dbPTM

H4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H4_HUMAN
UniProt AC	P62805
Protein Name	Histone H4
Gene Name	HIST1H4A
Organism	Homo sapiens (Human).
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	17967882
2	Phosphorylation	------MSGRGKGGK ------CCCCCCCCC	36.88	16319397
4	Asymmetric dimethylarginine	----MSGRGKGGKGL ----CCCCCCCCCCC	36.02	-
4	Citrullination	----MSGRGKGGKGL ----CCCCCCCCCCC	36.02	15345777
4	Methylation	----MSGRGKGGKGL ----CCCCCCCCCCC	36.02	11387442
6	N6-crotonyl-L-lysine	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	Acetylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	19608861
6	Butyrylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	27105113
6	Crotonylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	21925322
6	Glutarylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	31542297
6	Lactoylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	31645732
6	Lactylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	31645732
6	Neddylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
6	Other	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	24681537
6	Propionylation	--MSGRGKGGKGLGK --CCCCCCCCCCCCC	64.23	-
9	N6-crotonyl-L-lysine	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	2-Hydroxyisobutyrylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	Acetylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	19608861
9	Butyrylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	27105113
9	Crotonylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	21925322
9	Lactoylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	31645732
9	Lactylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	31645732
9	Neddylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	-
9	Other	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	27105115
9	Propionylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	17267393
9	Sumoylation	SGRGKGGKGLGKGGA CCCCCCCCCCCCCHH	60.68	2474456
13	N6-crotonyl-L-lysine	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Acetylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	17967882
13	Butyrylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	27105113
13	Crotonylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	21925322
13	Glutarylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	31542297
13	Lactoylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	31645732
13	Lactylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	31645732
13	Methylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	17967882
13	Neddylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Other	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	27105115
13	Propionylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	-
13	Succinylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	17967882
13	Sumoylation	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	17967882
13	Ubiquitination	KGGKGLGKGGAKRHR CCCCCCCCCHHHHHH	60.25	17967882
17	N6-crotonyl-L-lysine	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	Acetylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	17967882
17	Butyrylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	27105113
17	Crotonylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	Lactoylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	31645732
17	Lactylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	31645732
17	Methylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	Neddylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	-
17	Other	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	24681537
17	Propionylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	17267393
17	Sumoylation	GLGKGGAKRHRKVLR CCCCCHHHHHHHHHH	52.60	17967882
21	"N6,N6,N6-trimethyllysine"	GGAKRHRKVLRDNIQ CHHHHHHHHHHHHCC	39.22	-
21	Acetylation	GGAKRHRKVLRDNIQ CHHHHHHHHHHHHCC	39.22	17967882
21	Methylation	GGAKRHRKVLRDNIQ CHHHHHHHHHHHHCC	39.22	15964846
21	Neddylation	GGAKRHRKVLRDNIQ CHHHHHHHHHHHHCC	39.22	-
21	Sumoylation	GGAKRHRKVLRDNIQ CHHHHHHHHHHHHCC	39.22	17967882
24	Methylation	KRHRKVLRDNIQGIT HHHHHHHHHHCCCCC	37.61	-
31	Phosphorylation	RDNIQGITKPAIRRL HHHCCCCCHHHHHHH	37.49	30266825
32	2-Hydroxyisobutyrylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
32	Acetylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	19608861
32	Butyrylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	17267393
32	Glutarylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	31542297
32	Lactoylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	31645732
32	Methylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	19608861
32	Neddylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	-
32	Other	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	27105115
32	Propionylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	17267393
32	Succinylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	19608861
32	Sumoylation	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	28112733
