Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone H2A.Z

Gene

H2AFZ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • chromatin DNA binding Source: UniProtKB
  • nucleosomal DNA binding Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II core promoter sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • cellular response to estradiol stimulus Source: UniProtKB
  • chromatin silencing Source: GO_Central
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000164032-MONOMER.
ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-171306. Packaging Of Telomere Ends.
R-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-427359. SIRT1 negatively regulates rRNA Expression.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5334118. DNA methylation.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
R-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-HSA-73728. RNA Polymerase I Promoter Opening.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-912446. Meiotic recombination.
R-HSA-977225. Amyloid fiber formation.
SIGNORiP0C0S5.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A.Z
Short name:
H2A/z
Gene namesi
Name:H2AFZ
Synonyms:H2AZ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:4741. H2AFZ.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • nuclear euchromatin Source: UniProtKB
  • nuclear heterochromatin Source: UniProtKB
  • nucleosome Source: UniProtKB-KW
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi3015.
OpenTargetsiENSG00000164032.
PharmGKBiPA29119.

Polymorphism and mutation databases

BioMutaiH2AFZ.
DMDMi83288408.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000552972 – 128Histone H2A.ZAdd BLAST127

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5N6-acetyllysine; alternateCombined sources1 Publication1
Modified residuei5N6-methyllysine; alternate1 Publication1
Modified residuei8N6-acetyllysine; alternateCombined sources1 Publication1
Modified residuei8N6-methyllysine; alternate1 Publication1
Modified residuei12N6-acetyllysineCombined sources1 Publication1
Modified residuei14N6-acetyllysineCombined sources1
Cross-linki122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression.1 Publication
Acetylated on Lys-5, Lys-8 and Lys-12 during interphase. Acetylation disappears at mitosis (By similarity).By similarity
Monomethylated on Lys-5 and Lys-8 by SETD6. SETD6 predominantly methylates Lys-8, lys-5 being a possible secondary site.1 Publication
Not phosphorylated.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Ubl conjugation

Proteomic databases

EPDiP0C0S5.
MaxQBiP0C0S5.
PaxDbiP0C0S5.
PeptideAtlasiP0C0S5.
PRIDEiP0C0S5.
TopDownProteomicsiP0C0S5.

PTM databases

iPTMnetiP0C0S5.
PhosphoSitePlusiP0C0S5.
SwissPalmiP0C0S5.

Miscellaneous databases

PMAP-CutDBP0C0S5.

Expressioni

Gene expression databases

BgeeiENSG00000164032.
CleanExiHS_H2AFZ.
GenevisibleiP0C0S5. HS.

Organism-specific databases

HPAiCAB022549.
HPA045242.

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 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.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ZNHIT1O432573EBI-1199859,EBI-347522

Protein-protein interaction databases

BioGridi109269. 61 interactors.
DIPiDIP-38593N.
IntActiP0C0S5. 4 interactors.
MINTiMINT-1605675.
STRINGi9606.ENSP00000296417.

Structurei

Secondary structure

1128
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi20 – 23Combined sources4
Helixi30 – 39Combined sources10
Beta strandi43 – 45Combined sources3
Helixi49 – 76Combined sources28
Beta strandi80 – 82Combined sources3
Helixi84 – 92Combined sources9
Helixi95 – 106Combined sources12
Helixi116 – 118Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F66X-ray2.60C/G1-128[»]
3WA9X-ray3.07C/G1-128[»]
4CAYX-ray1.48A19-128[»]
4NFTX-ray2.61A/B/C/D16-114[»]
5B31X-ray2.20G1-128[»]
5B32X-ray2.35G1-128[»]
5B33X-ray2.92C/G1-128[»]
5CHLX-ray1.89B22-113[»]
5FUGX-ray2.70A/D/G/J19-128[»]
ProteinModelPortaliP0C0S5.
SMRiP0C0S5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0S5.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 17Required for interaction with INCENPBy similarityAdd BLAST16
Regioni89 – 100M6 cassetteAdd BLAST12
Regioni93 – 103Required for interaction with INCENPBy similarityAdd BLAST11

