H2AZ_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2AZ_MOUSE
• UniProt AC: P0C0S6
• Protein Name: Histone H2A.Z
• Gene Name: H2afz
• Organism: Mus musculus (Mouse).
• Sequence Length: 128
• Subcellular Localization: Nucleus . Chromosome . Enriched in constitutive heterochromatin (PubMed:12660166, PubMed:15195148). Absent from facultative heterochromatin of the inactive X chromosome (PubMed:12660166).
• Protein Description: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division. Essential for early development..
• Protein Sequence: MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV

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
5	Methylation	---MAGGKAGKDSGK ---CCCCCCCCCCCC	53.71	-
5	Acetylation	---MAGGKAGKDSGK ---CCCCCCCCCCCC	53.71	16204459
8	Acetylation	MAGGKAGKDSGKAKT CCCCCCCCCCCCCCC	54.29	16204459
8	Methylation	MAGGKAGKDSGKAKT CCCCCCCCCCCCCCC	54.29	-
12	Acetylation	KAGKDSGKAKTKAVS CCCCCCCCCCCHHCC	51.14	16204459
12	Lactoylation	KAGKDSGKAKTKAVS CCCCCCCCCCCHHCC	51.14	31645732
14	Lactoylation	GKDSGKAKTKAVSRS CCCCCCCCCHHCCHH	54.78	-
14	Acetylation	GKDSGKAKTKAVSRS CCCCCCCCCHHCCHH	54.78	23864654
99	Phosphorylation	RGDEELDSLIKATIA CCCHHHHHHHHHHHC	44.62	28066266
102	Acetylation	EELDSLIKATIAGGG HHHHHHHHHHHCCCC	44.78	23806337
102	Succinylation	EELDSLIKATIAGGG HHHHHHHHHHHCCCC	44.78	23806337
116	Acetylation	GVIPHIHKSLIGKKG CCCHHHHHHHCCCCC	46.48	23806337
116	Ubiquitination	GVIPHIHKSLIGKKG CCCHHHHHHHCCCCC	46.48	-
116	Lactoylation	GVIPHIHKSLIGKKG CCCHHHHHHHCCCCC	46.48	31645732
117	Phosphorylation	VIPHIHKSLIGKKGQ CCHHHHHHHCCCCCC	15.85	-
121	Ubiquitination	IHKSLIGKKGQQKTV HHHHHCCCCCCCCCC	46.89	-
122	Ubiquitination	HKSLIGKKGQQKTV- HHHHCCCCCCCCCC-	57.66	-
126	Ubiquitination	IGKKGQQKTV----- CCCCCCCCCC-----	43.28	-

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

Oops, there are no upstream regulatory protein records of H2AZ_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
5	K	Acetylation	Acetylated on Lys-5, Lys-8 and Lys-12 during interphase; acetylation disappears at mitosis.	16204459
5	K	Acetylation	Acetylated on Lys-5, Lys-8, Lys-12 and Lys-14 by KAT2A; KAT2A is recruited by the XPC complex in absence of DNA damage (By similarity).	16204459
5	K	Methylation	Monomethylated on Lys-5 and Lys-8 by SETD6.	16204459
5	K	Methylation	SETD6 predominantly methylates Lys-8, lys-5 being a possible secondary site.	16204459
8	K	Acetylation	Acetylated on Lys-5, Lys-8 and Lys-12 during interphase; acetylation disappears at mitosis.	16204459
8	K	Acetylation	Acetylated on Lys-5, Lys-8, Lys-12 and Lys-14 by KAT2A; KAT2A is recruited by the XPC complex in absence of DNA damage (By similarity).	16204459
8	K	Methylation	Monomethylated on Lys-5 and Lys-8 by SETD6.	16204459
8	K	Methylation	SETD6 predominantly methylates Lys-8, lys-5 being a possible secondary site.	16204459
12	K	Acetylation	Acetylated on Lys-5, Lys-8 and Lys-12 during interphase; acetylation disappears at mitosis.	16204459
12	K	Acetylation	Acetylated on Lys-5, Lys-8, Lys-12 and Lys-14 by KAT2A; KAT2A is recruited by the XPC complex in absence of DNA damage (By similarity).	16204459
14	K	Acetylation	Acetylated on Lys-5, Lys-8, Lys-12 and Lys-14 by KAT2A; KAT2A is recruited by the XPC complex in absence of DNA damage (By similarity).	7217105
122	K	ubiquitylation	Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of H2AZ_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
H2AZ_MOUSE	H2afz	physical	11101893
H2B11_XENLA	hist1h2bj	physical	11101893

Drug and Disease Associations

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