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P04911 (H2A1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 151. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H2A.1
Gene names
Name:HTA1
Synonyms:H2A1, SPT11
Ordered Locus Names:YDR225W
ORF Names:YD9934.10
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length132 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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. Ref.8 Ref.12 Ref.14 Ref.17

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.

Subcellular location

Nucleus. Chromosome.

Domain

The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.

Post-translational modification

Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases MEC1/ATR and TEL1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A interacts with ARP4, a shared component of the NuA4 histone acetyltransferase complex and the INO80 and SWR1 chromatin remodeling complexes, and serves to recruit first NuA4, mediating histone H4 acetylation, and subsequently the INO80/SWR1 complexes, facilitating DNA resection, to DSB sites. Gamma-H2A is required for sequestering cohesin around the break site, which is important for efficient post-replicative double-strand break repair by homologous recombination, holding the damaged chromatid close to its undamaged sister template. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated by PPH3, a component of the histone H2A phosphatase complex (HTP-C). Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint. Ref.8 Ref.12 Ref.14 Ref.17

N-acetylated by NAT4. Ref.7 Ref.10 Ref.11

Acetylated by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex, to form H2AK4ac and H2AK7ac. Ref.7 Ref.10 Ref.11

Glutamine methylation at Gln-106 (H2AQ105me) by NOP1 is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex (Ref.18).

Sumoylated to from H2AK126su. May lead to transcriptional repression. Ref.16

Miscellaneous

In contrast to vertebrates and insects, its C-terminus is not monoubiquitinated.

Sequence similarities

Belongs to the histone H2A family.

Caution

To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2AK4ac = acetylated Lys-5; H2AK7ac = acetylated Lys-8; H2AK126su = sumoylated Lys-127; H2AS128ph = phosphorylated Ser-129.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 132131Histone H2A.1
PRO_0000055326

Regions

Motif129 – 1302[ST]-Q motif

Sites

Site1201Not ubiquitinated

Amino acid modifications

Modified residue21N-acetylserine Ref.11
Modified residue51N6-acetyllysine Ref.7
Modified residue81N6-acetyllysine Ref.7 Ref.10
Modified residue1061N5-methylglutamine Ref.18
Modified residue1291Phosphoserine Ref.8
Cross-link127Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.16

Experimental info

Mutagenesis120 – 1212KK → RR: No effect. No effect; when associated with R-124 and R-127. Ref.6
Mutagenesis1221S → A or E: Causes hypersensitivity to DNA-damage-inducing agents and impairs sporulation. Ref.6 Ref.15
Mutagenesis1241K → R: No effect; when associated with R-120; R-121 and R-127. Ref.6 Ref.9
Mutagenesis1271K → R: No effect; when associated with R-120; R-121 and R-124. Ref.6 Ref.9
Mutagenesis1291S → A: Causes hypersensitivity to DNA-damage-inducing agents. Ref.6 Ref.8
Mutagenesis1291S → E or T: No effect. Ref.6 Ref.8

Secondary structure

................... 132
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04911 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A908C94A0363D13F

FASTA13213,989
        10         20         30         40         50         60 
MSGGKGGKAG SAAKASQSRS AKAGLTFPVG RVHRLLRRGN YAQRIGSGAP VYLTAVLEYL 

        70         80         90        100        110        120 
AAEILELAGN AARDNKKTRI IPRHLQLAIR NDDELNKLLG NVTIAQGGVL PNIHQNLLPK 

       130 
KSAKATKASQ EL 

« Hide

References

« Hide 'large scale' references
[1]"The two yeast histone H2A genes encode similar protein subtypes."
Choe J., Kolodrubetz D., Grunstein M.
Proc. Natl. Acad. Sci. U.S.A. 79:1484-1487(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Insertion site specificity of the transposon Tn3."
Davies C.J., Hutchison C.A. III
Nucleic Acids Res. 23:507-514(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Analysis and in vivo disruption of the gene coding for adenylate kinase (ADK1) in the yeast Saccharomyces cerevisiae."
Konrad M.
J. Biol. Chem. 263:19468-19474(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-132.
[6]"A conserved sequence in histone H2A which is a ubiquitination site in higher eucaryotes is not required for growth in Saccharomyces cerevisiae."
Swerdlow P.S., Schuster T., Finley D.
Mol. Cell. Biol. 10:4905-4911(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: LACK OF UBIQUITINATION, MUTAGENESIS OF 120-LYS-LYS-121.
[7]"Esa1p is an essential histone acetyltransferase required for cell cycle progression."
Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L.
Mol. Cell. Biol. 19:2515-2526(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-5 AND LYS-8.
[8]"A role for Saccharomyces cerevisiae histone H2A in DNA repair."
Downs J.A., Lowndes N.F., Jackson S.P.
Nature 408:1001-1004(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-129, PHOSPHORYLATION AT SER-129.
[9]"Rad6-dependent ubiquitination of histone H2B in yeast."
Robzyk K., Recht J., Osley M.A.
Science 287:501-504(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: LACK OF UBIQUITINATION, MUTAGENESIS OF 120-LYS-LYS-121; LYS-124 AND LYS-127.
[10]"Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin."
Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M.
Mol. Cell 8:473-479(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-8.
[11]"An Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A."
Song O.-K., Wang X., Waterborg J.H., Sternglanz R.
J. Biol. Chem. 278:38109-38112(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT SER-2.
[12]"Distribution and dynamics of chromatin modification induced by a defined DNA double-strand break."
Shroff R., Arbel-Eden A., Pilch D.R., Ira G., Bonner W.M., Petrini J.H.J., Haber J.E., Lichten M.
Curr. Biol. 14:1703-1711(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[13]"Binding of chromatin-modifying activities to phosphorylated histone H2A at DNA damage sites."
Downs J.A., Allard S., Jobin-Robitaille O., Javaheri A., Auger A., Bouchard N., Kron S.J., Jackson S.P., Cote J.
Mol. Cell 16:979-990(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARP4.
[14]"DNA damage response pathway uses histone modification to assemble a double-strand break-specific cohesin domain."
Uenal E., Arbel-Eden A., Sattler U., Shroff R., Lichten M., Haber J.E., Koshland D.
Mol. Cell 16:991-1002(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION.
[15]"Saccharomyces cerevisiae histone H2A Ser122 facilitates DNA repair."
Harvey A.C., Jackson S.P., Downs J.A.
Genetics 170:543-553(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-122.
[16]"Histone sumoylation is a negative regulator in Saccharomyces cerevisiae and shows dynamic interplay with positive-acting histone modifications."
Nathan D., Ingvarsdottir K., Sterner D.E., Bylebyl G.R., Dokmanovic M., Dorsey J.A., Whelan K.A., Krsmanovic M., Lane W.S., Meluh P.B., Johnson E.S., Berger S.L.
Genes Dev. 20:966-976(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-127.
[17]"A phosphatase complex that dephosphorylates gamma-H2AX regulates DNA damage checkpoint recovery."
Keogh M.-C., Kim J.-A., Downey M., Fillingham J., Chowdhury D., Harrison J.C., Onishi M., Datta N., Galicia S., Emili A., Lieberman J., Shen X., Buratowski S., Haber J.E., Durocher D., Greenblatt J.F., Krogan N.J.
Nature 439:497-501(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEPHOSPHORYLATION.
[18]"Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification."
Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J., Nielsen M.L., Kouzarides T.
Nature 505:564-568(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT GLN-106.
[19]"Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions."
White C.L., Suto R.K., Luger K.
EMBO J. 20:5207-5218(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01304 Genomic DNA. Translation: CAA24611.1.
U13239 Genomic DNA. Translation: AAC33142.1.
Z48612 Genomic DNA. Translation: CAA88505.1.
M18455 Genomic DNA. Translation: AAA66318.1.
BK006938 Genomic DNA. Translation: DAA12067.1.
PIRHSBYA1. S05813.
RefSeqNP_010511.3. NM_001180533.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ID3X-ray3.10C/G2-132[»]
3T7KX-ray2.03C/D125-132[»]
ProteinModelPortalP04911.
SMRP04911. Positions 17-122.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32277. 410 interactions.
DIPDIP-419N.
IntActP04911. 22 interactions.
MINTMINT-398033.
STRING4932.YDR225W.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR225W; YDR225W; YDR225W.
GeneID851811.
KEGGsce:YDR225W.

Organism-specific databases

SGDS000002633. HTA1.

Phylogenomic databases

GeneTreeENSGT00740000115227.
HOGENOMHOG000234652.
KOK11251.
OMAGYKRAGP.
OrthoDBEOG7GN30N.

Enzyme and pathway databases

BioCycYEAST:G3O-29805-MONOMER.

Gene expression databases

GenevestigatorP04911.

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

EvolutionaryTraceP04911.
NextBio969665.

Entry information

Entry nameH2A1_YEAST
AccessionPrimary (citable) accession number: P04911
Secondary accession number(s): D6VSK7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references