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Protein

Histone H2A.V

Gene

H2AFV

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

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.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2A.V
Alternative name(s):
H2A.F/Z
Gene namesi
Name:H2AFV
Synonyms:H2AV
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:20664. H2AFV.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • nuclear chromatin Source: GO_Central
  • nucleosome Source: UniProtKB-KW
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi94239.
OpenTargetsiENSG00000105968.
PharmGKBiPA134895050.

Polymorphism and mutation databases

BioMutaiH2AFV.
DMDMi74749787.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002390681 – 128Histone H2A.VAdd BLAST128

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5N6-acetyllysineBy similarity1
Modified residuei8N6-acetyllysineBy similarity1
Modified residuei12N6-acetyllysineBy similarity1

Post-translational modificationi

Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression.By similarity
Acetylated on Lys-5, Lys-8 and Lys-12 during interphase. Acetylation disappears at mitosis (By similarity).By similarity

Keywords - PTMi

Acetylation, Ubl conjugation

Proteomic databases

EPDiQ71UI9.
MaxQBiQ71UI9.
PaxDbiQ71UI9.
PeptideAtlasiQ71UI9.
PRIDEiQ71UI9.
TopDownProteomicsiQ71UI9-1. [Q71UI9-1]
Q71UI9-3. [Q71UI9-3]
Q71UI9-4. [Q71UI9-4]

PTM databases

iPTMnetiQ71UI9.
PhosphoSitePlusiQ71UI9.
SwissPalmiQ71UI9.

Expressioni

Gene expression databases

BgeeiENSG00000105968.
CleanExiHS_H2AFV.
ExpressionAtlasiQ71UI9. baseline and differential.
GenevisibleiQ71UI9. HS.

Organism-specific databases

HPAiHPA045242.

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 H2AFV forms a heterodimer with H2B (By similarity).By similarity

Protein-protein interaction databases

BioGridi125150. 38 interactors.
IntActiQ71UI9. 10 interactors.
MINTiMINT-4828370.
STRINGi9606.ENSP00000308405.

Structurei

Secondary structure

1128
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi20 – 23Combined sources4
Helixi30 – 38Combined sources9
Helixi49 – 75Combined sources27
Turni76 – 78Combined sources3
Beta strandi80 – 82Combined sources3
Helixi84 – 93Combined sources10
Helixi95 – 100Combined sources6
Beta strandi103 – 105Combined sources3
Helixi116 – 118Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WAAX-ray3.20C/G1-128[»]
ProteinModelPortaliQ71UI9.
SMRiQ71UI9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGiKOG1757. Eukaryota.
COG5262. LUCA.
GeneTreeiENSGT00710000106735.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiQ71UI9.
KOiK11251.
OMAiIHRYLMN.
OrthoDBiEOG091G0XGD.
PhylomeDBiQ71UI9.
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]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q71UI9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGGKAGKDS GKAKAKAVSR SQRAGLQFPV GRIHRHLKTR TTSHGRVGAT
60 70 80 90 100
AAVYSAAILE YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL
110 120
IKATIAGGGV IPHIHKSLIG KKGQQKTA
Length:128
Mass (Da):13,509
Last modified:January 23, 2007 - v3
Checksum:i1F3C388F6854041C
GO
Isoform 2 (identifier: Q71UI9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     109-128: GVIPHIHKSLIGKKGQQKTA → EKRRCS

Note: No experimental confirmation available.
Show »
Length:114
Mass (Da):12,146
Checksum:i4CF80C91A39397B4
GO
Isoform 3 (identifier: Q71UI9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     28-65: Missing.

Note: No experimental confirmation available.
Show »
Length:90
Mass (Da):9,375
Checksum:i34DA01283B7A93F1
GO
Isoform 4 (identifier: Q71UI9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: MAGGKAGKDSGKAKAKAVSRSQRAGLQ → M

Note: No experimental confirmation available.
Show »
Length:102
Mass (Da):10,999
Checksum:i0E6071539B4139F9
GO
Isoform 5 (identifier: Q71UI9-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     67-128: Missing.

Note: No experimental confirmation available.
Show »
Length:66
Mass (Da):6,892
Checksum:i90DA3A9820A88CB0
GO

Sequence cautioni

The sequence BAD92238 differs from that shown. Reason: Erroneous initiation.Curated

Mass spectrometryi

Molecular mass is 13369.4 Da from positions 2 - 128. Determined by ESI. Monoisotopic, not modified.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_059312125Q → R.Corresponds to variant rs1802437dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0452321 – 27MAGGK…RAGLQ → M in isoform 4. 1 PublicationAdd BLAST27
Alternative sequenceiVSP_04463328 – 65Missing in isoform 3. 1 PublicationAdd BLAST38
Alternative sequenceiVSP_04678367 – 128Missing in isoform 5. CuratedAdd BLAST62
Alternative sequenceiVSP_042855109 – 128GVIPH…QQKTA → EKRRCS in isoform 2. 1 PublicationAdd BLAST20

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081192 mRNA. Translation: AAC31938.1.
AK023973 mRNA. Translation: BAG51243.1.
AB209001 mRNA. Translation: BAD92238.1. Different initiation.
AC004854 Genomic DNA. Translation: AAS00365.1.
CH471128 Genomic DNA. Translation: EAW61075.1.
CH471128 Genomic DNA. Translation: EAW61077.1.
BC000098 mRNA. Translation: AAH00098.1.
BC004274 mRNA. Translation: AAH04274.3.
BC014885 mRNA. Translation: AAH14885.1.
BC070169 mRNA. Translation: AAH70169.1.
BE742590 mRNA. No translation available.
BU543626 mRNA. No translation available.
CCDSiCCDS47581.1. [Q71UI9-5]
CCDS5495.1. [Q71UI9-2]
CCDS5496.1. [Q71UI9-1]
CCDS5497.1. [Q71UI9-4]
CCDS5498.1. [Q71UI9-3]
RefSeqiNP_036544.1. NM_012412.4. [Q71UI9-1]
NP_619541.1. NM_138635.3. [Q71UI9-2]
NP_958844.1. NM_201436.2. [Q71UI9-4]
NP_958924.1. NM_201516.2. [Q71UI9-5]
NP_958925.1. NM_201517.2. [Q71UI9-3]
UniGeneiHs.488189.

