P62805; Q9BVI0: PHF20; NbExp=3; IntAct=EBI-302023, EBI-2560802;
CC P62805; A8MW92: PHF20L1; NbExp=2; IntAct=EBI-302023, EBI-2560834;
CC P62805; P17252: PRKCA; NbExp=3; IntAct=EBI-302023, EBI-1383528;
CC P62805; Q99873: PRMT1; NbExp=2; IntAct=EBI-302023, EBI-78738;
CC P62805; O14744: PRMT5; NbExp=6; IntAct=EBI-302023, EBI-351098;
CC P62805; P62826: RAN; NbExp=2; IntAct=EBI-302023, EBI-286642;
CC P62805; Q16576: RBBP7; NbExp=9; IntAct=EBI-302023, EBI-352227;
CC P62805; Q14684-1: RRP1B; NbExp=3; IntAct=EBI-302023, EBI-5280110;
CC P62805; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-302023, EBI-9090795;
CC P62805; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-302023, EBI-747107;
CC P62805; O60264: SMARCA5; NbExp=2; IntAct=EBI-302023, EBI-352588;
CC P62805; Q12824: SMARCB1; NbExp=2; IntAct=EBI-302023, EBI-358419;
CC P62805; Q04724: TLE1; NbExp=6; IntAct=EBI-302023, EBI-711424;
CC P62805; Q12888: TP53BP1; NbExp=14; IntAct=EBI-302023, EBI-396540;
CC P62805; Q12888-1: TP53BP1; NbExp=3; IntAct=EBI-302023, EBI-8022649;
CC P62805; P61981: YWHAG; NbExp=3; IntAct=EBI-302023, EBI-359832;
CC P62805; P63104: YWHAZ; NbExp=3; IntAct=EBI-302023, EBI-347088;
CC P62805; P45481: Crebbp; Xeno; NbExp=2; IntAct=EBI-302023, EBI-296306;
CC P62805; Q9QR71: LANA1; Xeno; NbExp=2; IntAct=EBI-302023, EBI-15602554;
CC P62805; Q582G4: PRMT7; Xeno; NbExp=4; IntAct=EBI-302023, EBI-16101095;
CC P62805; P38890: SET5; Xeno; NbExp=2; IntAct=EBI-302023, EBI-24263;
CC P62805; Q9VK33: Sfmbt; Xeno; NbExp=10; IntAct=EBI-302023, EBI-117801;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac)
CC and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in
CC heterochromatin. {ECO:0000269|PubMed:17967882,
CC ECO:0000269|PubMed:2474456, ECO:0000269|PubMed:7664735}.
CC -!- PTM: Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation.
CC {ECO:0000269|PubMed:11387442, ECO:0000269|PubMed:11448779,
CC ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:16567635}.
CC -!- PTM: Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and
CC H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac)
CC and Lys-13 (H4K12ac). Demethylation is performed by JMJD6. Symmetric
CC dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a
CC crucial role in the germ-cell lineage. {ECO:0000269|PubMed:11387442,
CC ECO:0000269|PubMed:11448779, ECO:0000269|PubMed:15345777}.
CC -!- PTM: Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1,
CC H4K20me2, H4K20me3) (PubMed:12086618, PubMed:15964846,
CC PubMed:17967882). Monomethylation is performed by KMT5A/SET8
CC (PubMed:15964846). Dimethylation and trimethylation is performed by
CC KMT5B and KMT5C and induces gene silencing (By similarity).
CC Monomethylated at Lys-13 (H4K12me1) by N6AMT1; H4K12me1 modification is
CC present at the promoters of numerous genes encoding cell cycle
CC regulators (PubMed:31061526). {ECO:0000250|UniProtKB:P62806,
CC ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:15964846,
CC ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:31061526}.
CC -!- PTM: Phosphorylated by PAK2 at Ser-48 (H4S47ph). This phosphorylation
CC increases the association of H3.3-H4 with the histone chaperone HIRA,
CC thus promoting nucleosome assembly of H3.3-H4 and inhibiting nucleosome
CC assembly of H3.1-H4. {ECO:0000269|PubMed:17967882,
CC ECO:0000269|PubMed:21724829}.
CC -!- PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to
CC ultraviolet irradiation. This may weaken the interaction between
CC histones and DNA and facilitate DNA accessibility to repair proteins.
CC Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in response to DNA
CC damage. The exact role of H4K91ub1 in DNA damage response is still
CC unclear but it may function as a licensing signal for additional
CC histone H4 post-translational modifications such as H4 Lys-21
CC methylation (H4K20me). {ECO:0000269|PubMed:12086618,
CC ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:16678110,
CC ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:19818714}.
CC -!- PTM: Ufmylated; monofmylated by UFL1 at Lys-32 (H4K31Ufm1) in response
CC to DNA damage. {ECO:0000269|PubMed:30886146}.
CC -!- PTM: Sumoylated, which is associated with transcriptional repression.
CC {ECO:0000269|PubMed:14578449}.
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ cells and
CC marks testis-specific genes in post-meiotic cells, including X-linked
CC genes that escape sex chromosome inactivation in haploid cells.
CC Crotonylation marks active promoters and enhancers and confers
CC resistance to transcriptional repressors. It is also associated with
CC post-meiotically activated genes on autosomes.
CC {ECO:0000269|PubMed:21925322}.
CC -!- PTM: Butyrylation of histones marks active promoters and competes with
CC histone acetylation. {ECO:0000250|UniProtKB:P62806}.
CC -!- PTM: Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by
CC promoting dissociation of the H2A-H2B dimers from nucleosomes.
CC {ECO:0000269|PubMed:31542297}.
CC -!- PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA
CC directly derived from endogenous or exogenous lactate, leading to
CC stimulates gene transcription. {ECO:0000269|PubMed:31645732}.
CC -!- DISEASE: Note=Chromosomal aberrations involving HISTONE H4 is a cause
CC of B-cell non-Hodgkin lymphomas (B-cell NHL). Translocation
CC t(3;6)(q27;p21), with BCL6. {ECO:0000269|PubMed:12414651}.
CC -!- SIMILARITY: Belongs to the histone H4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI28106.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X00038; CAA24918.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M16707; AAA52652.1; -; Genomic_DNA.
DR EMBL; M60749; AAA63188.1; -; Genomic_DNA.
DR EMBL; X60481; CAA43011.1; -; Genomic_DNA.
DR EMBL; X60482; CAA43012.1; -; Genomic_DNA.
DR EMBL; X60483; CAA43013.1; -; Genomic_DNA.
DR EMBL; X60484; CAA43014.1; -; Genomic_DNA.
DR EMBL; X60486; CAA43016.1; -; Genomic_DNA.
DR EMBL; X60487; CAA43017.1; -; Genomic_DNA.
DR EMBL; X67081; CAA47464.1; -; Genomic_DNA.
DR EMBL; Z80787; CAB02549.1; -; Genomic_DNA.
DR EMBL; X83548; CAA58538.1; -; Genomic_DNA.
DR EMBL; AF525682; AAM83108.1; -; Genomic_DNA.
DR EMBL; AY128653; AAN01438.1; -; Genomic_DNA.
DR EMBL; AY128654; AAN01439.1; -; Genomic_DNA.
DR EMBL; AY128655; AAN01440.1; -; Genomic_DNA.
DR EMBL; AY128656; AAN01441.1; -; Genomic_DNA.
DR EMBL; AY128657; AAN01442.1; -; Genomic_DNA.
DR EMBL; AY128658; AAN01443.1; -; Genomic_DNA.
DR EMBL; AY128659; AAN01444.1; -; Genomic_DNA.
DR EMBL; AY128661; AAN01446.1; -; Genomic_DNA.
DR EMBL; AY128662; AAN01447.1; -; Genomic_DNA.
DR EMBL; AY128663; AAN01448.1; -; Genomic_DNA.
DR EMBL; AY128664; AAN01449.1; -; Genomic_DNA.
DR EMBL; AY128665; AAN01450.1; -; Genomic_DNA.
DR EMBL; AB000905; BAA19208.1; -; Genomic_DNA.
DR EMBL; AY648850; AAT68253.1; -; Genomic_DNA.
DR EMBL; CR542169; CAG46966.1; -; mRNA.
DR EMBL; CR542172; CAG46969.1; -; mRNA.
