H2A2C_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2A2C_MOUSE
• UniProt AC: Q64523
• Protein Name: Histone H2A type 2-C
• Gene Name: Hist2h2ac
• 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: MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHKAKSK

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	-
4	Citrullination	----MSGRGKQGGKA ----CCCCCCCCHHH	41.66	-
4	Methylation	----MSGRGKQGGKA ----CCCCCCCCHHH	41.66	16699504
4	Citrullination	----MSGRGKQGGKA ----CCCCCCCCHHH	41.66	-
6	Acetylation	--MSGRGKQGGKARA --CCCCCCCCHHHHH	44.39	20612063
6	Other	--MSGRGKQGGKARA --CCCCCCCCHHHHH	44.39	27105115
10	Acetylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	20612059
10	Lactoylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	-
10	Succinylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	-
10	Other	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	24681537
37	N6-crotonyl-L-lysine	RVHRLLRKGNYAERV HHHHHHHCCCHHHHC	52.02	-
37	Other	RVHRLLRKGNYAERV HHHHHHHCCCHHHHC	52.02	27105115
37	Crotonylation	RVHRLLRKGNYAERV HHHHHHHCCCHHHHC	52.02	21925322
37	Ubiquitination	RVHRLLRKGNYAERV HHHHHHHCCCHHHHC	52.02	-
75	Other	GNAARDNKKTRIIPR CHHHHCCCCCCEEHH	60.87	24681537
76	Other	NAARDNKKTRIIPRH HHHHCCCCCCEEHHH	49.65	24681537
96	Other	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	24681537
96	Succinylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	-
96	Glutarylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	-
96	Crotonylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	22693562
96	Methylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	22693562
96	Acetylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	23864654
96	Ubiquitination	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	-
100	Methylation	ELNKLLGKVTIAQGG HHHHHHCCEEECCCC	35.85	22693562
100	Ubiquitination	ELNKLLGKVTIAQGG HHHHHHCCEEECCCC	35.85	-
100	Acetylation	ELNKLLGKVTIAQGG HHHHHHCCEEECCCC	35.85	22733758
100	"N6,N6-dimethyllysine"	ELNKLLGKVTIAQGG HHHHHHCCEEECCCC	35.85	-
100	Glutarylation	ELNKLLGKVTIAQGG HHHHHHCCEEECCCC	35.85	-
102	Phosphorylation	NKLLGKVTIAQGGVL HHHHCCEEECCCCCC	17.68	27180971
105	Methylation	LGKVTIAQGGVLPNI HCCEEECCCCCCCCE	45.37	24352239
119	Glutarylation	IQAVLLPKKTESHKA EEEEECCCCCHHHCC	72.76	-
119	Ubiquitination	IQAVLLPKKTESHKA EEEEECCCCCHHHCC	72.76	-
119	N6-crotonyl-L-lysine	IQAVLLPKKTESHKA EEEEECCCCCHHHCC	72.76	-
119	Other	IQAVLLPKKTESHKA EEEEECCCCCHHHCC	72.76	24681537
119	Crotonylation	IQAVLLPKKTESHKA EEEEECCCCCHHHCC	72.76	21925322
119	Acetylation	IQAVLLPKKTESHKA EEEEECCCCCHHHCC	72.76	22641301
120	Glutarylation	QAVLLPKKTESHKAK EEEECCCCCHHHCCC	56.43	-
120	Crotonylation	QAVLLPKKTESHKAK EEEECCCCCHHHCCC	56.43	15509584
120	Other	QAVLLPKKTESHKAK EEEECCCCCHHHCCC	56.43	27105115
120	Acetylation	QAVLLPKKTESHKAK EEEECCCCCHHHCCC	56.43	30589213
120	N6-crotonyl-L-lysine	QAVLLPKKTESHKAK EEEECCCCCHHHCCC	56.43	-
120	Ubiquitination	QAVLLPKKTESHKAK EEEECCCCCHHHCCC	56.43	15509584
121	Phosphorylation	AVLLPKKTESHKAKS EEECCCCCHHHCCCC	49.17	27600695
123	Phosphorylation	LLPKKTESHKAKSK- ECCCCCHHHCCCCC-	35.20	-
125	N6-crotonyl-L-lysine	PKKTESHKAKSK--- CCCCHHHCCCCC---	67.78	-
125	Other	PKKTESHKAKSK--- CCCCHHHCCCCC---	67.78	27105115
125	Crotonylation	PKKTESHKAKSK--- CCCCHHHCCCCC---	67.78	-
125	Ubiquitination	PKKTESHKAKSK--- CCCCHHHCCCCC---	67.78	-

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.	-
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.	16699504
14	K	ubiquitylation	Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity).	15509584
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	Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (By similarity).	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 H2A2C_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of H2A2C_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

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