H33_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H33_HUMAN
• UniProt AC: P84243
• Protein Name: Histone H3.3
• Gene Name: H3F3A
• Organism: Homo sapiens (Human).
• Sequence Length: 136
• Subcellular Localization: Nucleus. Chromosome.
• Protein Description: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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: MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA

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	16457588
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	20228790
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	Methylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	11242053
10	Other	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	27105115
11	ADP-ribosylation	TKQTARKSTGGKAPR CCHHHHHCCCCCCCH	27.08	28190768
11	O-linked_Glycosylation	TKQTARKSTGGKAPR CCHHHHHCCCCCCCH	27.08	28510447
11	Phosphorylation	TKQTARKSTGGKAPR CCHHHHHCCCCCCCH	27.08	10469656
12	Phosphorylation	KQTARKSTGGKAPRK CHHHHHCCCCCCCHH	53.65	26074081
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	17194708
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	16267050
19	Other	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	27105115
19	Sumoylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	17194708
19	Ubiquitination	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	21890473
24	N6-crotonyl-L-lysine	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	17194708
24	Other	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	27105115
24	Sumoylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	17194708
24	Ubiquitination	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	17194708
27	Citrullination	QLATKAARKSAPSTG HHHHHHHHHHCCCCC	38.02	-
27	Citrullination	QLATKAARKSAPSTG HHHHHHHHHHCCCCC	38.02	16567635
28	"N6,N6,N6-trimethyllysine"	LATKAARKSAPSTGG HHHHHHHHHCCCCCC	46.36	-
28	Acetylation	LATKAARKSAPSTGG HHHHHHHHHCCCCCC	46.36	17194708
28	Crotonylation	LATKAARKSAPSTGG HHHHHHHHHCCCCCC	46.36	21925322
28	Glutarylation	LATKAARKSAPSTGG HHHHHHHHHCCCCCC	46.36	31542297
28	Lactoylation	LATKAARKSAPSTGG HHHHHHHHHCCCCCC	46.36	31645732
28	Methylation	LATKAARKSAPSTGG HHHHHHHHHCCCCCC	46.36	17194708
28	Other	LATKAARKSAPSTGG HHHHHHHHHCCCCCC	46.36	27105115
28	Ubiquitination	LATKAARKSAPSTGG HHHHHHHHHCCCCCC	46.36	17194708
29	ADP-ribosylation	ATKAARKSAPSTGGV HHHHHHHHCCCCCCC	39.60	28190768
29	Phosphorylation	ATKAARKSAPSTGGV HHHHHHHHCCCCCCC	39.60	25159151
32	Phosphorylation	AARKSAPSTGGVKKP HHHHHCCCCCCCCCC	39.13	25159151
33	Phosphorylation	ARKSAPSTGGVKKPH HHHHCCCCCCCCCCC	36.57	23403867
37	"N6,N6,N6-trimethyllysine"	APSTGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	-
37	Acetylation	APSTGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	17194708
37	Methylation	APSTGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	17194708
37	Other	APSTGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	24681537
37	Ubiquitination	APSTGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	21906983
38	Acetylation	PSTGGVKKPHRYRPG CCCCCCCCCCCCCCC	43.58	26051181
38	Methylation	PSTGGVKKPHRYRPG CCCCCCCCCCCCCCC	43.58	24129315
38	Ubiquitination	PSTGGVKKPHRYRPG CCCCCCCCCCCCCCC	43.58	-
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	17194708
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 HHHHHHHHHCHHHHH	49.79	-
80	Acetylation	REIAQDFKTDLRFQS HHHHHHHHHCHHHHH	49.79	29211711
80	Glutarylation	REIAQDFKTDLRFQS HHHHHHHHHCHHHHH	49.79	31542297
80	Lactoylation	REIAQDFKTDLRFQS HHHHHHHHHCHHHHH	49.79	31645732
80	Methylation	REIAQDFKTDLRFQS HHHHHHHHHCHHHHH	49.79	29211711
80	Other	REIAQDFKTDLRFQS HHHHHHHHHCHHHHH	49.79	27105115
80	Succinylation	REIAQDFKTDLRFQS HHHHHHHHHCHHHHH	49.79	29211711
80	Sumoylation	REIAQDFKTDLRFQS HHHHHHHHHCHHHHH	49.79	29211711
80	Ubiquitination	REIAQDFKTDLRFQS HHHHHHHHHCHHHHH	49.79	29211711
81	Phosphorylation	EIAQDFKTDLRFQSA HHHHHHHHCHHHHHH	40.01	23401153
84	Methylation	QDFKTDLRFQSAAIG HHHHHCHHHHHHHHH	30.30	-
87	Phosphorylation	KTDLRFQSAAIGALQ HHCHHHHHHHHHHHH	19.56	20068231
97	Phosphorylation	IGALQEASEAYLVGL HHHHHHHHHHHHHHH	23.23	28464451
100	Phosphorylation	LQEASEAYLVGLFED HHHHHHHHHHHHHCC	9.62	20068231
108	Phosphorylation	LVGLFEDTNLCAIHA HHHHHCCCCEEEEEE	23.93	20068231
111	S-nitrosylation	LFEDTNLCAIHAKRV HHCCCCEEEEEEEEC	3.47	25040305
116	Acetylation	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	19520870
116	Glutarylation	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	31542297
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	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	19520870
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	-	Uniprot
7	T	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
10	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
10	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
10	S	Phosphorylation	Kinase	FYN	P06241	PSP
11	S	Phosphorylation	Kinase	AURKB	Q96GD4	PhosphoELM
11	S	Phosphorylation	Kinase	ALTERNATE	-	Uniprot
11	S	Phosphorylation	Kinase	PAK1	Q13153	GPS
11	S	Phosphorylation	Kinase	RPS6KA5	O75582	GPS
11	S	Phosphorylation	Kinase	RPS6KA4	O75676	GPS
11	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
11	S	Phosphorylation	Kinase	AURKC	Q9UQB9	GPS
12	T	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
12	T	Phosphorylation	Kinase	PKC	-	Uniprot
28	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
28	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
29	S	Phosphorylation	Kinase	RPS6KA5	O75582	GPS
29	S	Phosphorylation	Kinase	AURKC	Q9UQB9	GPS
29	S	Phosphorylation	Kinase	ALTERNATE	-	Uniprot
29	S	Phosphorylation	Kinase	AURKB	Q96GD4	PhosphoELM
31	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
45	T	Phosphorylation	Kinase	DYRK3	O43781	PSP
45	T	Phosphorylation	Kinase	DYRK2	Q92630	PSP
45	T	Phosphorylation	Kinase	DYRK1B	Q9Y463	PSP
45	T	Phosphorylation	Kinase	DYRK1A	Q63470	PSP