DR EMBL; CR542180; CAG46977.1; -; mRNA.
DR EMBL; CR542187; CAG46984.1; -; mRNA.
DR EMBL; CR542189; CAG46986.1; -; mRNA.
DR EMBL; AL021807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL021917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z98744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591493; CAI12560.1; -; Genomic_DNA.
DR EMBL; AL591493; CAI12567.1; -; Genomic_DNA.
DR EMBL; CH471087; EAW55509.1; -; Genomic_DNA.
DR EMBL; CH471087; EAW55510.1; -; Genomic_DNA.
DR EMBL; CH471087; EAW55538.1; -; Genomic_DNA.
DR EMBL; CH471087; EAW55549.1; -; Genomic_DNA.
DR EMBL; CH471087; EAW55555.1; -; Genomic_DNA.
DR EMBL; CH471094; EAW96325.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03086.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03111.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03112.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03121.1; -; Genomic_DNA.
DR EMBL; BC017361; AAH17361.1; -; mRNA.
DR EMBL; BC054014; AAH54014.1; -; mRNA.
DR EMBL; BC066248; AAH66248.1; -; mRNA.
DR EMBL; BC066249; AAH66249.1; -; mRNA.
DR EMBL; BC066250; AAH66250.1; -; mRNA.
DR EMBL; BC067495; AAH67495.1; -; mRNA.
DR EMBL; BC067496; AAH67496.1; -; mRNA.
DR EMBL; BC067497; AAH67497.1; -; mRNA.
DR EMBL; BC069288; AAH69288.1; -; mRNA.
DR EMBL; BC069392; AAH69392.1; -; mRNA.
DR EMBL; BC069467; AAH69467.1; -; mRNA.
DR EMBL; BC069654; AAH69654.1; -; mRNA.
DR EMBL; BC093763; AAH93763.1; -; mRNA.
DR EMBL; BC093765; AAH93765.1; -; mRNA.
DR EMBL; BC093969; AAH93969.1; -; mRNA.
DR EMBL; BC111093; AAI11094.1; -; mRNA.
DR EMBL; BC111434; AAI11435.1; -; mRNA.
DR EMBL; BC112193; AAI12194.1; -; mRNA.
DR EMBL; BC120939; AAI20940.1; -; mRNA.
DR EMBL; BC128104; AAI28105.1; -; mRNA.
DR EMBL; BC128105; AAI28106.1; ALT_FRAME; mRNA.
DR EMBL; BC130558; AAI30559.1; -; mRNA.
DR EMBL; BC130560; AAI30561.1; -; mRNA.
DR EMBL; BC143045; AAI43046.1; -; mRNA.
DR CCDS; CCDS30847.1; -.
DR CCDS; CCDS30851.1; -.
DR CCDS; CCDS4571.1; -.
DR CCDS; CCDS4572.1; -.
DR CCDS; CCDS4583.1; -.
DR CCDS; CCDS4589.1; -.
DR CCDS; CCDS4593.1; -.
DR CCDS; CCDS4598.1; -.
DR CCDS; CCDS4604.1; -.
DR CCDS; CCDS4620.1; -.
DR CCDS; CCDS4630.1; -.
DR CCDS; CCDS4631.1; -.
DR CCDS; CCDS4637.1; -.
DR CCDS; CCDS8665.1; -.
DR PIR; D40335; HSHU4.
DR RefSeq; NP_001029249.1; NM_001034077.4.
DR RefSeq; NP_003486.1; NM_003495.2.
DR RefSeq; NP_003529.1; NM_003538.3.
DR RefSeq; NP_003530.1; NM_003539.3.
DR RefSeq; NP_003531.1; NM_003540.3.
DR RefSeq; NP_003532.1; NM_003541.2.
DR RefSeq; NP_003533.1; NM_003542.3.
DR RefSeq; NP_003534.1; NM_003543.3.
DR RefSeq; NP_003535.1; NM_003544.2.
DR RefSeq; NP_003536.1; NM_003545.3.
DR RefSeq; NP_003537.1; NM_003546.2.
DR RefSeq; NP_003539.1; NM_003548.2.
DR RefSeq; NP_068803.1; NM_021968.3.
DR RefSeq; NP_778224.1; NM_175054.2.
DR PDB; 1ZKK; X-ray; 1.45 A; E/F/G/H=16-25.
DR PDB; 2BQZ; X-ray; 1.50 A; B/F=18-26.
DR PDB; 2CV5; X-ray; 2.50 A; B/F=1-103.
DR PDB; 2IG0; X-ray; 1.70 A; B=17-26.
DR PDB; 2KWN; NMR; -; B=10-24.
DR PDB; 2KWO; NMR; -; B=2-21.
DR PDB; 2LVM; NMR; -; B=15-28.
DR PDB; 2QQS; X-ray; 2.82 A; C/D=17-26.
DR PDB; 2RJE; X-ray; 1.86 A; P/Q=16-26.
DR PDB; 2RNY; NMR; -; B=14-28.
DR PDB; 2RS9; NMR; -; A=2-11.
DR PDB; 3A6N; X-ray; 2.70 A; B/F=1-103.
DR PDB; 3AFA; X-ray; 2.50 A; B/F=1-103.
DR PDB; 3AN2; X-ray; 3.60 A; B/F=1-103.
DR PDB; 3AV1; X-ray; 2.50 A; B/F=1-103.
DR PDB; 3AV2; X-ray; 2.80 A; B/F=1-103.
DR PDB; 3AYW; X-ray; 2.90 A; B/F=1-103.
DR PDB; 3AZE; X-ray; 3.00 A; B/F=1-103.
DR PDB; 3AZF; X-ray; 2.70 A; B/F=1-103.
DR PDB; 3AZG; X-ray; 2.40 A; B/F=1-103.
DR PDB; 3AZH; X-ray; 3.49 A; B/F=1-103.
DR PDB; 3AZI; X-ray; 2.70 A; B/F=1-103.
DR PDB; 3AZJ; X-ray; 2.89 A; B/F=1-103.
DR PDB; 3AZK; X-ray; 3.20 A; B/F=1-103.
DR PDB; 3AZL; X-ray; 2.70 A; B/F=1-103.
DR PDB; 3AZM; X-ray; 2.89 A; B/F=1-103.
DR PDB; 3AZN; X-ray; 3.00 A; B/F=1-103.
DR PDB; 3CFS; X-ray; 2.40 A; E=28-42.
DR PDB; 3CFV; X-ray; 2.60 A; E/F=25-42.
DR PDB; 3F9W; X-ray; 1.60 A; E/F/G/H=16-25.
DR PDB; 3F9X; X-ray; 1.25 A; E/F/G/H=16-25.
DR PDB; 3F9Y; X-ray; 1.50 A; E/F=16-25.
DR PDB; 3F9Z; X-ray; 1.60 A; E/F/G/H=16-25.
DR PDB; 3IJ1; X-ray; 2.10 A; B=16-26.
DR PDB; 3JPX; X-ray; 2.05 A; B=14-28.
DR PDB; 3NQJ; X-ray; 2.10 A; B=21-103.
DR PDB; 3NQU; X-ray; 2.50 A; B=1-103.
DR PDB; 3O36; X-ray; 1.70 A; D/E=15-20.
DR PDB; 3QBY; X-ray; 1.95 A; H=16-26.
DR PDB; 3QZS; X-ray; 1.80 A; C/D=13-22.
DR PDB; 3QZT; X-ray; 1.50 A; B=13-22.
DR PDB; 3QZV; X-ray; 2.00 A; C=8-18.
DR PDB; 3R45; X-ray; 2.60 A; B=1-103.
DR PDB; 3UVW; X-ray; 1.37 A; B=2-12.
DR PDB; 3UVX; X-ray; 1.91 A; B=12-22.
DR PDB; 3UVY; X-ray; 2.02 A; B=16-26.
DR PDB; 3UW9; X-ray; 2.30 A; E/F=8-18.
DR PDB; 3W96; X-ray; 3.00 A; B/F=1-103.
DR PDB; 3W97; X-ray; 3.20 A; B/F=1-103.
DR PDB; 3W98; X-ray; 3.42 A; B/F=1-103.
DR PDB; 3W99; X-ray; 3.00 A; B/F=17-103.
DR PDB; 3WA9; X-ray; 3.07 A; B/F=1-103.
