dbPTM

H2A2C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2A2C_HUMAN
UniProt AC	Q16777
Protein Name	Histone H2A type 2-C
Gene Name	HIST2H2AC
Organism	Homo sapiens (Human).
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

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGRGKQGG ------CCCCCCCCH	36.88	15823041
2	Acetylation	------MSGRGKQGG ------CCCCCCCCH	36.88	15823041
4	Citrullination	----MSGRGKQGGKA ----CCCCCCCCHHH	41.66	-
4	Methylation	----MSGRGKQGGKA ----CCCCCCCCHHH	41.66	-
4	Citrullination	----MSGRGKQGGKA ----CCCCCCCCHHH	41.66	15823041
6	Methylation	--MSGRGKQGGKARA --CCCCCCCCHHHHH	44.39	20612061
6	Acetylation	--MSGRGKQGGKARA --CCCCCCCCHHHHH	44.39	16457589
6	Other	--MSGRGKQGGKARA --CCCCCCCCHHHHH	44.39	24681537
10	Acetylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	22389435
10	Lactoylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	-
10	Other	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	27105115
10	Succinylation	GRGKQGGKARAKAKS CCCCCCHHHHHHHHH	41.34	22389435
14	Acetylation	QGGKARAKAKSRSSR CCHHHHHHHHHHHHC	51.28	20167786
14	Ubiquitination	QGGKARAKAKSRSSR CCHHHHHHHHHHHHC	51.28	22980979
14	Other	QGGKARAKAKSRSSR CCHHHHHHHHHHHHC	51.28	27105115
16	Ubiquitination	GKARAKAKSRSSRAG HHHHHHHHHHHHCCC	45.77	22980979
17	Phosphorylation	KARAKAKSRSSRAGL HHHHHHHHHHHCCCC	42.10	23882029
19	Phosphorylation	RAKAKSRSSRAGLQF HHHHHHHHHCCCCCC	31.13	30622161
20	Phosphorylation	AKAKSRSSRAGLQFP HHHHHHHHCCCCCCC	25.66	27966365
21	Methylation	KAKSRSSRAGLQFPV HHHHHHHCCCCCCCH	33.64	-
30	Methylation	GLQFPVGRVHRLLRK CCCCCHHHHHHHHHC	22.69	-
37	Other	RVHRLLRKGNYAERV HHHHHHHCCCHHHHC	52.02	27105115
37	Crotonylation	RVHRLLRKGNYAERV HHHHHHHCCCHHHHC	52.02	21925322
37	Ubiquitination	RVHRLLRKGNYAERV HHHHHHHCCCHHHHC	52.02	27667366
37	N6-crotonyl-L-lysine	RVHRLLRKGNYAERV HHHHHHHCCCHHHHC	52.02	-
40	Phosphorylation	RLLRKGNYAERVGAG HHHHCCCHHHHCCCC	20.64	28152594
51	Phosphorylation	VGAGAPVYMAAVLEY CCCCHHHHHHHHHHH	4.68	-
52	Sulfoxidation	GAGAPVYMAAVLEYL CCCHHHHHHHHHHHH	1.64	28183972
58	Phosphorylation	YMAAVLEYLTAEILE HHHHHHHHHHHHHHH	12.75	-
72	Methylation	ELAGNAARDNKKTRI HHCCHHHHCCCCCCE	45.70	-
72	Dimethylation	ELAGNAARDNKKTRI HHCCHHHHCCCCCCE	45.70	-
75	Other	GNAARDNKKTRIIPR CHHHHCCCCCCEEHH	60.87	24681537
76	Other	NAARDNKKTRIIPRH HHHHCCCCCCEEHHH	49.65	24681537
77	Phosphorylation	AARDNKKTRIIPRHL HHHCCCCCCEEHHHH	28.80	23882029
82	Methylation	KKTRIIPRHLQLAIR CCCCEEHHHHHHHHC	32.51	-
89	Methylation	RHLQLAIRNDEELNK HHHHHHHCCHHHHHH	38.65	-
96	Glutarylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	31542297
96	Other	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	27105115
96	Acetylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	22389435
96	Ubiquitination	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	23000965
96	Neddylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	32015554
96	Succinylation	RNDEELNKLLGKVTI CCHHHHHHHHCCEEE	58.68	22389435
100	Acetylation	ELNKLLGKVTIAQGG HHHHHHCCEEECCCC	35.85	24470651
100	Ubiquitination	ELNKLLGKVTIAQGG HHHHHHCCEEECCCC	35.85	23000965
100	Glutarylation	ELNKLLGKVTIAQGG HHHHHHCCEEECCCC	35.85	31542297
102	Phosphorylation	NKLLGKVTIAQGGVL HHHHCCEEECCCCCC	17.68	29802988
105	Methylation	LGKVTIAQGGVLPNI HCCEEECCCCCCCCE	45.37	24352239
119	Neddylation	IQAVLLPKKTESHKA EEEEECCCCCHHHCC	72.76	32015554
119	Acetylation	IQAVLLPKKTESHKA EEEEECCCCCHHHCC	72.76	26051181
119	N6-crotonyl-L-lysine	IQAVLLPKKTESHKA EEEEECCCCCHHHCC	72.76	-
119	Ubiquitination	IQAVLLPKKTESHKA EEEEECCCCCHHHCC	72.76	23000965
119	Other	IQAVLLPKKTESHKA EEEEECCCCCHHHCC	72.76	27105115
119	Glutarylation	IQAVLLPKKTESHKA EEEEECCCCCHHHCC	72.76	31542297
119	Crotonylation	IQAVLLPKKTESHKA EEEEECCCCCHHHCC	72.76	21925322
119	Sumoylation	IQAVLLPKKTESHKA EEEEECCCCCHHHCC	72.76	-
120	Ubiquitination	QAVLLPKKTESHKAK EEEECCCCCHHHCCC	56.43	23000965
120	N6-crotonyl-L-lysine	QAVLLPKKTESHKAK EEEECCCCCHHHCCC	56.43	-
120	Acetylation	QAVLLPKKTESHKAK EEEECCCCCHHHCCC	56.43	30589211
120	Glutarylation	QAVLLPKKTESHKAK EEEECCCCCHHHCCC	56.43	31542297
120	Crotonylation	QAVLLPKKTESHKAK EEEECCCCCHHHCCC	56.43	21925322
121	Phosphorylation	AVLLPKKTESHKAKS EEECCCCCHHHCCCC	49.17	21712546
123	Phosphorylation	LLPKKTESHKAKSK- ECCCCCHHHCCCCC-	35.20	21712546
125	N6-crotonyl-L-lysine	PKKTESHKAKSK--- CCCCHHHCCCCC---	67.78	-
125	Ubiquitination	PKKTESHKAKSK--- CCCCHHHCCCCC---	67.78	23000965
125	Crotonylation	PKKTESHKAKSK--- CCCCHHHCCCCC---	67.78	21925322