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	Specifically enriched in modifications associated with active chromatin such as methylation at Lys-5 (H3K4me), Lys-37 and Lys-80.	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
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), which are linked to gene repression, are underrepresented.	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), which are linked to gene repression, are underrepresented.	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
32	S	Phosphorylation	Phosphorylation on Ser-32 (H3S31ph) is specific to regions bordering centromeres in metaphase chromosomes.	16267050
37	K	Methylation	Specifically enriched in modifications associated with active chromatin such as methylation at Lys-5 (H3K4me), Lys-37 and Lys-80.	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	Succinylation	Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes.	29211711
80	K	ubiquitylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	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	Specifically enriched in modifications associated with active chromatin such as methylation at Lys-5 (H3K4me), Lys-37 and Lys-80.	16267050
120	K	Methylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	16267050
120	K	ubiquitylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	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
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

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of H33_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HIRA_HUMAN	HIRA	physical	20211137
HIRA_HUMAN	HIRA	physical	14718166
NASP_HUMAN	NASP	physical	14718166
IPO4_HUMAN	IPO4	physical	14718166
RBBP4_HUMAN	RBBP4	physical	14718166
HAT1_HUMAN	HAT1	physical	14718166
ASF1A_HUMAN	ASF1A	physical	14718166
ASF1B_HUMAN	ASF1B	physical	14718166
ASH1L_HUMAN	ASH1L	physical	17403666
CARM1_HUMAN	CARM1	physical	17403666
EHMT1_HUMAN	EHMT1	physical	17403666
EHMT2_HUMAN	EHMT2	physical	17403666
KMT2C_HUMAN	KMT2C	physical	17403666
KDM4C_HUMAN	KDM4C	physical	17403666
HDAC5_HUMAN	HDAC5	physical	17403666
HDAC9_HUMAN	HDAC9	physical	17403666
NUCL_HUMAN	NCL	physical	17403666
SSRP1_HUMAN	SSRP1	physical	17403666
SP16H_HUMAN	SUPT16H	physical	17403666
CHD4_HUMAN	CHD4	physical	17403666
SF3B1_HUMAN	SF3B1	physical	17403666
TR150_HUMAN	THRAP3	physical	17403666
SP130_HUMAN	SAP130	physical	17403666
TIF1B_HUMAN	TRIM28	physical	17403666
PARP1_HUMAN	PARP1	physical	17403666
SF3B2_HUMAN	SF3B2	physical	17403666
HNRPK_HUMAN	HNRNPK	physical	17403666
CCD71_HUMAN	CCDC71	physical	17403666
RNF41_HUMAN	RNF41	physical	17403666
FBRL_HUMAN	FBL	physical	17403666
DHR12_HUMAN	DHRS12	physical	17403666
H2B2E_HUMAN	HIST2H2BE	physical	17403666
CBX3_HUMAN	CBX3	physical	17403666
H15_HUMAN	HIST1H1B	physical	17403666
HMGB1_HUMAN	HMGB1	physical	17403666
CBX5_HUMAN	CBX5	physical	17403666
CBX1_HUMAN	CBX1	physical	17403666
DAXX_HUMAN	DAXX	physical	20651253
ATRX_HUMAN	ATRX	physical	20651253
ASF1B_HUMAN	ASF1B	physical	20651253
KAT2B_HUMAN	KAT2B	physical	20651253
PARP1_HUMAN	PARP1	physical	20525793
PRKDC_HUMAN	PRKDC	physical	20504901
TOP2A_HUMAN	TOP2A	physical	20504901
ATRX_HUMAN	ATRX	physical	20504901
DAXX_HUMAN	DAXX	physical	20504901
IMA3_HUMAN	KPNA4	physical	20504901
PARP1_HUMAN	PARP1	physical	20504901
PARP2_HUMAN	PARP2	physical	20504901
