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 27-MAR-2024, entry version 219. 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=H4C16; Synonyms=H4-16, 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 H4C16). RX PubMed=12408966; DOI=10.1016/s0888-7543(02)96850-3; 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] {ECO:0007744|PDB:8SB6} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-16 IN COMPLEX WITH BRD2, RP ACETYLATION AT LYS-6 AND LYS-13, AND METHYLATION AT LYS-6 AND LYS-13. RX PubMed=37731000; DOI=10.1038/s41586-023-06565-9; RA Lu-Culligan W.J., Connor L.J., Xie Y., Ekundayo B.E., Rose B.T., RA Machyna M., Pintado-Urbanc A.P., Zimmer J.T., Vock I.W., Bhanu N.V., RA King M.C., Garcia B.A., Bleichert F., Simon M.D.; RT "Acetyl-methyllysine marks chromatin at active transcription start sites."; RL Nature 622:173-179(2023). RN [68] 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). RN [69] RP VARIANTS TEBIVANED1 ARG-92 AND GLN-92, CHARACTERIZATION OF VARIANTS RP TEBIVANED1 ARG-92 AND GLN-92, AND INVOLVEMENT IN TEBIVANED1. RX PubMed=28920961; DOI=10.1038/ng.3956; RG Deciphering Developmental Disorders Study; RA Tessadori F., Giltay J.C., Hurst J.A., Massink M.P., Duran K., Vos H.R., RA van Es R.M., Scott R.H., van Gassen K.L.I., Bakkers J., van Haaften G.; RT "Germline mutations affecting the histone H4 core cause a developmental RT syndrome by altering DNA damage response and cell cycle control."; RL Nat. Genet. 49:1642-1646(2017). RN [70] RP VARIANT TEBIVANED2 GLU-92, CHARACTERIZATION OF VARIANT TEBIVANED2 GLU-92, RP AND INVOLVEMENT IN TEBIVANED2. RX PubMed=31804630; DOI=10.1038/s41431-019-0552-9; RA Tessadori F., Rehman A.U., Giltay J.C., Xia F., Streff H., Duran K., RA Bakkers J., Lalani S.R., van Haaften G.; RT "A de novo variant in the human HIST1H4J gene causes a syndrome analogous RT to the HIST1H4C-associated neurodevelopmental disorder."; RL Eur. J. Hum. Genet. 28:674-678(2020). RN [71] RP VARIANTS TEBIVANED1 ALA-33; LEU-33 AND GLN-92, VARIANT TEBIVANED2 CYS-41, RP VARIANTS TEBIVANED3 THR-32; ARG-33; TRP-36; PRO-38; CYS-41; CYS-46 AND RP HIS-99, VARIANTS TEBIVANED4 LEU-41 AND ARG-76, CHARACTERIZATION OF VARIANT RP TEBIVANED1 GLN-92, CHARACTERIZATION OF VARIANT TEBIVANED2 CYS-41, RP CHARACTERIZATION OF VARIANTS TEBIVANED3 THR-32; ARG-33; TRP-36; PRO-38; RP CYS-41 AND HIS-99, CHARACTERIZATION OF VARIANTS TEBIVANED4 LEU-41 AND RP ARG-76, VARIANTS HIS-41 AND ARG-95, CHARACTERIZATION OF VARIANTS HIS-41 AND RP ARG-95, INVOLVEMENT IN TEBIVANED1, INVOLVEMENT IN TEBIVANED2, INVOLVEMENT RP IN TEBIVANED3, AND INVOLVEMENT IN TEBIVANED4. RX PubMed=35202563; DOI=10.1016/j.ajhg.2022.02.003; RG Deciphering Developmental Disorders Study; RA Tessadori F., Duran K., Knapp K., Fellner M., Smithson S., RA Beleza Meireles A., Elting M.W., Waisfisz Q., O'Donnell-Luria A., Nowak C., RA Douglas J., Ronan A., Brunet T., Kotzaeridou U., Svihovec S., Saenz M.S., RA Thiffault I., Del Viso F., Devine P., Rego S., Tenney J., van Haeringen A., RA Ruivenkamp C.A.L., Koene S., Robertson S.P., Deshpande C., Pfundt R., RA Verbeek N., van de Kamp J.M., Weiss J.M.M., Ruiz A., Gabau E., Banne E., RA Pepler A., Bottani A., Laurent S., Guipponi M., Bijlsma E., Bruel A.L., RA Sorlin A., Willis M., Powis Z., Smol T., Vincent-Delorme C., Baralle D., RA Colin E., Revencu N., Calpena E., Wilkie A.O.M., Chopra M., RA Cormier-Daire V., Keren B., Afenjar A., Niceta M., Terracciano A., RA Specchio N., Tartaglia M., Rio M., Barcia G., Rondeau S., Colson C., RA Bakkers J., Mace P.D., Bicknell L.S., van Haaften G.; RT "Recurrent de novo missense variants across multiple histone H4 genes RT underlie a neurodevelopmental syndrome."; RL Am. J. Hum. Genet. 