H2A3_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2A3_RAT
• UniProt AC: Q4FZT6
• Protein Name: Histone H2A type 3
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 130
• 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: MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK

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 ------CCCCCCCCH	36.88	-
2	Acetylation	------MSGRGKQGG ------CCCCCCCCH	36.88	-
4	Citrullination	----MSGRGKQGGKA ----CCCCCCCCHHH	41.66	-
4	Methylation	----MSGRGKQGGKA ----CCCCCCCCHHH	41.66	-
4	Citrullination	----MSGRGKQGGKA ----CCCCCCCCHHH	41.66	-
6	Acetylation	--MSGRGKQGGKARA --CCCCCCCCHHHHH	44.39	24846265
6	Other	--MSGRGKQGGKARA --CCCCCCCCHHHHH	44.39	-
10	Succinylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	-
10	Lactoylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	-
10	Other	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	-
10	Acetylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	24846275
37	N6-crotonyl-L-lysine	RVHRLLRKGNYSERV HHHHHHHCCCCHHCC	52.02	-
37	Crotonylation	RVHRLLRKGNYSERV HHHHHHHCCCCHHCC	52.02	-
37	Other	RVHRLLRKGNYSERV HHHHHHHCCCCHHCC	52.02	-
75	Other	GNAARDNKKTRIIPR CHHHHCCCCCCEEHH	60.87	-
76	Other	NAARDNKKTRIIPRH HHHHCCCCCCEEHHH	49.65	-
96	Succinylation	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	-
96	Other	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	-
96	Glutarylation	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	-
96	Acetylation	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	37418439
102	Phosphorylation	NKLLGRVTIAQGGVL HHHHCCEEECCCCCC	14.83	22673903
105	Methylation	LGRVTIAQGGVLPNI HCCEEECCCCCCCCE	45.37	-
119	Glutarylation	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	-
119	Crotonylation	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	-
119	Other	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	-
119	N6-crotonyl-L-lysine	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	-
120	Crotonylation	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	-
120	Glutarylation	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	-
120	N6-crotonyl-L-lysine	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	-
121	Phosphorylation	AVLLPKKTESHHKAK EEECCCCCHHHHHCC	49.17	23984901
123	Phosphorylation	LLPKKTESHHKAKGK ECCCCCHHHHHCCCC	35.80	23589303
126	Crotonylation	KKTESHHKAKGK--- CCCHHHHHCCCC---	46.50	-
126	N6-crotonyl-L-lysine	KKTESHHKAKGK--- CCCHHHHHCCCC---	46.50	-
126	Glutarylation	KKTESHHKAKGK--- CCCHHHHHCCCC---	46.50	-

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
2	S	Phosphorylation	Kinase	RPS6KA5	-	Uniprot
121	T	Phosphorylation	Kinase	DCAF1	-	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.	-
4	R	Methylation	Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.	-
14	K	ubiquitylation	Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro.	-
16	K	ubiquitylation	Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro.	-
27	K	Methylation	Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me).	-
27	K	ubiquitylation	Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me).	-
63	K	ubiquitylation	Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage.	-
105	Q	Methylation	Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I.	-
120	K	ubiquitylation	Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM37 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals.	-
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.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of H2A3_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of H2A3_RAT !!

Drug and Disease Associations

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