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Q9QZQ8 (H2AY_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Core histone macro-H2A.1

Short name=Histone macroH2A1
Short name=mH2A1
Alternative name(s):
H2A.y
H2A/y
Gene names
Name:H2afy
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. 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. Involved in stable X chromosome inactivation. Inhibits the binding of transcription factors and interferes with the activity of remodeling SWI/SNF complexes. Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin. In addition, isoform 1, but not isoform 2, binds ADP-ribose and O-acetyl-ADP-ribose, and may be involved in ADP-ribose-mediated chromatin modulation. Ref.7

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. Interacts with SPOP. Part of a complex consisting of H2AFY, CUL3 and SPOP. Interacts with HDAC1 and HDAC2 By similarity. Ref.2 Ref.7

Subcellular location

Nucleus. Chromosome. Note: Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin. In quiescent lymphocytes, associated with centromeric constitutive heterochromatin. Ref.4 Ref.6

Tissue specificity

Ubiquitously expressed, with high levels in testis. Present in liver, kidney and adrenal gland (at protein level). In the liver, present in hepatocytes and at a lesser extent in cells of the bile ducts. In the kidney, present in proximal and distal convoluted tubules and in straight proximal tubules. In the adrenal gland, present in inner cells of the cortex and medulla. Ref.1 Ref.5

Post-translational modification

Monoubiquitinated at either Lys-116 or Lys-117. May also be polyubiquitinated. Ubiquitination is mediated by the CUL3/SPOP E3 complex and does not promote proteasomal degradation. Instead, it is required for enrichment in inactive X chromosome chromatin By similarity.

Sequence similarities

Contains 1 histone H2A domain.

Contains 1 Macro domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: Q9QZQ8-1)

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.
Note: Major form.
Isoform 1 (identifier: Q9QZQ8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     198-217: NLIHSEISNLAGFEVEAIIN → QVVQADIASIDSDAVVH
     221-229: ADIDLKDDL → TDFYTGGEV

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 372372Core histone macro-H2A.1
PRO_0000227904

Regions

Domain2 – 117116Histone H2A
Domain184 – 370187Macro
Compositional bias116 – 16146Lys-rich

Amino acid modifications

Modified residue181N6-methyllysine By similarity
Modified residue1161N6-acetyllysine; alternate Ref.9
Modified residue1231N6-acetyllysine Ref.9
Modified residue1291Phosphothreonine Ref.8
Modified residue1701Phosphoserine By similarity
Modified residue1731Phosphoserine By similarity
Modified residue1781Phosphothreonine By similarity
Cross-link116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Cross-link117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence198 – 21720NLIHS…EAIIN → QVVQADIASIDSDAVVH in isoform 1.
VSP_017596
Alternative sequence221 – 2299ADIDLKDDL → TDFYTGGEV in isoform 1.
VSP_017597

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 076CF76A34FACAA0

FASTA37239,735
        10         20         30         40         50         60 
MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI 

        70         80         90        100        110        120 
LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS 

       130        140        150        160        170        180 
KGKLEAIITP PPAKKAKSPS QKKPVAKKTG GKKGARKSKK KQGEVSKAAS ADSTTEGTPT 

       190        200        210        220        230        240 
DGFTVLSTKS LFLGQKLNLI HSEISNLAGF EVEAIINPTN ADIDLKDDLG NTLEKKGGKE 

       250        260        270        280        290        300 
FVEAVLELRK KNGPLEVAGA AISAGHGLPA KFVIHCNSPV WGADKCEELL EKTVKNCLAL 

       310        320        330        340        350        360 
ADDRKLKSIA FPSIGSGRNG FPKQTAAQLI LKAISSYFVS TMSSSIKTVY FMLFDSESIG 

       370 
IYVQEMAKLD AN 

« Hide

Isoform 1 [UniParc].