109:750-758(2022). 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: Acetyl-methylated at Lys-6 and Lys-13 (H4K5acme and H4K12acme, CC respectively), acetyl-methylation is an epigenetic mark of active CC chromatin associated with increased transcriptional initiation CC (PubMed:37731000). Acetyl-methylation is formed by acetylation by CC EP300/p300 of lysine residues that are already monomethylated on the CC same side chain (PubMed:37731000). H4K5acme and H4K12acme marks CC specifically bind BRD2 (PubMed:37731000). CC {ECO:0000269|PubMed:37731000}. 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: Tessadori-Bicknell-Van Haaften neurodevelopmental syndrome 1 CC (TEBIVANED1) [MIM:619758]: An autosomal dominant disorder with onset in CC infancy, characterized by poor overall growth, microcephaly, hypotonia, CC profound global developmental delay, impaired intellectual development, CC poor or absent speech, and characteristic dysmorphic facial features, CC including hypertelorism and abnormal nose. Other variable neurologic CC and systemic features may also occur. {ECO:0000269|PubMed:28920961, CC ECO:0000269|PubMed:35202563}. Note=The disease is caused by variants CC affecting the gene represented in this entry. TEBIVANED1 is caused by CC variants in H4C3. {ECO:0000269|PubMed:28920961, CC ECO:0000269|PubMed:35202563}. CC -!- DISEASE: Tessadori-Bicknell-Van Haaften neurodevelopmental syndrome 2 CC (TEBIVANED2) [MIM:619759]: An autosomal dominant disorder characterized CC by poor overall growth, microcephaly, hypotonia, profound global CC developmental delay, impaired intellectual development, absent speech, CC and characteristic dysmorphic facial features, including hypertelorism, CC abnormal nose, and wide mouth. {ECO:0000269|PubMed:31804630, CC ECO:0000269|PubMed:35202563}. Note=The disease is caused by variants CC affecting the gene represented in this entry. TEBIVANED2 is caused by CC variants in H4C11. {ECO:0000269|PubMed:31804630, CC ECO:0000269|PubMed:35202563}. CC -!- DISEASE: Tessadori-Bicknell-Van Haaften neurodevelopmental syndrome 3 CC (TEBIVANED3) [MIM:619950]: An autosomal dominant disorder characterized CC by global developmental delay with poor overall growth, impaired CC intellectual development, and speech difficulties. More variable CC features include hypotonia, microcephaly, and dysmorphic facies. CC {ECO:0000269|PubMed:35202563}. Note=The disease is caused by variants CC affecting the gene represented in this entry. TEBIVANED3 is caused by CC variants in H4C5. {ECO:0000269|PubMed:35202563}. CC -!- DISEASE: Tessadori-Bicknell-Van Haaften neurodevelopmental syndrome 4 CC (TEBIVANED4) [MIM:619951]: An autosomal dominant disorder characterized CC by global developmental delay with poor overall growth, variably CC impaired intellectual development, learning difficulties, distal CC skeletal anomalies, and dysmorphic facies. Some patients have visual or CC hearing deficits. {ECO:0000269|PubMed:35202563}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC TEBIVANED4 is caused by variants in H4C9. CC {ECO:0000269|PubMed:35202563}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 7EID; X-ray; 2.00 A; C/D=6-15. 