DR PDB; 3WAA; X-ray; 3.20 A; B/F=1-103.
DR PDB; 3WKJ; X-ray; 2.80 A; B/F=1-103.
DR PDB; 3WTP; X-ray; 2.67 A; B/F=1-103.
DR PDB; 3X1S; X-ray; 2.81 A; B/F=2-103.
DR PDB; 3X1T; X-ray; 2.81 A; B/F=2-103.
DR PDB; 3X1U; X-ray; 3.25 A; B/F=2-103.
DR PDB; 3X1V; X-ray; 2.92 A; B/F=2-103.
DR PDB; 4GQB; X-ray; 2.06 A; C=2-22.
DR PDB; 4H9N; X-ray; 1.95 A; B=2-103.
DR PDB; 4H9O; X-ray; 2.05 A; B=2-103.
DR PDB; 4H9P; X-ray; 2.20 A; B=2-103.
DR PDB; 4H9Q; X-ray; 1.95 A; B=2-103.
DR PDB; 4H9R; X-ray; 2.20 A; B=2-103.
DR PDB; 4H9S; X-ray; 2.60 A; C/D=21-103.
DR PDB; 4HGA; X-ray; 2.80 A; C=1-103.
DR PDB; 4M38; X-ray; 2.20 A; E/F=2-22.
DR PDB; 4N3W; X-ray; 1.90 A; C=14-28.
DR PDB; 4N4F; X-ray; 1.83 A; C=6-26.
DR PDB; 4QUT; X-ray; 1.70 A; B=10-16.
DR PDB; 4QUU; X-ray; 1.80 A; B=4-16.
DR PDB; 4QYD; X-ray; 1.94 A; B=5-18.
DR PDB; 4U9W; X-ray; 2.49 A; E/F/G/H=2-6.
DR PDB; 4YM5; X-ray; 4.00 A; B/F=1-103.
DR PDB; 4YM6; X-ray; 3.51 A; B/F=1-103.
DR PDB; 4YY6; X-ray; 1.45 A; Z=2-12.
DR PDB; 4YYD; X-ray; 1.52 A; Z=2-12.
DR PDB; 4YYG; X-ray; 2.10 A; B=2-12.
DR PDB; 4YYH; X-ray; 1.74 A; Y/Z=2-12.
DR PDB; 4YYI; X-ray; 1.50 A; C/F=2-12.
DR PDB; 4YYJ; X-ray; 1.85 A; C/F=2-12.
DR PDB; 4YYK; X-ray; 1.79 A; C/F=2-12.
DR PDB; 4YYM; X-ray; 1.50 A; Z=2-12.
DR PDB; 4YYN; X-ray; 1.85 A; Z=2-12.
DR PDB; 4Z2M; X-ray; 2.98 A; H/J=1-103.
DR PDB; 4Z5T; X-ray; 2.80 A; B/F=1-103.
DR PDB; 5AV5; X-ray; 2.40 A; B/F=1-103.
DR PDB; 5AV6; X-ray; 2.20 A; B/F=1-103.
DR PDB; 5AV8; X-ray; 2.20 A; B/F=1-103.
DR PDB; 5AV9; X-ray; 2.20 A; B/F=1-103.
DR PDB; 5AVB; X-ray; 2.40 A; B/F=1-103.
DR PDB; 5AVC; X-ray; 2.40 A; B/F=1-103.
DR PDB; 5AY8; X-ray; 2.80 A; B/F=1-103.
DR PDB; 5B0Y; X-ray; 2.56 A; B/F=1-103.
DR PDB; 5B0Z; X-ray; 1.99 A; B/F=1-103.
DR PDB; 5B24; X-ray; 3.60 A; B/F=1-103.
DR PDB; 5B2I; X-ray; 3.00 A; B/F=1-103.
DR PDB; 5B2J; X-ray; 2.60 A; B/F=1-103.
DR PDB; 5B31; X-ray; 2.20 A; B/F=1-103.
DR PDB; 5B32; X-ray; 2.35 A; B/F=1-103.
DR PDB; 5B33; X-ray; 2.92 A; B/F=1-103.
DR PDB; 5B40; X-ray; 3.33 A; B/F=1-103.
DR PDB; 5BNV; X-ray; 2.79 A; B/E=2-103.
DR PDB; 5BNX; X-ray; 2.31 A; B=2-103.
DR PDB; 5BO0; X-ray; 2.91 A; B=2-103.
DR PDB; 5C3I; X-ray; 3.50 A; C/G/K/O/S/W=1-103.
DR PDB; 5CPI; X-ray; 2.90 A; B/F=1-103.
DR PDB; 5CPJ; X-ray; 3.15 A; B/F=1-103.
DR PDB; 5CPK; X-ray; 2.63 A; B/F=1-103.
DR PDB; 5FA5; X-ray; 2.34 A; C=2-21.
DR PDB; 5FFW; X-ray; 1.50 A; C=2-11.
DR PDB; 5FWE; X-ray; 2.05 A; C/D=2-16.
DR PDB; 5GSE; X-ray; 3.14 A; B/F/L/P=1-103.
DR PDB; 5GSU; X-ray; 3.10 A; B/F=2-103.
DR PDB; 5GT0; X-ray; 2.82 A; B/F=2-103.
DR PDB; 5GT3; X-ray; 2.91 A; B/F=2-103.
DR PDB; 5GTC; X-ray; 2.70 A; B/F=1-103.
DR PDB; 5GXQ; X-ray; 2.85 A; B/F=1-103.
DR PDB; 5JA4; X-ray; 2.42 A; B=2-103.
DR PDB; 5JRG; X-ray; 2.50 A; B/F=1-103.
DR PDB; 5KDM; X-ray; 3.50 A; B=2-103.
DR PDB; 5TEG; X-ray; 1.30 A; D/E=17-24.
DR PDB; 5X7X; X-ray; 2.18 A; B/F=1-103.
DR PDB; 5XF3; X-ray; 2.60 A; B/F=1-103.
DR PDB; 5XF4; X-ray; 2.87 A; B/F=1-103.
DR PDB; 5XF5; X-ray; 2.82 A; B/F=1-103.
DR PDB; 5Y0C; X-ray; 2.09 A; B/F=1-103.
DR PDB; 5Y0D; X-ray; 1.99 A; B/F=1-103.
DR PDB; 5YE3; X-ray; 1.70 A; C=2-13.
DR PDB; 5YE4; X-ray; 1.80 A; E/F=2-13.
DR PDB; 5Z23; X-ray; 2.73 A; B/F=1-103.
DR PDB; 5Z30; X-ray; 2.45 A; B/F=1-103.
DR PDB; 5ZBX; X-ray; 2.58 A; B/F=1-103.
DR PDB; 5ZGC; X-ray; 2.90 A; G/H/I/J/K/L=12-22.
DR PDB; 6A5L; EM; 5.60 A; b/f=1-103.
DR PDB; 6A5O; EM; 9.90 A; b/f=1-103.
DR PDB; 6A5P; EM; 7.00 A; b/f=1-103.
DR PDB; 6A5R; EM; 8.70 A; b/f=1-103.
DR PDB; 6A5T; EM; 6.70 A; b/f=1-103.
DR PDB; 6A5U; EM; 7.60 A; b/f=1-103.
DR PDB; 6ACP; X-ray; 2.30 A; B=89-95.
DR PDB; 6BUZ; EM; 3.92 A; B/F=1-103.
DR PDB; 6C0W; EM; 4.00 A; B/F=1-102.
DR PDB; 6E0C; EM; 2.63 A; B/F=1-103.
DR PDB; 6E0P; EM; 2.60 A; B/F=1-103.
DR PDB; 6FML; EM; 4.34 A; N/R=2-103.
DR PDB; 6HKT; X-ray; 9.70 A; B/F/L/P/V/Z/b/f/l/p/v/z=1-103.
DR PDB; 6HTS; EM; 4.80 A; J/N=1-103.
DR PDB; 6INQ; EM; 6.90 A; b/f=1-103.
DR PDB; 6IR9; EM; 3.80 A; b/f=1-103.
DR PDB; 6J4W; EM; 7.90 A; b/f=1-103.
DR PDB; 6J4X; EM; 4.30 A; b/f=1-103.
DR PDB; 6J4Y; EM; 4.30 A; b/f=1-103.
DR PDB; 6J4Z; EM; 4.10 A; b/f=1-103.
