ID H4_YEAST Reviewed; 103 AA.
AC P02309; D6VQ10;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 233.
DE RecName: Full=Histone H4;
GN Name=HHF1; OrderedLocusNames=YBR009C; ORFNames=YBR0122;
GN and
GN Name=HHF2; OrderedLocusNames=YNL030W; ORFNames=N2752;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6355483; DOI=10.1016/s0022-2836(83)80164-8;
RA Smith M.M., Andresson O.S.;
RT "DNA sequences of yeast H3 and H4 histone genes from two non-allelic gene
RT sets encode identical H3 and H4 proteins.";
RL J. Mol. Biol. 169:663-690(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RA Lohan A.J.E., Wolfe K.H.;
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Carlsbergensis;
RX PubMed=6310494; DOI=10.1093/nar/11.16.5347;
RA Woudt L.P., Pastink A., Kempers-Veenstra A.E., Jansen A.E.M., Mager W.H.,
RA Planta R.J.;
RT "The genes coding for histone H3 and H4 in Neurospora crassa are unique and
RT contain intervening sequences.";
RL Nucleic Acids Res. 11:5347-5360(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHF1).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHF2).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [6]
RP GENOME REANNOTATION (HHF1 AND HHF2).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [8]
RP PROTEIN SEQUENCE OF 25-48; 69-83 AND 86-100, AND PROBABLE CLEAVAGE OF
RP INITIATOR METHIONINE.
RX PubMed=7002547; DOI=10.1111/j.1432-1033.1980.tb04841.x;
RA Brandt W.F., Patterson K., von Holt C.;
RT "The histones of yeast. The isolation and partial structure of the core
RT histones.";
RL Eur. J. Biochem. 110:67-76(1980).
RN [9]
RP IDENTIFICATION IN THE UAF COMPLEX.
RX PubMed=9391047; DOI=10.1073/pnas.94.25.13458;
RA Keener J., Dodd J.A., Lalo D., Nomura M.;
RT "Histones H3 and H4 are components of upstream activation factor required
RT for the high-level transcription of yeast rDNA by RNA polymerase I.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13458-13462(1997).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP ACETYLATION AT LYS-6; LYS-9; LYS-13 AND LYS-17, BUTYRYLATION AT LYS-9, AND
RP METHYLATION AT ARG-56.
RX PubMed=19113941; DOI=10.1021/pr8005155;
RA Zhang K., Chen Y., Zhang Z., Zhao Y.;
RT "Identification and verification of lysine propionylation and butyrylation
RT in yeast core histones using PTMap software.";
RL J. Proteome Res. 8:900-906(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-65, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [15]
RP SUCCINYLATION AT LYS-32 AND LYS-78.
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 [16]
RP METHYLATION AT LYS-6; LYS-9 AND LYS-13.
RX PubMed=22343720; DOI=10.1038/nsmb.2252;
RA Green E.M., Mas G., Young N.L., Garcia B.A., Gozani O.;
RT "Methylation of H4 lysines 5, 8 and 12 by yeast Set5 calibrates chromatin
RT stress responses.";
RL Nat. Struct. Mol. Biol. 19:361-363(2012).
RN [17]
RP BUTYRYLATION AT LYS-13.
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 [18]
RP GLUTARYLATION AT LYS-92, AND MUTAGENESIS OF 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 [19]
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 16-30, AND ACETYLATION AT LYS-17.
RX PubMed=11080160; DOI=10.1093/emboj/19.22.6141;
RA Owen D.J., Ornaghi P., Yang J.C., Lowe N., Evans P.R., Ballario P.,
RA Neuhaus D., Filetici P., Travers A.A.;
RT "The structural basis for the recognition of acetylated histone H4 by the
RT bromodomain of histone acetyltransferase gcn5p.";
RL EMBO J. 19:6141-6149(2000).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF H4 IN NUCLEOSOME COMPLEX.
RX PubMed=11566884; DOI=10.1093/emboj/20.18.5207;
RA White C.L., Suto R.K., Luger K.;
RT "Structure of the yeast nucleosome core particle reveals fundamental
RT changes in internucleosome interactions.";
RL EMBO J. 20:5207-5218(2001).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 13-22, AND ACETYLATION AT LYS-17.
