UniProt Accession

 H2A1_YEAST; P04911; D6VSK7 

Genbank Protein ID

 V01304; U13239; Z48612; M18455; BK006938 

Genbank Nucleotide ID

 CAA24611.1; AAC33142.1; CAA88505.1; AAA66318.1; DAA12067.1 

Protein Name

 Histone H2A.1 

Protein Synonyms/Alias

  

Gene Name

 HTA1 

Gene Synonyms/Alias

 H2A1; SPT11; YDR225W; YD9934.10 

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
5	***MSGGKGGKAGSA	acetylation	[1, 2]
8	MSGGKGGKAGSAAKA	acetylation	[1, 2]
22	ASQSRSAKAGLTFPV	acetylation	[2]
22	ASQSRSAKAGLTFPV	ubiquitination	[3]
97	RNDDELNKLLGNVTI	ubiquitination	[3]
124	LLPKKSAKATKASQE	acetylation	[2]
127	KKSAKATKASQEL**	acetylation	[2]

Reference

 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] 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]
 [3] 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:0000122; P:negative regulation of transcription from RNA polymerase II promoter; 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.