H31_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H31_HUMAN
• UniProt AC: P68431
• Protein Name: Histone H3.1
• Gene Name: HIST1H3A
• Organism: Homo sapiens (Human).
• Sequence Length: 136
• 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: MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA

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
3	Asymmetric dimethylarginine	-----MARTKQTARK -----CCCCCHHHHH	40.95	-
3	Citrullination	-----MARTKQTARK -----CCCCCHHHHH	40.95	16567635
3	Methylation	-----MARTKQTARK -----CCCCCHHHHH	40.95	18077460
4	Acetylation	----MARTKQTARKS ----CCCCCHHHHHC	20.26	44085
4	Phosphorylation	----MARTKQTARKS ----CCCCCHHHHHC	20.26	16185088
5	Allysine	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
5	Acetylation	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	16267050
5	Crotonylation	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	21925322
5	Deamination	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	27735137
5	Methylation	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	16457588
5	Other	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	27105115
6	Formation of an isopeptide bond	--MARTKQTARKSTG --CCCCCHHHHHCCC	39.52	32273471
6	Serotonylation	--MARTKQTARKSTG --CCCCCHHHHHCCC	39.52	30867594
7	Phosphorylation	-MARTKQTARKSTGG -CCCCCHHHHHCCCC	29.95	22817900
9	Citrullination	ARTKQTARKSTGGKA CCCCHHHHHCCCCCC	36.52	-
9	Citrullination	ARTKQTARKSTGGKA CCCCHHHHHCCCCCC	36.52	15345777
9	Methylation	ARTKQTARKSTGGKA CCCCHHHHHCCCCCC	36.52	-
10	"N6,N6,N6-trimethyllysine"	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
10	Acetylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	11242053
10	Butyrylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	27105113
10	Crotonylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	21925322
10	Lactoylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	31645732
10	Lactylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	31645732
10	Methylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	11242053
10	Other	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	27105115
10	Ubiquitination	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	22817900
11	ADP-ribosylation	TKQTARKSTGGKAPR CCHHHHHCCCCCCCH	27.08	28190768
11	O-linked_Glycosylation	TKQTARKSTGGKAPR CCHHHHHCCCCCCCH	27.08	22371497
11	Phosphorylation	TKQTARKSTGGKAPR CCHHHHHCCCCCCCH	27.08	20171103
12	Phosphorylation	KQTARKSTGGKAPRK CHHHHHCCCCCCCHH	53.65	18066052
15	Acetylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	16457588
15	Glutarylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	31542297
15	Lactoylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
15	Lactylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	31645732
15	Methylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	16457588
15	Other	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	27105115
15	Succinylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	16457588
15	Sumoylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	16457588
15	Ubiquitination	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	23000965
18	Asymmetric dimethylarginine	STGGKAPRKQLATKA CCCCCCCHHHHHHHH	44.18	-
18	Citrullination	STGGKAPRKQLATKA CCCCCCCHHHHHHHH	44.18	16567635
18	Methylation	STGGKAPRKQLATKA CCCCCCCHHHHHHHH	44.18	15345777
19	N6-crotonyl-L-lysine	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Acetylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	16267050
19	Butyrylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	27105113
19	Crotonylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	21925322
19	Glutarylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	31542297
19	Lactoylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	31645732
19	Lactylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	31645732
19	Methylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	16267050
19	Other	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	27105115
19	Sumoylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	17194708
19	Ubiquitination	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	23000965
24	N6-crotonyl-L-lysine	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Acetylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	16457588
24	Butyrylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	27105113
24	Crotonylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	21925322
24	Glutarylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	31542297
24	Lactoylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	31645732
24	Lactylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	31645732
24	Methylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	16457588
24	Other	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	27105115
24	Propionylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Sumoylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	17194708
24	Ubiquitination	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	23000965
27	Citrullination	QLATKAARKSAPATG HHHHHHHHHHCCCCC	38.02	-
27	Citrullination	QLATKAARKSAPATG HHHHHHHHHHCCCCC	38.02	16567635
27	Methylation	QLATKAARKSAPATG HHHHHHHHHHCCCCC	38.02	-
28	"N6,N6,N6-trimethyllysine"	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	-
28	Acetylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	17194708
28	Crotonylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	21925322
28	Glutarylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	31542297
28	Lactoylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	31645732
28	Lactylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	31645732
28	Methylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	17194708
28	Other	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	27105115
28	Ubiquitination	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	23000965
29	ADP-ribosylation	ATKAARKSAPATGGV HHHHHHHHCCCCCCC	33.65	28190768
29	O-linked_Glycosylation	ATKAARKSAPATGGV HHHHHHHHCCCCCCC	33.65	22371497
29	Phosphorylation	ATKAARKSAPATGGV HHHHHHHHCCCCCCC	33.65	25159151
33	O-linked_Glycosylation	ARKSAPATGGVKKPH HHHHCCCCCCCCCCC	33.15	22371497
33	Phosphorylation	ARKSAPATGGVKKPH HHHHCCCCCCCCCCC	33.15	23403867
37	"N6,N6,N6-trimethyllysine"	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	-
37	Acetylation	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	17194708
37	Methylation	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	17194708
37	Other	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	24681537
37	Ubiquitination	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	23000965
38	Acetylation	PATGGVKKPHRYRPG CCCCCCCCCCCCCCC	43.58	26051181
38	Methylation	PATGGVKKPHRYRPG CCCCCCCCCCCCCCC	43.58	15983376
38	Ubiquitination	PATGGVKKPHRYRPG CCCCCCCCCCCCCCC	43.58	23000965
41	Methylation	GGVKKPHRYRPGTVA CCCCCCCCCCCCCHH	37.37	-
42	Phosphorylation	GVKKPHRYRPGTVAL CCCCCCCCCCCCHHH	20.37	27155012
43	Methylation	VKKPHRYRPGTVALR CCCCCCCCCCCHHHH	24.11	-
46	O-linked_Glycosylation	PHRYRPGTVALREIR CCCCCCCCHHHHHHH	12.80	22371497
46	Phosphorylation	PHRYRPGTVALREIR CCCCCCCCHHHHHHH	12.80	30266825
50	Methylation	RPGTVALREIRRYQK CCCCHHHHHHHHHHH	27.79	-
55	Phosphorylation	ALREIRRYQKSTELL HHHHHHHHHHCHHHH	15.50	22817900
57	"N6,N6,N6-trimethyllysine"	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Acetylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	17194708
57	Crotonylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	21925322
57	Glutarylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	31542297
57	Hydroxylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	24681537
57	Lactoylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Lactylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	31645732
57	Malonylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	26320211
57	Methylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	17194708
57	Other	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	27105115
57	Succinylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	22389435
57	Sumoylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	22389435
57	Ubiquitination	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	27667366
58	Phosphorylation	EIRRYQKSTELLIRK HHHHHHHCHHHHHHH	16.16	23401153
59	Phosphorylation	IRRYQKSTELLIRKL HHHHHHCHHHHHHHC	37.37	30266825
64	Methylation	KSTELLIRKLPFQRL HCHHHHHHHCCHHHH	34.13	-
65	Acetylation	STELLIRKLPFQRLV CHHHHHHHCCHHHHH	54.22	25825284
65	Methylation	STELLIRKLPFQRLV CHHHHHHHCCHHHHH	54.22	16267050
65	Other	STELLIRKLPFQRLV CHHHHHHHCCHHHHH	54.22	24681537
65	Ubiquitination	STELLIRKLPFQRLV CHHHHHHHCCHHHHH	54.22	-
80	"N6,N6,N6-trimethyllysine"	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	-
80	Acetylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	29211711
80	Glutarylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	31542297
80	Lactoylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	31645732
80	Malonylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	26320211
80	Methylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	29211711
80	Other	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	27105115
80	Succinylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	29211711
80	Sumoylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	29211711
80	Ubiquitination	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	27667366
81	Phosphorylation	EIAQDFKTDLRFQSS HHHHHHCCCHHHHHH	40.01	23401153
84	Methylation	QDFKTDLRFQSSAVM HHHCCCHHHHHHHHH	30.30	-
87	Phosphorylation	KTDLRFQSSAVMALQ CCCHHHHHHHHHHHH	19.97	-
88	Phosphorylation	TDLRFQSSAVMALQE CCHHHHHHHHHHHHH	17.69	-
97	S-nitrosylation	VMALQEACEAYLVGL HHHHHHHHHHHHHHH	2.79	25040305
100	Phosphorylation	LQEACEAYLVGLFED HHHHHHHHHHHHHCC	4.61	22817900
108	Phosphorylation	LVGLFEDTNLCAIHA HHHHHCCCCEEEEEE	23.93	22817900
116	Acetylation	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	19520870
116	Glutarylation	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	31542297
116	Ubiquitination	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	21987572
119	Phosphorylation	AIHAKRVTIMPKDIQ EEEEEECEECHHHHH	18.65	20068231
121	Sulfoxidation	HAKRVTIMPKDIQLA EEEECEECHHHHHHH	2.17	28183972
123	Acetylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	19520870
123	Glutarylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	31542297
123	Malonylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	26320211
123	Methylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	19520870
123	Other	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	27105115
123	Succinylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	19520870
123	Sumoylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	19520870
123	Ubiquitination	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	23000965
129	Methylation	PKDIQLARRIRGERA HHHHHHHHHHHCCCC	43.05	-