32	Ubiquitination	DNIQGITKPAIRRLA HHCCCCCHHHHHHHH	30.45	20639865
45	Acetylation	LARRGGVKRISGLIY HHHCCCCCEEECCCH	47.49	17267393
45	Butyrylation	LARRGGVKRISGLIY HHHCCCCCEEECCCH	47.49	17267393
45	Other	LARRGGVKRISGLIY HHHCCCCCEEECCCH	47.49	24681537
45	Propionylation	LARRGGVKRISGLIY HHHCCCCCEEECCCH	47.49	17267393
46	Methylation	ARRGGVKRISGLIYE HHCCCCCEEECCCHH	26.37	-
48	O-linked_Glycosylation	RGGVKRISGLIYEET CCCCCEEECCCHHHH	31.42	21045127
48	Phosphorylation	RGGVKRISGLIYEET CCCCCEEECCCHHHH	31.42	29255136
52	Nitration	KRISGLIYEETRGVL CEEECCCHHHHHHHH	16.86	-
52	Phosphorylation	KRISGLIYEETRGVL CEEECCCHHHHHHHH	16.86	23927012
55	Phosphorylation	SGLIYEETRGVLKVF ECCCHHHHHHHHHHH	22.30	23927012
56	Methylation	GLIYEETRGVLKVFL CCCHHHHHHHHHHHH	36.18	-
60	2-Hydroxyisobutyrylation	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	-
60	Acetylation	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	21466224
60	Glutarylation	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	31542297
60	Methylation	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	12937907
60	Other	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	24681537
60	Sumoylation	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	28112733
60	Ubiquitination	EETRGVLKVFLENVI HHHHHHHHHHHHHHH	28.65	21906983
68	Methylation	VFLENVIRDAVTYTE HHHHHHHHHHHHCCH	22.89	-
72	Phosphorylation	NVIRDAVTYTEHAKR HHHHHHHHCCHHHCC	26.84	28152594
73	Nitration	VIRDAVTYTEHAKRK HHHHHHHCCHHHCCC	11.97	-
73	Phosphorylation	VIRDAVTYTEHAKRK HHHHHHHCCHHHCCC	11.97	25159151
74	Phosphorylation	IRDAVTYTEHAKRKT HHHHHHCCHHHCCCE	16.36	28152594
78	2-Hydroxyisobutyrylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	-
78	Acetylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	26051181
78	Butyrylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	17267393
78	Glutarylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	31542297
78	Hydroxylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	24681537
78	Lactoylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	31645732
78	Methylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	22389435
78	Other	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	27105115
78	Propionylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	17267393
78	Succinylation	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	22389435
78	Ubiquitination	VTYTEHAKRKTVTAM HHCCHHHCCCEECHH	57.23	21890473
80	2-Hydroxyisobutyrylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	-
80	Acetylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	25825284
80	Butyrylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	17267393
80	Glutarylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	31542297
80	Malonylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	26320211
80	Methylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	23161681
80	Other	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	24681537
80	Propionylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	17267393
80	Succinylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	-
80	Sumoylation	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	28112733
80	Ubiquitination	YTEHAKRKTVTAMDV CCHHHCCCEECHHHH	46.79	21890473
81	Phosphorylation	TEHAKRKTVTAMDVV CHHHCCCEECHHHHH	27.41	20164059
83	Phosphorylation	HAKRKTVTAMDVVYA HHCCCEECHHHHHHH	22.84	21712546
85	Sulfoxidation	KRKTVTAMDVVYALK CCCEECHHHHHHHHH	2.68	28465586
89	Nitration	VTAMDVVYALKRQGR ECHHHHHHHHHHCCC	13.18	-
89	Phosphorylation	VTAMDVVYALKRQGR ECHHHHHHHHHHCCC	13.18	20164059
92	2-Hydroxyisobutyrylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Acetylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	22389435
92	Butyrylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	17267393
92	Glutarylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	31542297
92	Lactoylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	31645732
92	Methylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	22389435
92	Other	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	27105115
92	Propionylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	17267393
92	Succinylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	-
92	Succinylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	22389435
92	Sumoylation	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	28112733
92	Ubiquitination	MDVVYALKRQGRTLY HHHHHHHHHCCCCEE	34.21	21890473
97	Phosphorylation	ALKRQGRTLYGFGG- HHHHCCCCEECCCC-	31.02	28152594
99	Phosphorylation	KRQGRTLYGFGG--- HHCCCCEECCCC---	15.14	28152594

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
1	S	Phosphorylation	Kinase	TRPM6	Q9BX84	GPS
47	S	Phosphorylation	Kinase	PAK2	Q13177	PSP
48	S	Phosphorylation	Kinase	PAK2	Q13177	Uniprot
88	Y	Phosphorylation	Kinase	TNK2	Q07912	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	DTX3L	Q8TDB6	PMID:19818714
-	K	Ubiquitination	E3 ubiquitin ligase	HUWE1	Q7Z6Z7	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
4	R	Citrullination	30275017
Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation.
4	R	Methylation	30275017
Citrullination at Arg-4 (H4R3ci) by PADI4 impairs methylation.
4	R	Methylation	30275017
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	30275017
Symmetric dimethylation on Arg-4 (H4R3me2s) by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.
4	R	Acetylation	30275017
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	2474456
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	15345777
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	15345777
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	2474456
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	23546875
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	23546875
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	23546875
Monomethylated at Lys-13 (H4K12me1) by N6AMT1; H4K12me1 modification is present at the promoters of numerous genes encoding cell cycle regulators.
13	K	Methylation	23546875
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	2474456
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	17967882
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).
21	K	Methylation	12086618
Monomethylated, dimethylated or trimethylated at Lys-21 (H4K20me1, H4K20me2, H4K20me3).
48	S	Phosphorylation	17967882
Phosphorylated by PAK2 at Ser-48 (H4S47ph).
92	K	Glutarylation	31542297
Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes.
92	K	ubiquitylation	17967882
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
BPTF_HUMAN	BPTF	physical	21596426
A4_HUMAN	APP	physical	21832049

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
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.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
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 H4_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Certain and progressive methylation of histone H4 at lysine 20 duringthe cell cycle."; Pesavento J.J., Yang H., Kelleher N.L., Mizzen C.A.; Mol. Cell. Biol. 28:468-486(2008). Cited for: ACETYLATION AT SER-2; LYS-13 AND LYS-17, PHOSPHORYLATION AT SER-2, ANDMETHYLATION AT LYS-21.	17967882 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13; LYS-17;LYS-32 AND LYS-60, AND MASS SPECTROMETRY.	19608861 [Abstract]
"BBAP monoubiquitylates histone H4 at lysine 91 and selectivelymodulates the DNA damage response."; Yan Q., Dutt S., Xu R., Graves K., Juszczynski P., Manis J.P.,Shipp M.A.; Mol. Cell 36:110-120(2009). Cited for: ACETYLATION AT LYS-92, AND UBIQUITINATION AT LYS-92.	19818714 [Abstract]
"Characterization of histones H2A and H2B variants and their post-translational modifications by mass spectrometry."; Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.; Mol. Cell. Proteomics 5:541-552(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9 AND LYS-13,METHYLATION AT LYS-21, PHOSPHORYLATION AT SER-2, AND MASSSPECTROMETRY.	16319397 [Abstract]
"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]
"Histone H4 acetylation in human cells. Frequency of acetylation atdifferent sites defined by immunolabeling with site-specificantibodies."; Turner B.M., O'Neill L.P., Allan I.M.; FEBS Lett. 253:141-145(1989). Cited for: ACETYLATION AT LYS-6; LYS-9; LYS-13 AND LYS-17.	2474456 [Abstract]
"Histone H4 acetylation distinguishes coding regions of the humangenome from heterochromatin in a differentiation-dependent buttranscription-independent manner."; O'Neill L.P., Turner B.M.; EMBO J. 14:3946-3957(1995). Cited for: ACETYLATION AT LYS-6; LYS-9; LYS-13 AND LYS-17.	7664735 [Abstract]
Methylation
Reference	PubMed
"Human PAD4 regulates histone arginine methylation levels viademethylimination."; Wang Y., Wysocka J., Sayegh J., Lee Y.-H., Perlin J.R., Leonelli L.,Sonbuchner L.S., McDonald C.H., Cook R.G., Dou Y., Roeder R.G.,Clarke S., Stallcup M.R., Allis C.D., Coonrod S.A.; Science 306:279-283(2004). Cited for: CITRULLINATION AT ARG-4, AND METHYLATION AT ARG-4.	15345777 [Abstract]
