dbPTM

H4_BOVIN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H4_BOVIN
UniProt AC	P62803
Protein Name	Histone H4
Gene Name
Organism	Bos taurus (Bovine).
Sequence Length	103
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	MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGRGKGGK ------CCCCCCCCC	36.88	-
2	Acetylation	------MSGRGKGGK ------CCCCCCCCC	36.88	4321977
4	Citrullination	----MSGRGKGGKGL ----CCCCCCCCCCC	36.02	-
4	Methylation	----MSGRGKGGKGL ----CCCCCCCCCCC	36.02	-
4	Asymmetric dimethylarginine	----MSGRGKGGKGL ----CCCCCCCCCCC	36.02	-
6	Acetylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	Other	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	Lactoylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	Glutarylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	Crotonylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	Butyrylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	N6-crotonyl-L-lysine	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
9	Other	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	N6-crotonyl-L-lysine	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	Acetylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	Propionylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	Butyrylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	Crotonylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	Lactoylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
13	Other	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Succinylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Glutarylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Butyrylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Methylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Crotonylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Lactoylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Acetylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	N6-crotonyl-L-lysine	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
17	Other	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	N6-crotonyl-L-lysine	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	Acetylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	4321977
17	Crotonylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	Lactoylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	Butyrylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	Propionylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
21	Methylation	GGAKRHRKVLRDNIQ CHHHHHHHHHHHHCC	39.22	4321977
21	"N6,N6,N6-trimethyllysine"	GGAKRHRKVLRDNIQ CHHHHHHHHHHHHCC	39.22	-
32	Glutarylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
32	Propionylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
32	Lactoylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
32	Succinylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
32	Butyrylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
32	Acetylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
32	Other	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
45	Propionylation	LARRGGVKRISGLIY HHHCCCCCEEECCCH	47.49	-
45	Butyrylation	LARRGGVKRISGLIY HHHCCCCCEEECCCH	47.49	-
45	Other	LARRGGVKRISGLIY HHHCCCCCEEECCCH	47.49	-
48	Phosphorylation	RGGVKRISGLIYEET CCCCCEEECCCHHHH	31.42	-
52	Phosphorylation	KRISGLIYEETRGVL CEEECCCHHHHHHHH	16.86	-
60	Other	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	-
60	Glutarylation	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	-
78	Other	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
78	Lactoylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
78	Propionylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
78	Butyrylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
78	Glutarylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
78	Succinylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
80	Butyrylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	-
80	Propionylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	-
80	Glutarylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	-
80	Succinylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	-
80	Other	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	-
81	Phosphorylation	TEHAKRKTVTAMDVV CHHHCCCEECHHHHH	27.41	-
89	Phosphorylation	VTAMDVVYALKRQGR ECHHHHHHHHHHCCC	13.18	-
92	Lactoylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Glutarylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Succinylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Acetylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Other	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Butyrylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Propionylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Succinylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-

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
48	S	Phosphorylation	Kinase	PAK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of H4_BOVIN !!

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 H4_BOVIN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
BRM_ARATH	BRM	physical	17825834

Drug and Disease Associations

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

Regulatory Network of H4_BOVIN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Structure of the glycine-rich, arginine-rich histone of the Novikoffhepatoma."; Wilson R.K., Starbuck W.C., Taylor C.W., Jordan J.J., Busch H.; Cancer Res. 30:2942-2951(1970). Cited for: PROTEIN SEQUENCE OF 2-103, ACETYLATION AT SER-2 AND LYS-17, ANDMETHYLATION AT LYS-21.	4321977 [Abstract]
Methylation
Reference	PubMed
"Structure of the glycine-rich, arginine-rich histone of the Novikoffhepatoma."; Wilson R.K., Starbuck W.C., Taylor C.W., Jordan J.J., Busch H.; Cancer Res. 30:2942-2951(1970). Cited for: PROTEIN SEQUENCE OF 2-103, ACETYLATION AT SER-2 AND LYS-17, ANDMETHYLATION AT LYS-21.	4321977 [Abstract]