H32_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H32_MOUSE
• UniProt AC: P84228
• Protein Name: Histone H3.2
• Gene Name: Hist1h3b
• Organism: Mus musculus (Mouse).
• 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	15339660
3	Methylation	-----MARTKQTARK -----CCCCCHHHHH	40.95	-
4	Phosphorylation	----MARTKQTARKS ----CCCCCHHHHHC	20.26	14987995
5	Allysine	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
5	Acetylation	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	17194708
5	Crotonylation	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	21925322
5	Deamination	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
5	Methylation	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	17194708
5	Other	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	27105115
6	Formation of an isopeptide bond	--MARTKQTARKSTG --CCCCCHHHHHCCC	39.52	-
6	Serotonylation	--MARTKQTARKSTG --CCCCCHHHHHCCC	39.52	30867594
7	Phosphorylation	-MARTKQTARKSTGG -CCCCCHHHHHCCCC	29.95	-
9	Citrullination	ARTKQTARKSTGGKA CCCCHHHHHCCCCCC	36.52	-
9	Citrullination	ARTKQTARKSTGGKA CCCCHHHHHCCCCCC	36.52	15339660
9	Methylation	ARTKQTARKSTGGKA CCCCHHHHHCCCCCC	36.52	15485929
10	"N6,N6,N6-trimethyllysine"	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
10	Acetylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	17194708
10	Crotonylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	21925322
10	Lactoylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
10	Methylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	17194708
10	Other	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	27105115
11	ADP-ribosylation	TKQTARKSTGGKAPR CCHHHHHCCCCCCCH	27.08	-
11	Phosphorylation	TKQTARKSTGGKAPR CCHHHHHCCCCCCCH	27.08	10469656
12	Phosphorylation	KQTARKSTGGKAPRK CHHHHHCCCCCCCHH	53.65	18243098
15	Acetylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	13678296
15	Glutarylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
15	Lactoylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	31645732
15	Methylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
15	Other	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	27105115
15	Succinylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
18	Asymmetric dimethylarginine	STGGKAPRKQLATKA CCCCCCCHHHHHHHH	44.18	-
18	Citrullination	STGGKAPRKQLATKA CCCCCCCHHHHHHHH	44.18	15339660
18	Methylation	STGGKAPRKQLATKA CCCCCCCHHHHHHHH	44.18	11751582
19	N6-crotonyl-L-lysine	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Acetylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	13678296
19	Butyrylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	27105113
19	Crotonylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	21925322
19	Glutarylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Lactoylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	31645732
19	Methylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	17194708
19	Other	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	27105115
24	N6-crotonyl-L-lysine	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Acetylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	13678296
24	Butyrylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	27105113
24	Crotonylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	21925322
24	Glutarylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Lactoylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	31645732
24	Malonylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	26073543
24	Methylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	17194708
24	Other	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	27105115
27	Citrullination	QLATKAARKSAPATG HHHHHHHHHHCCCCC	38.02	-
27	Citrullination	QLATKAARKSAPATG HHHHHHHHHHCCCCC	38.02	15339660
28	"N6,N6,N6-trimethyllysine"	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	-
28	Acetylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	17194708
28	Butyrylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	27105113
28	Crotonylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	21925322
28	Glutarylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	-
28	Lactoylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	31645732
28	Methylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	17194708
28	Other	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	24681537
29	ADP-ribosylation	ATKAARKSAPATGGV HHHHHHHHCCCCCCC	33.65	-
29	Phosphorylation	ATKAARKSAPATGGV HHHHHHHHCCCCCCC	33.65	26824392
37	"N6,N6,N6-trimethyllysine"	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	-
37	Acetylation	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	17189264
37	Butyrylation	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	27105113
37	Methylation	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	17194708
37	Other	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	24681537
38	Butyrylation	PATGGVKKPHRYRPG CCCCCCCCCCCCCCC	43.58	27105113
38	Methylation	PATGGVKKPHRYRPG CCCCCCCCCCCCCCC	43.58	-
42	Phosphorylation	GVKKPHRYRPGTVAL CCCCCCCCCCCCHHH	20.37	28066266
46	Phosphorylation	PHRYRPGTVALREIR CCCCCCCCHHHHHHH	12.80	14729942
55	Phosphorylation	ALREIRRYQKSTELL HHHHHHHHHHCHHHH	15.50	25159016
57	"N6,N6,N6-trimethyllysine"	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Acetylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Crotonylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	21925322
57	Glutarylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Lactoylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	31645732
57	Malonylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	26073543
57	Methylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Other	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	27105115
57	Succinylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	22389435
58	Phosphorylation	EIRRYQKSTELLIRK HHHHHHHCHHHHHHH	16.16	26824392
59	Phosphorylation	IRRYQKSTELLIRKL HHHHHHCHHHHHHHC	37.37	25521595
65	Methylation	STELLIRKLPFQRLV CHHHHHHHCCHHHHH	54.22	-
65	Other	STELLIRKLPFQRLV CHHHHHHHCCHHHHH	54.22	24681537
80	"N6,N6,N6-trimethyllysine"	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	-
80	Acetylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	-
80	Butyrylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	27105113
80	Glutarylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	-
80	Lactoylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	-
80	Malonylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	26073543
80	Methylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	17194708
80	Other	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	24681537
80	Succinylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHCH	49.79	22389435
81	Phosphorylation	EIAQDFKTDLRFQSS HHHHHHCCCHHHCHH	40.01	25521595
87	Phosphorylation	KTDLRFQSSAVMALQ CCCHHHCHHHHHHHH	19.97	26239621
88	Phosphorylation	TDLRFQSSAVMALQE CCHHHCHHHHHHHHH	17.69	26239621
97	Phosphorylation	VMALQEASEAYLVGL HHHHHHHHHHHHHHH	23.23	26239621
100	Phosphorylation	LQEASEAYLVGLFED HHHHHHHHHHHHHCC	9.62	26239621
108	Phosphorylation	LVGLFEDTNLCAIHA HHHHHCCCCEEEEEE	23.93	26239621
111	S-palmitoylation	LFEDTNLCAIHAKRV HHCCCCEEEEEEEEC	3.47	-
116	Acetylation	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	-
116	Butyrylation	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	-
116	Glutarylation	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	-
119	Phosphorylation	AIHAKRVTIMPKDIQ EEEEEECEECHHHHH	18.65	29109428
123	Acetylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	Butyrylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	27105113
123	Crotonylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	Glutarylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	Malonylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	26073543
123	Methylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	13678296
123	Other	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	24681537
123	Succinylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-