DR PDB; 6J50; EM; 4.70 A; b/f=1-103.
DR PDB; 6J51; EM; 4.20 A; b/f=1-103.
DR PDB; 6JOU; X-ray; 2.17 A; B/F=1-103.
DR PDB; 6JR0; X-ray; 2.50 A; B/F=1-103.
DR PDB; 6JR1; X-ray; 2.40 A; B/F=1-103.
DR PDB; 6K1I; X-ray; 2.75 A; B/F=1-103.
DR PDB; 6K1J; X-ray; 2.85 A; B/F=1-103.
DR PDB; 6K1K; X-ray; 2.20 A; B/F=1-103.
DR PDB; 6KE9; X-ray; 2.22 A; B/F=17-103.
DR PDB; 6KVD; X-ray; 2.21 A; B/F=1-103.
DR PDB; 6KXV; X-ray; 3.63 A; B/F=1-103.
DR PDB; 6L49; EM; 18.90 A; B/F/L/P/T/X=1-103.
DR PDB; 6L4A; EM; 12.30 A; B/F/L/P/T/X=1-103.
DR PDB; 6L9H; X-ray; 2.60 A; B/F=17-103.
DR PDB; 6L9Z; X-ray; 2.50 A; B/F/L/P=1-103.
DR PDB; 6LA2; X-ray; 3.89 A; B/F/L/P/V/Z/f/j=1-103.
DR PDB; 6LA8; X-ray; 3.40 A; B/F/L/P=1-103.
DR PDB; 6LA9; X-ray; 3.70 A; B/F/L/P=1-103.
DR PDB; 6LAB; X-ray; 3.20 A; B/F/L/P=1-103.
DR PDB; 6LE9; X-ray; 2.60 A; B/F=17-103.
DR PDB; 6LER; X-ray; 3.00 A; B/F/L/P=1-103.
DR PDB; 6M3V; X-ray; 4.60 A; B/F/L/P=1-103.
DR PDB; 6M44; X-ray; 3.81 A; B/F/L/P=1-103.
DR PDB; 6M4D; EM; 4.40 A; B/F=1-103.
DR PDB; 6M4G; EM; 2.80 A; B/F=1-103.
DR PDB; 6M4H; EM; 3.90 A; B/F=1-103.
DR PDB; 6MLC; X-ray; 1.80 A; E/F=2-21.
DR PDB; 6MUO; EM; 3.60 A; B/F=9-102.
DR PDB; 6MUP; EM; 3.50 A; B/F=9-102.
DR PDB; 6O1D; EM; 3.40 A; B/F=1-103.
DR PDB; 6R0C; EM; 4.20 A; B/F=1-103.
DR PDB; 6R8Y; EM; 4.30 A; B/F=1-103.
DR PDB; 6R8Z; EM; 3.90 A; B/F=1-103.
DR PDB; 6R90; EM; 4.50 A; B/F=1-103.
DR PDB; 6R91; EM; 4.10 A; B/F=1-103.
DR PDB; 6R92; EM; 4.80 A; B/F=1-103.
DR PDB; 6R93; EM; 4.00 A; B/F=1-103.
DR PDB; 6R94; EM; 3.50 A; B/F=1-103.
DR PDB; 6RNY; EM; 3.90 A; B/F=1-103.
DR PDB; 6RXS; X-ray; 1.60 A; B=13-23.
DR PDB; 6SE0; EM; 3.80 A; B/F=1-103.
DR PDB; 6SE6; EM; 3.50 A; B/F=1-103.
DR PDB; 6SEE; EM; 4.20 A; B/F=1-103.
DR PDB; 6SEF; EM; 3.70 A; B/F=1-103.
DR PDB; 6SEG; EM; 3.10 A; B/F=1-103.
DR PDB; 6T79; EM; 3.20 A; B/F=1-103.
DR PDB; 6T7A; EM; 3.70 A; B/F=1-103.
DR PDB; 6T7B; EM; 5.10 A; B/F=1-103.
DR PDB; 6T7C; EM; 4.00 A; B/F=1-103.
DR PDB; 6T7D; EM; 4.40 A; B/F=1-103.
DR PDB; 6T90; EM; 3.05 A; B/F=1-103.
DR PDB; 6T93; EM; 3.49 A; B/F=1-103.
DR PDB; 6UPK; EM; 4.90 A; B/F=1-103.
DR PDB; 6UPL; EM; 7.40 A; B/F=1-103.
DR PDB; 6USJ; EM; 10.50 A; B/F/L/P=1-103.
DR PDB; 6V2K; X-ray; 2.60 A; B/F=1-103.
DR PDB; 6V92; EM; 20.00 A; b/f=1-103.
DR PDB; 6VO5; X-ray; 1.60 A; C/D=2-21.
DR PDB; 6X59; EM; 2.98 A; B/F=2-103.
DR PDB; 6X5A; EM; 4.36 A; B/F=2-103.
DR PDB; 6XJD; EM; 6.80 A; B/F=2-103.
DR PDB; 6Y5D; EM; 4.10 A; B/F/N/R=1-103.
DR PDB; 6YOV; EM; 3.42 A; B/F=1-103.
DR PDB; 7A08; EM; 3.11 A; e/i=2-103.
DR PDB; 7BWD; EM; 4.32 A; B/F=2-103.
DR PDB; 7BXT; EM; 4.20 A; B/F=2-103.
DR PDB; 7BY0; EM; 4.50 A; B/F=1-102.
DR PDB; 7C0M; EM; 3.90 A; B/F/b/f=2-103.
DR PDB; 7CCQ; EM; 3.80 A; B/F=24-103.
DR PDB; 7CCR; EM; 4.90 A; B/F/M/Q=24-103.
DR PDB; 7CIZ; X-ray; 1.80 A; B/F/J=2-103.
DR PDB; 7CJ0; X-ray; 2.50 A; C/F=2-103.
DR PDB; 7COW; X-ray; 2.86 A; B/F/L/P=1-103.
DR PDB; 7D1Z; EM; 3.15 A; B/F=2-103.
DR PDB; 7D20; EM; 3.00 A; B/F=2-103.
DR PDB; 7DBP; EM; 4.50 A; B/F=1-103.
DR PDB; 7E8D; EM; 2.80 A; B/F=2-103.
DR PDB; 7EIC; X-ray; 1.95 A; C=2-13.
DR PDB; 7JO9; EM; 3.30 A; B/F=1-103.
DR PDB; 7JOA; EM; 3.30 A; B/F=1-103.
DR PDB; 7JZV; EM; 3.90 A; Q/q=2-103.
DR PDB; 7K5X; EM; 2.93 A; B/F=1-103.
DR PDB; 7K5Y; EM; 2.76 A; B/F=1-103.
DR PDB; 7K60; EM; 3.12 A; B/F=1-103.
DR PDB; 7K61; EM; 2.85 A; B/F=1-103.
DR PDB; 7K63; EM; 3.03 A; B/F=1-103.
DR PDB; 7LMK; X-ray; 2.65 A; F/G/H/I=15-27.
DR PDB; 7LMM; X-ray; 2.80 A; F/G/H/I=15-27.
DR PDB; 7LYA; EM; 2.91 A; B/F=1-103.
DR PDB; 7LYB; EM; 3.28 A; B/F=1-103.
DR PDB; 7LYC; EM; 2.94 A; B/F=1-103.
DR PDB; 7M98; X-ray; 1.60 A; B=2-16.
DR PDB; 7NL0; EM; 3.50 A; B/F=1-103.
DR PDB; 7SCY; EM; 4.10 A; B/F=1-103.
DR PDB; 7SCZ; EM; 3.50 A; B/F=1-103.
DR PDB; 7U46; EM; 2.68 A; B/F=1-103.
DR PDB; 7U47; EM; 7.50 A; B/F/M/Q=1-103.
DR PDB; 7U4D; EM; 8.10 A; B/F/M/Q=1-103.
DR PDB; 7V6Q; X-ray; 3.00 A; C/G=3-103.
DR PDBsum; 1ZKK; -.
DR PDBsum; 2BQZ; -.
DR PDBsum; 2CV5; -.
DR PDBsum; 2IG0; -.
DR PDBsum; 2KWN; -.
DR PDBsum; 2KWO; -.
DR PDBsum; 2LVM; -.
DR PDBsum; 2QQS; -.