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; 7PET; EM; 9.50 A; B/F/L/P/b/f/l/p=1-103. DR PDB; 7PEU; EM; 7.20 A; B/F/L/P/b/f=1-103. DR PDB; 7PEV; EM; 6.00 A; B/F/L/P=1-103. DR PDB; 7PEW; EM; 4.60 A; B/F=1-103. DR PDB; 7PEX; EM; 5.10 A; b/f=1-103. DR PDB; 7PEY; EM; 4.50 A; L/P=1-103. DR PDB; 7PEZ; EM; 7.90 A; l/p=1-103. DR PDB; 7PF0; EM; 11.00 A; B/F/L/P/b/f=1-103. DR PDB; 7PF2; EM; 5.10 A; B/F/L/P=1-103. DR PDB; 7PF3; EM; 4.00 A; l/p=1-103. DR PDB; 7PF4; EM; 4.00 A; L/P=1-103. DR PDB; 7PF5; EM; 3.80 A; b/f=1-103. DR PDB; 7PF6; EM; 4.00 A; B/F=1-103. DR PDB; 7PFA; EM; 9.70 A; B/F/L/P/b/f=1-103. DR PDB; 7PFC; EM; 6.40 A; B/F/L/P=1-103. DR PDB; 7PFD; EM; 4.40 A; B/F=1-103. DR PDB; 7PFE; EM; 4.40 A; b/f=1-103. DR PDB; 7PFF; EM; 4.30 A; L/P=1-103. DR PDB; 7PFT; EM; 9.80 A; B/F/L/P/b/f=1-103. DR PDB; 7PFU; EM; 5.00 A; B/F/L/P=1-103. DR PDB; 7PFV; EM; 4.40 A; B/F=1-103. DR PDB; 7PFW; EM; 5.20 A; b/f=1-103. DR PDB; 7PFX; EM; 4.30 A; L/P=1-103. DR PDB; 7PII; EM; 2.68 A; B/F=1-103. DR PDB; 7R5R; EM; 2.44 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; 7TAN; EM; 3.00 A; B/F=1-103. DR PDB; 7U0G; EM; 2.60 A; B/F=1-103. DR PDB; 7U0I; EM; 2.60 A; B/F=1-103. DR PDB; 7U0J; EM; 2.70 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; 7U50; EM; 3.40 A; B/F=2-103. DR PDB; 7U51; EM; 3.10 A; B/F=2-103. DR PDB; 7U52; EM; 3.40 A; B/F=2-103. DR PDB; 7U53; EM; 4.00 A; B/F=2-103. DR PDB; 7UV9; EM; 3.20 A; B/F=2-103. DR PDB; 7V1M; X-ray; 2.83 A; C/E=2-103. DR PDB; 7V6Q; X-ray; 3.00 A; C/G=3-103. DR PDB; 7V90; EM; 3.50 A; B/F=1-103. DR PDB; 7V96; EM; 3.92 A; B/F/L/P=1-103. DR PDB; 7V9C; EM; 4.50 A; B/F/L/P=1-103. DR PDB; 7V9J; EM; 8.00 A; B/F/L/P/T/X=1-103. DR PDB; 7V9K; EM; 8.10 A; B/F/L/P/T/X/b/f=1-103. DR PDB; 7V9S; EM; 11.00 A; B/F/L/P/T/X=1-103. DR PDB; 7VA4; EM; 14.00 A; B/F/L/P/T/X/b/f=1-103. DR PDB; 7VCQ; X-ray; 3.00 A; B/E/H=1-103. DR PDB; 7VZ4; EM; 1.89 A; B/F=2-103. DR PDB; 7W9V; EM; 3.95 A; B/F=1-103. DR PDB; 7WBV; EM; 4.10 A; b/f=2-103. DR PDB; 7WBW; EM; 7.10 A; b/f=2-103. DR PDB; 7WBX; EM; 4.00 A; b/f=2-103. DR PDB; 7X57; EM; 3.63 A; B/D/F/H=1-103. DR PDB; 7X58; EM; 3.93 A; B/D/F/H=2-103. DR PDB; 7XCR; EM; 2.57 A; B/F=16-103. DR PDB; 7XCT; EM; 2.72 A; B/F=16-103. DR PDB; 7XD0; EM; 3.48 A; B/F=21-103. DR PDB; 7XD1; EM; 3.20 A; B/F=23-102. DR PDB; 7XSE; EM; 3.60 A; b/f=1-103. DR PDB; 7XSX; EM; 3.80 A; b/f=1-103. DR PDB; 7XSZ; EM; 3.40 A; b/f=1-103. DR PDB; 7XT7; EM; 4.20 A; b/f=1-103. DR PDB; 7XTD; EM; 3.90 A; b/f=1-103. DR PDB; 7XTI; EM; 3.90 A; b/f=1-103. DR PDB; 7XVL; X-ray; 3.51 A; B/F/L/P/V/Z/f/j=1-103. DR PDB; 7XVM; X-ray; 2.84 A; B/F/L/P=1-103. DR PDB; 7XX5; X-ray; 3.19 A; B/F/L/P=1-103. DR PDB; 7XX6; X-ray; 3.39 A; B/F/L/P/V/Z/f/j=1-103. DR PDB; 7XX7; X-ray; 2.70 A; B/F/L/P=1-103. DR PDB; 7XZX; EM; 4.53 A; B/F=1-103. DR PDB; 7XZY; EM; 3.97 A; B/F=1-103. DR PDB; 7XZZ; EM; 4.07 A; B/F=1-103. DR PDB; 7Y00; EM; 3.96 A; B/F=1-103. DR PDB; 7Y5U; EM; 3.80 A; E=1-103. DR PDB; 7Y5V; EM; 6.10 A; E/J=1-103. DR PDB; 7Y5W; EM; 3.50 A; B/D/F/H=1-103. DR PDB; 7Y60; EM; 3.80 A; B/D/F/H=1-103. DR PDB; 7Y61; EM; 5.60 A; B/D/F/H=1-103. DR PDB; 7Y7I; EM; 3.42 A; B/F=1-103. DR PDB; 7Y8R; EM; 4.40 A; B/F=2-103. DR PDB; 7YOZ; EM; 4.30 A; B/D/F/H=1-103. DR PDB; 7YQK; EM; 3.38 A; B/F=21-103. DR PDB; 7YRD; EM; 3.20 A; B/F=2-103. DR PDB; 7YWX; EM; 12.00 A; B/F=1-103. DR PDB; 7YYH; EM; 8.90 A; B/F=1-103. DR PDB; 7ZI4; EM; 3.20 A; J/N=1-103. DR PDB; 8AAG; EM; 10.00 A; B/F=1-103. DR PDB; 8ATF; EM; 3.45 A; N/R=2-103. DR PDB; 8AV6; EM; 4.68 A; N/R=2-103. DR PDB; 8B5A; X-ray; 1.92 A; B=19-26. DR PDB; 8B5B; X-ray; 1.92 A; D/E=2-13. DR PDB; 8B5C; X-ray; 1.58 A; B=2-13. DR PDB; 8DK5; EM; 2.71 A; B/F=1-103. DR PDB; 8EVG; EM; 2.75 A; B/F=1-103. DR PDB; 8EVH; EM; 2.85 A; B/F=1-103. DR PDB; 8EVI; EM; 2.64 A; B/F=1-103. DR PDB; 8EVJ; EM; 4.10 A; B/F=1-103. DR PDB; 8GUI; EM; 2.81 A; B/F=2-103. DR PDB; 8GUJ; EM; 2.80 A; B/F=2-103. DR PDB; 8GUK; EM; 2.51 A; B/F=2-103. DR PDB; 8H0V; EM; 3.80 A; b/f=1-103. DR PDB; 8H0W; EM; 4.60 A; b/f=1-103. DR PDB; 8H1T; EM; 3.00 A; B/F=1-103. DR PDB; 8HAG; EM; 3.20 A; B/F=2-103. DR PDB; 8HAH; EM; 3.90 A; B/F=2-103. DR PDB; 8HAI; EM; 4.70 A; B/F=2-103. DR PDB; 8HAJ; EM; 4.80 A; B/F=2-103. DR PDB; 