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
3	T	Phosphorylation	Kinase	VRK1	Q99986	PSP
3	T	Phosphorylation	Kinase	TRPM6	Q9BX84	GPS
3	T	Phosphorylation	Kinase	HASPIN	Q8TF76	PSP
3	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
4	T	Phosphorylation	Kinase	VRK1	Q99986	PhosphoELM
4	T	Phosphorylation	Kinase	HASPIN	Q8TF76	Uniprot
6	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
6	T	Phosphorylation	Kinase	PRKCB	P05771	GPS
6	T	Phosphorylation	Kinase	TRPM6	Q9BX84	GPS
7	T	Phosphorylation	Kinase	PKC	-	Uniprot
10	S	Phosphorylation	Kinase	TGM2	P21980	PSP
10	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
10	S	Phosphorylation	Kinase	PIM1	P11309	PSP
10	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
10	S	Phosphorylation	Kinase	RPS6KA5	O75582	GPS
10	S	Phosphorylation	Kinase	RSK2	P18654	PSP
10	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
10	S	Phosphorylation	Kinase	TLK1	Q9UKI8	PSP
10	S	Phosphorylation	Kinase	PBK	Q96KB5	PSP
10	S	Phosphorylation	Kinase	PRKCQ	Q04759	GPS
10	S	Phosphorylation	Kinase	VRK1	Q99986	PSP
10	S	Phosphorylation	Kinase	AKT2	P31751	PSP
10	S	Phosphorylation	Kinase	PRKACA	P36887	GPS
10	S	Phosphorylation	Kinase	AURKA	O14965	GPS
10	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
10	S	Phosphorylation	Kinase	AURB	Q9N0X0	PSP
10	S	Phosphorylation	Kinase	AURKC	Q9UQB9	GPS
10	S	Phosphorylation	Kinase	CDK8	P49336	PSP
11	T	Phosphorylation	Kinase	PKN1	Q16512	PSP
11	S	Phosphorylation	Kinase	VRK1	Q99986	PhosphoELM
11	S	Phosphorylation	Kinase	AURKA	O14965	PhosphoELM
11	S	Phosphorylation	Kinase	AURKB	Q96GD4	PhosphoELM
11	T	Phosphorylation	Kinase	CHEK1	O14757	GPS
11	S	Phosphorylation	Kinase	ALTERNATE	-	Uniprot
12	T	Phosphorylation	Kinase	CHEK1	O14757	Uniprot
12	T	Phosphorylation	Kinase	DAPK3	O43293	PhosphoELM
12	T	Phosphorylation	Kinase	PKC	-	Uniprot
28	S	Phosphorylation	Kinase	ZAK	Q9NYL2	PSP
28	S	Phosphorylation	Kinase	RPS6KA5	O75582	GPS
28	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
28	S	Phosphorylation	Kinase	TGM2	P21980	PSP
28	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
28	S	Phosphorylation	Kinase	AKT2	P31751	PSP
29	S	Phosphorylation	Kinase	MAPK_GROUP	-	PhosphoELM
29	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
29	S	Phosphorylation	Kinase	ALTERNATE	-	Uniprot
29	S	Phosphorylation	Kinase	AURKB	Q96GD4	PhosphoELM
41	Y	Phosphorylation	Kinase	IGF1R	P08069	PSP
41	Y	Phosphorylation	Kinase	JAK1	P23458	PSP
41	Y	Phosphorylation	Kinase	JAK2	O60674	PSP
45	T	Phosphorylation	Kinase	AKT2	P31751	PSP
45	T	Phosphorylation	Kinase	PRKCD	Q05655	GPS
45	T	Phosphorylation	Kinase	AKT1	P31749	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	UHRF1	Q96T88	PMID:17967883
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:28300060