"Methylation of histone H4 at arginine 3 facilitating transcriptionalactivation by nuclear hormone receptor."; Wang H., Huang Z.-Q., Xia L., Feng Q., Erdjument-Bromage H.,Strahl B.D., Briggs S.D., Allis C.D., Wong J., Tempst P., Zhang Y.; Science 293:853-857(2001). Cited for: METHYLATION AT ARG-4.	11387442 [Abstract]
"Methylation of histone H4 at arginine 3 occurs in vivo and ismediated by the nuclear receptor coactivator PRMT1."; Strahl B.D., Briggs S.D., Brame C.J., Caldwell J.A., Koh S.S., Ma H.,Cook R.G., Shabanowitz J., Hunt D.F., Stallcup M.R., Allis C.D.; Curr. Biol. 11:996-1000(2001). Cited for: METHYLATION AT ARG-4.	11448779 [Abstract]
"Certain and progressive methylation of histone H4 at lysine 20 duringthe cell cycle."; Pesavento J.J., Yang H., Kelleher N.L., Mizzen C.A.; Mol. Cell. Biol. 28:468-486(2008). Cited for: ACETYLATION AT SER-2; LYS-13 AND LYS-17, PHOSPHORYLATION AT SER-2, ANDMETHYLATION AT LYS-21.	17967882 [Abstract]
"Characterization of histones H2A and H2B variants and their post-translational modifications by mass spectrometry."; Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.; Mol. Cell. Proteomics 5:541-552(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9 AND LYS-13,METHYLATION AT LYS-21, PHOSPHORYLATION AT SER-2, AND MASSSPECTROMETRY.	16319397 [Abstract]
"SET8 recognizes the sequence RHRK20VLRDN within the N terminus ofhistone H4 and mono-methylates lysine 20."; Yin Y., Liu C., Tsai S.N., Zhou B., Ngai S.M., Zhu G.; J. Biol. Chem. 280:30025-30031(2005). Cited for: METHYLATION AT LYS-21.	15964846 [Abstract]
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC."; Ong S.E., Mittler G., Mann M.; Nat. Methods 1:119-126(2004). Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT LYS-21, AND MASS SPECTROMETRY.	15782174 [Abstract]
"PR-Set7 is a nucleosome-specific methyltransferase that modifieslysine 20 of histone H4 and is associated with silent chromatin."; Nishioka K., Rice J.C., Sarma K., Erdjument-Bromage H., Werner J.,Wang Y., Chuikov S., Valenzuela P., Tempst P., Steward R., Lis J.T.,Allis C.D., Reinberg D.; Mol. Cell 9:1201-1213(2002). Cited for: METHYLATION AT LYS-21.	12086618 [Abstract]
Phosphorylation
Reference	PubMed
"Phosphorylation of H4 Ser 47 promotes HIRA-mediated nucleosomeassembly."; Kang B., Pu M., Hu G., Wen W., Dong Z., Zhao K., Stillman B.,Zhang Z.; Genes Dev. 25:1359-1364(2011). Cited for: PHOSPHORYLATION AT SER-48.	21724829 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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 SER-48, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Certain and progressive methylation of histone H4 at lysine 20 duringthe cell cycle."; Pesavento J.J., Yang H., Kelleher N.L., Mizzen C.A.; Mol. Cell. Biol. 28:468-486(2008). Cited for: ACETYLATION AT SER-2; LYS-13 AND LYS-17, PHOSPHORYLATION AT SER-2, ANDMETHYLATION AT LYS-21.	17967882 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Phosphoproteomic analysis of the human pituitary."; Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.; Pituitary 9:109-120(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY.	16807684 [Abstract]
"Characterization of histones H2A and H2B variants and their post-translational modifications by mass spectrometry."; Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.; Mol. Cell. Proteomics 5:541-552(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9 AND LYS-13,METHYLATION AT LYS-21, PHOSPHORYLATION AT SER-2, AND MASSSPECTROMETRY.	16319397 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52 AND TYR-89, AND MASSSPECTROMETRY.	18083107 [Abstract]
Ubiquitylation
Reference	PubMed
"BBAP monoubiquitylates histone H4 at lysine 91 and selectivelymodulates the DNA damage response."; Yan Q., Dutt S., Xu R., Graves K., Juszczynski P., Manis J.P.,Shipp M.A.; Mol. Cell 36:110-120(2009). Cited for: ACETYLATION AT LYS-92, AND UBIQUITINATION AT LYS-92.	19818714 [Abstract]

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