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	HASPIN	Q9Z0R0	Uniprot
7	T	Phosphorylation	Kinase	PKC	-	Uniprot
11	S	Phosphorylation	Kinase	ALTERNATE	-	Uniprot
12	T	Phosphorylation	Kinase	PKC	-	Uniprot
29	S	Phosphorylation	Kinase	ALTERNATE	-	Uniprot

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).	15339660
4	T	Phosphorylation	Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and dephosphorylated during anaphase.	15681610
5	K	ubiquitylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	17194708
5	K	Acetylation	Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4.	17194708
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).	17194708
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.	17194708
5	K	Methylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	17194708
5	K	Methylation	Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4.	17194708
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.	17194708
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.	17194708
5	K	Methylation	Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation.	17194708
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.	13678296
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.	13678296
9	R	Methylation	Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression.	15339660
9	R	Methylation	Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.	15339660
9	R	Methylation	Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s).	15339660
9	R	Citrullination	Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.	15339660
9	R	Acetylation	Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s).	15339660
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).	13678296
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.	13678296
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.	13678296
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.	13678296
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.	13678296
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.	13678296
10	K	Acetylation	Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s).	13678296
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.	13678296
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.	13678296
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).	13678296
10	K	Methylation	Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s).	13678296
10	K	Methylation	Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin.	13678296
10	K	Methylation	Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression.	13678296
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.	13678296
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.	10464286
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.	10464286
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).	10464286
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.	10464286
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.	10464286
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.	10464286
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.	10464286
11	S	Phosphorylation	Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis.	10464286
11	S	Phosphorylation	Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin.	10464286
11	S	Phosphorylation	Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation.	10464286
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.	10464286
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).	10464286
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.	13678296
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.	13678296
12	T	Phosphorylation	At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1.	13678296
18	R	Citrullination	Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.	12498683
18	R	Acetylation	Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me).	12498683
18	R	Methylation	Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me).	12498683
18	R	Methylation	Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation.	12498683
18	R	Methylation	Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.	12498683
19	K	Methylation	Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me).	12498683
19	K	Acetylation	Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me).	12498683
24	K	Methylation	Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me).	12498683
24	K	Acetylation	Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me).	12498683
28	K	Methylation	Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression.	13678296
28	K	Methylation	Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin.	13678296
29	S	Phosphorylation	Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation.	10464286
37	K	Methylation	Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation.	13678296
57	K	Methylation	Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication.	21925322
80	K	Methylation	Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1.	13678296
80	K	Methylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	13678296
80	K	Methylation	Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation.	13678296
80	K	ubiquitylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	13678296
80	K	Succinylation	Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes.	13678296
120	K	ubiquitylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	13678296
120	K	Methylation	Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'.	13678296
123	K	Succinylation	Desuccinylation at Lys-123 (H3K122succ) by SIRT7 in response to DNA damage promotes chromatin condensation and double-strand breaks (DSBs) repair.	13678296
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.	13678296