Genome annotation databases

EnsembliENST00000222690; ENSP00000222690; ENSG00000105968. [Q71UI9-2]
ENST00000308153; ENSP00000308405; ENSG00000105968. [Q71UI9-1]
ENST00000349299; ENSP00000342714; ENSG00000105968. [Q71UI9-3]
ENST00000350771; ENSP00000340708; ENSG00000105968. [Q71UI9-4]
ENST00000381124; ENSP00000370516; ENSG00000105968. [Q71UI9-5]
GeneIDi94239.
KEGGihsa:94239.
UCSCiuc003tlz.3. human. [Q71UI9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081192 mRNA. Translation: AAC31938.1.
AK023973 mRNA. Translation: BAG51243.1.
AB209001 mRNA. Translation: BAD92238.1. Different initiation.
AC004854 Genomic DNA. Translation: AAS00365.1.
CH471128 Genomic DNA. Translation: EAW61075.1.
CH471128 Genomic DNA. Translation: EAW61077.1.
BC000098 mRNA. Translation: AAH00098.1.
BC004274 mRNA. Translation: AAH04274.3.
BC014885 mRNA. Translation: AAH14885.1.
BC070169 mRNA. Translation: AAH70169.1.
BE742590 mRNA. No translation available.
BU543626 mRNA. No translation available.
CCDSiCCDS47581.1. [Q71UI9-5]
CCDS5495.1. [Q71UI9-2]
CCDS5496.1. [Q71UI9-1]
CCDS5497.1. [Q71UI9-4]
CCDS5498.1. [Q71UI9-3]
RefSeqiNP_036544.1. NM_012412.4. [Q71UI9-1]
NP_619541.1. NM_138635.3. [Q71UI9-2]
NP_958844.1. NM_201436.2. [Q71UI9-4]
NP_958924.1. NM_201516.2. [Q71UI9-5]
NP_958925.1. NM_201517.2. [Q71UI9-3]
UniGeneiHs.488189.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WAAX-ray3.20C/G1-128[»]
ProteinModelPortaliQ71UI9.
SMRiQ71UI9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125150. 38 interactors.
IntActiQ71UI9. 10 interactors.
MINTiMINT-4828370.
STRINGi9606.ENSP00000308405.

PTM databases

iPTMnetiQ71UI9.
PhosphoSitePlusiQ71UI9.
SwissPalmiQ71UI9.

Polymorphism and mutation databases

BioMutaiH2AFV.
DMDMi74749787.

Proteomic databases

EPDiQ71UI9.
MaxQBiQ71UI9.
PaxDbiQ71UI9.
PeptideAtlasiQ71UI9.
PRIDEiQ71UI9.
TopDownProteomicsiQ71UI9-1. [Q71UI9-1]
Q71UI9-3. [Q71UI9-3]
Q71UI9-4. [Q71UI9-4]

Protocols and materials databases

DNASUi94239.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000222690; ENSP00000222690; ENSG00000105968. [Q71UI9-2]
ENST00000308153; ENSP00000308405; ENSG00000105968. [Q71UI9-1]
ENST00000349299; ENSP00000342714; ENSG00000105968. [Q71UI9-3]
ENST00000350771; ENSP00000340708; ENSG00000105968. [Q71UI9-4]
ENST00000381124; ENSP00000370516; ENSG00000105968. [Q71UI9-5]
GeneIDi94239.
KEGGihsa:94239.
UCSCiuc003tlz.3. human. [Q71UI9-1]

Organism-specific databases

CTDi94239.
DisGeNETi94239.
GeneCardsiH2AFV.
HGNCiHGNC:20664. H2AFV.
HPAiHPA045242.
neXtProtiNX_Q71UI9.
OpenTargetsiENSG00000105968.
PharmGKBiPA134895050.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1757. Eukaryota.
COG5262. LUCA.
GeneTreeiENSGT00710000106735.
HOGENOMiHOG000234652.
HOVERGENiHBG009342.
InParanoidiQ71UI9.
KOiK11251.
OMAiIHRYLMN.
OrthoDBiEOG091G0XGD.
PhylomeDBiQ71UI9.
TreeFamiTF354232.

Enzyme and pathway databases

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.

Miscellaneous databases

ChiTaRSiH2AFV. human.
GeneWikiiH2AFV.
GenomeRNAii94239.
PROiQ71UI9.

Gene expression databases

BgeeiENSG00000105968.
CleanExiHS_H2AFV.
ExpressionAtlasiQ71UI9. baseline and differential.
GenevisibleiQ71UI9. 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 nameiH2AV_HUMAN
AccessioniPrimary (citable) accession number: Q71UI9
Secondary accession number(s): A6NFA8
, A6NKY0, A6NN01, A8MQC5, Q59GV8, Q6PK98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 128 of the entry and version 3 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 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.