RX PubMed=15150415; DOI=10.1073/pnas.0401057101;
RA Zhao K., Harshaw R., Chai X., Marmorstein R.;
RT "Structural basis for nicotinamide cleavage and ADP-ribose transfer by
RT NAD(+)-dependent Sir2 histone/protein deacetylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8563-8568(2004).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 76-86, AND ACETYLATION AT LYS-80.
RX PubMed=16768447; DOI=10.1021/bi0526332;
RA Cosgrove M.S., Bever K., Avalos J.L., Muhammad S., Zhang X., Wolberger C.;
RT "The structural basis of sirtuin substrate affinity.";
RL Biochemistry 45:7511-7521(2006).
RN [23]
RP 3D-STRUCTURE MODELING.
RX PubMed=16631569; DOI=10.1016/j.cub.2006.03.054;
RA Bloom K.S., Sharma S., Dokholyan N.V.;
RT "The path of DNA in the kinetochore.";
RL Curr. Biol. 16:R276-R278(2006).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-16, AND ACETYLATION AT LYS-6
RP AND LYS-13.
RA Padmanabhan B., Umehara T., Nakano K., Jang M.K., Ozato K., Yokohama S.;
RT "Structural basis for diacetylated histone H4 tail recognition by the
RT second bromodomain of human BRD2.";
RL Submitted (NOV-2006) to the PDB data bank.
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 13-23, AND ACETYLATION AT LYS-17.
RX PubMed=17289592; DOI=10.1016/j.molcel.2006.12.022;
RA Sanders B.D., Zhao K., Slama J.T., Marmorstein R.;
RT "Structural basis for nicotinamide inhibition and base exchange in Sir2
RT enzymes.";
RL Mol. Cell 25:463-472(2007).
RN [26]
RP STRUCTURE BY NMR OF 42-103.
RX PubMed=21412236; DOI=10.1038/nature09854;
RA Zhou Z., Feng H., Zhou B.R., Ghirlando R., Hu K., Zwolak A.,
RA Miller Jenkins L.M., Xiao H., Tjandra N., Wu C., Bai Y.;
RT "Structural basis for recognition of centromere histone variant CenH3 by
RT the chaperone Scm3.";
RL Nature 472:234-237(2011).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 12-23.
RX PubMed=22020126; DOI=10.1038/emboj.2011.382;
RA Yuan H., Rossetto D., Mellert H., Dang W., Srinivasan M., Johnson J.,
RA Hodawadekar S., Ding E.C., Speicher K., Abshiru N., Perry R., Wu J.,
RA Yang C., Zheng Y.G., Speicher D.W., Thibault P., Verreault A.,
RA Johnson F.B., Berger S.L., Sternglanz R., McMahon S.B., Cote J.,
RA Marmorstein R.;
RT "MYST protein acetyltransferase activity requires active site lysine
RT autoacetylation.";
RL EMBO J. 31:58-70(2012).
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. Component of the UAF (upstream
CC activation factor) complex which interacts with the upstream element of
CC the RNA polymerase I promoter and forms a stable preinitiation complex.
CC Together with SPT15/TBP UAF seems to stimulate basal transcription to a
CC fully activated level.
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
CC DNA. Histone H4 is a component of the UAF (upstream activation factor)
CC complex which consists of UAF30, RRN5, RRN9, RRN10, and histones H3 and
CC H4. {ECO:0000269|PubMed:9391047}.
CC -!- INTERACTION:
CC P02309; P32447: ASF1; NbExp=5; IntAct=EBI-8113, EBI-3003;
CC P02309; Q08649: ESA1; NbExp=5; IntAct=EBI-8113, EBI-6648;
CC P02309; Q06205: FPR4; NbExp=5; IntAct=EBI-8113, EBI-6956;
CC P02309; P61830: HHT2; NbExp=9; IntAct=EBI-8113, EBI-8098;
CC P02309; Q12373: HIF1; NbExp=5; IntAct=EBI-8113, EBI-31911;
CC P02309; P36124: SET3; NbExp=2; IntAct=EBI-8113, EBI-16993;
CC P02309; P38890: SET5; NbExp=3; IntAct=EBI-8113, EBI-24263;
CC P02309; P22082: SNF2; NbExp=2; IntAct=EBI-8113, EBI-17526;
CC P02309; P32597: STH1; NbExp=4; IntAct=EBI-8113, EBI-18410;
CC P02309; Q9H7Z6: KAT8; Xeno; NbExp=2; IntAct=EBI-8113, EBI-896414;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
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 -!- MISCELLANEOUS: Present with 524000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the histone H4 family. {ECO:0000305}.
