H2A2A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2A2A_MOUSE
• UniProt AC: Q6GSS7
• Protein Name: Histone H2A type 2-A
• Gene Name: Hist2h2aa1
• Organism: Mus musculus (Mouse).
• 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: MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHHKAKGK

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	7217105
2	Acetylation	------MSGRGKQGG ------CCCCCCCCH	36.88	7217105
4	Citrullination	----MSGRGKQGGKA ----CCCCCCCCHHH	41.66	-
4	Citrullination	----MSGRGKQGGKA ----CCCCCCCCHHH	41.66	-
4	Methylation	----MSGRGKQGGKA ----CCCCCCCCHHH	41.66	16699504
6	Other	--MSGRGKQGGKARA --CCCCCCCCHHHHH	44.39	27105115
6	Acetylation	--MSGRGKQGGKARA --CCCCCCCCHHHHH	44.39	7217105
10	Lactoylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	-
10	Succinylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	-
10	Other	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	24681537
10	Methylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	-
10	Acetylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	158669
37	Ubiquitination	RVHRLLRKGNYAERV HHHHHHHCCCHHHHC	52.02	-
37	Crotonylation	RVHRLLRKGNYAERV HHHHHHHCCCHHHHC	52.02	21925322
37	Other	RVHRLLRKGNYAERV HHHHHHHCCCHHHHC	52.02	27105115
37	N6-crotonyl-L-lysine	RVHRLLRKGNYAERV HHHHHHHCCCHHHHC	52.02	-
75	Acetylation	GNAARDNKKTRIIPR CHHHHCCCCCCEEHH	60.87	-
75	Other	GNAARDNKKTRIIPR CHHHHCCCCCCEEHH	60.87	24681537
76	Other	NAARDNKKTRIIPRH HHHHCCCCCCEEHHH	49.65	24681537
96	Other	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	24681537
96	Methylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	-
96	Crotonylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	-
96	Succinylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	-
96	Butyrylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	-
96	Glutarylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	-
96	Acetylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	22641287
96	Ubiquitination	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	-
100	Acetylation	ELNKLLGKVTIAQGG HHHHHHCCEEECCCC	35.85	158615
100	Glutarylation	ELNKLLGKVTIAQGG HHHHHHCCEEECCCC	35.85	-
100	"N6,N6-dimethyllysine"	ELNKLLGKVTIAQGG HHHHHHCCEEECCCC	35.85	-
100	Methylation	ELNKLLGKVTIAQGG HHHHHHCCEEECCCC	35.85	-
100	Ubiquitination	ELNKLLGKVTIAQGG HHHHHHCCEEECCCC	35.85	-
102	Phosphorylation	NKLLGKVTIAQGGVL HHHHCCEEECCCCCC	17.68	27180971
105	Methylation	LGKVTIAQGGVLPNI HCCEEECCCCCCCCE	45.37	24352239
119	Ubiquitination	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	-
119	Acetylation	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	158655
119	Crotonylation	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	21925322
119	Other	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	24681537
119	N6-crotonyl-L-lysine	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	-
119	Glutarylation	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	-
120	Acetylation	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	164055
120	N6-crotonyl-L-lysine	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	-
120	Other	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	27105115
120	Ubiquitination	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	15509584
120	Methylation	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	-
120	Crotonylation	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	15509584
120	Glutarylation	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	-
121	Phosphorylation	AVLLPKKTESHHKAK EEECCCCCHHHHHCC	49.17	25266776
123	Phosphorylation	LLPKKTESHHKAKGK ECCCCCHHHHHCCCC	35.80	25266776
126	Glutarylation	KKTESHHKAKGK--- CCCHHHHHCCCC---	46.50	-
126	Other	KKTESHHKAKGK--- CCCHHHHHCCCC---	46.50	27105115
126	N6-crotonyl-L-lysine	KKTESHHKAKGK--- CCCHHHHHCCCC---	46.50	-
126	Crotonylation	KKTESHHKAKGK--- CCCHHHHHCCCC---	46.50	-
126	Ubiquitination	KKTESHHKAKGK--- CCCHHHHHCCCC---	46.50	-
128	Acetylation	TESHHKAKGK----- CHHHHHCCCC-----	72.53	-
130	Acetylation	SHHKAKGK------- HHHHCCCC-------	57.36	-

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	Q8C050	Uniprot
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.	7217105
2	S	Phosphorylation	Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1.	7217105
2	S	Phosphorylation	Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis.	7217105
2	S	Phosphorylation	Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription.	7217105
4	R	Methylation	Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.	16699504
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.	15509584
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.	15509584
27	K	Methylation	Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me).	15509584
27	K	ubiquitylation	Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me).	15509584
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.	15509584
105	Q	Methylation	Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I.	24352239
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.	15525528
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 H2A2A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KAT2B_MOUSE	Kat2b	physical	26474655

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"Quantitative determination of histone modification. H2A acetylationand phosphorylation.";
Pantazis P., Bonner W.M.;
J. Biol. Chem. 256:4669-4675(1981).
Cited for: PHOSPHORYLATION AT SER-2, AND ACETYLATION AT SER-2 AND LYS-6.
PubMed: 7217105

Phosphorylation

"Quantitative determination of histone modification. H2A acetylationand phosphorylation.";
Pantazis P., Bonner W.M.;
J. Biol. Chem. 256:4669-4675(1981).
Cited for: PHOSPHORYLATION AT SER-2, AND ACETYLATION AT SER-2 AND LYS-6.
PubMed: 7217105

Ubiquitylation

"Ring1b-mediated H2A ubiquitination associates with inactive Xchromosomes and is involved in initiation of X inactivation.";
Fang J., Chen T., Chadwick B., Li E., Zhang Y.;
J. Biol. Chem. 279:52812-52815(2004).
Cited for: UBIQUITINATION AT LYS-120.
PubMed: 15509584

"Polycomb group proteins Ring1A/B link ubiquitylation of histone H2Ato heritable gene silencing and X inactivation.";
de Napoles M., Mermoud J.E., Wakao R., Tang Y.A., Endoh M.,Appanah R., Nesterova T.B., Silva J., Otte A.P., Vidal M., Koseki H.,Brockdorff N.;
Dev. Cell 7:663-676(2004).
Cited for: UBIQUITINATION AT LYS-120.
PubMed: 15525528