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Protein

Histone H2A.Z

Gene

pht1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Variant histone H2A which can replace H2A in some nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Important for chromosomal structure and function, possibly including a role in controlling the fidelity of chromosomal segregation during mitosis. Plays an important role in maintaining a silenced chromatin state at centromeres and in the architecture of anaphase chromosomes.3 Publications

GO - Molecular functioni

GO - Biological processi

  • chromatin modification Source: UniProtKB-KW
  • chromatin organization Source: PomBase
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A.Z
Gene namesi
Name:pht1
ORF Names:pi001, SPBC11B10.10c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC11B10.10c.
PomBaseiSPBC11B10.10c. pht1.

Subcellular locationi

GO - Cellular componenti

  • Ino80 complex Source: PomBase
  • mitochondrion Source: PomBase
  • nucleosome Source: UniProtKB-KW
  • nucleus Source: PomBase
  • Swr1 complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 139139Histone H2A.ZPRO_0000055337Add
BLAST

Post-translational modificationi

Acetylated at the N-terminus. N-terminal acetylation is essential for function.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP48003.
PRIDEiP48003.

Interactioni

Subunit structurei

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. H2A or its variant H2A.Z forms a heterodimer with H2B. Component of the SWR1 and INO80 chromatin-remodeling complexes.1 Publication

Protein-protein interaction databases

BioGridi276223. 227 interactions.
DIPiDIP-59185N.
MINTiMINT-4690421.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

HOGENOMiHOG000234652.
InParanoidiP48003.
KOiK11251.
OMAiIHRYLMN.
OrthoDBiEOG7GN30N.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR002119. Histone_H2A.
IPR007125. Histone_H2A/H2B/H3.
IPR032454. Histone_H2A_C.
IPR032458. Histone_H2A_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
PF16211. Histone_H2A_C. 1 hit.
[Graphical view]
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00046. HISTONE_H2A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48003-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGGGKGKHV GGKGGSKIGE RGQMSHSARA GLQFPVGRVR RFLKAKTQNN
60 70 80 90 100
MRVGAKSAVY SAAVLEYLTA EVLELAGNAA KDLKVKRITP RHLQLAIRGD
110 120 130
EELDTLIRAT IAGGGVLPHI NKQLLIRTKE KYPEEEEII
Length:139
Mass (Da):15,025
Last modified:July 11, 2012 - v3
Checksum:i6D88B7ADABAD7E83
GO

Sequence cautioni

The sequence AAB32938.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA21378.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74633 Genomic DNA. Translation: AAB32938.1. Different initiation.
AB004534 Genomic DNA. Translation: BAA21378.1. Different initiation.
CU329671 Genomic DNA. Translation: CAC37514.3.
PIRiS52560.
RefSeqiNP_595630.3. NM_001021524.3.

Genome annotation databases

EnsemblFungiiSPBC11B10.10c.1; SPBC11B10.10c.1:pep; SPBC11B10.10c.
GeneIDi2539668.
KEGGispo:SPBC11B10.10c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74633 Genomic DNA. Translation: AAB32938.1. Different initiation.
AB004534 Genomic DNA. Translation: BAA21378.1. Different initiation.
CU329671 Genomic DNA. Translation: CAC37514.3.
PIRiS52560.
RefSeqiNP_595630.3. NM_001021524.3.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276223. 227 interactions.
DIPiDIP-59185N.
MINTiMINT-4690421.

Proteomic databases

MaxQBiP48003.
PRIDEiP48003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC11B10.10c.1; SPBC11B10.10c.1:pep; SPBC11B10.10c.
GeneIDi2539668.
KEGGispo:SPBC11B10.10c.

Organism-specific databases

EuPathDBiFungiDB:SPBC11B10.10c.
PomBaseiSPBC11B10.10c. pht1.

Phylogenomic databases

HOGENOMiHOG000234652.
InParanoidiP48003.
KOiK11251.
OMAiIHRYLMN.
OrthoDBiEOG7GN30N.

Miscellaneous databases

PROiP48003.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR002119. Histone_H2A.
IPR007125. Histone_H2A/H2B/H3.
IPR032454. Histone_H2A_C.
IPR032458. Histone_H2A_CS.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
PF16211. Histone_H2A_C. 1 hit.
[Graphical view]
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00046. HISTONE_H2A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of a histone H2A variant from fission yeast: evidence for a role in chromosome stability."
    Carr A.M., Dorrington S.M., Hindley J., Phear G.A., Aves S.J., Nurse P.
    Mol. Gen. Genet. 245:628-635(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A 38 kb segment containing the cdc2 gene from the left arm of fission yeast chromosome II: sequence analysis and characterization of the genomic DNA and cDNAs encoded on the segment."
    Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K., Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y., Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.
    Yeast 16:71-80(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  4. "Comparative functional genomics of the fission yeasts."
    Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N., Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.
    , Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W., Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.
    Science 332:930-936(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVISION OF GENE MODEL.
  5. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. "Msc1 acts through histone H2A.Z to promote chromosome stability in Schizosaccharomyces pombe."
    Ahmed S., Dul B., Qiu X., Walworth N.C.
    Genetics 177:1487-1497(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Chromatin Central: towards the comparative proteome by accurate mapping of the yeast proteomic environment."
    Shevchenko A., Roguev A., Schaft D., Buchanan L., Habermann B., Sakalar C., Thomas H., Krogan N.J., Shevchenko A., Stewart A.F.
    Genome Biol. 9:R167.1-R167.22(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SWR1 AND INO80 COMPLEXES, IDENTIFICATION BY MASS SPECTROMETRY.
  8. Cited for: ACETYLATION, FUNCTION.
  9. "Histone variant H2A.Z regulates centromere silencing and chromosome segregation in fission yeast."
    Hou H., Wang Y., Kallgren S.P., Thompson J., Yates J.R. III, Jia S.
    J. Biol. Chem. 285:1909-1918(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiH2AZ_SCHPO
AccessioniPrimary (citable) accession number: P48003
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 11, 2012
Last modified: June 8, 2016
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.