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DR EMBL; X00724; CAA25311.1; -; Genomic_DNA.
DR EMBL; X00725; CAA25313.1; -; Genomic_DNA.
DR EMBL; K03154; AAA34660.1; -; Genomic_DNA.
DR EMBL; Z35878; CAA84947.1; -; Genomic_DNA.
DR EMBL; Z71306; CAA95892.1; -; Genomic_DNA.
DR EMBL; AY692960; AAT92979.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07130.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10515.1; -; Genomic_DNA.
DR PIR; A02647; HSBY4.
DR RefSeq; NP_009563.1; NM_001178357.1.
DR RefSeq; NP_014368.1; NM_001182869.1.
DR PDB; 1E6I; X-ray; 1.87 A; P=16-30.
DR PDB; 1ID3; X-ray; 3.10 A; B/F=2-103.
DR PDB; 1Q1A; X-ray; 1.50 A; B=13-22.
DR PDB; 1SZC; X-ray; 1.75 A; B=13-22.
DR PDB; 1SZD; X-ray; 1.50 A; B=13-22.
DR PDB; 2DVQ; X-ray; 2.04 A; P/Q=2-16.
DR PDB; 2DVR; X-ray; 2.30 A; P/Q=2-16.
DR PDB; 2E3K; X-ray; 2.30 A; Q/R=2-16.
DR PDB; 2H2H; X-ray; 2.20 A; B=76-86.
DR PDB; 2L5A; NMR; -; A=42-103.
DR PDB; 2QQF; X-ray; 2.00 A; B=13-23.
DR PDB; 2QQG; X-ray; 2.05 A; B=13-23.
DR PDB; 3TO6; X-ray; 2.10 A; B=12-23.
DR PDB; 4JJN; X-ray; 3.09 A; B/F=2-103.
DR PDB; 4KUD; X-ray; 3.20 A; B/F=1-103.
DR PDB; 4PSX; X-ray; 2.51 A; C/F=2-49.
DR PDB; 4TWI; X-ray; 1.79 A; B=9-21.
DR PDB; 4TWJ; X-ray; 1.65 A; B=9-21.
DR PDB; 5W0V; X-ray; 2.82 A; C/D=2-35.
DR PDB; 5ZBA; X-ray; 3.50 A; D=1-103.
DR PDB; 5ZBB; X-ray; 3.60 A; D=1-103.
DR PDB; 6GEJ; EM; 3.60 A; C/D=1-103.
DR PDB; 6GEN; EM; 3.60 A; C/D=1-103.
DR PDB; 6QLD; EM; 4.15 A; b/f=25-103.
DR PDB; 6RXJ; X-ray; 1.60 A; C/D=13-22.
DR PDB; 6RXK; X-ray; 1.35 A; B=13-23.
DR PDB; 6RXL; X-ray; 2.30 A; B=13-23.
DR PDB; 6RXM; X-ray; 1.92 A; G/H/I/J/K/L=13-23.
DR PDB; 6RXO; X-ray; 1.95 A; C/D=13-23.
DR PDB; 6RXP; X-ray; 1.80 A; C/D=13-23.
DR PDB; 6RXQ; X-ray; 1.70 A; E/F/G/H=13-23.
DR PDB; 6RXR; X-ray; 1.70 A; E/F/G/H=13-23.
DR PDB; 7E9C; EM; 3.50 A; B/F=1-103.
DR PDB; 7E9F; EM; 4.00 A; B/F=1-103.
DR PDB; 7K78; EM; 3.10 A; B/F=1-103.
DR PDB; 7K7G; EM; 4.20 A; B/F=1-103.
DR PDB; 7ON1; EM; 3.35 A; b/f=1-103.
