dbPTM

H2A1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2A1B_HUMAN
UniProt AC	P04908
Protein Name	Histone H2A type 1-B/E
Gene Name	HIST1H2AB
Organism	Homo sapiens (Human).
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	MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGRGKQGG ------CCCCCCCCC	36.88	15823041
2	Acetylation	------MSGRGKQGG ------CCCCCCCCC	36.88	15823041
4	Methylation	----MSGRGKQGGKA ----CCCCCCCCCHH	41.66	-
4	Citrullination	----MSGRGKQGGKA ----CCCCCCCCCHH	41.66	15823041
4	Citrullination	----MSGRGKQGGKA ----CCCCCCCCCHH	41.66	-
6	Methylation	--MSGRGKQGGKARA --CCCCCCCCCHHCH	44.39	30589189
6	Other	--MSGRGKQGGKARA --CCCCCCCCCHHCH	44.39	24681537
6	Acetylation	--MSGRGKQGGKARA --CCCCCCCCCHHCH	44.39	16319397
10	Lactoylation	GRGKQGGKARAKAKT CCCCCCCHHCHHHHH	41.34	-
10	Other	GRGKQGGKARAKAKT CCCCCCCHHCHHHHH	41.34	27105115
10	Succinylation	GRGKQGGKARAKAKT CCCCCCCHHCHHHHH	41.34	22389435
10	Acetylation	GRGKQGGKARAKAKT CCCCCCCHHCHHHHH	41.34	21466224
14	Acetylation	QGGKARAKAKTRSSR CCCHHCHHHHHHHHC	44.88	-
14	Other	QGGKARAKAKTRSSR CCCHHCHHHHHHHHC	44.88	27105115
14	Ubiquitination	QGGKARAKAKTRSSR CCCHHCHHHHHHHHC	44.88	22980979
16	Ubiquitination	GKARAKAKTRSSRAG CHHCHHHHHHHHCCC	43.71	22980979
17	Phosphorylation	KARAKAKTRSSRAGL HHCHHHHHHHHCCCC	40.41	23882029
19	Phosphorylation	RAKAKTRSSRAGLQF CHHHHHHHHCCCCCC	29.43	23312004
20	Phosphorylation	AKAKTRSSRAGLQFP HHHHHHHHCCCCCCC	23.90	27966365
21	Methylation	KAKTRSSRAGLQFPV HHHHHHHCCCCCCCH	33.64	-
30	Methylation	GLQFPVGRVHRLLRK CCCCCHHHHHHHHHC	22.69	-
37	Other	RVHRLLRKGNYSERV HHHHHHHCCCCHHCC	52.02	27105115
37	Crotonylation	RVHRLLRKGNYSERV HHHHHHHCCCCHHCC	52.02	21925322
37	N6-crotonyl-L-lysine	RVHRLLRKGNYSERV HHHHHHHCCCCHHCC	52.02	-
37	Ubiquitination	RVHRLLRKGNYSERV HHHHHHHCCCCHHCC	52.02	-
58	Phosphorylation	YLAAVLEYLTAEILE HHHHHHHHHHHHHHH	12.75	-
75	Other	GNAARDNKKTRIIPR CHHHHCCCCCCEEHH	60.87	24681537
75	Methylation	GNAARDNKKTRIIPR CHHHHCCCCCCEEHH	60.87	12937907
76	Methylation	NAARDNKKTRIIPRH HHHHCCCCCCEEHHH	49.65	12937907
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	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	31542297
96	Malonylation	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	26320211
96	Succinylation	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	19608861
96	Other	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	27105115
96	Ubiquitination	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	19608861
96	Acetylation	RNDEELNKLLGRVTI CCHHHHHHHHCCEEE	58.68	25825284
100	Methylation	ELNKLLGRVTIAQGG HHHHHHCCEEECCCC	23.52	-
102	Phosphorylation	NKLLGRVTIAQGGVL HHHHCCEEECCCCCC	14.83	24732914
105	Methylation	LGRVTIAQGGVLPNI HCCEEECCCCCCCCE	45.37	24352239
119	Sumoylation	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	-
119	Ubiquitination	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	21890473
119	Ubiquitination	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	15852347
119	Other	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	27105115
119	N6-crotonyl-L-lysine	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	-
119	Neddylation	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	-
119	Acetylation	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	25953088
119	Glutarylation	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	31542297
119	Crotonylation	IQAVLLPKKTESHHK EEEEECCCCCHHHHH	72.76	21925322
120	Neddylation	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	-
120	N6-crotonyl-L-lysine	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	-
120	Ubiquitination	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	25470042
120	Acetylation	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	30589197
120	Sumoylation	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	-
120	Crotonylation	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	21925322
120	Glutarylation	QAVLLPKKTESHHKA EEEECCCCCHHHHHC	56.43	31542297
121	Phosphorylation	AVLLPKKTESHHKAK EEECCCCCHHHHHCC	49.17	25159151
123	Phosphorylation	LLPKKTESHHKAKGK ECCCCCHHHHHCCCC	35.80	25159151
126	Crotonylation	KKTESHHKAKGK--- CCCHHHHHCCCC---	46.50	21925322
126	Acetylation	KKTESHHKAKGK--- CCCHHHHHCCCC---	46.50	19666589
126	Ubiquitination	KKTESHHKAKGK--- CCCHHHHHCCCC---	46.50	-
126	N6-crotonyl-L-lysine	KKTESHHKAKGK--- CCCHHHHHCCCC---	46.50	-
126	Glutarylation	KKTESHHKAKGK--- CCCHHHHHCCCC---	46.50	31542297
128	Acetylation	TESHHKAKGK----- CHHHHHCCCC-----	72.53	19666589
128	Ubiquitination	TESHHKAKGK----- CHHHHHCCCC-----	72.53	-
130	Acetylation	SHHKAKGK------- HHHHCCCC-------	57.36	19666589
130	Ubiquitination	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	O75582	Uniprot
121	T	Phosphorylation	Kinase	DCAF1	Q9Y4B6	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	DZIP3	Q86Y13	PMID:18206970
-	K	Ubiquitination	E3 ubiquitin ligase	BRCA1	P38398	PMID:25131202
-	K	Ubiquitination	E3 ubiquitin ligase	PRC1	O43663	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	BMI1	P35226	PMID:16359901
-	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 H2A1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of H2A1B_HUMAN !!

Drug and Disease Associations

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

Regulatory Network of H2A1B_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.	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]
"Global regulation of post-translational modifications on corehistones."; Galasinski S.C., Louie D.F., Gloor K.K., Resing K.A., Ahn N.G.; J. Biol. Chem. 277:2579-2588(2002). Cited for: IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-2, ANDACETYLATION AT SER-2.	11709551 [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
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-119, AND MASSSPECTROMETRY.	18781797 [Abstract]
"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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