DR PDBsum; 2RJE; -.
DR PDBsum; 2RNY; -.
DR PDBsum; 2RS9; -.
DR PDBsum; 3A6N; -.
DR PDBsum; 3AFA; -.
DR PDBsum; 3AN2; -.
DR PDBsum; 3AV1; -.
DR PDBsum; 3AV2; -.
DR PDBsum; 3AYW; -.
DR PDBsum; 3AZE; -.
DR PDBsum; 3AZF; -.
DR PDBsum; 3AZG; -.
DR PDBsum; 3AZH; -.
DR PDBsum; 3AZI; -.
DR PDBsum; 3AZJ; -.
DR PDBsum; 3AZK; -.
DR PDBsum; 3AZL; -.
DR PDBsum; 3AZM; -.
DR PDBsum; 3AZN; -.
DR PDBsum; 3CFS; -.
DR PDBsum; 3CFV; -.
DR PDBsum; 3F9W; -.
DR PDBsum; 3F9X; -.
DR PDBsum; 3F9Y; -.
DR PDBsum; 3F9Z; -.
DR PDBsum; 3IJ1; -.
DR PDBsum; 3JPX; -.
DR PDBsum; 3NQJ; -.
DR PDBsum; 3NQU; -.
DR PDBsum; 3O36; -.
DR PDBsum; 3QBY; -.
DR PDBsum; 3QZS; -.
DR PDBsum; 3QZT; -.
DR PDBsum; 3QZV; -.
DR PDBsum; 3R45; -.
DR PDBsum; 3UVW; -.
DR PDBsum; 3UVX; -.
DR PDBsum; 3UVY; -.
DR PDBsum; 3UW9; -.
DR PDBsum; 3W96; -.
DR PDBsum; 3W97; -.
DR PDBsum; 3W98; -.
DR PDBsum; 3W99; -.
DR PDBsum; 3WA9; -.
DR PDBsum; 3WAA; -.
DR PDBsum; 3WKJ; -.
DR PDBsum; 3WTP; -.
DR PDBsum; 3X1S; -.
DR PDBsum; 3X1T; -.
DR PDBsum; 3X1U; -.
DR PDBsum; 3X1V; -.
DR PDBsum; 4GQB; -.
DR PDBsum; 4H9N; -.
DR PDBsum; 4H9O; -.
DR PDBsum; 4H9P; -.
DR PDBsum; 4H9Q; -.
DR PDBsum; 4H9R; -.
DR PDBsum; 4H9S; -.
DR PDBsum; 4HGA; -.
DR PDBsum; 4M38; -.
DR PDBsum; 4N3W; -.
DR PDBsum; 4N4F; -.
DR PDBsum; 4QUT; -.
DR PDBsum; 4QUU; -.
DR PDBsum; 4QYD; -.
DR PDBsum; 4U9W; -.
DR PDBsum; 4YM5; -.
DR PDBsum; 4YM6; -.
DR PDBsum; 4YY6; -.
DR PDBsum; 4YYD; -.
DR PDBsum; 4YYG; -.
DR PDBsum; 4YYH; -.
DR PDBsum; 4YYI; -.
DR PDBsum; 4YYJ; -.
DR PDBsum; 4YYK; -.
DR PDBsum; 4YYM; -.
DR PDBsum; 4YYN; -.
DR PDBsum; 4Z2M; -.
DR PDBsum; 4Z5T; -.
DR PDBsum; 5AV5; -.
DR PDBsum; 5AV6; -.
DR PDBsum; 5AV8; -.
DR PDBsum; 5AV9; -.
DR PDBsum; 5AVB; -.
DR PDBsum; 5AVC; -.
DR PDBsum; 5AY8; -.
DR PDBsum; 5B0Y; -.
DR PDBsum; 5B0Z; -.
DR PDBsum; 5B24; -.
DR PDBsum; 5B2I; -.
DR PDBsum; 5B2J; -.
DR PDBsum; 5B31; -.
DR PDBsum; 5B32; -.
DR PDBsum; 5B33; -.
DR PDBsum; 5B40; -.
DR PDBsum; 5BNV; -.
DR PDBsum; 5BNX; -.
DR PDBsum; 5BO0; -.
DR PDBsum; 5C3I; -.
DR PDBsum; 5CPI; -.
DR PDBsum; 5CPJ; -.
DR PDBsum; 5CPK; -.
DR PDBsum; 5FA5; -.
DR PDBsum; 5FFW; -.
DR PDBsum; 5FWE; -.
DR PDBsum; 5GSE; -.
DR PDBsum; 5GSU; -.
DR PDBsum; 5GT0; -.
DR PDBsum; 5GT3; -.
DR PDBsum; 5GTC; -.
DR PDBsum; 5GXQ; -.
DR PDBsum; 5JA4; -.
DR PDBsum; 5JRG; -.
DR PDBsum; 5KDM; -.
DR PDBsum; 5TEG; -.
DR PDBsum; 5X7X; -.
DR PDBsum; 5XF3; -.
DR PDBsum; 5XF4; -.
DR PDBsum; 5XF5; -.
DR PDBsum; 5Y0C; -.
DR PDBsum; 5Y0D; -.
DR PDBsum; 5YE3; -.
DR PDBsum; 5YE4; -.
DR PDBsum; 5Z23; -.
DR PDBsum; 5Z30; -.
DR PDBsum; 5ZBX; -.
DR PDBsum; 5ZGC; -.
DR PDBsum; 6A5L; -.
DR PDBsum; 6A5O; -.
DR PDBsum; 6A5P; -.
DR PDBsum; 6A5R; -.
DR PDBsum; 6A5T; -.
DR PDBsum; 6A5U; -.
DR PDBsum; 6ACP; -.
DR PDBsum; 6BUZ; -.
DR PDBsum; 6C0W; -.
DR PDBsum; 6E0C; -.
DR PDBsum; 6E0P; -.
DR PDBsum; 6FML; -.
DR PDBsum; 6HKT; -.
DR PDBsum; 6HTS; -.
DR PDBsum; 6INQ; -.
DR PDBsum; 6IR9; -.
DR PDBsum; 6J4W; -.
DR PDBsum; 6J4X; -.
DR PDBsum; 6J4Y; -.
DR PDBsum; 6J4Z; -.
DR PDBsum; 6J50; -.
DR PDBsum; 6J51; -.
DR PDBsum; 6JOU; -.
DR PDBsum; 6JR0; -.
DR PDBsum; 6JR1; -.
DR PDBsum; 6K1I; -.
DR PDBsum; 6K1J; -.
DR PDBsum; 6K1K; -.
DR PDBsum; 6KE9; -.
DR PDBsum; 6KVD; -.
DR PDBsum; 6KXV; -.
DR PDBsum; 6L49; -.
DR PDBsum; 6L4A; -.
DR PDBsum; 6L9H; -.
DR PDBsum; 6L9Z; -.
DR PDBsum; 6LA2; -.
DR PDBsum; 6LA8; -.
DR PDBsum; 6LA9; -.
DR PDBsum; 6LAB; -.
DR PDBsum; 6LE9; -.
DR PDBsum; 6LER; -.
DR PDBsum; 6M3V; -.
DR PDBsum; 6M44; -.
DR PDBsum; 6M4D; -.
DR PDBsum; 6M4G; -.
DR PDBsum; 6M4H; -.
DR PDBsum; 6MLC; -.
DR PDBsum; 6MUO; -.
DR PDBsum; 6MUP; -.
DR PDBsum; 6O1D; -.
DR PDBsum; 6R0C; -.
DR PDBsum; 6R8Y; -.
DR PDBsum; 6R8Z; -.
DR PDBsum; 6R90; -.
DR PDBsum; 6R91; -.
DR PDBsum; 6R92; -.
DR PDBsum; 6R93; -.
DR PDBsum; 6R94; -.
DR PDBsum; 6RNY; -.
DR PDBsum; 6RXS; -.
DR PDBsum; 6SE0; -.
DR PDBsum; 6SE6; -.
DR PDBsum; 6SEE; -.
DR PDBsum; 6SEF; -.
DR PDBsum; 6SEG; -.
DR PDBsum; 6T79; -.
DR PDBsum; 6T7A; -.
DR PDBsum; 6T7B; -.
DR PDBsum; 6T7C; -.
DR PDBsum; 6T7D; -.