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGiKOG1757. Eukaryota.
COG5262. LUCA.
GeneTreeiENSGT00710000106735.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP0C0S5.
KOiK11251.
OMAiLRNKNAN.
OrthoDBiEOG091G0XGD.
PhylomeDBiP0C0S5.
TreeFamiTF354232.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0C0S5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGGKAGKDS GKAKTKAVSR SQRAGLQFPV GRIHRHLKSR TTSHGRVGAT
60 70 80 90 100
AAVYSAAILE YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL
110 120
IKATIAGGGV IPHIHKSLIG KKGQQKTV
Length:128
Mass (Da):13,553
Last modified:January 23, 2007 - v2
Checksum:iE024E53818230371
GO

Mass spectrometryi

Molecular mass is 13413.4 Da from positions 2 - 128. Determined by ESI. Monoisotopic, not modified.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3654.1.
PIRiA35881.
RefSeqiNP_002097.1. NM_002106.3.
UniGeneiHs.119192.

Genome annotation databases

EnsembliENST00000296417; ENSP00000296417; ENSG00000164032.
GeneIDi3015.
KEGGihsa:3015.
UCSCiuc003hvo.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3654.1.
PIRiA35881.
RefSeqiNP_002097.1. NM_002106.3.
UniGeneiHs.119192.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F66X-ray2.60C/G1-128[»]
3WA9X-ray3.07C/G1-128[»]
4CAYX-ray1.48A19-128[»]
4NFTX-ray2.61A/B/C/D16-114[»]
5B31X-ray2.20G1-128[»]
5B32X-ray2.35G1-128[»]
5B33X-ray2.92C/G1-128[»]
5CHLX-ray1.89B22-113[»]
5FUGX-ray2.70A/D/G/J19-128[»]
ProteinModelPortaliP0C0S5.
SMRiP0C0S5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109269. 61 interactors.
DIPiDIP-38593N.
IntActiP0C0S5. 4 interactors.
MINTiMINT-1605675.
STRINGi9606.ENSP00000296417.

PTM databases

iPTMnetiP0C0S5.
PhosphoSitePlusiP0C0S5.
SwissPalmiP0C0S5.

Polymorphism and mutation databases

BioMutaiH2AFZ.
DMDMi83288408.

Proteomic databases

EPDiP0C0S5.
MaxQBiP0C0S5.
PaxDbiP0C0S5.
PeptideAtlasiP0C0S5.
PRIDEiP0C0S5.
TopDownProteomicsiP0C0S5.

Protocols and materials databases

DNASUi3015.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296417; ENSP00000296417; ENSG00000164032.
GeneIDi3015.
KEGGihsa:3015.
UCSCiuc003hvo.2. human.

Organism-specific databases

CTDi3015.
DisGeNETi3015.
GeneCardsiH2AFZ.
HGNCiHGNC:4741. H2AFZ.
HPAiCAB022549.
HPA045242.
MIMi142763. gene.
neXtProtiNX_P0C0S5.
OpenTargetsiENSG00000164032.
PharmGKBiPA29119.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1757. Eukaryota.
COG5262. LUCA.
GeneTreeiENSGT00710000106735.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiP0C0S5.
KOiK11251.
OMAiLRNKNAN.
OrthoDBiEOG091G0XGD.
PhylomeDBiP0C0S5.
TreeFamiTF354232.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000164032-MONOMER.
ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-171306. Packaging Of Telomere Ends.
R-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-427359. SIRT1 negatively regulates rRNA Expression.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5334118. DNA methylation.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-5625886. Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
R-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-HSA-73728. RNA Polymerase I Promoter Opening.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-912446. Meiotic recombination.
R-HSA-977225. Amyloid fiber formation.
SIGNORiP0C0S5.

Miscellaneous databases

ChiTaRSiH2AFZ. human.
EvolutionaryTraceiP0C0S5.
GeneWikiiH2AFZ.
GenomeRNAii3015.
PMAP-CutDBP0C0S5.
PROiP0C0S5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000164032.
CleanExiHS_H2AFZ.
GenevisibleiP0C0S5. HS.

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...

Entry informationi

Entry nameiH2AZ_HUMAN
AccessioniPrimary (citable) accession number: P0C0S5
Secondary accession number(s): B2RD56, P17317, Q6I9U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.