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
3	R	Methylation	Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3).	16567635
4	T	Phosphorylation	Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and dephosphorylated during anaphase.	16185088
5	K	Acetylation	Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4.	16267050
5	K	Methylation	Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3).	16267050
5	K	ubiquitylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	16267050
5	K	Methylation	H3Q5ser is associated with trimethylation of Lys-5 (H3K4me3) and enhances general transcription factor IID (TFIID) complex-binding to H3K4me3, thereby facilitating transcription.	16267050
5	K	Methylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	16267050
5	K	Methylation	Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4.	16267050
5	K	Methylation	Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation.	16267050
5	K	Methylation	Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A.	16267050
5	K	Phosphorylation	Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A.	16267050
7	T	Phosphorylation	Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A.	20228790
7	T	Methylation	Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A.	20228790
9	R	Methylation	Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression.	15345777
9	R	Methylation	Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.	15345777
9	R	Methylation	Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s).	15345777
9	R	Citrullination	Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.	15345777
9	R	Acetylation	Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s).	15345777
10	K	Phosphorylation	Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac).	16185088
10	K	Phosphorylation	Phosphorylation at Thr-12 (H3T11ph) by chromatin-associated CHEK1 regulates the transcription of cell cycle regulatory genes by modulating acetylation of Lys-10 (H3K9ac).	16185088
10	K	Phosphorylation	Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C.	16185088
10	K	Phosphorylation	Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4.	16185088
10	K	Methylation	Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C.	16185088
10	K	Methylation	Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression.	16185088
10	K	Methylation	Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin.	16185088
10	K	Methylation	Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s).	16185088
10	K	Acetylation	Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac).	16185088
10	K	Acetylation	Phosphorylation at Thr-12 (H3T11ph) by chromatin-associated CHEK1 regulates the transcription of cell cycle regulatory genes by modulating acetylation of Lys-10 (H3K9ac).	16185088
10	K	Acetylation	Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4.	16185088
10	K	Acetylation	Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4.	16185088
10	K	Acetylation	Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s).	16185088
10	K	Phosphorylation	Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4.	16185088
10	K	Methylation	Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4.	16185088
10	K	Methylation	Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4.	16185088
11	S	Methylation	Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4.	16185088
11	S	Methylation	Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4.	16185088
11	S	Acetylation	Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac).	16185088
11	S	Acetylation	Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4.	16185088
11	S	Acetylation	Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4.	16185088
11	S	Phosphorylation	In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun.	16185088
11	S	Phosphorylation	Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4.	16185088
11	S	Phosphorylation	Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis.	16185088
11	S	Phosphorylation	Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin.	16185088
11	S	Phosphorylation	Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation.	16185088
11	S	Phosphorylation	Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4.	16185088
11	S	Phosphorylation	Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac).	16185088
12	T	Phosphorylation	Phosphorylation at Thr-12 (H3T11ph) by chromatin-associated CHEK1 regulates the transcription of cell cycle regulatory genes by modulating acetylation of Lys-10 (H3K9ac).	12560483
12	T	Acetylation	Phosphorylation at Thr-12 (H3T11ph) by chromatin-associated CHEK1 regulates the transcription of cell cycle regulatory genes by modulating acetylation of Lys-10 (H3K9ac).	12560483
12	T	Methylation	Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C.	12560483
12	T	Phosphorylation	At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1.	12560483
12	T	Phosphorylation	Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C.	12560483
18	R	Citrullination	Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.	15471871
18	R	Acetylation	Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me).	15471871
18	R	Methylation	Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me).	15471871
18	R	Methylation	Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation.	15471871
18	R	Methylation	Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.	15471871
19	K	Methylation	Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me).	16267050
19	K	Acetylation	Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me).	16267050
24	K	Methylation	Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me).	16267050
24	K	Acetylation	Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me).	16267050
28	K	Methylation	Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression.	16185088
28	K	Methylation	Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin.	16185088
29	S	Phosphorylation	Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation.	16185088
37	K	Methylation	Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation.	16185088
57	K	Methylation	Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication.	17194708
80	K	ubiquitylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	15525939
80	K	Methylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	15525939
80	K	Methylation	Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation.	15525939
80	K	Methylation	Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1.	15525939
80	K	Succinylation	Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes.	15525939
120	K	ubiquitylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	16267050
120	K	Methylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	16267050
123	K	Succinylation	Desuccinylation at Lys-123 (H3K122succ) by SIRT7 in response to DNA damage promotes chromatin condensation and double-strand breaks (DSBs) repair.	16267050
123	K	Acetylation	Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability.	16267050

