H2AZ_SCHPO
ID H2AZ_SCHPO Reviewed; 139 AA.
AC P48003;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Histone H2A.Z;
GN Name=pht1; ORFNames=pi001, SPBC11B10.10c;
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].
RX PubMed=7808414; DOI=10.1007/bf00282226;
RA Carr A.M., Dorrington S.M., Hindley J., Phear G.A., Aves S.J., Nurse P.;
RT "Analysis of a histone H2A variant from fission yeast: evidence for a role
RT in chromosome stability.";
RL Mol. Gen. Genet. 245:628-635(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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].
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17947424; DOI=10.1534/genetics.107.078691;
RA Ahmed S., Dul B., Qiu X., Walworth N.C.;
RT "Msc1 acts through histone H2A.Z to promote chromosome stability in
RT Schizosaccharomyces pombe.";
RL Genetics 177:1487-1497(2007).
RN [7]
RP IDENTIFICATION IN THE SWR1 AND INO80 COMPLEXES, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=19040720; DOI=10.1186/gb-2008-9-11-r167;
RA Shevchenko A., Roguev A., Schaft D., Buchanan L., Habermann B., Sakalar C.,
RA Thomas H., Krogan N.J., Shevchenko A., Stewart A.F.;
RT "Chromatin Central: towards the comparative proteome by accurate mapping of
RT the yeast proteomic environment.";
RL Genome Biol. 9:R167.1-R167.22(2008).
RN [8]
RP ACETYLATION, AND FUNCTION.
RX PubMed=19915592; DOI=10.1038/nsmb.1688;
RA Kim H.S., Vanoosthuyse V., Fillingham J., Roguev A., Watt S., Kislinger T.,
RA Treyer A., Carpenter L.R., Bennett C.S., Emili A., Greenblatt J.F.,
RA Hardwick K.G., Krogan N.J., Bahler J., Keogh M.C.;
RT "An acetylated form of histone H2A.Z regulates chromosome architecture in
RT Schizosaccharomyces pombe.";
RL Nat. Struct. Mol. Biol. 16:1286-1293(2009).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19910462; DOI=10.1074/jbc.m109.058487;
RA Hou H., Wang Y., Kallgren S.P., Thompson J., Yates J.R. III, Jia S.;
RT "Histone variant H2A.Z regulates centromere silencing and chromosome
RT segregation in fission yeast.";
RL J. Biol. Chem. 285:1909-1918(2010).
CC -!- FUNCTION: Variant histone H2A which can replace H2A in some
CC nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting
CC DNA accessibility to the cellular machineries which require DNA as a
CC template. Histones thereby play a central role in transcription
CC regulation, DNA repair, DNA replication and chromosomal stability. DNA
CC accessibility is regulated via a complex set of post-translational
CC modifications of histones, also called histone code, and nucleosome
CC remodeling. Important for chromosomal structure and function, possibly
CC including a role in controlling the fidelity of chromosomal segregation
CC during mitosis. Plays an important role in maintaining a silenced
CC chromatin state at centromeres and in the architecture of anaphase
CC chromosomes. {ECO:0000269|PubMed:17947424, ECO:0000269|PubMed:19910462,
CC ECO:0000269|PubMed:19915592}.
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. H2A or its variant H2A.Z forms a heterodimer with H2B. Component
CC of the SWR1 and INO80 chromatin-remodeling complexes.
CC {ECO:0000269|PubMed:19040720}.
CC -!- INTERACTION:
CC P48003; Q9Y7R3: cnd2; NbExp=2; IntAct=EBI-15929575, EBI-1149594;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Chromosome
CC {ECO:0000269|PubMed:17947424, ECO:0000269|PubMed:19910462}.
CC -!- PTM: Acetylated at the N-terminus. N-terminal acetylation is essential
CC for function. {ECO:0000269|PubMed:19915592}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB32938.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA21378.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; S74633; AAB32938.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB004534; BAA21378.1; ALT_INIT; Genomic_DNA.
DR EMBL; CU329671; CAC37514.3; -; Genomic_DNA.
DR PIR; S52560; S52560.
DR RefSeq; NP_595630.3; NM_001021524.3.
DR AlphaFoldDB; P48003; -.
DR SMR; P48003; -.
DR BioGRID; 276223; 234.
DR DIP; DIP-59185N; -.
DR IntAct; P48003; 4.
DR STRING; 4896.SPBC11B10.10c.1; -.
DR MaxQB; P48003; -.
DR PaxDb; P48003; -.
DR PRIDE; P48003; -.
DR EnsemblFungi; SPBC11B10.10c.1; SPBC11B10.10c.1:pep; SPBC11B10.10c.
DR GeneID; 2539668; -.
DR KEGG; spo:SPBC11B10.10c; -.
DR PomBase; SPBC11B10.10c; pht1.
DR VEuPathDB; FungiDB:SPBC11B10.10c; -.
DR eggNOG; KOG1757; Eukaryota.
DR HOGENOM; CLU_062828_2_2_1; -.
DR InParanoid; P48003; -.
DR OMA; FPCGRIK; -.
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-427359; SIRT1 negatively regulates rRNA expression.
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-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:P48003; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0031011; C:Ino80 complex; IDA:PomBase.
DR GO; GO:0000786; C:nucleosome; ISM:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000812; C:Swr1 complex; IDA: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:0034080; P:CENP-A containing chromatin assembly; IGI:PomBase.
DR GO; GO:0006325; P:chromatin organization; IMP:PomBase.
DR GO; GO:0006338; P:chromatin remodeling; IPI:PomBase.
DR GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:PomBase.
DR CDD; cd00074; H2A; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR032454; Histone_H2A_C.
DR InterPro; IPR032458; Histone_H2A_CS.
DR PANTHER; PTHR23430; PTHR23430; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00046; HISTONE_H2A; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromatin regulator; Chromosome; DNA-binding; Nucleosome core;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..139
FT /note="Histone H2A.Z"
FT /id="PRO_0000055337"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 139 AA; 15025 MW; 6D88B7ADABAD7E83 CRC64;
MSGGGKGKHV GGKGGSKIGE RGQMSHSARA GLQFPVGRVR RFLKAKTQNN MRVGAKSAVY
SAAVLEYLTA EVLELAGNAA KDLKVKRITP RHLQLAIRGD EELDTLIRAT IAGGGVLPHI
NKQLLIRTKE KYPEEEEII