8HAK; EM; 4.50 A; B/F=2-103. DR PDB; 8HAL; EM; 4.40 A; B/F=2-103. DR PDB; 8HAM; EM; 4.50 A; B/F=2-103. DR PDB; 8HAN; EM; 4.20 A; B/F=2-103. DR PDB; 8HE5; EM; 6.95 A; b/f=1-103. DR PDB; 8HLW; X-ray; 2.50 A; B=14-21. DR PDB; 8IEG; EM; 3.44 A; F/L=23-102. DR PDB; 8IEJ; EM; 3.12 A; F/L=23-102. DR PDB; 8IQF; EM; 4.60 A; E/J=1-103. DR PDB; 8IQG; EM; 3.50 A; E=1-103. DR PDB; 8J6S; EM; 3.80 A; B/D/F/H=1-103. DR PDB; 8J6T; EM; 6.60 A; B/D/F/H=1-103. DR PDB; 8JH2; EM; 5.70 A; b/f=1-103. DR PDB; 8JH3; EM; 3.70 A; b/f=1-103. DR PDB; 8JH4; EM; 3.20 A; b/f=1-103. DR PDB; 8JHF; EM; 3.68 A; B/F=18-103. DR PDB; 8JHG; EM; 3.58 A; B/F=18-103. DR PDB; 8JL9; EM; 2.65 A; B/F=1-103. DR PDB; 8JLA; EM; 3.44 A; B/F=17-103. DR PDB; 8JLB; EM; 2.36 A; B/F=1-103. DR PDB; 8JLD; EM; 2.48 A; B/F=1-103. DR PDB; 8KB5; EM; 2.26 A; B/F=1-103. DR PDB; 8OFF; EM; 3.40 A; Da/Db=1-103. DR PDB; 8OO7; EM; 2.80 A; N/R=2-103. DR PDB; 8OOA; EM; 3.18 A; N/R=2-103. DR PDB; 8OOP; EM; 2.70 A; N/R=2-103. DR PDB; 8OOS; EM; 3.29 A; N/R=2-103. DR PDB; 8OSJ; EM; 6.20 A; B/F=1-103. DR PDB; 8OSK; EM; 3.60 A; B/F=1-103. DR PDB; 8OSL; EM; 4.90 A; B/F=1-103. DR PDB; 8OTS; EM; 3.30 A; B/F=1-103. DR PDB; 8OTT; EM; 3.30 A; B/F=22-103. DR PDB; 8OX0; EM; 2.52 A; B/F=1-103. DR PDB; 8OX1; EM; 2.70 A; B/F=1-103. DR PDB; 8SB6; X-ray; 1.80 A; D/E=2-16. DR PDB; 8SPS; EM; 3.00 A; B/F=1-103. DR PDB; 8SPU; EM; 2.80 A; B/F=1-103. DR PDB; 8SYP; EM; 2.60 A; B/F=1-103. 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; 7EID; -. 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; 7PET; -. DR PDBsum; 7PEU; -. DR PDBsum; 7PEV; -. DR PDBsum; 7PEW; -. DR PDBsum; 7PEX; -. DR PDBsum; 7PEY; -. DR PDBsum; 7PEZ; -. DR PDBsum; 7PF0; -. DR PDBsum; 7PF2; -. DR PDBsum; 7PF3; -. DR PDBsum; 7PF4; -. DR PDBsum; 7PF5; -. DR PDBsum; 7PF6; -. DR PDBsum; 7PFA; -. DR PDBsum; 7PFC; -. DR PDBsum; 7PFD; -. DR PDBsum; 7PFE; -. DR PDBsum; 7PFF; -. DR PDBsum; 7PFT; -. DR PDBsum; 7PFU; -. DR PDBsum; 7PFV; -. DR PDBsum; 7PFW; -. DR PDBsum; 7PFX; -. DR PDBsum; 7PII; -. DR PDBsum; 7R5R; -. DR PDBsum; 7SCY; -. DR PDBsum; 7SCZ; -. DR PDBsum; 7TAN; -. DR PDBsum; 7U0G; -. DR PDBsum; 7U0I; -. DR PDBsum; 7U0J; -. DR PDBsum; 7U46; -. DR PDBsum; 7U47; -. DR PDBsum; 7U4D; -. DR PDBsum; 7U50; -. DR PDBsum; 7U51; -. DR PDBsum; 7U52; -. DR PDBsum; 7U53; -. DR PDBsum; 7UV9; -. DR PDBsum; 7V1M; -. DR PDBsum; 7V6Q; -. DR PDBsum; 7V90; -. DR PDBsum; 7V96; -. DR PDBsum; 7V9C; -. DR PDBsum; 7V9J; -. DR PDBsum; 7V9K; -. DR PDBsum; 7V9S; -. DR PDBsum; 7VA4; -. DR PDBsum; 7VCQ; -. DR PDBsum; 7VZ4; -. DR PDBsum; 7W9V; -. DR PDBsum; 7WBV; -. DR PDBsum; 7WBW; -. DR PDBsum; 7WBX; -. DR PDBsum; 7X57; -. DR PDBsum; 7X58; -. DR PDBsum; 7XCR; -. DR PDBsum; 7XCT; -. DR PDBsum; 7XD0; -. DR PDBsum; 7XD1; -. DR PDBsum; 7XSE; -. DR PDBsum; 7XSX; -. DR PDBsum; 7XSZ; -. DR PDBsum; 7XT7; -. DR PDBsum; 7XTD; -. DR PDBsum; 7XTI; -. DR PDBsum; 7XVL; -. DR PDBsum; 7XVM; -. DR PDBsum; 7XX5; -. DR PDBsum; 7XX6; -. DR PDBsum; 7XX7; -. DR PDBsum; 7XZX; -. DR PDBsum; 7XZY; -. DR PDBsum; 7XZZ; -. DR PDBsum; 7Y00; -. DR PDBsum; 7Y5U; -. DR PDBsum; 7Y5V; -. DR PDBsum; 7Y5W; -. DR PDBsum; 7Y60; -. DR PDBsum; 7Y61; -. DR PDBsum; 7Y7I; -. DR PDBsum; 7Y8R; -. DR PDBsum; 7YOZ; -. DR PDBsum; 7YQK; -. DR PDBsum; 7YRD; -. DR PDBsum; 7YWX; -. DR PDBsum; 7YYH; -. DR PDBsum; 7ZI4; -. DR PDBsum; 8AAG; -. DR PDBsum; 8ATF; -. DR PDBsum; 8AV6; -. DR PDBsum; 8B5A; -. DR PDBsum; 8B5B; -. DR PDBsum; 8B5C; -. DR PDBsum; 8DK5; -. DR PDBsum; 8EVG; -. DR PDBsum; 8EVH; -. DR PDBsum; 8EVI; -. DR PDBsum; 8EVJ; -. DR PDBsum; 8GUI; -. DR PDBsum; 8GUJ; -. DR PDBsum; 8GUK; -. DR PDBsum; 8H0V; -. DR PDBsum; 8H0W; -. DR PDBsum; 8H1T; -. DR PDBsum; 8HAG; -. DR PDBsum; 8HAH; -. DR PDBsum; 8HAI; -. DR PDBsum; 8HAJ; -. DR PDBsum; 8HAK; -. DR PDBsum; 8HAL; -. DR PDBsum; 8HAM; -. DR PDBsum; 8HAN; -. DR PDBsum; 8HE5; -. DR PDBsum; 8HLW; -. DR PDBsum; 8IEG; -. DR PDBsum; 8IEJ; -. DR PDBsum; 8IQF; -. DR PDBsum; 8IQG; -. DR PDBsum; 8J6S; -. DR PDBsum; 8J6T; -. DR PDBsum; 8JH2; -. DR PDBsum; 8JH3; -. DR PDBsum; 8JH4; -. DR PDBsum; 8JHF; -. DR PDBsum; 8JHG; -. DR PDBsum; 8JL9; -. DR PDBsum; 8JLA; -. DR PDBsum; 8JLB; -. DR PDBsum; 8JLD; -. DR PDBsum; 8KB5; -. DR PDBsum; 8OFF; -. DR PDBsum; 8OO7; -. DR PDBsum; 8OOA; -. DR PDBsum; 8OOP; -. DR PDBsum; 8OOS; -. DR PDBsum; 8OSJ; -. DR PDBsum; 8OSK; -. DR PDBsum; 8OSL; -. DR PDBsum; 8OTS; -. DR PDBsum; 8OTT; -. DR PDBsum; 8OX0; -. DR PDBsum; 8OX1; -. DR PDBsum; 8SB6; -. DR PDBsum; 8SPS; -. DR PDBsum; 8SPU; -. DR PDBsum; 8SYP; -. DR AlphaFoldDB; P62805; -. DR EMDB; EMD-0586; -. DR EMDB; EMD-0671; -. DR EMDB; EMD-0672; -. DR EMDB; EMD-0673; -. DR EMDB; EMD-0674; -. DR EMDB; EMD-0675; -. DR EMDB; EMD-0676; -. DR EMDB; EMD-10151; -. DR EMDB; EMD-10152; -. DR EMDB; EMD-10153; -. DR EMDB; EMD-10154; -. DR EMDB; EMD-10155; -. DR EMDB; EMD-10390; -. DR EMDB; EMD-10391; -. DR EMDB; EMD-10392; -. DR EMDB; EMD-10393; -. DR EMDB; EMD-10394; -. DR EMDB; EMD-10406; -. DR EMDB; EMD-10408; -. DR EMDB; EMD-10694; -. DR EMDB; EMD-10864; -. DR EMDB; EMD-11005; -. DR EMDB; EMD-11006; -. DR EMDB; EMD-11601; -. DR EMDB; EMD-12453; -. DR EMDB; EMD-13356; -. DR EMDB; EMD-13357; -. DR EMDB; EMD-13358; -. DR EMDB; EMD-13359; -. DR EMDB; EMD-13360; -. DR EMDB; EMD-13361; -. DR EMDB; EMD-13362; -. DR EMDB; EMD-13363; -. DR EMDB; EMD-13365; -. DR EMDB; EMD-13366; -. DR EMDB; EMD-13367; -. DR EMDB; EMD-13368; -. DR EMDB; EMD-13369; -. DR EMDB; EMD-13370; -. DR EMDB; EMD-13371; -. DR EMDB; EMD-13372; -. DR EMDB; EMD-13373; -. DR EMDB; EMD-13374; -. DR EMDB; EMD-13379; -. DR EMDB; EMD-13380; -. DR EMDB; EMD-13381; -. DR EMDB; EMD-13382; -. DR EMDB; EMD-13383; -. DR EMDB; EMD-13437; -. DR EMDB; EMD-14334; -. DR EMDB; EMD-14351; -. DR EMDB; EMD-14375; -. DR EMDB; EMD-14737; -. DR EMDB; EMD-16859; -. DR EMDB; EMD-17006; -. DR EMDB; EMD-17008; -. DR EMDB; EMD-17025; -. DR EMDB; EMD-17027; -. DR EMDB; EMD-17155; -. DR EMDB; EMD-17157; -. DR EMDB; EMD-17160; -. DR EMDB; EMD-17183; -. DR EMDB; EMD-17184; -. DR EMDB; EMD-17251; -. DR EMDB; EMD-17252; -. DR EMDB; EMD-17253; -. DR EMDB; EMD-20840; -. DR EMDB; EMD-20841; -. DR EMDB; EMD-20864; -. DR EMDB; EMD-21114; -. DR EMDB; EMD-22046; -. DR EMDB; EMD-22047; -. DR EMDB; EMD-22206; -. DR EMDB; EMD-22408; -. DR EMDB; EMD-22409; -. DR EMDB; EMD-22581; -. DR EMDB; EMD-22683; -. DR EMDB; EMD-22684; -. DR EMDB; EMD-22685; -. DR EMDB; EMD-22686; -. DR EMDB; EMD-22687; -. DR EMDB; EMD-22688; -. DR EMDB; EMD-23590; -. DR EMDB; EMD-23591; -. DR EMDB; EMD-23592; -. DR EMDB; EMD-25042; -. DR EMDB; EMD-25043; -. DR EMDB; EMD-25777; -. DR EMDB; EMD-25778; -. DR EMDB; EMD-26258; -. DR EMDB; EMD-26260; -. DR EMDB; EMD-26261; -. DR EMDB; EMD-26330; -. DR EMDB; EMD-26331; -. DR EMDB; EMD-26332; -. DR EMDB; EMD-26336; -. DR EMDB; EMD-26337; -. DR EMDB; EMD-26338; -. DR EMDB; EMD-26339; -. DR EMDB; EMD-26809; -. DR EMDB; EMD-26810; -. DR EMDB; EMD-27483; -. DR EMDB; EMD-28628; -. DR EMDB; EMD-28629; -. DR EMDB; EMD-28630; -. DR EMDB; EMD-28631; -. DR EMDB; EMD-30076; -. DR EMDB; EMD-30077; -. DR EMDB; EMD-30078; -. DR EMDB; EMD-30232; -. DR EMDB; EMD-30237; -. DR EMDB; EMD-30239; -. DR EMDB; EMD-30267; -. DR EMDB; EMD-30339; -. DR EMDB; EMD-30340; -. DR EMDB; EMD-30551; -. DR EMDB; EMD-30552; -. DR EMDB; EMD-31015; -. DR EMDB; EMD-31806; -. DR EMDB; EMD-31810; -. DR EMDB; EMD-31815; -. DR EMDB; EMD-31816; -. DR EMDB; EMD-31823; -. DR EMDB; EMD-31826; -. DR EMDB; EMD-31832; -. DR EMDB; EMD-32373; -. DR