dbPTM

H4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H4_MOUSE
UniProt AC	P62806
Protein Name	Histone H4
Gene Name	Hist1h4a
Organism	Mus musculus (Mouse).
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	Acetylation	------MSGRGKGGK ------CCCCCCCCC	36.88	-
2	Phosphorylation	------MSGRGKGGK ------CCCCCCCCC	36.88	16980586
4	Asymmetric dimethylarginine	----MSGRGKGGKGL ----CCCCCCCCCCC	36.02	-
4	Citrullination	----MSGRGKGGKGL ----CCCCCCCCCCC	36.02	-
4	Methylation	----MSGRGKGGKGL ----CCCCCCCCCCC	36.02	16699504
6	N6-crotonyl-L-lysine	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	Acetylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	23806337
6	Butyrylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	27105113
6	Crotonylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	21925322
6	Glutarylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	Hydroxylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	24681537
6	Lactoylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	Methylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	22693562
6	Other	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	27105115
9	N6-crotonyl-L-lysine	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	Acetylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	23806337
9	Butyrylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	27105113
9	Crotonylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	21925322
9	Hydroxylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	24681537
9	Lactoylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	31645732
9	Malonylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	26320211
9	Other	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	27105115
9	Propionylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
13	N6-crotonyl-L-lysine	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Acetylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	23806337
13	Butyrylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	27105113
13	Crotonylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Glutarylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Hydroxylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	24681537
13	Lactoylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	31645732
13	Methylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Other	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	27105115
13	Succinylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
17	N6-crotonyl-L-lysine	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	Acetylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	23806337
17	Butyrylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	Crotonylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	21925322
17	Hydroxylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	24681537
17	Lactoylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	Methylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	22693562
17	Other	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	24681537
17	Propionylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
21	"N6,N6,N6-trimethyllysine"	GGAKRHRKVLRDNIQ CHHHHHHHHHHHHCC	39.22	-
21	Acetylation	GGAKRHRKVLRDNIQ CHHHHHHHHHHHHCC	39.22	19737024
21	Methylation	GGAKRHRKVLRDNIQ CHHHHHHHHHHHHCC	39.22	15145825
24	Methylation	KRHRKVLRDNIQGIT HHHHHHHHHHCCCCC	37.61	-
32	Acetylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	23806337
32	Butyrylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
32	Glutarylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
32	Hydroxylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	24681537
32	Lactoylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	31645732
32	Malonylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	26320211
32	Other	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	24681537
32	Propionylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
32	Succinylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	22389435
32	Ubiquitination	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
36	Methylation	GITKPAIRRLARRGG CCCHHHHHHHHHCCC	29.66	-
45	Butyrylation	LARRGGVKRISGLIY HHHCCCCCEEECCCH	47.49	-
45	Hydroxylation	LARRGGVKRISGLIY HHHCCCCCEEECCCH	47.49	24681537
45	Other	LARRGGVKRISGLIY HHHCCCCCEEECCCH	47.49	24681537
45	Propionylation	LARRGGVKRISGLIY HHHCCCCCEEECCCH	47.49	-
48	Phosphorylation	RGGVKRISGLIYEET CCCCCEEECCCHHHH	31.42	27087446
52	Phosphorylation	KRISGLIYEETRGVL CEEECCCHHHHHHHH	16.86	21082442
55	Phosphorylation	SGLIYEETRGVLKVF ECCCHHHHHHHHHHH	22.30	19060867
60	Acetylation	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	22826441
60	Glutarylation	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	-
60	Hydroxylation	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	24681537
60	Other	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	24681537
60	Ubiquitination	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	-
73	Phosphorylation	VIRDAVTYTEHAKRK HHHHHHHCCHHHCCC	11.97	25367039
74	Phosphorylation	IRDAVTYTEHAKRKT HHHHHHCCHHHCCCE	16.36	25367039
78	Acetylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	22826441
78	Butyrylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
78	Glutarylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
78	Hydroxylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	24681537
78	Lactoylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
78	Malonylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	26320211
78	Other	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	24681537
78	Propionylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
78	Succinylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	22389435
78	Ubiquitination	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
80	Acetylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	22826441
80	Butyrylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	-
80	Glutarylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	-
80	Hydroxylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	24681537
80	Other	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	24681537
80	Propionylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	-
80	Succinylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	22389435
81	Phosphorylation	TEHAKRKTVTAMDVV CHHHCCCEECHHHHH	27.41	25521595
83	Phosphorylation	HAKRKTVTAMDVVYA HHCCCEECHHHHHHH	22.84	24704852
85	Sulfoxidation	KRKTVTAMDVVYALK CCCEECHHHHHHHHH	2.68	21406390
89	Phosphorylation	VTAMDVVYALKRQGR ECHHHHHHHHHHCCC	13.18	25521595
92	Acetylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	22826441
92	Butyrylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Crotonylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	22693562
92	Glutarylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Hydroxylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	24681537
92	Lactoylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	31645732
92	Other	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	24681537
92	Propionylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Succinylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Succinylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	23806337
92	Ubiquitination	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
97	Phosphorylation	ALKRQGRTLYGFGG- HHHHCCCCEECCCC-	31.02	29514104
99	Phosphorylation	KRQGRTLYGFGG--- HHCCCCEECCCC---	15.14	26026062

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
Oops, there are no upstream regulatory protein records of H4_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
4	R	Citrullination	15145825
Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation.
4	R	Methylation	15145825
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	24049080
Monomethylated at Lys-13 (H4K12me1) by N6AMT1; H4K12me1 modification is present at the promoters of numerous genes encoding cell cycle regulators (By similarity).
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	24049080
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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of H4_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of H4_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of H4_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13 AND LYS-17,AND MASS SPECTROMETRY.	16916647 [Abstract]
Methylation
Reference	PubMed
"Blimp1 associates with Prmt5 and directs histone arginine methylationin mouse germ cells."; Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J.,Kouzarides T., Surani M.A.; Nat. Cell Biol. 8:623-630(2006). Cited for: METHYLATION AT ARG-4.	16699504 [Abstract]
"A silencing pathway to induce H3-K9 and H4-K20 trimethylation atconstitutive heterochromatin."; Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G.,Reinberg D., Jenuwein T.; Genes Dev. 18:1251-1262(2004). Cited for: METHYLATION AT LYS-21.	15145825 [Abstract]
Phosphorylation
Reference	PubMed
"Phosphorylation of histone H4 Ser1 regulates sporulation in yeast andis conserved in fly and mouse spermatogenesis."; Krishnamoorthy T., Chen X., Govin J., Cheung W.L., Dorsey J.,Schindler K., Winter E., Allis C.D., Guacci V., Khochbin S.,Fuller M.T., Berger S.L.; Genes Dev. 20:2580-2592(2006). Cited for: PHOSPHORYLATION AT SER-2.	16980586 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52 AND TYR-89, AND MASSSPECTROMETRY.	18034455 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, AND MASSSPECTROMETRY.	17947660 [Abstract]

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show

show