H4_SCHPO
ID H4_SCHPO Reviewed; 103 AA.
AC P09322;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Histone H4;
GN Name=hhf1; Synonyms=h4.1; ORFNames=SPAC1834.03c;
GN and
GN Name=hhf2; Synonyms=h4.2; ORFNames=pi061, SPBC8D2.03c;
GN and
GN Name=hhf3; Synonyms=h4.3; ORFNames=SPBC1105.12;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HHF1; HHF2 AND HHF3).
RX PubMed=4092687; DOI=10.1002/j.1460-2075.1985.tb04113.x;
RA Matsumoto S., Yanagida M.;
RT "Histone gene organization of fission yeast: a common upstream sequence.";
RL EMBO J. 4:3531-3538(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHF2).
RC STRAIN=972 / ATCC 24843;
RX PubMed=10620777;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT yeast chromosome II: sequence analysis and characterization of the genomic
RT DNA and cDNAs encoded on the segment.";
RL Yeast 16:71-80(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HHF1; HHF2 AND HHF3).
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [5]
RP HYDROXYBUTYRYLATION AT LYS-9.
RX PubMed=29192674; DOI=10.1038/cr.2017.149;
RA Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J.,
RA Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.;
RT "Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation
RT pathway.";
RL Cell Res. 28:111-125(2018).
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
CC DNA.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- PTM: Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by
CC promoting dissociation of the H2A-H2B dimers from nucleosomes.
CC {ECO:0000250|UniProtKB:P02309}.
CC -!- SIMILARITY: Belongs to the histone H4 family. {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; X05222; CAA28850.1; -; Genomic_DNA.
DR EMBL; X05223; CAA28853.1; -; Genomic_DNA.
DR EMBL; X05224; CAA28855.1; -; Genomic_DNA.
DR EMBL; AB004538; BAA21442.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB75771.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA17818.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB50975.1; -; Genomic_DNA.
DR PIR; D27399; HSZP4.
DR RefSeq; NP_594682.1; NM_001020111.2.
DR RefSeq; NP_595566.1; NM_001021461.2.
DR RefSeq; NP_596468.1; NM_001022387.2.
DR PDB; 6S1R; X-ray; 1.80 A; B=14-44.
DR PDBsum; 6S1R; -.
DR AlphaFoldDB; P09322; -.
DR BMRB; P09322; -.
DR SMR; P09322; -.
DR BioGRID; 276535; 14.
DR BioGRID; 277714; 74.
DR BioGRID; 278924; 63.
DR STRING; 4896.SPAC1834.03c.1; -.
DR iPTMnet; P09322; -.
DR MaxQB; P09322; -.
DR PaxDb; P09322; -.
DR PRIDE; P09322; -.
DR EnsemblFungi; SPAC1834.03c.1; SPAC1834.03c.1:pep; SPAC1834.03c.
DR EnsemblFungi; SPBC1105.12.1; SPBC1105.12.1:pep; SPBC1105.12.
DR EnsemblFungi; SPBC8D2.03c.1; SPBC8D2.03c.1:pep; SPBC8D2.03c.
DR GeneID; 2539991; -.
DR GeneID; 2541200; -.
DR GeneID; 2542463; -.
DR KEGG; spo:SPAC1834.03c; -.
DR KEGG; spo:SPBC1105.12; -.
DR KEGG; spo:SPBC8D2.03c; -.
DR PomBase; SPAC1834.03c; hhf1.
DR PomBase; SPBC8D2.03c; hhf2.
DR PomBase; SPBC1105.12; hhf3.
DR VEuPathDB; FungiDB:SPAC1834.03c; -.
DR VEuPathDB; FungiDB:SPBC1105.12; -.
DR VEuPathDB; FungiDB:SPBC8D2.03c; -.
DR eggNOG; KOG3467; Eukaryota.
DR HOGENOM; CLU_109117_2_3_1; -.
DR InParanoid; P09322; -.
DR OMA; QKEHING; -.
DR PhylomeDB; P09322; -.
DR Reactome; R-SPO-212300; PRC2 methylates histones and DNA.
DR Reactome; R-SPO-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-SPO-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-SPO-3214815; HDACs deacetylate histones.
DR Reactome; R-SPO-3214841; PKMTs methylate histone lysines.
DR Reactome; R-SPO-3214842; HDMs demethylate histones.
DR Reactome; R-SPO-3214847; HATs acetylate histones.
DR Reactome; R-SPO-3214858; RMTs methylate histone arginines.
DR Reactome; R-SPO-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-SPO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SPO-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-SPO-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SPO-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:P09322; -.
DR Proteomes; UP000002485; Chromosome I.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000786; C:nucleosome; ISM:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003677; F:DNA binding; ISM:PomBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR CDD; cd00076; H4; 1.
DR Gene3D; 1.10.20.10; -; 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 Pfam; PF15511; CENP-T_C; 1.
DR PRINTS; PR00623; HISTONEH4.
DR SMART; SM00417; H4; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00047; HISTONE_H4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; DNA-binding; Hydroxylation; Nucleosome core;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..103
FT /note="Histone H4"
FT /id="PRO_0000158357"
FT DNA_BIND 17..21
FT MOD_RES 9
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:29192674"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 92
FT /note="N6-glutaryllysine"
FT /evidence="ECO:0000250|UniProtKB:P02309"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:6S1R"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:6S1R"
SQ SEQUENCE 103 AA; 11423 MW; 6D9C9F96ABEB0D98 CRC64;
MSGRGKGGKG LGKGGAKRHR KILRDNIQGI TKPAIRRLAR RGGVKRISAL VYEETRAVLK
LFLENVIRDA VTYTEHAKRK TVTSLDVVYS LKRQGRTIYG FGG
