UniProt Accession

 H2A2_YEAST; P04912; D6VPZ9 

Genbank Protein ID

 V01305; Z26494; Z35764; AY693115; BK006936 

Genbank Nucleotide ID

 CAA24612.1; CAA81267.1; CAA84818.1; AAT93134.1; DAA07119.1 

Protein Name

 Histone H2A.2 

Protein Synonyms/Alias

  

Gene Name

 HTA2 

Gene Synonyms/Alias

 H2A2; YBL003C; YBL0103 

Created Date

 July 27, 2013 

Organism

 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 

NCBI Taxa ID

 559292 

Lysine Modification

Position	Peptide	Type	References
14	GKAGSAAKASQSRSA	succinylation	[1]
22	ASQSRSAKAGLTFPV	succinylation	[1]
97	RNDDELNKLLGNVTI	ubiquitination	[2]
120	IHQNLLPKKSAKTAK	malonylation	[1]
121	HQNLLPKKSAKTAKA	acetylation	[3]
124	LLPKKSAKTAKASQE	acetylation	[3]
127	KKSAKTAKASQEL**	acetylation	[3]
127	KKSAKTAKASQEL**	ubiquitination	[4]

Reference

 [1] Lysine succinylation and lysine malonylation in histones.
 Xie Z, Dai J, Dai L, Tan M, Cheng Z, Wu Y, Boeke JD, Zhao Y.
 Mol Cell Proteomics. 2012 May;11(5):100-7. [PMID: 22389435]
 [2] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [3] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591]
 [4] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 

Functional Description

 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. 

Sequence Annotation

 MOTIF 129 130 [ST]-Q motif.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 5 5 N6-acetyllysine.
 MOD_RES 8 8 N6-acetyllysine.
 MOD_RES 129 129 Phosphoserine.
 CROSSLNK 127 127 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 3D-structure; Acetylation; Chromosome; Complete proteome; DNA damage; DNA repair; DNA-binding; Isopeptide bond; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 132 AA 

Protein Sequence

Gene Ontology

 GO:0000788; C:nuclear nucleosome; TAS:SGD.
 GO:0031298; C:replication fork protection complex; IDA:SGD.
 GO:0003677; F:DNA binding; TAS:SGD.
 GO:0006333; P:chromatin assembly or disassembly; TAS:SGD.
 GO:0006281; P:DNA repair; IMP:SGD.
 GO:0006334; P:nucleosome assembly; IEA:InterPro. 

Interpro

 IPR009072; Histone-fold.
 IPR007125; Histone_core_D.
 IPR002119; Histone_H2A. 

Pfam

 PF00125; Histone 

SMART

 SM00414; H2A 

PROSITE

 PS00046; HISTONE_H2A 

PRINTS

 PR00620; HISTONEH2A.