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of H31_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PHF8_HUMAN	PHF8	physical	20208542
EHMT1_HUMAN	EHMT1	physical	20084102
EED_HUMAN	EED	physical	17210640
CDYL_HUMAN	CDYL	physical	19808672
CTCFL_HUMAN	CTCFL	physical	17048991
WDR5_HUMAN	WDR5	physical	17041588
DDB1_HUMAN	DDB1	physical	17041588
CUL4A_HUMAN	CUL4A	physical	17041588
BPTF_HUMAN	BPTF	physical	16728976
CHD3_HUMAN	CHD3	physical	16728976
SMCA1_HUMAN	SMARCA1	physical	16728976
RBBP4_HUMAN	RBBP4	physical	16728976
DEK_HUMAN	DEK	physical	16696975
KIBRA_HUMAN	WWC1	physical	16684779
P66A_HUMAN	GATAD2A	physical	16415179
P66B_HUMAN	GATAD2B	physical	16415179
NCOR1_HUMAN	NCOR1	physical	12840002
EHMT2_HUMAN	EHMT2	physical	16185068
CHD3_HUMAN	CHD3	physical	11850410
MTA2_HUMAN	MTA2	physical	11850410
HDAC1_HUMAN	HDAC1	physical	11850410
HDAC2_HUMAN	HDAC2	physical	11850410
RBBP4_HUMAN	RBBP4	physical	11850410
WDR5_HUMAN	WDR5	physical	15960974
CBX1_HUMAN	CBX1	physical	15960974
THAP7_HUMAN	THAP7	physical	15561719
HNF1B_HUMAN	HNF1B	physical	11242053
PELP1_HUMAN	PELP1	physical	15456770
ERCC6_HUMAN	ERCC6	physical	11003660
AN32A_HUMAN	ANP32A	physical	15136563
TAF1B_HUMAN	TAF1B	physical	15136563
TAF1A_HUMAN	TAF1A	physical	15136563
EP300_HUMAN	EP300	physical	15136563
CBX1_HUMAN	CBX1	physical	15136563
CBX3_HUMAN	CBX3	physical	15136563
SET_HUMAN	SET	physical	15100215
AN32A_HUMAN	ANP32A	physical	15100215
CBX1_HUMAN	CBX1	physical	15100215
CAF1A_HUMAN	CHAF1A	physical	14718166
NASP_HUMAN	NASP	physical	14718166
IPO4_HUMAN	IPO4	physical	14718166
CAF1B_HUMAN	CHAF1B	physical	14718166
RBBP4_HUMAN	RBBP4	physical	14718166
HAT1_HUMAN	HAT1	physical	14718166
ASF1A_HUMAN	ASF1A	physical	14718166
ASF1B_HUMAN	ASF1B	physical	14718166
H31_HUMAN	HIST1H3A	physical	14718166
KMT2A_HUMAN	KMT2A	physical	20452361
PELP1_HUMAN	PELP1	physical	20448663
NBN_HUMAN	NBN	physical	21187428
XRCC6_HUMAN	XRCC6	physical	21187428
CBX5_HUMAN	CBX5	physical	20011120
CBX3_HUMAN	CBX3	physical	20011120
SMCA4_HUMAN	SMARCA4	physical	20011120
SMCA2_HUMAN	SMARCA2	physical	20011120
UHRF1_MOUSE	Uhrf1	physical	14993289
H2A2C_HUMAN	HIST2H2AC	physical	8598932
RBP56_HUMAN	TAF15	physical	8598932
IPO4_HUMAN	IPO4	physical	19410544
MED16_HUMAN	MED16	physical	19410544
NASP_HUMAN	NASP	physical	19410544
CAF1B_HUMAN	CHAF1B	physical	19410544
RBBP7_HUMAN	RBBP7	physical	19410544
HAT1_HUMAN	HAT1	physical	19410544
UBR7_HUMAN	UBR7	physical	19410544
RBBP4_HUMAN	RBBP4	physical	19410544
DNJC9_HUMAN	DNAJC9	physical	19410544
ASF1A_HUMAN	ASF1A	physical	19410544
TAF1_HUMAN	TAF1	physical	14731392
BRD4_HUMAN	BRD4	physical	19766566
CBP_HUMAN	CREBBP	physical	15616580
SMCA4_HUMAN	SMARCA4	physical	15616580
SMCA5_HUMAN	SMARCA5	physical	15616580
SSRP1_HUMAN	SSRP1	physical	15616580
1433Z_HUMAN	YWHAZ	physical	16246723
1433E_HUMAN	YWHAE	physical	16246723
1433G_HUMAN	YWHAG	physical	16246723
PHF8_HUMAN	PHF8	physical	20421419
CTR9_HUMAN	CTR9	physical	22451921
CDC73_HUMAN	CDC73	physical	22451921
WDR61_HUMAN	WDR61	physical	22451921
LEO1_HUMAN	LEO1	physical	22451921
PAF1_HUMAN	PAF1	physical	22451921
DCAF1_HUMAN	VPRBP	physical	22184063
ASF1A_HUMAN	ASF1A	physical	15664198
ASF1B_HUMAN	ASF1B	physical	15664198
CAF1A_HUMAN	CHAF1A	physical	15664198
CAF1B_HUMAN	CHAF1B	physical	15664198
LMBL2_HUMAN	L3MBTL2	physical	24369422
H2AY_HUMAN	H2AFY	physical	23319141
H14_HUMAN	HIST1H1E	physical	23319141
H15_HUMAN	HIST1H1B	physical	23319141
H12_HUMAN	HIST1H1C	physical	23319141
H2AX_HUMAN	H2AFX	physical	23319141
SMCA5_HUMAN	SMARCA5	physical	23319141
BAZ1B_HUMAN	BAZ1B	physical	23319141
FBLI1_HUMAN	FBLIM1	physical	25416956
KAT2B_HUMAN	KAT2B	physical	23667505
H2AZ_HUMAN	H2AFZ	physical	23415232
KMT2A_HUMAN	KMT2A	physical	24680668
BCAS3_HUMAN	BCAS3	physical	17505058
HDAC1_HUMAN	HDAC1	physical	24722339
HDAC2_HUMAN	HDAC2	physical	24722339
HDAC3_HUMAN	HDAC3	physical	24722339
HDAC5_HUMAN	HDAC5	physical	24722339
HDAC6_HUMAN	HDAC6	physical	24722339
EP300_HUMAN	EP300	physical	24722339
NASP_HUMAN	NASP	physical	25281560
SMHD1_HUMAN	SMCHD1	physical	25281560
XRCC6_HUMAN	XRCC6	physical	25281560
SHPRH_HUMAN	SHPRH	physical	25281560
CAF1A_HUMAN	CHAF1A	physical	25281560
KIF23_HUMAN	KIF23	physical	25281560
ASF1B_HUMAN	ASF1B	physical	25281560
ZN512_HUMAN	ZNF512	physical	25281560
CAF1B_HUMAN	CHAF1B	physical	25281560
Z512B_HUMAN	ZNF512B	physical	25281560
KIFC1_HUMAN	KIFC1	physical	25281560
RFC1_HUMAN	RFC1	physical	25281560
DNLI3_HUMAN	LIG3	physical	25281560
HIRA_HUMAN	HIRA	physical	25281560
INCE_HUMAN	INCENP	physical	25281560
ATAD5_HUMAN	ATAD5	physical	25281560
MECP2_HUMAN	MECP2	physical	25281560
ASF1A_HUMAN	ASF1A	physical	25281560
CDCA2_HUMAN	CDCA2	physical	25281560
H2AW_HUMAN	H2AFY2	physical	25281560
NSD2_HUMAN	WHSC1	physical	25281560
CBX5_HUMAN	CBX5	physical	25281560
KIF22_HUMAN	KIF22	physical	25281560
PB1_HUMAN	PBRM1	physical	25281560
UBN2_HUMAN	UBN2	physical	25281560
KI18B_HUMAN	KIF18B	physical	25281560
HAT1_HUMAN	HAT1	physical	25281560
BOREA_HUMAN	CDCA8	physical	25281560
UBR7_HUMAN	UBR7	physical	25281560
RN169_HUMAN	RNF169	physical	25281560
PHIP_HUMAN	PHIP	physical	25281560
CDAN1_HUMAN	CDAN1	physical	25281560
ATAD2_HUMAN	ATAD2	physical	25281560
UHRF1_HUMAN	UHRF1	physical	25281560
CBX2_HUMAN	CBX2	physical	25281560
CDCA5_HUMAN	CDCA5	physical	25281560
RECQ1_HUMAN	RECQL	physical	25281560
DNM3A_HUMAN	DNMT3A	physical	25281560
VRK1_HUMAN	VRK1	physical	25281560
RFX5_HUMAN	RFX5	physical	25281560
NUSAP_HUMAN	NUSAP1	physical	25281560
UBN1_HUMAN	UBN1	physical	25281560
MORC3_HUMAN	MORC3	physical	25281560
TONSL_HUMAN	TONSL	physical	25281560
RHGBA_HUMAN	ARHGAP11A	physical	25281560
NEUA_HUMAN	CMAS	physical	25281560
BARD1_HUMAN	BARD1	physical	25281560
XPC_HUMAN	XPC	physical	25281560
BRD3_HUMAN	BRD3	physical	25281560
UBP48_HUMAN	USP48	physical	25281560
WDR76_HUMAN	WDR76	physical	25281560
BAF_HUMAN	BANF1	physical	25281560
BRD2_HUMAN	BRD2	physical	25281560
FWCH2_HUMAN	FLYWCH2	physical	25281560
GBB4_HUMAN	GNB4	physical	25281560
ELF2_HUMAN	ELF2	physical	25281560
KDM1B_HUMAN	KDM1B	physical	25281560
RLF_HUMAN	RLF	physical	25281560
DNJC9_HUMAN	DNAJC9	physical	25281560
ZN711_HUMAN	ZNF711	physical	25281560
LRIF1_HUMAN	LRIF1	physical	25281560
PARP2_HUMAN	PARP2	physical	25281560
LCOR_HUMAN	C10orf12	physical	25281560
CABIN_HUMAN	CABIN1	physical	25281560
HMGA2_HUMAN	HMGA2	physical	25281560
UBP3_HUMAN	USP3	physical	25281560
HDGF_HUMAN	HDGF	physical	25281560
MS3L1_HUMAN	MSL3	physical	25281560
PRC1_HUMAN	PRC1	physical	25281560
PINX1_HUMAN	PINX1	physical	25281560
SMC6_HUMAN	SMC6	physical	25281560
RECQ5_HUMAN	RECQL5	physical	25281560
ZMAT2_HUMAN	ZMAT2	physical	25281560
BRD1_HUMAN	BRD1	physical	25281560
CPVL_HUMAN	CPVL	physical	25281560
UNG_HUMAN	UNG	physical	25281560
MSL1_HUMAN	MSL1	physical	25281560
SRBD1_HUMAN	SRBD1	physical	25281560
PCGF1_HUMAN	PCGF1	physical	25281560
RD23B_HUMAN	RAD23B	physical	25281560
RSF1_HUMAN	RSF1	physical	25281560
CO041_HUMAN	C15orf41	physical	25281560
HMGB3_HUMAN	HMGB3	physical	25281560
HMGN4_HUMAN	HMGN4	physical	25281560
MEN1_HUMAN	MEN1	physical	25281560
TDIF1_HUMAN	DNTTIP1	physical	25281560
EDF1_HUMAN	EDF1	physical	25281560
FLOT1_HUMAN	FLOT1	physical	25281560
ZN257_HUMAN	ZNF257	physical	25281560
H2B1B_HUMAN	HIST1H2BB	physical	25533843
CREB1_HUMAN	CREB1	physical	12933667
CAF1A_HUMAN	CHAF1A	physical	28514442
UBR7_HUMAN	UBR7	physical	28514442
FBLI1_HUMAN	FBLIM1	physical	28514442
TONSL_HUMAN	TONSL	physical	28514442
SP16H_HUMAN	SUPT16H	physical	28514442
DAXX_HUMAN	DAXX	physical	28514442
CAF1B_HUMAN	CHAF1B	physical	28514442
MMS22_HUMAN	MMS22L	physical	28514442
NASP_HUMAN	NASP	physical	28514442
CBX5_HUMAN	CBX5	physical	28514442
IPO4_HUMAN	IPO4	physical	28514442
XPC_HUMAN	XPC	physical	28514442
ASF1B_HUMAN	ASF1B	physical	28514442
H2A2B_HUMAN	HIST2H2AB	physical	28514442
MCM2_HUMAN	MCM2	physical	28514442
MCM4_HUMAN	MCM4	physical	28514442
MCM6_HUMAN	MCM6	physical	28514442
PARP2_HUMAN	PARP2	physical	28514442
SSRP1_HUMAN	SSRP1	physical	28514442
H2AY_HUMAN	H2AFY	physical	28514442
ASF1A_HUMAN	ASF1A	physical	28514442
MCM7_HUMAN	MCM7	physical	28514442
SHPRH_HUMAN	SHPRH	physical	28400511
FACD2_HUMAN	FANCD2	physical	22828868
RBBP4_HUMAN	RBBP4	physical	27098840
ROA1_HUMAN	HNRNPA1	physical	26912663
ROAA_HUMAN	HNRNPAB	physical	26912663
PSIP1_HUMAN	PSIP1	physical	26912663
HDGR3_HUMAN	HDGFRP3	physical	26912663
DNM3A_HUMAN	DNMT3A	physical	26912663
DNM3B_HUMAN	DNMT3B	physical	26912663
MSH6_HUMAN	MSH6	physical	26912663
NSD2_HUMAN	WHSC1	physical	26912663
NSD3_HUMAN	WHSC1L1	physical	26912663
MBD5_HUMAN	MBD5	physical	26912663
GLYR1_HUMAN	GLYR1	physical	26912663
NSD1_HUMAN	NSD1	physical	26912663

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

Related Literatures of Post-Translational Modification

Acetylation

"Identification of histone H3 lysine 36 acetylation as a highlyconserved histone modification.";
Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L.,Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
J. Biol. Chem. 282:7632-7640(2007).
Cited for: ACETYLATION AT LYS-37.
PubMed: 17189264

"Organismal differences in post-translational modifications inhistones H3 and H4.";
Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.;
J. Biol. Chem. 282:7641-7655(2007).
Cited for: ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37;LYS-57 AND LYS-80, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24;LYS-28; LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123, AND MASSSPECTROMETRY.
PubMed: 17194708

"Coactivator-associated arginine methyltransferase-1 enhances nuclearfactor-kappaB-mediated gene transcription through methylation ofhistone H3 at arginine 17.";
Miao F., Li S., Chavez V., Lanting L., Natarajan R.;
Mol. Endocrinol. 20:1562-1573(2006).
Cited for: ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT ARG-18, ANDCITRULLINATION AT ARG-18.
PubMed: 16497732

"Quantitative proteomic analysis of post-translational modificationsof human histones.";
Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M.,Finn P., Grauslund M., Hansen A.M., Jensen O.N.;
Mol. Cell. Proteomics 5:1314-1325(2006).
Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, METHYLATIONAT LYS-28; LYS-37 AND LYS-80, AND MASS SPECTROMETRY.
PubMed: 16627869

"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-10; LYS-15; LYS-19; LYS-24;LYS-28 AND LYS-37, AND MASS SPECTROMETRY.
PubMed: 16916647

"Mass spectrometric characterization of human histone H3: a bird's eyeview.";
Thomas C.E., Kelleher N.L., Mizzen C.A.;
J. Proteome Res. 5:240-247(2006).
Cited for: METHYLATION AT LYS-5 AND LYS-10, ACETYLATION AT LYS-10; LYS-15 ANDLYS-24, PHOSPHORYLATION AT SER-11 AND SER-29, AND MASS SPECTROMETRY.
PubMed: 16457588

"Expression patterns and post-translational modifications associatedwith mammalian histone H3 variants.";
Hake S.B., Garcia B.A., Duncan E.M., Kauer M., Dellaire G.,Shabanowitz J., Bazett-Jones D.P., Allis C.D., Hunt D.F.;
J. Biol. Chem. 281:559-568(2006).
Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19 AND LYS-24, METHYLATION ATLYS-5; LYS-10; LYS-19; LYS-28; LYS-37; LYS-65; LYS-80 AND LYS-123, ANDMASS SPECTROMETRY.
PubMed: 16267050

"Modifications of human histone H3 variants during mitosis.";
Garcia B.A., Barber C.M., Hake S.B., Ptak C., Turner F.B., Busby S.A.,Shabanowitz J., Moran R.G., Allis C.D., Hunt D.F.;
Biochemistry 44:13202-13213(2005).
Cited for: PROTEIN SEQUENCE OF 2-20, METHYLATION AT LYS-10; LYS-28 AND LYS-37,PHOSPHORYLATION AT THR-4; SER-11 AND SER-29, ACETYLATION AT LYS-10 ANDLYS-15, AND MASS SPECTROMETRY.
PubMed: 16185088

Methylation

"Arginine methylation of the histone H3 tail impedes effectorbinding.";
Iberg A.N., Espejo A., Cheng D., Kim D., Michaud-Levesque J.,Richard S., Bedford M.T.;
J. Biol. Chem. 283:3006-3010(2008).
Cited for: METHYLATION AT ARG-3 BY PRMT6.
PubMed: 18077460

"Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex aremutually exclusive.";
Guccione E., Bassi C., Casadio F., Martinato F., Cesaroni M.,Schuchlautz H., Luescher B., Amati B.;
Nature 449:933-937(2007).
Cited for: METHYLATION AT ARG-3 BY PRMT6.
PubMed: 17898714

"PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4trimethylation.";
Hyllus D., Stein C., Schnabel K., Schiltz E., Imhof A., Dou Y.,Hsieh J., Bauer U.M.;
Genes Dev. 21:3369-3380(2007).
Cited for: METHYLATION AT ARG-3 BY PRMT6.
PubMed: 18079182

"Coactivator-associated arginine methyltransferase-1 enhances nuclearfactor-kappaB-mediated gene transcription through methylation ofhistone H3 at arginine 17.";
Miao F., Li S., Chavez V., Lanting L., Natarajan R.;
Mol. Endocrinol. 20:1562-1573(2006).
Cited for: ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT ARG-18, ANDCITRULLINATION AT ARG-18.
PubMed: 16497732

"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-9 AND ARG-18, AND METHYLATION AT ARG-18.
PubMed: 15345777

"Ligand-dependent activation of the farnesoid X-receptor directsarginine methylation of histone H3 by CARM1.";
Ananthanarayanan M., Li S., Balasubramaniyan N., Suchy F.J.,Walsh M.J.;
J. Biol. Chem. 279:54348-54357(2004).
Cited for: METHYLATION AT ARG-18.
PubMed: 15471871

"Histone H3 lysine 56 methylation regulates DNA replication throughits interaction wwith PCNA.";
Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A.,Carey M.F., Grunstein M.;
Mol. Cell 46:7-17(2012).
Cited for: METHYLATION AT LYS-57.
PubMed: 22387026

"Organismal differences in post-translational modifications inhistones H3 and H4.";
Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.;
J. Biol. Chem. 282:7641-7655(2007).
Cited for: ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37;LYS-57 AND LYS-80, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24;LYS-28; LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123, AND MASSSPECTROMETRY.
PubMed: 17194708

"Quantitative proteomic analysis of post-translational modificationsof human histones.";
Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M.,Finn P., Grauslund M., Hansen A.M., Jensen O.N.;
Mol. Cell. Proteomics 5:1314-1325(2006).
Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, METHYLATIONAT LYS-28; LYS-37 AND LYS-80, AND MASS SPECTROMETRY.
PubMed: 16627869

"Mass spectrometric characterization of human histone H3: a bird's eyeview.";
Thomas C.E., Kelleher N.L., Mizzen C.A.;
J. Proteome Res. 5:240-247(2006).
Cited for: METHYLATION AT LYS-5 AND LYS-10, ACETYLATION AT LYS-10; LYS-15 ANDLYS-24, PHOSPHORYLATION AT SER-11 AND SER-29, AND MASS SPECTROMETRY.
PubMed: 16457588

"Expression patterns and post-translational modifications associatedwith mammalian histone H3 variants.";
Hake S.B., Garcia B.A., Duncan E.M., Kauer M., Dellaire G.,Shabanowitz J., Bazett-Jones D.P., Allis C.D., Hunt D.F.;
J. Biol. Chem. 281:559-568(2006).
Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19 AND LYS-24, METHYLATION ATLYS-5; LYS-10; LYS-19; LYS-28; LYS-37; LYS-65; LYS-80 AND LYS-123, ANDMASS SPECTROMETRY.
PubMed: 16267050

"Protein identification using sequential ion/ion reactions and tandemmass spectrometry.";
Coon J.J., Ueberheide B., Syka J.E.P., Dryhurst D.D., Ausio J.,Shabanowitz J., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 102:9463-9468(2005).
Cited for: METHYLATION AT LYS-37 AND LYS-38, AND MASS SPECTROMETRY.
PubMed: 15983376

"Methylation of histone H3 lysine 9 creates a binding site for HP1proteins.";
Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.;
Nature 410:116-120(2001).
Cited for: METHYLATION AT LYS-10.
PubMed: 11242053

"Modifications of human histone H3 variants during mitosis.";
Garcia B.A., Barber C.M., Hake S.B., Ptak C., Turner F.B., Busby S.A.,Shabanowitz J., Moran R.G., Allis C.D., Hunt D.F.;
Biochemistry 44:13202-13213(2005).
Cited for: PROTEIN SEQUENCE OF 2-20, METHYLATION AT LYS-10; LYS-28 AND LYS-37,PHOSPHORYLATION AT THR-4; SER-11 AND SER-29, ACETYLATION AT LYS-10 ANDLYS-15, AND MASS SPECTROMETRY.
PubMed: 16185088

"Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strandbreaks.";
Huyen Y., Zgheib O., Ditullio R.A. Jr., Gorgoulis V.G., Zacharatos P.,Petty T.J., Sheston E.A., Mellert H.S., Stavridi E.S.,Halazonetis T.D.;
Nature 432:406-411(2004).
Cited for: METHYLATION AT LYS-80.
PubMed: 15525939

Phosphorylation

"Quantitative interaction proteomics and genome-wide profiling ofepigenetic histone marks and their readers.";
Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S.,Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G.,Mann M.;
Cell 142:967-980(2010).
Cited for: PHOSPHORYLATION AT SER-58 AND THR-81.
PubMed: 20850016

"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-29, AND MASSSPECTROMETRY.
PubMed: 19007248

"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASSSPECTROMETRY.
PubMed: 17924679

"Mass spectrometric characterization of human histone H3: a bird's eyeview.";
Thomas C.E., Kelleher N.L., Mizzen C.A.;
J. Proteome Res. 5:240-247(2006).
Cited for: METHYLATION AT LYS-5 AND LYS-10, ACETYLATION AT LYS-10; LYS-15 ANDLYS-24, PHOSPHORYLATION AT SER-11 AND SER-29, AND MASS SPECTROMETRY.
PubMed: 16457588

"Phosphorylation of Ser28 in histone H3 mediated by mixed lineagekinase-like mitogen-activated protein triple kinase alpha.";
Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.;
J. Biol. Chem. 280:13545-13553(2005).
Cited for: PHOSPHORYLATION AT SER-29.
PubMed: 15684425

"The kinase haspin is required for mitotic histone H3 Thr 3phosphorylation and normal metaphase chromosome alignment.";
Dai J., Sultan S., Taylor S.S., Higgins J.M.G.;
Genes Dev. 19:472-488(2005).
Cited for: PHOSPHORYLATION AT THR-4; SER-11 AND SER-29.
PubMed: 15681610

"Novel mitosis-specific phosphorylation of histone H3 at Thr11mediated by Dlk/ZIP kinase.";
Preuss U., Landsberg G., Scheidtmann K.H.;
Nucleic Acids Res. 31:878-885(2003).
Cited for: PHOSPHORYLATION AT SER-11 AND THR-12.
PubMed: 12560483

"Aurora-B phosphorylates Histone H3 at serine28 with regard to themitotic chromosome condensation.";
Goto H., Yasui Y., Nigg E.A., Inagaki M.;
Genes Cells 7:11-17(2002).
Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
PubMed: 11856369

"Identification of a novel phosphorylation site on histone H3 coupledwith mitotic chromosome condensation.";
Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M.,Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.;
J. Biol. Chem. 274:25543-25549(1999).
Cited for: PROTEIN SEQUENCE OF 58-64; 117-120 AND 124-135, AND PHOSPHORYLATION ATSER-11 AND SER-29.
PubMed: 10464286

"Modifications of human histone H3 variants during mitosis.";
Garcia B.A., Barber C.M., Hake S.B., Ptak C., Turner F.B., Busby S.A.,Shabanowitz J., Moran R.G., Allis C.D., Hunt D.F.;
Biochemistry 44:13202-13213(2005).
Cited for: PROTEIN SEQUENCE OF 2-20, METHYLATION AT LYS-10; LYS-28 AND LYS-37,PHOSPHORYLATION AT THR-4; SER-11 AND SER-29, ACETYLATION AT LYS-10 ANDLYS-15, AND MASS SPECTROMETRY.
PubMed: 16185088

"Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylationat histone H3K4.";
Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N.,Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N.,Beisenherz-Huss C., Gunther T., Buettner R., Schule R.;
Nature 464:792-796(2010).
Cited for: PHOSPHORYLATION AT THR-7.
PubMed: 20228790

"Phosphorylation of histone H3 at threonine 11 establishes a novelchromatin mark for transcriptional regulation.";
Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K.,Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H.,Buettner R., Schule R.;
Nat. Cell Biol. 10:53-60(2008).
Cited for: PHOSPHORYLATION AT THR-12.
PubMed: 18066052

"Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-induced transcriptional repression.";
Shimada M., Niida H., Zineldeen D.H., Tagami H., Tanaka M., Saito H.,Nakanishi M.;
Cell 132:221-232(2008).
Cited for: PHOSPHORYLATION AT THR-12 BY CHEK1.
PubMed: 18243098

"JAK2 phosphorylates histone H3Y41 and excludes HP1alpha fromchromatin.";
Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T.,Green A.R., Kouzarides T.;
Nature 461:819-822(2009).
Cited for: PHOSPHORYLATION AT TYR-42.
PubMed: 19783980