DR PDB; 7XAY; X-ray; 3.30 A; E=8-103.
DR PDB; 7Z0O; EM; 2.80 A; B=1-103.
DR PDB; 8OW0; EM; 3.40 A; b/f=1-103.
DR PDB; 8OW1; EM; 3.70 A; b/f=1-103.
DR PDBsum; 1E6I; -.
DR PDBsum; 1ID3; -.
DR PDBsum; 1Q1A; -.
DR PDBsum; 1SZC; -.
DR PDBsum; 1SZD; -.
DR PDBsum; 2DVQ; -.
DR PDBsum; 2DVR; -.
DR PDBsum; 2E3K; -.
DR PDBsum; 2H2H; -.
DR PDBsum; 2L5A; -.
DR PDBsum; 2QQF; -.
DR PDBsum; 2QQG; -.
DR PDBsum; 3TO6; -.
DR PDBsum; 4JJN; -.
DR PDBsum; 4KUD; -.
DR PDBsum; 4PSX; -.
DR PDBsum; 4TWI; -.
DR PDBsum; 4TWJ; -.
DR PDBsum; 5W0V; -.
DR PDBsum; 5ZBA; -.
DR PDBsum; 5ZBB; -.
DR PDBsum; 6GEJ; -.
DR PDBsum; 6GEN; -.
DR PDBsum; 6QLD; -.
DR PDBsum; 6RXJ; -.
DR PDBsum; 6RXK; -.
DR PDBsum; 6RXL; -.
DR PDBsum; 6RXM; -.
DR PDBsum; 6RXO; -.
DR PDBsum; 6RXP; -.
DR PDBsum; 6RXQ; -.
DR PDBsum; 6RXR; -.
DR PDBsum; 7E9C; -.
DR PDBsum; 7E9F; -.
DR PDBsum; 7K78; -.
DR PDBsum; 7K7G; -.
DR PDBsum; 7ON1; -.
DR PDBsum; 7XAY; -.
DR PDBsum; 7Z0O; -.
DR PDBsum; 8OW0; -.
DR PDBsum; 8OW1; -.
DR AlphaFoldDB; P02309; -.
DR BMRB; P02309; -.
DR EMDB; EMD-12993; -.
DR EMDB; EMD-14428; -.
DR EMDB; EMD-17226; -.
DR EMDB; EMD-17227; -.
DR EMDB; EMD-22696; -.
DR EMDB; EMD-22698; -.
DR EMDB; EMD-31029; -.
DR EMDB; EMD-31030; -.
DR EMDB; EMD-4395; -.
DR EMDB; EMD-4396; -.
DR EMDB; EMD-4579; -.
DR SMR; P02309; -.
DR BioGRID; 32710; 796.
DR BioGRID; 35797; 525.
DR ComplexPortal; CPX-1101; RNA polymerase I upstream activating factor complex.
DR ComplexPortal; CPX-1610; Nucleosome, variant HTA2-HTB2.
DR ComplexPortal; CPX-1611; Nucleosome, variant HTA2-HTB1.
DR ComplexPortal; CPX-1612; Nucleosome, variant HTA1-HTB1.
DR ComplexPortal; CPX-1613; Nucleosome, variant HTZ1-HTB1.
DR ComplexPortal; CPX-1614; Nucleosome, variant HTZ1-HTB2.
DR ComplexPortal; CPX-2566; Nucleosome, variant HTA1-HTB2.
DR DIP; DIP-418N; -.
DR IntAct; P02309; 313.
DR MINT; P02309; -.
DR STRING; 4932.YBR009C; -.
DR iPTMnet; P02309; -.
DR MaxQB; P02309; -.
DR PaxDb; 4932-YBR009C; -.
DR PeptideAtlas; P02309; -.
DR ABCD; P02309; 1 sequenced antibody.
DR EnsemblFungi; YBR009C_mRNA; YBR009C; YBR009C.
DR EnsemblFungi; YNL030W_mRNA; YNL030W; YNL030W.
DR GeneID; 852294; -.
DR GeneID; 855701; -.
DR KEGG; sce:YBR009C; -.
DR KEGG; sce:YNL030W; -.
DR AGR; SGD:S000000213; -.
DR AGR; SGD:S000004975; -.