DR PDBsum; 6T90; -.
DR PDBsum; 6T93; -.
DR PDBsum; 6UPK; -.
DR PDBsum; 6UPL; -.
DR PDBsum; 6USJ; -.
DR PDBsum; 6V2K; -.
DR PDBsum; 6V92; -.
DR PDBsum; 6VO5; -.
DR PDBsum; 6X59; -.
DR PDBsum; 6X5A; -.
DR PDBsum; 6XJD; -.
DR PDBsum; 6Y5D; -.
DR PDBsum; 6YOV; -.
DR PDBsum; 7A08; -.
DR PDBsum; 7BWD; -.
DR PDBsum; 7BXT; -.
DR PDBsum; 7BY0; -.
DR PDBsum; 7C0M; -.
DR PDBsum; 7CCQ; -.
DR PDBsum; 7CCR; -.
DR PDBsum; 7CIZ; -.
DR PDBsum; 7CJ0; -.
DR PDBsum; 7COW; -.
DR PDBsum; 7D1Z; -.
DR PDBsum; 7D20; -.
DR PDBsum; 7DBP; -.
DR PDBsum; 7E8D; -.
DR PDBsum; 7EIC; -.
DR PDBsum; 7JO9; -.
DR PDBsum; 7JOA; -.
DR PDBsum; 7JZV; -.
DR PDBsum; 7K5X; -.
DR PDBsum; 7K5Y; -.
DR PDBsum; 7K60; -.
DR PDBsum; 7K61; -.
DR PDBsum; 7K63; -.
DR PDBsum; 7LMK; -.
DR PDBsum; 7LMM; -.
DR PDBsum; 7LYA; -.
DR PDBsum; 7LYB; -.
DR PDBsum; 7LYC; -.
DR PDBsum; 7M98; -.
DR PDBsum; 7NL0; -.
DR PDBsum; 7SCY; -.
DR PDBsum; 7SCZ; -.
DR PDBsum; 7U46; -.
DR PDBsum; 7U47; -.
DR PDBsum; 7U4D; -.
DR PDBsum; 7V6Q; -.
DR AlphaFoldDB; P62805; -.
DR SMR; P62805; -.
DR BioGRID; 113899; 102.
DR BioGRID; 113955; 1640.
DR BioGRID; 113956; 27.
DR BioGRID; 113957; 67.
DR BioGRID; 113958; 59.
DR BioGRID; 113959; 42.
DR BioGRID; 113960; 44.
DR BioGRID; 113961; 33.
DR BioGRID; 113962; 54.
DR BioGRID; 113963; 32.
DR BioGRID; 113964; 60.
DR BioGRID; 113966; 89.
DR BioGRID; 125732; 118.
DR BioGRID; 299853; 41.
DR ComplexPortal; CPX-2556; Nucleosome, variant H3.1-H2A.2-H2B.1.
DR ComplexPortal; CPX-2564; Nucleosome, variant H3.1t-H2A.2-H2B.1.
DR ComplexPortal; CPX-5647; CENP-A nucleosome complex.
DR ComplexPortal; CPX-5668; Nucleosome, variant H3.2-H2A.2-H2B.1.
DR ComplexPortal; CPX-5670; Nucleosome, variant H3.1-H2A.Z-H2B.1.
DR ComplexPortal; CPX-5671; Nucleosome, variant H3.1-H2A.V-H2B.1.
DR CORUM; P62805; -.
DR DIP; DIP-33079N; -.
DR IntAct; P62805; 240.
DR MINT; P62805; -.
DR STRING; 9606.ENSP00000244537; -.
DR BindingDB; P62805; -.
DR ChEMBL; CHEMBL5876; -.
DR GlyGen; P62805; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62805; -.
DR MetOSite; P62805; -.
DR PhosphoSitePlus; P62805; -.
DR SwissPalm; P62805; -.
DR BioMuta; HIST4H4; -.
DR DMDM; 51317339; -.
DR SWISS-2DPAGE; P62805; -.
DR CPTAC; CPTAC-1055; -.
DR CPTAC; CPTAC-1056; -.
DR EPD; P62805; -.
DR jPOST; P62805; -.
DR MassIVE; P62805; -.
DR MaxQB; P62805; -.
DR PaxDb; P62805; -.
DR PeptideAtlas; P62805; -.
DR PRIDE; P62805; -.
DR ProteomicsDB; 57424; -.
DR TopDownProteomics; P62805; -.
DR ABCD; P62805; 4 sequenced antibodies.
DR Antibodypedia; 23657; 2141 antibodies from 39 providers.
DR Antibodypedia; 70431; 12 antibodies from 7 providers.
DR Antibodypedia; 73583; 121 antibodies from 11 providers.
DR Antibodypedia; 73812; 14 antibodies from 8 providers.
DR Antibodypedia; 73941; 609 antibodies from 13 providers.
DR Antibodypedia; 74197; 154 antibodies from 6 providers.
DR Antibodypedia; 75448; 5 antibodies from 3 providers.
DR Antibodypedia; 75564; 42 antibodies from 6 providers.
DR Antibodypedia; 76313; 19 antibodies from 5 providers.
DR Antibodypedia; 76498; 1 antibodies from 1 providers.
DR Antibodypedia; 76521; 5 antibodies from 4 providers.
DR Antibodypedia; 76797; 48 antibodies from 6 providers.
DR DNASU; 8294; -.
DR Ensembl; ENST00000244537.6; ENSP00000244537.6; ENSG00000274618.2.
DR Ensembl; ENST00000355057.3; ENSP00000347168.2; ENSG00000197238.5.
DR Ensembl; ENST00000358064.3; ENSP00000350767.3; ENSG00000197837.4.
DR Ensembl; ENST00000377727.2; ENSP00000366956.1; ENSG00000158406.6.
DR Ensembl; ENST00000377745.5; ENSP00000366974.2; ENSG00000278705.3.
DR Ensembl; ENST00000377803.4; ENSP00000367034.3; ENSG00000197061.5.
DR Ensembl; ENST00000539745.2; ENSP00000443017.1; ENSG00000197837.4.
DR Ensembl; ENST00000578186.3; ENSP00000462667.1; ENSG00000270882.3.
DR Ensembl; ENST00000579512.3; ENSP00000462355.1; ENSG00000270276.3.
DR Ensembl; ENST00000611927.2; ENSP00000479794.2; ENSG00000273542.2.
DR Ensembl; ENST00000612061.1; ENSP00000482412.1; ENSG00000270276.3.
DR Ensembl; ENST00000613412.1; ENSP00000481343.1; ENSG00000270882.3.
DR Ensembl; ENST00000614247.2; ENSP00000479461.2; ENSG00000277157.2.
DR Ensembl; ENST00000614272.1; ENSP00000478519.1; ENSG00000270882.3.
DR Ensembl; ENST00000615164.3; ENSP00000484789.1; ENSG00000276966.3.
DR Ensembl; ENST00000615353.2; ENSP00000481486.1; ENSG00000276180.2.
DR Ensembl; ENST00000617569.2; ENSP00000479106.2; ENSG00000278637.2.
DR Ensembl; ENST00000618193.1; ENSP00000478786.1; ENSG00000270882.3.
DR Ensembl; ENST00000618305.2; ENSP00000480960.2; ENSG00000275126.2.
DR Ensembl; ENST00000621520.1; ENSP00000481507.1; ENSG00000270276.3.
DR Ensembl; ENST00000634560.1; ENSP00000489319.1; ENSG00000158406.6.
DR Ensembl; ENST00000634956.1; ENSP00000489567.1; ENSG00000158406.6.
DR GeneID; 121504; -.
DR GeneID; 554313; -.
DR GeneID; 8294; -.
DR GeneID; 8359; -.
DR GeneID; 8360; -.
DR GeneID; 8361; -.
DR GeneID; 8362; -.
DR GeneID; 8363; -.
DR GeneID; 8364; -.
DR GeneID; 8365; -.
DR GeneID; 8366; -.
DR GeneID; 8367; -.
DR GeneID; 8368; -.
DR GeneID; 8370; -.
DR KEGG; hsa:121504; -.
DR KEGG; hsa:554313; -.
DR KEGG; hsa:8294; -.
DR KEGG; hsa:8359; -.
DR KEGG; hsa:8360; -.
DR KEGG; hsa:8361; -.
DR KEGG; hsa:8362; -.
DR KEGG; hsa:8363; -.
DR KEGG; hsa:8364; -.
DR KEGG; hsa:8365; -.
DR KEGG; hsa:8366; -.
DR KEGG; hsa:8367; -.
DR KEGG; hsa:8368; -.
DR KEGG; hsa:8370; -.
DR MANE-Select; ENST00000244537.6; ENSP00000244537.6; NM_003540.4; NP_003531.1.
DR MANE-Select; ENST00000355057.3; ENSP00000347168.2; NM_021968.4; NP_068803.1.
DR MANE-Select; ENST00000377727.2; ENSP00000366956.1; NM_003543.4; NP_003534.1.
DR MANE-Select; ENST00000377745.5; ENSP00000366974.2; NM_003544.3; NP_003535.1.
DR MANE-Select; ENST00000377803.4; ENSP00000367034.3; NM_003542.4; NP_003533.1.
DR MANE-Select; ENST00000539745.2; ENSP00000443017.1; NM_175054.2; NP_778224.1.
DR MANE-Select; ENST00000578186.3; ENSP00000462667.1; NM_003548.2; NP_003539.1.
DR MANE-Select; ENST00000579512.3; ENSP00000462355.1; NM_001034077.4; NP_001029249.1.
DR MANE-Select; ENST00000611927.2; ENSP00000479794.2; NM_003541.3; NP_003532.1.
DR MANE-Select; ENST00000614247.2; ENSP00000479461.2; NM_003539.4; NP_003530.1.
DR MANE-Select; ENST00000615164.3; ENSP00000484789.1; NM_003545.4; NP_003536.1.
DR MANE-Select; ENST00000615353.2; ENSP00000481486.1; NM_003495.3; NP_003486.1.
DR MANE-Select; ENST00000617569.2; ENSP00000479106.2; NM_003538.4; NP_003529.1.
DR MANE-Select; ENST00000618305.2; ENSP00000480960.2; NM_003546.3; NP_003537.1.
DR UCSC; uc001ess.4; human.
DR CTD; 121504; -.
DR CTD; 554313; -.
DR CTD; 8294; -.
DR CTD; 8359; -.
DR CTD; 8360; -.
DR CTD; 8361; -.
DR CTD; 8362; -.
DR CTD; 8363; -.
DR CTD; 8364; -.
DR CTD; 8365; -.
DR CTD; 8366; -.
DR CTD; 8367; -.
DR CTD; 8368; -.
DR CTD; 8370; -.
DR DisGeNET; 121504; -.
DR DisGeNET; 554313; -.
DR DisGeNET; 8294; -.
DR DisGeNET; 8359; -.
DR DisGeNET; 8360; -.
DR DisGeNET; 8361; -.
DR DisGeNET; 8362; -.
DR DisGeNET; 8363; -.
DR DisGeNET; 8364; -.
DR DisGeNET; 8365; -.
DR DisGeNET; 8366; -.
DR DisGeNET; 8367; -.
DR DisGeNET; 8368; -.
DR DisGeNET; 8370; -.
DR GeneCards; H4-16; -.
DR GeneCards; H4C1; -.
DR GeneCards; H4C11; -.
DR GeneCards; H4C12; -.
DR GeneCards; H4C13; -.
DR GeneCards; H4C14; -.
DR GeneCards; H4C15; -.
DR GeneCards; H4C2; -.
DR GeneCards; H4C3; -.
DR GeneCards; H4C4; -.
DR GeneCards; H4C5; -.
DR GeneCards; H4C6; -.
DR GeneCards; H4C8; -.
DR GeneCards; H4C9; -.
DR HGNC; HGNC:20510; H4-16.
DR HGNC; HGNC:4781; H4C1.
DR HGNC; HGNC:4785; H4C11.
DR HGNC; HGNC:4784; H4C12.
DR HGNC; HGNC:4791; H4C13.
DR HGNC; HGNC:4794; H4C14.
DR HGNC; HGNC:29607; H4C15.
DR HGNC; HGNC:4789; H4C2.
DR HGNC; HGNC:4787; H4C3.
DR HGNC; HGNC:4782; H4C4.
DR HGNC; HGNC:4790; H4C5.
DR HGNC; HGNC:4783; H4C6.
DR HGNC; HGNC:4788; H4C8.
DR HGNC; HGNC:4793; H4C9.
DR HPA; ENSG00000158406; Tissue enriched (brain).
DR HPA; ENSG00000197061; Tissue enriched (brain).
DR HPA; ENSG00000197238; Tissue enhanced (liver).
DR HPA; ENSG00000197837; Tissue enhanced (brain).
DR HPA; ENSG00000270276; Low tissue specificity.
DR HPA; ENSG00000270882; Tissue enhanced (brain).
DR HPA; ENSG00000273542; Tissue enhanced (bone marrow, brain).
DR HPA; ENSG00000274618; Tissue enriched (brain).
DR HPA; ENSG00000275126; Group enriched (brain, choroid plexus).
DR HPA; ENSG00000276180; Low tissue specificity.
DR HPA; ENSG00000276966; Tissue enriched (brain).
DR HPA; ENSG00000277157; Tissue enriched (brain).
DR HPA; ENSG00000278637; Tissue enriched (brain).
DR HPA; ENSG00000278705; Tissue enriched (brain).
DR MIM; 142750; gene.
DR MIM; 602822; gene.
DR MIM; 602823; gene.
DR MIM; 602824; gene.
DR MIM; 602825; gene.
DR MIM; 602826; gene.
DR MIM; 602827; gene.
DR MIM; 602828; gene.
DR MIM; 602829; gene.
DR MIM; 602830; gene.
DR MIM; 602831; gene.
DR MIM; 602833; gene.
DR MIM; 615069; gene.
DR neXtProt; NX_P62805; -.
DR OpenTargets; ENSG00000158406; -.
DR OpenTargets; ENSG00000197061; -.
DR OpenTargets; ENSG00000197238; -.
DR OpenTargets; ENSG00000197837; -.
DR OpenTargets; ENSG00000270276; -.
DR OpenTargets; ENSG00000270882; -.
DR OpenTargets; ENSG00000273542; -.
DR OpenTargets; ENSG00000274618; -.
DR OpenTargets; ENSG00000275126; -.
DR OpenTargets; ENSG00000276180; -.
DR OpenTargets; ENSG00000276966; -.
DR OpenTargets; ENSG00000277157; -.
DR OpenTargets; ENSG00000278637; -.
DR OpenTargets; ENSG00000278705; -.
DR VEuPathDB; HostDB:ENSG00000158406; -.
DR VEuPathDB; HostDB:ENSG00000197061; -.
DR VEuPathDB; HostDB:ENSG00000197238; -.
DR VEuPathDB; HostDB:ENSG00000197837; -.
DR VEuPathDB; HostDB:ENSG00000270276; -.
DR VEuPathDB; HostDB:ENSG00000270882; -.
DR VEuPathDB; HostDB:ENSG00000273542; -.
DR VEuPathDB; HostDB:ENSG00000274618; -.
DR VEuPathDB; HostDB:ENSG00000275126; -.
DR VEuPathDB; HostDB:ENSG00000276180; -.
DR VEuPathDB; HostDB:ENSG00000276966; -.
DR VEuPathDB; HostDB:ENSG00000277157; -.
DR VEuPathDB; HostDB:ENSG00000278637; -.
DR VEuPathDB; HostDB:ENSG00000278705; -.
DR eggNOG; KOG3467; Eukaryota.
DR GeneTree; ENSGT01030000234703; -.
DR GeneTree; ENSGT01050000244867; -.
DR HOGENOM; CLU_109117_2_3_1; -.
DR InParanoid; P62805; -.
DR OMA; QKEHING; -.
DR OrthoDB; 1594208at2759; -.
DR PhylomeDB; P62805; -.
DR PathwayCommons; P62805; -.
DR Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
DR Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-HSA-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-HSA-110331; Cleavage of the damaged purine.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR Reactome; R-HSA-171306; Packaging Of Telomere Ends.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-5334118; DNA methylation.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-912446; Meiotic recombination.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
DR Reactome; R-HSA-9710421; Defective pyroptosis.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SignaLink; P62805; -.
DR SIGNOR; P62805; -.
DR BioGRID-ORCS; 121504; 16 hits in 1065 CRISPR screens.