XRCC5_HUMAN	XRCC5	physical	20504901
XRCC6_HUMAN	XRCC6	physical	20504901
TOP1_HUMAN	TOP1	physical	20504901
NASP_HUMAN	NASP	physical	20504901
HAT1_HUMAN	HAT1	physical	20504901
ASF1A_HUMAN	ASF1A	physical	20504901
ASF1B_HUMAN	ASF1B	physical	20504901
CABIN_HUMAN	CABIN1	physical	22195966
UBN1_HUMAN	UBN1	physical	22195966
HIRA_HUMAN	HIRA	physical	22195966
CBX3_HUMAN	CBX3	physical	22684280
DAXX_HUMAN	DAXX	physical	23142979
DAXX_HUMAN	DAXX	physical	23075851
ASF1A_HUMAN	ASF1A	physical	23075851
ASF1B_HUMAN	ASF1B	physical	23075851
CAF1A_HUMAN	CHAF1A	physical	23075851
HIRA_HUMAN	HIRA	physical	24209620
DAXX_HUMAN	DAXX	physical	24209620
H2AY_HUMAN	H2AFY	physical	23319141
ZMY11_HUMAN	ZMYND11	physical	24590075
ATRX_HUMAN	ATRX	physical	24530302
DAXX_HUMAN	DAXX	physical	24530302
ATRX_HUMAN	ATRX	physical	25538301
AF9_HUMAN	MLLT3	physical	25417107
AF9_YEAST	YAF9	physical	25417107
AF9_SCHPO	yaf9	physical	25417107
AF9_MOUSE	Mllt3	physical	25417107
ACTB_RABIT	ACTB	physical	23689370
ASF1A_HUMAN	ASF1A	physical	18971269

Drug and Disease Associations

• Kegg Disease
• 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.
• 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 LYS-80, AND MASSSPECTROMETRY.
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

"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, AND MASSSPECTROMETRY.
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; 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-5; LYS-10; LYS-28 ANDLYS-37, PHOSPHORYLATION AT THR-4; SER-11; SER-29 AND SER-32,ACETYLATION AT LYS-10 AND LYS-15, AND MASS SPECTROMETRY.
PubMed: 16185088

"Human spleen histone H3. Isolation and amino acid sequence.";
Ohe Y., Iwai K.;
J. Biochem. 90:1205-1211(1981).
Cited for: PARTIAL PROTEIN SEQUENCE, METHYLATION AT LYS-10; LYS-28 AND LYS-37,AND ACETYLATION AT LYS-15 AND LYS-24.
PubMed: 7309716

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

"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, AND MASSSPECTROMETRY.
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; 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-5; LYS-10; LYS-28 ANDLYS-37, PHOSPHORYLATION AT THR-4; SER-11; SER-29 AND SER-32,ACETYLATION AT LYS-10 AND LYS-15, AND MASS SPECTROMETRY.
PubMed: 16185088

"Human spleen histone H3. Isolation and amino acid sequence.";
Ohe Y., Iwai K.;
J. Biochem. 90:1205-1211(1981).
Cited for: PARTIAL PROTEIN SEQUENCE, METHYLATION AT LYS-10; LYS-28 AND LYS-37,AND ACETYLATION AT LYS-15 AND LYS-24.
PubMed: 7309716

"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

"Serine 31 phosphorylation of histone variant H3.3 is specific toregions bordering centromeres in metaphase chromosomes.";
Hake S.B., Garcia B.A., Kauer M., Baker S.P., Shabanowitz J.,Hunt D.F., Allis C.D.;
Proc. Natl. Acad. Sci. U.S.A. 102:6344-6349(2005).
Cited for: PHOSPHORYLATION AT SER-11; SER-29 AND SER-32, AND MASS SPECTROMETRY.
PubMed: 15851689

"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-5; LYS-10; LYS-28 ANDLYS-37, PHOSPHORYLATION AT THR-4; SER-11; SER-29 AND SER-32,ACETYLATION AT LYS-10 AND LYS-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

"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 THR-108, AND MASSSPECTROMETRY.
PubMed: 19690332

"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