EMDB; EMD-33010; -. DR EMDB; EMD-33011; -. DR EMDB; EMD-33424; -. DR EMDB; EMD-33436; -. DR EMDB; EMD-33437; -. DR EMDB; EMD-33441; -. DR EMDB; EMD-33447; -. DR EMDB; EMD-33450; -. DR EMDB; EMD-33533; -. DR EMDB; EMD-33534; -. DR EMDB; EMD-33535; -. DR EMDB; EMD-33536; -. DR EMDB; EMD-33625; -. DR EMDB; EMD-33626; -. DR EMDB; EMD-33627; -. DR EMDB; EMD-33630; -. DR EMDB; EMD-33631; -. DR EMDB; EMD-33666; -. DR EMDB; EMD-33991; -. DR EMDB; EMD-34053; -. DR EMDB; EMD-34207; -. DR EMDB; EMD-34212; -. DR EMDB; EMD-34274; -. DR EMDB; EMD-34275; -. DR EMDB; EMD-34431; -. DR EMDB; EMD-34588; -. DR EMDB; EMD-34589; -. DR EMDB; EMD-34591; -. DR EMDB; EMD-34592; -. DR EMDB; EMD-34594; -. DR EMDB; EMD-34595; -. DR EMDB; EMD-34596; -. DR EMDB; EMD-34597; -. DR EMDB; EMD-35381; -. DR EMDB; EMD-35383; -. DR EMDB; EMD-35660; -. DR EMDB; EMD-35661; -. DR EMDB; EMD-36013; -. DR EMDB; EMD-36014; -. DR EMDB; EMD-36251; -. DR EMDB; EMD-36252; -. DR EMDB; EMD-36253; -. DR EMDB; EMD-36264; -. DR EMDB; EMD-36265; -. DR EMDB; EMD-36389; -. DR EMDB; EMD-36390; -. DR EMDB; EMD-36391; -. DR EMDB; EMD-36393; -. DR EMDB; EMD-37070; -. DR EMDB; EMD-3954; -. DR EMDB; EMD-40683; -. DR EMDB; EMD-40686; -. DR EMDB; EMD-40889; -. DR EMDB; EMD-4277; -. DR EMDB; EMD-4692; -. DR EMDB; EMD-4711; -. DR EMDB; EMD-4762; -. DR EMDB; EMD-4763; -. DR EMDB; EMD-4764; -. DR EMDB; EMD-4765; -. DR EMDB; EMD-4766; -. DR EMDB; EMD-4767; -. DR EMDB; EMD-4768; -. DR EMDB; EMD-4960; -. DR EMDB; EMD-6980; -. DR EMDB; EMD-6981; -. DR EMDB; EMD-6982; -. DR EMDB; EMD-6983; -. DR EMDB; EMD-6984; -. DR EMDB; EMD-6985; -. DR EMDB; EMD-6986; -. DR EMDB; EMD-7293; -. DR EMDB; EMD-7318; -. DR EMDB; EMD-7326; -. DR EMDB; EMD-8945; -. DR EMDB; EMD-8949; -. DR EMDB; EMD-9250; -. DR EMDB; EMD-9251; -. DR EMDB; EMD-9713; -. DR SASBDB; P62805; -. DR SMR; P62805; -. DR BioGRID; 113899; 104. DR BioGRID; 113955; 1692. DR BioGRID; 113956; 28. DR BioGRID; 113957; 68. DR BioGRID; 113958; 59. DR BioGRID; 113959; 44. DR BioGRID; 113960; 47. DR BioGRID; 113961; 36. DR BioGRID; 113962; 55. DR BioGRID; 113963; 32. DR BioGRID; 113964; 60. DR BioGRID; 113966; 96. DR BioGRID; 125732; 123. DR BioGRID; 299853; 42. 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; 247. DR MINT; P62805; -. DR STRING; 9606.ENSP00000244537; -. DR BindingDB; P62805; -. DR ChEMBL; CHEMBL5876; -. DR GlyCosmos; P62805; 1 site, 1 glycan. 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 CPTAC; CPTAC-1055; -. DR CPTAC; CPTAC-1056; -. DR EPD; P62805; -. DR jPOST; P62805; -. DR MassIVE; P62805; -. DR MaxQB; P62805; -. DR PaxDb; 9606-ENSP00000244537; -. DR PeptideAtlas; P62805; -. DR PRIDE; P62805; -. DR ProteomicsDB; 57424; -. DR Pumba; P62805; -. DR TopDownProteomics; P62805; -. DR ABCD; P62805; 4 sequenced antibodies. DR Antibodypedia; 23657; 2751 antibodies from 40 providers. DR Antibodypedia; 70431; 12 antibodies from 7 providers. DR Antibodypedia; 73583; 122 antibodies from 11 providers. DR Antibodypedia; 73812; 14 antibodies from 8 providers. DR Antibodypedia; 73941; 622 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; 5 antibodies from 5 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 AGR; HGNC:20510; -. DR AGR; HGNC:29607; -. DR AGR; HGNC:4781; -. DR AGR; HGNC:4782; -. DR AGR; HGNC:4783; -. DR AGR; HGNC:4784; -. DR AGR; HGNC:4785; -. DR AGR; HGNC:4787; -. DR AGR; HGNC:4788; -. DR AGR; HGNC:4789; -. DR AGR; HGNC:4790; -. DR AGR; HGNC:4791; -. DR AGR; HGNC:4793; -. DR AGR; HGNC:4794; -. 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; H4C1; -. DR GeneCards; H4C11; -. DR GeneCards; H4C12; -. DR GeneCards; H4C13; -. DR GeneCards; H4C14; -. DR GeneCards; H4C15; -. DR GeneCards; H4C16; -. DR GeneCards; H4C2; -. DR GeneCards; H4C3; -. DR GeneCards; H4C4; -. DR GeneCards; H4C5; -. DR GeneCards; H4C6; -. DR GeneCards; H4C8; -. DR GeneCards; H4C9; -. 