H32_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H32_HUMAN
• UniProt AC: Q71DI3
• Protein Name: Histone H3.2
• Gene Name: HIST2H3A
• 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: MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA

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	Phosphorylation	----MARTKQTARKS ----CCCCCHHHHHC	20.26	17938195
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	17194708
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	20228790
9	Citrullination	ARTKQTARKSTGGKA CCCCHHHHHCCCCCC	36.52	-
9	Citrullination	ARTKQTARKSTGGKA CCCCHHHHHCCCCCC	36.52	15345777
9	Methylation	ARTKQTARKSTGGKA CCCCHHHHHCCCCCC	36.52	8558401
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	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	Phosphorylation	TKQTARKSTGGKAPR CCHHHHHCCCCCCCH	27.08	10469656
12	Phosphorylation	KQTARKSTGGKAPRK CHHHHHCCCCCCCHH	53.65	26074081
15	Sumoylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
15	Acetylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	17194708
15	Glutarylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	31542297
15	Lactoylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
15	Methylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
15	Other	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	27105115
15	Succinylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	17194708
15	Sumoylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	17194708
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	17194708
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	Methylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	17194708
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	2-Hydroxyisobutyrylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Acetylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	17194708
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	Methylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	16267050
24	Other	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	27105115
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
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	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	Phosphorylation	ATKAARKSAPATGGV HHHHHHHHCCCCCCC	33.65	23401153
33	Phosphorylation	ARKSAPATGGVKKPH HHHHCCCCCCCCCCC	33.15	23403867
37	"N6,N6,N6-trimethyllysine"	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	-
37	2-Hydroxyisobutyrylation	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	"N6,N6-dimethyllysine"	PATGGVKKPHRYRPG CCCCCCCCCCCCCCC	43.58	-
38	Methylation	PATGGVKKPHRYRPG CCCCCCCCCCCCCCC	43.58	-
38	Ubiquitination	PATGGVKKPHRYRPG CCCCCCCCCCCCCCC	43.58	23000965
41	Dimethylation	GGVKKPHRYRPGTVA CCCCCCCCCCCCCHH	37.37	-
41	Methylation	GGVKKPHRYRPGTVA CCCCCCCCCCCCCHH	37.37	-
42	Phosphorylation	GVKKPHRYRPGTVAL CCCCCCCCCCCCHHH	20.37	28152594
43	Methylation	VKKPHRYRPGTVALR CCCCCCCCCCCHHHH	24.11	-
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	Lactoylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
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	Methylation	STELLIRKLPFQRLV CHHHHHHHCCHHHHH	54.22	16267050
65	Other	STELLIRKLPFQRLV CHHHHHHHCCHHHHH	54.22	24681537
80	"N6,N6,N6-trimethyllysine"	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	-
80	2-Hydroxyisobutyrylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	-
80	Acetylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	29211711
80	Glutarylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	31542297
80	Lactoylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	31645732
80	Methylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	29211711
80	Other	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	27105115
80	Succinylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	29211711
80	Sumoylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	29211711
80	Ubiquitination	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	27667366
81	Phosphorylation	EIAQDFKTDLRFQSS HHHHHHCCCHHHCHH	40.01	23401153
84	Methylation	QDFKTDLRFQSSAVM HHHCCCHHHCHHHHH	30.30	-
87	Phosphorylation	KTDLRFQSSAVMALQ CCCHHHCHHHHHHHH	19.97	23684312
88	Phosphorylation	TDLRFQSSAVMALQE CCHHHCHHHHHHHHH	17.69	28464451
97	Phosphorylation	VMALQEASEAYLVGL HHHHHHHHHHHHHHH	23.23	23684312
100	Phosphorylation	LQEASEAYLVGLFED HHHHHHHHHHHHHCC	9.62	23684312
108	Phosphorylation	LVGLFEDTNLCAIHA HHHHHCCCCEEEEEE	23.93	22817900
111	S-palmitoylation	LFEDTNLCAIHAKRV HHCCCCEEEEEEEEC	3.47	21076176
116	Acetylation	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	19520870
116	Glutarylation	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	31542297
116	Ubiquitination	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	-
119	Phosphorylation	AIHAKRVTIMPKDIQ EEEEEECEECHHHHH	18.65	20068231
121	Sulfoxidation	HAKRVTIMPKDIQLA EEEECEECHHHHHHH	2.17	28183972
123	Sumoylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	2-Hydroxyisobutyrylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	Acetylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	19520870
123	Glutarylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	31542297
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
4	T	Phosphorylation	Kinase	GSG2	Q8TF76	GPS
7	T	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
7	T	Phosphorylation	Kinase	PKC	-	Uniprot
11	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
11	S	Phosphorylation	Kinase	AURKC	Q9UQB9	GPS
11	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
11	S	Phosphorylation	Kinase	RPS6KA4	O75676	GPS
11	S	Phosphorylation	Kinase	RPS6KA5	O75582	GPS
11	S	Phosphorylation	Kinase	ALTERNATE	-	Uniprot
12	T	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
12	T	Phosphorylation	Kinase	PKC	-	Uniprot
29	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
29	S	Phosphorylation	Kinase	AURKC	Q9UQB9	GPS
29	S	Phosphorylation	Kinase	RPS6KA5	O75582	GPS
29	S	Phosphorylation	Kinase	ALTERNATE	-	Uniprot
46	T	Phosphorylation	Kinase	AKT1	P31749	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	HUWE1	Q7Z6Z7	PMID:22199232

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).	18077460
4	T	Phosphorylation	Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and dephosphorylated during anaphase.	16267050
5	K	ubiquitylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	16267050
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).	18077460
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.	30867594
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	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
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	Methylation	Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation.	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.	16267050
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.	16267050
9	R	Methylation	Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression.	18077460
9	R	Methylation	Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.	16567635
9	R	Methylation	Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s).	16267050
9	R	Citrullination	Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.	16567635
9	R	Acetylation	Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s).	16267050
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).	30257210
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.	16267050
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.	16267050
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.	16267050
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.	16267050
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.	16267050
10	K	Acetylation	Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s).	16267050
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.	16267050
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.	16267050
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).	30257210
10	K	Methylation	Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s).	16267050
10	K	Methylation	Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin.	16267050
10	K	Methylation	Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression.	16267050
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.	16267050
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.	16267050
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.	16267050
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).	30257210
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.	16267050
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.	16267050
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.	16267050
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.	16267050
11	S	Phosphorylation	Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis.	16267050
11	S	Phosphorylation	Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin.	16267050
11	S	Phosphorylation	Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation.	16267050
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.	16267050
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).	30257210
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.	16267050
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.	16267050
12	T	Phosphorylation	At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1.	16267050
18	R	Citrullination	Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.	16567635
18	R	Acetylation	Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me).	16267050
18	R	Methylation	Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me).	16267050
18	R	Methylation	Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation.	18077460
18	R	Methylation	Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.	16567635
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.	16267050
28	K	Methylation	Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin.	16267050
29	S	Phosphorylation	Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation.	16267050
37	K	Methylation	Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation.	16267050
57	K	Methylation	Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication.	16267050
80	K	Methylation	Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1.	16267050
80	K	Methylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	16267050
80	K	Methylation	Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation.	16267050
80	K	ubiquitylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	16267050
80	K	Succinylation	Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes.	29211711
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.	27436229
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 H32_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KAT6A_HUMAN	KAT6A	physical	20581860
PCNA_HUMAN	PCNA	physical	22387026
BAG6_HUMAN	BAG6	physical	22373577
DOT1L_HUMAN	DOT1L	physical	22373577
NRDC_HUMAN	NRD1	physical	22294699
PHF2_HUMAN	PHF2	physical	22294699
UHRF1_HUMAN	UHRF1	physical	22294699
MTA1_HUMAN	MTA1	physical	22294699
KAT5_HUMAN	KAT5	physical	22081016
STAT1_HUMAN	STAT1	physical	21689637
JAK2_HUMAN	JAK2	physical	21689637
INGR1_HUMAN	IFNGR1	physical	21689637
BIRC5_HUMAN	BIRC5	physical	20929775
BOREA_HUMAN	CDCA8	physical	20929775
AURKB_HUMAN	AURKB	physical	20929775
INCE_HUMAN	INCENP	physical	20929775
SYUA_HUMAN	SNCA	physical	16959795
BRD7_HUMAN	BRD7	physical	16265664

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

Related Literatures of Post-Translational Modification

Acetylation

"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-28, AND MASS SPECTROMETRY.
PubMed: 19608861

"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

"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; LYS-24 AND LYS-28, METHYLATIONAT LYS-5; LYS-10; LYS-19; LYS-28; LYS-37; LYS-65; LYS-80 AND LYS-123,AND MASS 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 28-41, 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

"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; LYS-24 AND LYS-28, METHYLATIONAT LYS-5; LYS-10; LYS-19; LYS-28; LYS-37; LYS-65; LYS-80 AND LYS-123,AND MASS SPECTROMETRY.
PubMed: 16267050

"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 28-41, 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

"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 28-41, 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

"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