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Protein

Histone H2A.Z

Gene

H2AFZ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

GO - Biological processi

Keywordsi

Molecular functionDNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-1221632 Meiotic synapsis
R-HSA-171306 Packaging Of Telomere Ends
R-HSA-1912408 Pre-NOTCH Transcription and Translation
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-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-9018519 Estrogen-dependent gene expression
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

EuPathDBiHostDB:ENSG00000164032.11
HGNCiHGNC:4741 H2AFZ
MIMi142763 gene
neXtProtiNX_P0C0S5

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi83T → I: Decreases interaction with VPS72. Almost abolishes interaction with VPS72; when associated with N-93. Abolishes interaction with VPS72; when associated with N-93 and IG-101. 1 Publication1
Mutagenesisi93G → N: Decreases interaction with VPS72. Almost abolishes interaction with VPS72; when associated with I-83. Abolishes interaction with VPS72; when associated with I-83 and IG-101. 1 Publication1
Mutagenesisi98D → N: No effect on interaction with VPS72. 1 Publication1
Mutagenesisi101I → IG: Abolishes interaction with VPS72; when associated with I-83 and N-93. 1 Publication1

Organism-specific databases

DisGeNETi3015
OpenTargetsiENSG00000164032
PharmGKBiPA29119

Polymorphism and mutation databases

BioMutaiH2AFZ
DMDMi83288408

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCurated
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
ProteomicsDBi52295
TopDownProteomicsiP0C0S5

PTM databases

iPTMnetiP0C0S5
PhosphoSitePlusiP0C0S5
SwissPalmiP0C0S5

Miscellaneous databases

PMAP-CutDBiP0C0S5

Expressioni

Gene expression databases

BgeeiENSG00000164032 Expressed in 239 organ(s), highest expression level in myometrium
CleanExiHS_H2AFZ
GenevisibleiP0C0S5 HS

Organism-specific databases

HPAiCAB022549
HPA057236

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. Heterodimer HIST1H2BJ and H2AFZ interacts with VPS72 (via N-terminal domain) (PubMed:26974126). Interacts with PWWP2A (PubMed:28645917).By similarity4 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi109269, 93 interactors
CORUMiP0C0S5
DIPiDIP-38593N
IntActiP0C0S5, 10 interactors
MINTiP0C0S5
STRINGi9606.ENSP00000296417

Structurei

Secondary structure

1128
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0C0S5
SMRiP0C0S5
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0S5

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 17Required for interaction with INCENPBy similarityAdd BLAST17
Regioni89 – 100M6 cassetteAdd BLAST12
Regioni93 – 103Required for interaction with INCENPBy similarityAdd BLAST11
Regioni120 – 128Required for interaction with PWWP2A1 Publication9

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGiKOG1757 Eukaryota
COG5262 LUCA
GeneTreeiENSGT00900000140979
HOGENOMiHOG000234652
HOVERGENiHBG009342
InParanoidiP0C0S5
KOiK11251
OMAiDKDKGKM
OrthoDBiEOG091G0XGD
PhylomeDBiP0C0S5
TreeFamiTF354232

Family and domain databases

CDDicd00074 H2A, 1 hit
Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR009072 Histone-fold
IPR002119 Histone_H2A
IPR007125 Histone_H2A/H2B/H3
IPR032454 Histone_H2A_C
IPR032458 Histone_H2A_CS
PfamiView protein in Pfam
PF00125 Histone, 1 hit
PF16211 Histone_H2A_C, 1 hit
PRINTSiPR00620 HISTONEH2A
SMARTiView protein in SMART
SM00414 H2A, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00046 HISTONE_H2A, 1 hit

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

Similar proteinsi

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[»]
5Z30X-ray2.45C/G1-128[»]
ProteinModelPortaliP0C0S5
SMRiP0C0S5
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109269, 93 interactors
CORUMiP0C0S5
DIPiDIP-38593N
IntActiP0C0S5, 10 interactors
MINTiP0C0S5
STRINGi9606.ENSP00000296417

PTM databases

iPTMnetiP0C0S5
PhosphoSitePlusiP0C0S5
SwissPalmiP0C0S5

Polymorphism and mutation databases

BioMutaiH2AFZ
DMDMi83288408

Proteomic databases

EPDiP0C0S5
MaxQBiP0C0S5
PaxDbiP0C0S5
PeptideAtlasiP0C0S5
PRIDEiP0C0S5
ProteomicsDBi52295
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
EuPathDBiHostDB:ENSG00000164032.11
GeneCardsiH2AFZ
HGNCiHGNC:4741 H2AFZ
HPAiCAB022549
HPA057236
MIMi142763 gene
neXtProtiNX_P0C0S5
OpenTargetsiENSG00000164032
PharmGKBiPA29119
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1757 Eukaryota
COG5262 LUCA
GeneTreeiENSGT00900000140979
HOGENOMiHOG000234652
HOVERGENiHBG009342
InParanoidiP0C0S5
KOiK11251
OMAiDKDKGKM
OrthoDBiEOG091G0XGD
PhylomeDBiP0C0S5
TreeFamiTF354232

Enzyme and pathway databases

ReactomeiR-HSA-1221632 Meiotic synapsis
R-HSA-171306 Packaging Of Telomere Ends
R-HSA-1912408 Pre-NOTCH Transcription and Translation
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-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-9018519 Estrogen-dependent gene expression
R-HSA-912446 Meiotic recombination
R-HSA-977225 Amyloid fiber formation
SIGNORiP0C0S5

Miscellaneous databases

ChiTaRSiH2AFZ human
EvolutionaryTraceiP0C0S5
GeneWikiiH2AFZ
GenomeRNAii3015
PMAP-CutDBiP0C0S5
PROiPR:P0C0S5
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000164032 Expressed in 239 organ(s), highest expression level in myometrium
CleanExiHS_H2AFZ
GenevisibleiP0C0S5 HS

Family and domain databases

CDDicd00074 H2A, 1 hit
Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR009072 Histone-fold
IPR002119 Histone_H2A
IPR007125 Histone_H2A/H2B/H3
IPR032454 Histone_H2A_C
IPR032458 Histone_H2A_CS
PfamiView protein in Pfam
PF00125 Histone, 1 hit
PF16211 Histone_H2A_C, 1 hit
PRINTSiPR00620 HISTONEH2A
SMARTiView protein in SMART
SM00414 H2A, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00046 HISTONE_H2A, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiH2AZ_HUMAN
AccessioniPrimary (citable) accession number: P0C0S5
Secondary accession number(s): B2RD56, P17317, Q6I9U0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 137 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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