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_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of H32_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"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 AND LYS-28,METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 ANDLYS-80, AND MASS SPECTROMETRY.
PubMed: 17194708

"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

"Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 andnegatively regulates expression of ST7 and NM23 tumor suppressorgenes.";
Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.;
Mol. Cell. Biol. 24:9630-9645(2004).
Cited for: METHYLATION AT ARG-9, AND ACETYLATION AT LYS-10.
PubMed: 15485929

"Identification of methylation and acetylation sites on mouse histoneH3 using matrix-assisted laser desorption/ionization time-of-flightand nanoelectrospray ionization tandem mass spectrometry.";
Cocklin R.R., Wang M.;
J. Protein Chem. 22:327-334(2003).
Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-10;LYS-28; LYS-37; LYS-80 AND LYS-123, AND MASS SPECTROMETRY.
PubMed: 13678296

"Crosstalk between CARM1 methylation and CBP acetylation on histoneH3.";
Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.;
Curr. Biol. 12:2090-2097(2002).
Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, AND METHYLATION AT ARG-18.
PubMed: 12498683

Methylation

"Arginine methyltransferase CARM1 is a promoter-specific regulator ofNF-kappaB-dependent gene expression.";
Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C.,Imhof R., Bedford M.T., Natoli G., Hottiger M.O.;
EMBO J. 24:85-96(2005).
Cited for: METHYLATION AT ARG-18.
PubMed: 15616592

"Methylation at arginine 17 of histone H3 is linked to geneactivation.";
Bauer U.-M., Daujat S., Nielsen S.J., Nightingale K., Kouzarides T.;
EMBO Rep. 3:39-44(2002).
Cited for: METHYLATION AT ARG-18.
PubMed: 11751582

"Crosstalk between CARM1 methylation and CBP acetylation on histoneH3.";
Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.;
Curr. Biol. 12:2090-2097(2002).
Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, AND METHYLATION AT ARG-18.
PubMed: 12498683

"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 AND LYS-28,METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 ANDLYS-80, AND MASS SPECTROMETRY.
PubMed: 17194708

"Identification of methylation and acetylation sites on mouse histoneH3 using matrix-assisted laser desorption/ionization time-of-flightand nanoelectrospray ionization tandem mass spectrometry.";
Cocklin R.R., Wang M.;
J. Protein Chem. 22:327-334(2003).
Cited for: ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-10;LYS-28; LYS-37; LYS-80 AND LYS-123, AND MASS SPECTROMETRY.
PubMed: 13678296

"Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 andnegatively regulates expression of ST7 and NM23 tumor suppressorgenes.";
Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.;
Mol. Cell. Biol. 24:9630-9645(2004).
Cited for: METHYLATION AT ARG-9, AND ACETYLATION AT LYS-10.
PubMed: 15485929

Phosphorylation

"Stimulation of the Ras-MAPK pathway leads to independentphosphorylation of histone H3 on serine 10 and 28.";
Dunn K.L., Davie J.R.;
Oncogene 24:3492-3502(2005).
Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
PubMed: 15735677

"MAP kinase-mediated phosphorylation of distinct pools of histone H3at S10 or S28 via mitogen- and stress-activated kinase 1/2.";
Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J.,Nightingale K., Iborra F.J., Mahadevan L.C.;
J. Cell Sci. 118:2247-2259(2005).
Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
PubMed: 15870105

"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 AND SER-11.
PubMed: 15681610

"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

"Ultraviolet B-induced phosphorylation of histone H3 at serine 28 ismediated by MSK1.";
Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M.,Ma W.-Y., Dong Z.;
J. Biol. Chem. 276:33213-33219(2001).
Cited for: PHOSPHORYLATION AT SER-29.
PubMed: 11441012

"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: PHOSPHORYLATION AT SER-11 AND SER-29.
PubMed: 10464286