DR BioGRID-ORCS; 554313; 83 hits in 969 CRISPR screens.
DR BioGRID-ORCS; 8294; 23 hits in 1078 CRISPR screens.
DR BioGRID-ORCS; 8359; 28 hits in 1059 CRISPR screens.
DR BioGRID-ORCS; 8360; 8 hits in 1065 CRISPR screens.
DR BioGRID-ORCS; 8361; 11 hits in 1061 CRISPR screens.
DR BioGRID-ORCS; 8362; 54 hits in 932 CRISPR screens.
DR BioGRID-ORCS; 8363; 92 hits in 628 CRISPR screens.
DR BioGRID-ORCS; 8364; 26 hits in 1083 CRISPR screens.
DR BioGRID-ORCS; 8365; 18 hits in 1081 CRISPR screens.
DR BioGRID-ORCS; 8366; 33 hits in 1030 CRISPR screens.
DR BioGRID-ORCS; 8367; 14 hits in 1025 CRISPR screens.
DR BioGRID-ORCS; 8368; 11 hits in 1053 CRISPR screens.
DR BioGRID-ORCS; 8370; 45 hits in 557 CRISPR screens.
DR ChiTaRS; HIST1H4A; human.
DR ChiTaRS; HIST1H4C; human.
DR ChiTaRS; HIST1H4E; human.
DR ChiTaRS; HIST1H4F; human.
DR ChiTaRS; HIST1H4H; human.
DR ChiTaRS; HIST1H4J; human.
DR ChiTaRS; HIST1H4K; human.
DR ChiTaRS; HIST2H4B; human.
DR EvolutionaryTrace; P62805; -.
DR GeneWiki; HIST1H4A; -.
DR GeneWiki; HIST1H4B; -.
DR GeneWiki; HIST1H4C; -.
DR GeneWiki; HIST1H4D; -.
DR GeneWiki; HIST1H4E; -.
DR GeneWiki; HIST1H4F; -.
DR GeneWiki; HIST1H4H; -.
DR GeneWiki; HIST1H4I; -.
DR GeneWiki; HIST1H4J; -.
DR GeneWiki; HIST1H4K; -.
DR GeneWiki; HIST1H4L; -.
DR GeneWiki; HIST2H4A; -.
DR GeneWiki; HIST4H4; -.
DR Pharos; P62805; Tchem.
DR PRO; PR:P62805; -.
DR Proteomes; UP000005640; Chromosome 1.
DR Proteomes; UP000005640; Chromosome 12.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P62805; protein.
DR Bgee; ENSG00000158406; Expressed in adrenal tissue and 143 other tissues.
DR ExpressionAtlas; P62805; baseline and differential.
DR Genevisible; P62805; HS.
DR GO; GO:0043505; C:CENP-A containing nucleosome; IPI:ComplexPortal.
DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000786; C:nucleosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR GO; GO:0061644; P:protein localization to CENP-A containing chromatin; IC:ComplexPortal.
DR GO; GO:0032200; P:telomere organization; TAS:BHF-UCL.
DR CDD; cd00076; H4; 1.
DR DisProt; DP02034; -.
DR Gene3D; 1.10.20.10; -; 1.
DR IDEAL; IID00058; -.
DR InterPro; IPR035425; CENP-T/H4_C.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR001951; Histone_H4.
DR InterPro; IPR019809; Histone_H4_CS.
DR InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR Pfam; PF15511; CENP-T_C; 1.
DR PRINTS; PR00623; HISTONEH4.
DR SMART; SM00417; H4; 1.
DR SMART; SM00803; TAF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00047; HISTONE_H4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosomal rearrangement; Chromosome;
KW Citrullination; Direct protein sequencing; DNA-binding; Hydroxylation;
KW Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17967882"
FT CHAIN 2..103
FT /note="Histone H4"
FT /id="PRO_0000158320"
FT DNA_BIND 17..21
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:17967882"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17967882"
FT MOD_RES 4
FT /note="Asymmetric dimethylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:11387442,
FT ECO:0000269|PubMed:11448779, ECO:0000269|PubMed:15345777"
FT MOD_RES 4
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000269|PubMed:15345777,
FT ECO:0000269|PubMed:16567635"
FT MOD_RES 4
FT /note="Omega-N-methylarginine; by PRMT1; alternate"
FT /evidence="ECO:0000269|PubMed:11387442,
FT ECO:0000269|PubMed:11448779, ECO:0000269|PubMed:15345777"
FT MOD_RES 4
FT /note="Symmetric dimethylarginine; by PRMT5 and PRMT7;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:P62806"
FT MOD_RES 6
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 6
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2474456,
FT ECO:0000269|PubMed:7664735, ECO:0007744|PubMed:19608861"
FT MOD_RES 6
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105113"
FT MOD_RES 6
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 6
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 6
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 9
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 9
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 9
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:2474456,
FT ECO:0000269|PubMed:7664735, ECO:0007744|PubMed:19608861"
FT MOD_RES 9
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17267393,
FT ECO:0000269|PubMed:27105113"
FT MOD_RES 9
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322,
FT ECO:0000269|PubMed:28497810"
FT MOD_RES 9
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 9
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17267393"
FT MOD_RES 13
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 13
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 13
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17967882,
FT ECO:0000269|PubMed:2474456, ECO:0000269|PubMed:7664735,
FT ECO:0007744|PubMed:19608861"
FT MOD_RES 13
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105113"
FT MOD_RES 13
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322,
FT ECO:0000269|PubMed:28497810"
FT MOD_RES 13
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 13
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 13
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31061526"
FT MOD_RES 13
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 17
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 17
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17967882,
FT ECO:0000269|PubMed:2474456, ECO:0000269|PubMed:7664735,
FT ECO:0007744|PubMed:19608861"
FT MOD_RES 17
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17267393,
FT ECO:0000269|PubMed:27105113"
FT MOD_RES 17
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62806"
FT MOD_RES 17
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 17
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17267393"
FT MOD_RES 21
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:12086618,
FT ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882"
FT MOD_RES 21
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:12086618,
FT ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882"
FT MOD_RES 21
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:12086618,
FT ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882,
FT ECO:0000269|PubMed:27338793"
FT MOD_RES 32
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 32
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 32
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 32
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17267393"
FT MOD_RES 32
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 32
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 32
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17267393"
FT MOD_RES 32
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 45
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 45
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17267393"
FT MOD_RES 45
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17267393"
FT MOD_RES 48
FT /note="Phosphoserine; by PAK2"
FT /evidence="ECO:0000269|PubMed:21724829,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 52
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 60
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 60
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 78
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 78
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 78
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17267393"
FT MOD_RES 78
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 78
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 78
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17267393"
FT MOD_RES 78
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 80
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 80
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17267393"
FT MOD_RES 80
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 80
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17267393"
FT MOD_RES 80
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62806"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62806"
FT MOD_RES 89
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 92
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 92
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 92
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:19818714"
FT MOD_RES 92
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17267393"
FT MOD_RES 92
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 92
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 92
FT /note="N6-propionyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:17267393"
FT MOD_RES 92
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
FT CROSSLNK 13
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in UFM1); alternate"
FT /evidence="ECO:0000269|PubMed:30886146"
FT CROSSLNK 60
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:19818714"
FT VARIANT 64
FT /note="E -> Q (in a breast cancer sample; somatic mutation;
FT dbSNP:rs747622981)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036206"
FT MUTAGEN 13
FT /note="K->A: Impaired methylation by N6AMT1."
FT /evidence="ECO:0000269|PubMed:31061526"
FT MUTAGEN 32
FT /note="K->R: Abolished ufmylation."
FT /evidence="ECO:0000269|PubMed:30886146"
FT CONFLICT 71
FT /note="V -> A (in Ref. 14; AAH67496)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="A -> P (in Ref. 11; CAG46986)"
FT /evidence="ECO:0000305"
FT TURN 7..10
FT /evidence="ECO:0007829|PDB:4YYM"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:6MLC"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3F9X"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:7CIZ"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:7CIZ"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6KE9"
FT HELIX 51..76
FT /evidence="ECO:0007829|PDB:7CIZ"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:7CIZ"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:7CIZ"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:4H9O"
SQ SEQUENCE 103 AA; 11367 MW; A9E5DFD3F8B97598 CRC64;
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG
