H2AY_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2AY_MOUSE
• UniProt AC: Q9QZQ8
• Protein Name: Core histone macro-H2A.1
• Gene Name: H2afy
• Organism: Mus musculus (Mouse).
• Sequence Length: 372
• Subcellular Localization: Nucleus . Chromosome . Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin (PubMed:9634239). In quiescent lymphocytes, associated with centromeric constitutive heterochromatin (PubMed:15564378).
• Protein Description: 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, including NF-kappa-B, and interferes with the activity of remodeling SWI/SNF complexes (By similarity). Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin (By similarity). [PubMed: 16107708; Isoform 1: Binds ADP-ribose and O-acetyl-ADP-ribose, and may be involved in ADP-ribose-mediated chromatin modulation (By similarity Increases the expression of genes involved in redox metabolism, including SOD3]
• Protein Sequence: MSSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAIITPPPAKKAKSPSQKKPVAKKTGGKKGARKSKKKQGEVSKAASADSTTEGTPTDGFTVLSTKSLFLGQKLNLIHSEISNLAGFEVEAIINPTNADIDLKDDLGNTLEKKGGKEFVEAVLELRKKNGPLEVAGAAISAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALADDRKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYFMLFDSESIGIYVQEMAKLDAN

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Lactoylation	-MSSRGGKKKSTKTS -CCCCCCCCCCCCCC	60.91	-
9	Lactoylation	SSRGGKKKSTKTSRS CCCCCCCCCCCCCHH	67.83	-
18	Methylation	TKTSRSAKAGVIFPV CCCCHHHCCEEEEEH	47.09	-
96	Ubiquitination	EELNQLLKGVTIASG HHHHHHHHCCEECCC	60.99	-
116	Acetylation	IHPELLAKKRGSKGK CCHHHHHHHCCCCCC	42.86	23806337
116	Ubiquitination	IHPELLAKKRGSKGK CCHHHHHHHCCCCCC	42.86	22790023
117	Ubiquitination	HPELLAKKRGSKGKL CHHHHHHHCCCCCCE	57.28	-
120	Phosphorylation	LLAKKRGSKGKLEAI HHHHHCCCCCCEEEE	42.12	-
121	Ubiquitination	LAKKRGSKGKLEAII HHHHCCCCCCEEEEE	63.99	-
123	Acetylation	KKRGSKGKLEAIITP HHCCCCCCEEEEECC	47.06	23806337
123	Ubiquitination	KKRGSKGKLEAIITP HHCCCCCCEEEEECC	47.06	22790023
123	Methylation	KKRGSKGKLEAIITP HHCCCCCCEEEEECC	47.06	-
129 (in isoform 2)	Phosphorylation	-	24.51	19144319
129	Phosphorylation	GKLEAIITPPPAKKA CCEEEEECCCCCCCC	24.51	26824392
138	Phosphorylation	PPAKKAKSPSQKKPV CCCCCCCCHHHCCCC	34.34	18227505
140	Phosphorylation	AKKAKSPSQKKPVAK CCCCCCHHHCCCCCH	62.82	22802335
167	Ubiquitination	KKQGEVSKAASADST CCCCCCHHHHCCCCC	53.82	-
170	Phosphorylation	GEVSKAASADSTTEG CCCHHHHCCCCCCCC	37.15	27087446
173	Phosphorylation	SKAASADSTTEGTPT HHHHCCCCCCCCCCC	36.62	25521595
174	Phosphorylation	KAASADSTTEGTPTD HHHCCCCCCCCCCCC	29.43	27087446
175	Phosphorylation	AASADSTTEGTPTDG HHCCCCCCCCCCCCC	36.05	25521595
178	Phosphorylation	ADSTTEGTPTDGFTV CCCCCCCCCCCCEEE	19.45	25521595
180	Phosphorylation	STTEGTPTDGFTVLS CCCCCCCCCCEEEEE	48.90	27742792
184	Phosphorylation	GTPTDGFTVLSTKSL CCCCCCEEEEEEHHH	26.51	25619855
187	Phosphorylation	TDGFTVLSTKSLFLG CCCEEEEEEHHHHHH	29.47	25619855
188	Phosphorylation	DGFTVLSTKSLFLGQ CCEEEEEEHHHHHHH	22.08	25619855
189	Ubiquitination	GFTVLSTKSLFLGQK CEEEEEEHHHHHHHH	41.61	22790023
202	Phosphorylation	QKLNLIHSEISNLAG HHHHHHHHHHHHHCC	29.63	22802335
205	Phosphorylation	NLIHSEISNLAGFEV HHHHHHHHHHCCCEE	23.03	22802335
235	Acetylation	DLGNTLEKKGGKEFV CHHHHHHHHCHHHHH	60.89	23954790
285	Malonylation	SPVWGADKCEELLEK CCCCCHHHHHHHHHH	42.91	26320211
285	Acetylation	SPVWGADKCEELLEK CCCCCHHHHHHHHHH	42.91	23806337
285	Ubiquitination	SPVWGADKCEELLEK CCCCCHHHHHHHHHH	42.91	-
292	Acetylation	KCEELLEKTVKNCLA HHHHHHHHHHHHHHH	59.60	22826441
292	Ubiquitination	KCEELLEKTVKNCLA HHHHHHHHHHHHHHH	59.60	22790023
295	Ubiquitination	ELLEKTVKNCLALAD HHHHHHHHHHHHHHC	47.37	-
307	Malonylation	LADDRKLKSIAFPSI HHCCCCCCCCCCCCC	42.74	26320211
307	Ubiquitination	LADDRKLKSIAFPSI HHCCCCCCCCCCCCC	42.74	-
313	Phosphorylation	LKSIAFPSIGSGRNG CCCCCCCCCCCCCCC	32.88	29472430
316	Phosphorylation	IAFPSIGSGRNGFPK CCCCCCCCCCCCCCH	32.67	29472430
336	Phosphorylation	LILKAISSYFVSTMS HHHHHHHHHHHHHCC	19.24	29899451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
-	K	Ubiquitination	E3 ubiquitin ligase	Spop	Q6ZWS8	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
116	K	ubiquitylation	Monoubiquitinated at either Lys-116 or Lys-117.	23806337
117	K	ubiquitylation	Monoubiquitinated at either Lys-116 or Lys-117.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of H2AY_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SPOP_MOUSE	Spop	physical	12183056

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, AND MASSSPECTROMETRY.
PubMed: 19144319