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	O75582	Uniprot
121	T	Phosphorylation	Kinase	DCAF1	Q9Y4B6	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	BRCA1	P38398	PMID:11927591
-	K	Ubiquitination	E3 ubiquitin ligase	BMI1	P35226	PMID:16714294
-	K	Ubiquitination	E3 ubiquitin ligase	RNF168	Q8IYW5	PMID:19203578
-	K	Ubiquitination	E3 ubiquitin ligase	RNF2	Q99496	PMID:20351251
-	K	Ubiquitination	E3 ubiquitin ligase	UBR2	Q8IWV8	PMID:22616001
-	K	Ubiquitination	E3 ubiquitin ligase	KDM2B	Q8NHM5	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	RNF8	O76064	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	HUWE1	Q7Z6Z7	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	BMI1#RNF2	P35226#Q99496	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
2	S	Acetylation	15010469
Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1.
2	S	Phosphorylation	15010469
Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1.
2	S	Phosphorylation	15010469
Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis.
2	S	Phosphorylation	15010469
Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription.
4	R	Methylation	15823041
Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.
14	K	ubiquitylation	22980979
Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired.
14	K	ubiquitylation	22980979
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	22980979
Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired.
16	K	ubiquitylation	22980979
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	15386022
Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me).
27	K	ubiquitylation	15386022
Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me).
63	K	ubiquitylation	15386022
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	24352239
Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I.
120	K	ubiquitylation	15386022
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.
120	K	ubiquitylation	15386022
Monoubiquitination of Lys-120 (H2AK119Ub) by TRIM37 may promote transformation of cells in a number of breast cancers.
121	T	Phosphorylation	15078818
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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of H2A2C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CTCFL_HUMAN	CTCFL	physical	17048991
DEK_HUMAN	DEK	physical	16696975
NUCL_HUMAN	NCL	physical	16601700
P66A_HUMAN	GATAD2A	physical	16415179
P66B_HUMAN	GATAD2B	physical	16415179
TAF1A_HUMAN	TAF1A	physical	15136563
AN32A_HUMAN	ANP32A	physical	15136563
TAF1B_HUMAN	TAF1B	physical	15136563
EP300_HUMAN	EP300	physical	15136563
H2B1A_HUMAN	HIST1H2BA	physical	8598932
H31_HUMAN	HIST1H3A	physical	8598932
RBP56_HUMAN	TAF15	physical	8598932
CND2_HUMAN	NCAPH	physical	21633354
H2B1A_HUMAN	HIST1H2BA	physical	22467210
H31_HUMAN	HIST1H3A	physical	22467210
TCF20_HUMAN	TCF20	physical	22081970
UIMC1_HUMAN	UIMC1	physical	19015238
RBBP7_HUMAN	RBBP7	physical	9427644
RBBP4_HUMAN	RBBP4	physical	9427644
UBC_HUMAN	UBC	physical	24526689
H2B2E_HUMAN	HIST2H2BE	physical	24526689
UBP15_HUMAN	USP15	physical	24526689
SART3_HUMAN	SART3	physical	24526689