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:20510; H4C16. 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 enhanced (lymphoid tissue, skeletal muscle). DR HPA; ENSG00000197061; Tissue enhanced (bone marrow, lymphoid tissue). DR HPA; ENSG00000197238; Tissue enhanced (liver). DR HPA; ENSG00000197837; Low tissue specificity. DR HPA; ENSG00000270276; Low tissue specificity. DR HPA; ENSG00000270882; Low tissue specificity. DR HPA; ENSG00000273542; Tissue enhanced (bone). DR HPA; ENSG00000274618; Not detected. DR HPA; ENSG00000275126; Not detected. DR HPA; ENSG00000276180; Tissue enhanced (lymphoid). DR HPA; ENSG00000276966; Low tissue specificity. DR HPA; ENSG00000277157; Tissue enhanced (lymphoid). DR HPA; ENSG00000278637; Tissue enhanced (bone marrow, lymphoid tissue). DR HPA; ENSG00000278705; Group enriched (bone marrow, choroid plexus, lymphoid tissue). DR MalaCards; H4C1; -. DR MalaCards; H4C11; -. DR MalaCards; H4C3; -. DR MalaCards; H4C5; -. DR MalaCards; H4C9; -. 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 MIM; 619758; phenotype. DR MIM; 619759; phenotype. DR MIM; 619950; phenotype. DR MIM; 619951; phenotype. 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 Orphanet; 528084; Non-specific syndromic intellectual disability. 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; ENSGT01060000248528; -. DR HOGENOM; CLU_109117_2_3_1; -. DR InParanoid; P62805; -. DR OMA; RRNRNMS; -. DR OrthoDB; 4702965at2759; -. 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 Reactome; R-HSA-9821002; Chromatin modifications during the maternal to zygotic transition (MZT). DR Reactome; R-HSA-9821993; Replacement of protamines by nucleosomes in the male pronucleus. DR SignaLink; P62805; -. DR SIGNOR; P62805; -. DR BioGRID-ORCS; 121504; 17 hits in 1139 CRISPR screens. DR BioGRID-ORCS; 554313; 85 hits in 1013 CRISPR screens. DR BioGRID-ORCS; 8294; 25 hits in 1146 CRISPR screens. DR BioGRID-ORCS; 8359; 28 hits in 1127 CRISPR screens. DR BioGRID-ORCS; 8360; 8 hits in 1133 CRISPR screens. DR BioGRID-ORCS; 8361; 11 hits in 1127 CRISPR screens. DR BioGRID-ORCS; 8362; 58 hits in 976 CRISPR screens. DR BioGRID-ORCS; 8363; 94 hits in 672 CRISPR screens. DR BioGRID-ORCS; 8364; 26 hits in 1157 CRISPR screens. DR BioGRID-ORCS; 8365; 20 hits in 1150 CRISPR screens. DR BioGRID-ORCS; 8366; 33 hits in 1110 CRISPR screens. DR BioGRID-ORCS; 8367; 15 hits in 1099 CRISPR screens. DR BioGRID-ORCS; 8368; 11 hits in 1121 CRISPR screens. DR BioGRID-ORCS; 8370; 46 hits in 599 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 145 other cell types or tissues. DR ExpressionAtlas; P62805; baseline and differential. 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: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: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; IDA:GO_Central. DR GO; GO:0006325; P:chromatin organization; NAS:ComplexPortal. 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; NAS: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; Histone, subunit A; 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 PANTHER; PTHR10484; HISTONE H4; 1. DR PANTHER; PTHR10484:SF0; HISTONE H4; 1. DR Pfam; PF15511; CENP-T_C; 1. DR PRINTS; PR00623; HISTONEH4. DR SMART; SM00417; H4; 1. DR SMART; SM00803; TAF; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS00047; HISTONE_H4; 1. DR SWISS-2DPAGE; P62805; -. DR Genevisible; P62805; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromosomal rearrangement; Chromosome; KW Citrullination; Direct protein sequencing; Disease