H2AJ_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2AJ_MOUSE
• UniProt AC: Q8R1M2
• Protein Name: Histone H2A.J
• Gene Name: H2afj
• Organism: Mus musculus (Mouse).
• Sequence Length: 129
• Subcellular Localization: Nucleus. Chromosome.
• Protein Description: Core component of nucleosome. 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..
• Protein Sequence: MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESQKVKSK

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
2	Phosphorylation	------MSGRGKQGG ------CCCCCCCCC	36.88	7217105
6	Acetylation	--MSGRGKQGGKVRA --CCCCCCCCCCCCH	44.39	23806337
10	Acetylation	GRGKQGGKVRAKAKS CCCCCCCCCCHHCCC	35.06	23806337
10	Lactoylation	GRGKQGGKVRAKAKS CCCCCCCCCCHHCCC	35.06	-
37	Ubiquitination	RVHRLLRKGNYAERV HHHHHHHCCCHHHHC	52.02	-
51	Phosphorylation	VGAGAPVYLAAVLEY CCCCHHHHHHHHHHH	6.92	26239621
58	Phosphorylation	YLAAVLEYLTAEILE HHHHHHHHHHHHHHH	12.75	26239621
96	Ubiquitination	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	27667366
96	Acetylation	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	8276305
102	Phosphorylation	NKLLGRVTIAQGGVL HHHHCCEEECCCCCC	14.83	27180971
105	Methylation	LGRVTIAQGGVLPNI HCCEEECCCCCCCCE	45.37	-
119	Methylation	IQAVLLPKKTESQKV EEEEECCCCCCCCCC	72.76	-
119	"N6,N6-dimethyllysine"	IQAVLLPKKTESQKV EEEEECCCCCCCCCC	72.76	-
119	Acetylation	IQAVLLPKKTESQKV EEEEECCCCCCCCCC	72.76	165963
119	Ubiquitination	IQAVLLPKKTESQKV EEEEECCCCCCCCCC	72.76	22790023
120	Acetylation	QAVLLPKKTESQKVK EEEECCCCCCCCCCC	56.43	14877785
120	Ubiquitination	QAVLLPKKTESQKVK EEEECCCCCCCCCCC	56.43	-
120	Phosphoglycerylation	QAVLLPKKTESQKVK EEEECCCCCCCCCCC	56.43	-
121	Phosphorylation	AVLLPKKTESQKVKS EEECCCCCCCCCCCC	47.17	-
125	Ubiquitination	PKKTESQKVKSK--- CCCCCCCCCCCC---	61.99	-

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
121	T	Phosphorylation	Kinase	DCAF1	Q80TR8	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
2	S	Acetylation	Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1.	-
2	S	Phosphorylation	Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1.	-
2	S	Phosphorylation	Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis.	-
2	S	Phosphorylation	Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription.	-
63	K	ubiquitylation	Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties (By similarity).	-
105	Q	Methylation	Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I.	-
120	K	ubiquitylation	Monoubiquitination of Lys-120 (H2AXK119ub) gives a specific tag for epigenetic transcriptional repression.	-
121	T	Phosphorylation	Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription (By similarity).	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of H2AJ_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of H2AJ_MOUSE !!

Drug and Disease Associations

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