Drug and Disease Associations

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

Regulatory Network of H2A2C_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Precise characterization of human histones in the H2A gene family bytop down mass spectrometry."; Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.; J. Proteome Res. 5:248-253(2006). Cited for: MASS SPECTROMETRY, AND ACETYLATION AT SER-2 AND LYS-6.	16457589 [Abstract]
"Deimination of histone H2A and H4 at arginine 3 in HL-60granulocytes."; Hagiwara T., Hidaka Y., Yamada M.; Biochemistry 44:5827-5834(2005). Cited for: ACETYLATION AT SER-2, CITRULLINATION AT ARG-4, AND MASS SPECTROMETRY.	15823041 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121 AND SER-123, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 duringmitosis in the early Drosophila embryo."; Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N.,Takio K., Kaneko M., Takeshima Y., Muramatsu M., Ito T.; Genes Dev. 18:877-888(2004). Cited for: PHOSPHORYLATION AT THR-121.	15078818 [Abstract]
Ubiquitylation
Reference	PubMed
"DNA damage triggers nucleotide excision repair-dependentmonoubiquitylation of histone H2A."; Bergink S., Salomons F.A., Hoogstraten D., Groothuis T.A.M.,de Waard H., Wu J., Yuan L., Citterio E., Houtsmuller A.B.,Neefjes J., Hoeijmakers J.H.J., Vermeulen W., Dantuma N.P.; Genes Dev. 20:1343-1352(2006). Cited for: UBIQUITINATION AT LYS-120.	16702407 [Abstract]
"Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox genesilencing."; Cao R., Tsukada Y., Zhang Y.; Mol. Cell 20:845-854(2005). Cited for: UBIQUITINATION AT LYS-120.	16359901 [Abstract]
"Role of histone H2A ubiquitination in Polycomb silencing."; Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P.,Jones R.S., Zhang Y.; Nature 431:873-878(2004). Cited for: UBIQUITINATION AT LYS-120.	15386022 [Abstract]

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