H4_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H4_RAT
• UniProt AC: P62804
• Protein Name: Histone H4
• Gene Name: Hist1h4b
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 103
• Subcellular Localization: Nucleus . Chromosome . Osteogenic growth peptide is secreted by a mechanism independent from a hydrophobic signal sequence. The mature peptide may be imported into secretory lysosomes by an ABCA1-related protein.
• 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.; Osteogenic growth peptide (OGP) stimulates osteogenesis and hematopoiesis..
• Protein Sequence: MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

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	Acetylation	------MSGRGKGGK ------CCCCCCCCC	36.88	5171427
2	Phosphorylation	------MSGRGKGGK ------CCCCCCCCC	36.88	-
4	Methylation	----MSGRGKGGKGL ----CCCCCCCCCCC	36.02	-
4	Asymmetric dimethylarginine	----MSGRGKGGKGL ----CCCCCCCCCCC	36.02	-
4	Citrullination	----MSGRGKGGKGL ----CCCCCCCCCCC	36.02	-
6	Glutarylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	Butyrylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	Crotonylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	Other	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	Acetylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	26302492
6	Lactoylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	N6-crotonyl-L-lysine	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
9	N6-crotonyl-L-lysine	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	Crotonylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	Other	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	Butyrylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	Lactoylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	Propionylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	Acetylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	26302492
13	Butyrylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Lactoylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	N6-crotonyl-L-lysine	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Methylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Glutarylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Acetylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	26302492
13	Crotonylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Succinylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Other	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
17	Acetylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	5171427
17	Crotonylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	Butyrylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	Lactoylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	N6-crotonyl-L-lysine	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	Propionylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	Other	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
21	"N6,N6,N6-trimethyllysine"	GGAKRHRKVLRDNIQ CHHHHHHHHHHHHCC	39.22	-
21	Methylation	GGAKRHRKVLRDNIQ CHHHHHHHHHHHHCC	39.22	5171427
32	Succinylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	26843850
32	Propionylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
32	Other	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
32	Lactoylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
32	Glutarylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
32	Acetylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	22902405
32	Butyrylation	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	23712012
52	Phosphorylation	KRISGLIYEETRGVL CEEECCCHHHHHHHH	16.86	27097102
55	Phosphorylation	SGLIYEETRGVLKVF ECCCHHHHHHHHHHH	22.30	27097102
60	Glutarylation	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	-
60	Acetylation	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	25786129
60	Other	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	-
78	Succinylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
78	Propionylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
78	Lactoylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
78	Acetylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	25786129
78	Glutarylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
78	Butyrylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
78	Other	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
80	Glutarylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	-
80	Butyrylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	-
80	Other	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	-
80	Propionylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	-
80	Succinylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	-
80	Acetylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	22902405
81	Phosphorylation	TEHAKRKTVTAMDVV CHHHCCCEECHHHHH	27.41	27097102
83	Phosphorylation	HAKRKTVTAMDVVYA HHCCCEECHHHHHHH	22.84	28432305
89	Phosphorylation	VTAMDVVYALKRQGR ECHHHHHHHHHHCCC	13.18	27097102
92	Succinylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Acetylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	25786129
92	Succinylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Propionylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Butyrylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Other	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Glutarylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Lactoylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of H4_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
4	R	Citrullination	Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation.	-
4	R	Methylation	Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation.	-
4	R	Methylation	Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac).	-
4	R	Methylation	Symmetric dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage (By similarity).	-
4	R	Acetylation	Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac).	-
6	K	Acetylation	Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in heterochromatin.	-
9	K	Methylation	Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac).	-
9	K	Acetylation	Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac).	-
9	K	Acetylation	Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in heterochromatin.	-
13	K	Acetylation	Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in heterochromatin.	-
13	K	Acetylation	Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac).	-
13	K	Methylation	Monomethylated at Lys-13 (H4K12me1) by N6AMT1; H4K12me1 modification is present at the promoters of numerous genes encoding cell cycle regulators.	-
13	K	Methylation	Monomethylation and asymmetric dimethylation at Arg-4 (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation at Lys-9 (H4K8ac) and Lys-13 (H4K12ac).	-
17	K	Acetylation	Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13 (H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the genome but not in heterochromatin.	-
21	K	Methylation	The exact role of H4K91ub1 in DNA damage response is still unclear but it may function as a licensing signal for additional histone H4 post-translational modifications such as H4 Lys-21 methylation (H4K20me) (By similarity).	-
21	K	Methylation	Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1, H4K20me2, H4K20me3).	-
48	S	Phosphorylation	Phosphorylated by PAK2 at Ser-48 (H4S47ph).	-
92	K	Glutarylation	Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes.	-
92	K	ubiquitylation	Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in response to DNA damage.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of H4_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of H4_RAT !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"Primary structure of glycine-rich and arginine-rich histone isolatedfrom chloroleukemic tumor of the rat.";
Sautiere P., Tyrou D., Moschetto Y., Biserte G.;
Biochimie 53:479-483(1971).
Cited for: PROTEIN SEQUENCE OF 2-103, ACETYLATION AT SER-2 AND LYS-17, ANDMETHYLATION AT LYS-21.
PubMed: 5171427

Methylation

"Primary structure of glycine-rich and arginine-rich histone isolatedfrom chloroleukemic tumor of the rat.";
Sautiere P., Tyrou D., Moschetto Y., Biserte G.;
Biochimie 53:479-483(1971).
Cited for: PROTEIN SEQUENCE OF 2-103, ACETYLATION AT SER-2 AND LYS-17, ANDMETHYLATION AT LYS-21.
PubMed: 5171427