variant; DNA-binding; KW Hydroxylation; Intellectual disability; Isopeptide bond; Methylation; KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome; KW 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-acetyl-N6-methyllysine; alternate" FT /evidence="ECO:0000269|PubMed:37731000" 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-acetyl-N6-methyllysine; alternate" FT /evidence="ECO:0000269|PubMed:37731000" 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 32 FT /note="K -> T (in TEBIVANED3; results in early FT developmental defects when expressed in zebrafish embryos)" FT /evidence="ECO:0000269|PubMed:35202563" FT /id="VAR_086990" FT VARIANT 33 FT /note="P -> A (in TEBIVANED1)" FT /evidence="ECO:0000269|PubMed:35202563" FT /id="VAR_086991" FT VARIANT 33 FT /note="P -> L (in TEBIVANED1)" FT /evidence="ECO:0000269|PubMed:35202563" FT /id="VAR_086992" FT VARIANT 33 FT /note="P -> R (in TEBIVANED3; results in early FT developmental defects when expressed in zebrafish embryos)" FT /evidence="ECO:0000269|PubMed:35202563" FT /id="VAR_086993" FT VARIANT 36 FT /note="R -> W (in TEBIVANED3; results in early FT developmental defects when expressed in zebrafish embryos)" FT /evidence="ECO:0000269|PubMed:35202563" FT /id="VAR_086994" FT VARIANT 38 FT /note="L -> P (in TEBIVANED3; results in early FT developmental defects when expressed in zebrafish embryos)" FT /evidence="ECO:0000269|PubMed:35202563" FT /id="VAR_086995" FT VARIANT 41 FT /note="R -> C (in TEBIVANED2 and TEBIVANED3; uncertain FT significance; does not affect early development when FT expressed in zebrafish embryos)" FT /evidence="ECO:0000269|PubMed:35202563" FT /id="VAR_086996" FT VARIANT 41 FT /note="R -> H (found in a patient with a neurodevelopmental FT disorder; uncertain significance; results in early FT developmental defects when expressed in zebrafish embryos)" FT /evidence="ECO:0000269|PubMed:35202563" FT /id="VAR_086997" FT VARIANT 41 FT /note="R -> L (in TEBIVANED4; results in early FT developmental defects when expressed in zebrafish embryos)" FT /evidence="ECO:0000269|PubMed:35202563" FT /id="VAR_086998" FT VARIANT 46 FT /note="R -> C (in TEBIVANED3)" FT /evidence="ECO:0000269|PubMed:35202563" FT /id="VAR_086999" 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 VARIANT 76 FT /note="H -> R (in TEBIVANED4; results in severe early FT developmental defects when expressed in zebrafish embryos)" FT /evidence="ECO:0000269|PubMed:35202563" FT /id="VAR_087000" FT VARIANT 92 FT /note="K -> E (in TEBIVANED2; results in severe early FT developmental defects when expressed in zebrafish embryos)" FT /evidence="ECO:0000269|PubMed:31804630" FT /id="VAR_087001" FT VARIANT 92 FT /note="K -> Q (in TEBIVANED1; results in severe early FT developmental defects when expressed in zebrafish embryos; FT results in defective cell cycle progression when expressed FT in zebrafish embryos)" FT /evidence="ECO:0000269|PubMed:28920961, FT ECO:0000269|PubMed:35202563" FT /id="VAR_087002" FT VARIANT 92 FT /note="K -> R (in TEBIVANED1; results in severe early FT developmental defects when expressed in zebrafish embryos; FT results in defective cell cycle progression when expressed FT in zebrafish embryos)" FT /evidence="ECO:0000269|PubMed:28920961" FT /id="VAR_087003" FT VARIANT 95 FT /note="G -> R (found in a patient with a neurodevelopmental FT disorder; uncertain significance)" FT /evidence="ECO:0000269|PubMed:35202563" FT /id="VAR_087004" FT VARIANT 99 FT /note="Y -> H (in TEBIVANED3; results in early FT developmental defects when expressed in zebrafish embryos)" FT /evidence="ECO:0000269|PubMed:35202563" FT /id="VAR_087005" 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 //