DR SGD; S000000213; HHF1.
DR SGD; S000004975; HHF2.
DR VEuPathDB; FungiDB:YBR009C; -.
DR VEuPathDB; FungiDB:YNL030W; -.
DR eggNOG; KOG3467; Eukaryota.
DR GeneTree; ENSGT01060000248528; -.
DR HOGENOM; CLU_109117_2_3_1; -.
DR InParanoid; P02309; -.
DR OMA; QKEHING; -.
DR OrthoDB; 2782612at2759; -.
DR BioCyc; YEAST:G3O-28996-MONOMER; -.
DR Reactome; R-SCE-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-SCE-3214842; HDMs demethylate histones.
DR Reactome; R-SCE-3214847; HATs acetylate histones.
DR Reactome; R-SCE-3214858; RMTs methylate histone arginines.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR BioGRID-ORCS; 852294; 5 hits in 10 CRISPR screens.
DR BioGRID-ORCS; 855701; 0 hits in 10 CRISPR screens.
DR ChiTaRS; HHF2; yeast.
DR EvolutionaryTrace; P02309; -.
DR PRO; PR:P02309; -.
DR Proteomes; UP000002311; Chromosome II.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P02309; Protein.
DR GO; GO:0000786; C:nucleosome; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR GO; GO:0031298; C:replication fork protection complex; IDA:SGD.
DR GO; GO:0000500; C:RNA polymerase I upstream activating factor complex; IPI:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; TAS:SGD.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:ComplexPortal.
DR CDD; cd00076; H4; 1.
DR DisProt; DP02260; -.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR035425; CENP-T/H4_C.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR001951; Histone_H4.
DR InterPro; IPR019809; Histone_H4_CS.
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 SUPFAM; SSF47113; Histone-fold; 1.
DR PROSITE; PS00047; HISTONE_H4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; Direct protein sequencing;
KW DNA-binding; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..103
FT /note="Histone H4"
FT /id="PRO_0000158377"
FT DNA_BIND 17..21
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="N6-acetyl-N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 6
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:19113941, ECO:0000269|Ref.24"
FT MOD_RES 6
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22343720"
FT MOD_RES 9
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:19113941, ECO:0000269|Ref.24"
FT MOD_RES 9
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:19113941"
FT MOD_RES 9
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22343720"
FT MOD_RES 13
FT /note="N6-acetyl-N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62805"
FT MOD_RES 13
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:19113941, ECO:0000269|Ref.24"
FT MOD_RES 13
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105113"
FT MOD_RES 13
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22343720"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:11080160,
FT ECO:0000269|PubMed:15150415, ECO:0000269|PubMed:17289592,
FT ECO:0000269|PubMed:19113941"
FT MOD_RES 32
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 56
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:19113941"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 78
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 80
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:16768447"
FT MOD_RES 92
FT /note="N6-glutaryllysine"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MUTAGEN 92
FT /note="K->E: Mimics glutarylation; delays in cell
FT proliferation; increased sensitivity to DNA damaging
FT agents."
FT /evidence="ECO:0000269|PubMed:31542297"
FT MUTAGEN 92
FT /note="K->Q: Mimics acetylation; does not show increased
FT sensitivity to DNA damaging agents."
FT /evidence="ECO:0000269|PubMed:31542297"
FT MUTAGEN 92
FT /note="K->R: Mimics unmodified residue; does not show
FT increased sensitivity to DNA damaging agents."
FT /evidence="ECO:0000269|PubMed:31542297"
FT CONFLICT 46
FT /note="R -> K (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:6RXQ"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:7Z0O"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:4PSX"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:4PSX"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:7K78"
FT HELIX 52..76
FT /evidence="ECO:0007829|PDB:7Z0O"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:7Z0O"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:7Z0O"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:7Z0O"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:4JJN"
SQ SEQUENCE 103 AA; 11368 MW; 69B7D1F89E62DE41 CRC64;
MSGRGKGGKG LGKGGAKRHR KILRDNIQGI TKPAIRRLAR RGGVKRISGL IYEEVRAVLK
SFLESVIRDS VTYTEHAKRK TVTSLDVVYA LKRQGRTLYG FGG
//