Checksum: 33F123DE5C9C46EC
Show »

FASTA36939,290

References

« Hide 'large scale' references
[1]"Messenger RNAs encoding mouse histone macroH2A1 isoforms are expressed at similar levels in male and female cells and result from alternative splicing."
Rasmussen T.P., Huang T., Mastrangelo M.-A., Loring J., Panning B., Jaenisch R.
Nucleic Acids Res. 27:3685-3689(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 197-229 (ISOFORM 1), TISSUE SPECIFICITY.
Strain: 129/SvEvTacfBr.
[2]"MacroH2A1.2 binds the nuclear protein Spop."
Takahashi I., Kameoka Y., Hashimoto K.
Biochim. Biophys. Acta 1591:63-68(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH SPOP.
Tissue: Brain.
[3]"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] (ISOFORM 1).
Strain: FVB/N.
Tissue: Mammary gland.
[4]"Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals."
Costanzi C., Pehrson J.R.
Nature 393:599-601(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[5]"MACROH2A2, a new member of the MACROH2A core histone family."
Costanzi C., Pehrson J.R.
J. Biol. Chem. 276:21776-21784(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Dynamic relocation of epigenetic chromatin markers reveals an active role of constitutive heterochromatin in the transition from proliferation to quiescence."
Grigoryev S.A., Nikitina T., Pehrson J.R., Singh P.B., Woodcock C.L.
J. Cell Sci. 117:6153-6162(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Structural characterization of the histone variant macroH2A."
Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y., Pehrson J.R., Khochbin S., Luger K.
Mol. Cell. Biol. 25:7616-7624(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC1 AND HDAC2, FUNCTION.
[8]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116 AND LYS-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF171080 mRNA. Translation: AAD53745.1.
AF171081 mRNA. Translation: AAD53746.1.
AB071988 mRNA. Translation: BAB68541.1.
BC006955 mRNA. Translation: AAH06955.1.
CCDSCCDS26557.1. [Q9QZQ8-1]
CCDS49278.1. [Q9QZQ8-2]
RefSeqNP_001152985.1. NM_001159513.1.
NP_001152986.1. NM_001159514.1. [Q9QZQ8-2]
NP_001152987.1. NM_001159515.1.
NP_036145.1. NM_012015.2. [Q9QZQ8-1]
UniGeneMm.283802.
Mm.478369.

3D structure databases

ProteinModelPortalQ9QZQ8.
SMRQ9QZQ8. Positions 10-117, 181-369.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid205061. 1 interaction.
IntActQ9QZQ8. 3 interactions.
MINTMINT-4121159.

PTM databases

PhosphoSiteQ9QZQ8.

Proteomic databases

MaxQBQ9QZQ8.
PaxDbQ9QZQ8.
PRIDEQ9QZQ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000016081; ENSMUSP00000016081; ENSMUSG00000015937. [Q9QZQ8-1]
ENSMUST00000045788; ENSMUSP00000038221; ENSMUSG00000015937. [Q9QZQ8-2]
GeneID26914.
KEGGmmu:26914.
UCSCuc007qsf.2. mouse. [Q9QZQ8-1]
uc007qsg.2. mouse. [Q9QZQ8-2]

Organism-specific databases

CTD9555.
MGIMGI:1349392. H2afy.

Phylogenomic databases

eggNOGCOG2110.
GeneTreeENSGT00740000115227.
HOGENOMHOG000234653.
HOVERGENHBG009342.
InParanoidQ9QZQ8.
KOK11251.
OMAQVVQADI.
OrthoDBEOG71G9VP.
PhylomeDBQ9QZQ8.
TreeFamTF332276.

Enzyme and pathway databases

ReactomeREACT_188804. Cell Cycle.
REACT_200794. Mus musculus biological processes.

Gene expression databases

BgeeQ9QZQ8.
CleanExMM_H2AFY.
GenevestigatorQ9QZQ8.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR021171. Core_histone_macro-H2A.
IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
IPR002589. Macro_dom.
[Graphical view]
PfamPF00125. Histone. 1 hit.
PF01661. Macro. 1 hit.
[Graphical view]
PIRSFPIRSF037942. Core_histone_macro-H2A. 1 hit.
PRINTSPR00620. HISTONEH2A.
SMARTSM00506. A1pp. 1 hit.
SM00414. H2A. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS51154. MACRO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSH2AFY. mouse.
NextBio304793.
PROQ9QZQ8.
SOURCESearch...

Entry information

Entry nameH2AY_MOUSE
AccessionPrimary (citable) accession number: Q9QZQ8
Secondary accession number(s): Q91VZ2, Q9QZQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot