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P0C0S5 (H2AZ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H2A.Z

Short name=H2A/z
Gene names
Name:H2AFZ
Synonyms:H2AZ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length128 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Variant histone H2A which replaces conventional H2A in a subset of 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. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division. Ref.9

Subunit structure

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 H2AFZ forms a heterodimer with H2B. H2AFZ interacts with INCENP By similarity. Interacts (via M6 cassette) with ANP32E; leading to removal of H2A.Z/H2AFZ from the nucleosome. Ref.15

Subcellular location

Nucleus. Chromosome.

Post-translational modification

Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression.

Acetylated on Lys-5, Lys-8 and Lys-12 during interphase. Acetylation disappears at mitosis By similarity. Ref.11

Not phosphorylated By similarity.

Sequence similarities

Belongs to the histone H2A family.

Mass spectrometry

Molecular mass is 13413.4 Da from positions 2 - 128. Determined by ESI. Monoisotopic, not modified. Ref.10

Ontologies

Keywords
   Cellular componentChromosome
Nucleosome core
Nucleus
   LigandDNA-binding
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to estradiol stimulus

Inferred from mutant phenotype PubMed 23637611. Source: UniProt

nucleosome assembly

Inferred from electronic annotation. Source: InterPro

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19834540PubMed 23637611. Source: UniProt

   Cellular_componentnuclear euchromatin

Inferred from direct assay PubMed 19834540PubMed 23637611. Source: UniProt

nuclear heterochromatin

Inferred from direct assay PubMed 19834540. Source: UniProt

nucleosome

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from direct assay Ref.10PubMed 21630459PubMed 22720776. Source: UniProt

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 19834540. Source: UniProt

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from direct assay PubMed 19633671PubMed 23637611. Source: UniProt

RNA polymerase II distal enhancer sequence-specific DNA binding

Inferred from direct assay PubMed 19633671PubMed 23637611. Source: UniProt

chromatin DNA binding

Inferred from direct assay PubMed 19834540PubMed 23637611. Source: UniProt

nucleosomal DNA binding

Inferred from direct assay PubMed 19633671. Source: UniProt

protein binding

Inferred from physical interaction PubMed 20473270. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ZNHIT1O432573EBI-1199859,EBI-347522

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 128127Histone H2A.Z
PRO_0000055297

Regions

Region2 – 1716Required for interaction with INCENP By similarity
Region89 – 10012M6 cassette
Region93 – 10311Required for interaction with INCENP By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.13
Modified residue51N6-acetyllysine Ref.11 Ref.12
Modified residue81N6-acetyllysine Ref.11 Ref.12 Ref.13
Modified residue121N6-acetyllysine Ref.11 Ref.13
Modified residue141N6-acetyllysine Ref.13
Cross-link122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8

Secondary structure

................. 128
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C0S5 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E024E53818230371

FASTA12813,553
        10         20         30         40         50         60 
MAGGKAGKDS GKAKTKAVSR SQRAGLQFPV GRIHRHLKSR TTSHGRVGAT AAVYSAAILE 

        70         80         90        100        110        120 
YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG 


KKGQQKTV 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of cDNAs for mammalian H2A.Z, an evolutionarily diverged but highly conserved basal histone H2A isoprotein species."
Hatch C.L., Bonner W.M.
Nucleic Acids Res. 16:1113-1124(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The human histone H2A.Z gene. Sequence and regulation."
Hatch C.L., Bonner W.M.
J. Biol. Chem. 265:15211-15218(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Tongue.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Skeletal muscle and Uterus.
[8]"Histone ubiquitination: a tagging tail unfolds?"
Jason L.J.M., Moore S.C., Lewis J.D., Lindsey G., Ausio J.
Bioessays 24:166-174(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-122.
[9]"Transcription-induced chromatin remodeling at the c-myc gene involves the local exchange of histone H2A.Z."
Farris S.D., Rubio E.D., Moon J.J., Gombert W.M., Nelson B.H., Krumm A.
J. Biol. Chem. 280:25298-25303(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Precise characterization of human histones in the H2A gene family by top down mass spectrometry."
Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.
J. Proteome Res. 5:248-253(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
[11]"Quantitative proteomic analysis of post-translational modifications of human histones."
Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M., Finn P., Grauslund M., Hansen A.M., Jensen O.N.
Mol. Cell. Proteomics 5:1314-1325(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-5; LYS-8 AND LYS-12, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"Characterization of histones H2A and H2B variants and their post-translational modifications by mass spectrometry."
Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.
Mol. Cell. Proteomics 5:541-552(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5 AND LYS-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-8; LYS-12 AND LYS-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[14]"Crystal structure of a nucleosome core particle containing the variant histone H2A.Z."
Suto R.K., Clarkson M.J., Tremethick D.J., Luger K.
Nat. Struct. Biol. 7:1121-1124(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH THE NUCLEOSOME.
[15]"ANP32E is a histone chaperone that removes H2A.Z from chromatin."
Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M., Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C., Hamiche A.
Nature 505:648-653(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 19-128 IN COMPLEX WITH ANP32E AND HISTONE H2B, INTERACTION WITH ANP32E.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52317 mRNA. Translation: CAA36553.1.
M37583 mRNA. Translation: AAA35984.1.
L10138 Genomic DNA. Translation: AAC61625.1.
CR457415 mRNA. Translation: CAG33696.1.
AK315413 mRNA. Translation: BAG37803.1.
AC097460 Genomic DNA. Translation: AAY41013.1.
CH471057 Genomic DNA. Translation: EAX06118.1.
BC018002 mRNA. Translation: AAH18002.1.
BC020936 mRNA. Translation: AAH20936.1.
BC103743 mRNA. Translation: AAI03744.1.
CCDSCCDS3654.1.
PIRA35881.
RefSeqNP_002097.1. NM_002106.3.
UniGeneHs.119192.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F66X-ray2.60C/G1-128[»]
3WA9X-ray3.07C/G1-128[»]
4CAYX-ray1.48A19-128[»]
4NFTX-ray2.61A/B/C/D16-114[»]
ProteinModelPortalP0C0S5.
SMRP0C0S5. Positions 17-123.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109269. 57 interactions.
DIPDIP-38593N.
IntActP0C0S5. 4 interactions.
MINTMINT-1605675.
STRING9606.ENSP00000296417.

PTM databases

PhosphoSiteP0C0S5.

Polymorphism databases

DMDM83288408.

Proteomic databases

MaxQBP0C0S5.
PaxDbP0C0S5.
PRIDEP0C0S5.

Protocols and materials databases

DNASU3015.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296417; ENSP00000296417; ENSG00000164032.
GeneID3015.
KEGGhsa:3015.
UCSCuc003hvo.1. human.

Organism-specific databases

CTD3015.
GeneCardsGC04M100869.
HGNCHGNC:4741. H2AFZ.
HPACAB022549.
HPA045242.
MIM142763. gene.
neXtProtNX_P0C0S5.
PharmGKBPA29119.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5262.
HOGENOMHOG000234652.
HOVERGENHBG009342.
InParanoidP0C0S5.
KOK11251.
OMADPQRKGN.
OrthoDBEOG7M0NTR.
PhylomeDBP0C0S5.
TreeFamTF354232.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_21300. Mitotic M-M/G1 phases.
REACT_71. Gene Expression.

Gene expression databases

BgeeP0C0S5.
CleanExHS_H2AFZ.
GenevestigatorP0C0S5.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00620. HISTONEH2A.
SMARTSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00046. HISTONE_H2A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSH2AFZ. human.
EvolutionaryTraceP0C0S5.
GeneWikiH2AFZ.
GenomeRNAi3015.
NextBio11952.
PMAP-CutDBP0C0S5.
PROP0C0S5.
SOURCESearch...

Entry information

Entry nameH2AZ_HUMAN
AccessionPrimary (citable) accession number: P0C0S5
Secondary accession number(s): B2RD56, P17317, Q6I9U0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM