H2AZ_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2AZ_RAT
• UniProt AC: P0C0S7
• Protein Name: Histone H2A.Z
• Gene Name: H2afz
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 128
• Subcellular Localization: Nucleus. Chromosome.
• 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 (By similarity)..
• 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	Acetylation	---MAGGKAGKDSGK ---CCCCCCCCCCCC	53.71	25786129
5	Methylation	---MAGGKAGKDSGK ---CCCCCCCCCCCC	53.71	-
8	Acetylation	MAGGKAGKDSGKAKT CCCCCCCCCCCCCCC	54.29	25786129
8	Methylation	MAGGKAGKDSGKAKT CCCCCCCCCCCCCCC	54.29	-
12	Acetylation	KAGKDSGKAKTKAVS CCCCCCCCCCCHHCC	51.14	25786129
12	Lactoylation	KAGKDSGKAKTKAVS CCCCCCCCCCCHHCC	51.14	-
14	Acetylation	GKDSGKAKTKAVSRS CCCCCCCCCHHCCHH	54.78	25786129
14	Lactoylation	GKDSGKAKTKAVSRS CCCCCCCCCHHCCHH	54.78	-
16	Acetylation	DSGKAKTKAVSRSQR CCCCCCCHHCCHHHH	46.19	26302492
99	Phosphorylation	RGDEELDSLIKATIA CCCHHHHHHHHHHHC	44.62	23984901
116	Lactoylation	GVIPHIHKSLIGKKG CCCHHHHHHHCCCCC	46.48	-
116	Acetylation	GVIPHIHKSLIGKKG CCCHHHHHHHCCCCC	46.48	22902405
121	Ubiquitination	IHKSLIGKKGQQKTV HHHHHCCCCCCCCCC	46.89	-
121	Acetylation	IHKSLIGKKGQQKTV HHHHHCCCCCCCCCC	46.89	25786129
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_RAT !!

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 (By similarity).	-
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).	-
5	K	Methylation	Monomethylated on Lys-5 and Lys-8 by SETD6.	-
5	K	Methylation	SETD6 predominantly methylates Lys-8, lys-5 being a possible secondary site.	-
8	K	Acetylation	Acetylated on Lys-5, Lys-8 and Lys-12 during interphase; acetylation disappears at mitosis (By similarity).	-
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).	-
8	K	Methylation	Monomethylated on Lys-5 and Lys-8 by SETD6.	-
8	K	Methylation	SETD6 predominantly methylates Lys-8, lys-5 being a possible secondary site.	-
12	K	Acetylation	Acetylated on Lys-5, Lys-8 and Lys-12 during interphase; acetylation disappears at mitosis (By similarity).	-
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).	-
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).	-
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_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of H2AZ_RAT !!

Drug and Disease Associations

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