dbPTM

H31_BOVIN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H31_BOVIN
UniProt AC	P68432
Protein Name	Histone H3.1
Gene Name
Organism	Bos taurus (Bovine).
Sequence Length	136
Subcellular Localization	Nucleus. Chromosome.
Protein Description	Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling..
Protein Sequence	MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA

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	-
3	Methylation	-----MARTKQTARK -----CCCCCHHHHH	40.95	-
4	Phosphorylation	----MARTKQTARKS ----CCCCCHHHHHC	20.26	-
5	Deamination	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
5	Other	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
5	Crotonylation	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
5	Allysine	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
5	Acetylation	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
5	Methylation	---MARTKQTARKST ---CCCCCHHHHHCC	39.85	-
6	Formation of an isopeptide bond	--MARTKQTARKSTG --CCCCCHHHHHCCC	39.52	-
6	Serotonylation	--MARTKQTARKSTG --CCCCCHHHHHCCC	39.52	-
7	Phosphorylation	-MARTKQTARKSTGG -CCCCCHHHHHCCCC	29.95	-
9	Citrullination	ARTKQTARKSTGGKA CCCCHHHHHCCCCCC	36.52	-
9	Methylation	ARTKQTARKSTGGKA CCCCHHHHHCCCCCC	36.52	-
9	Citrullination	ARTKQTARKSTGGKA CCCCHHHHHCCCCCC	36.52	-
10	Lactoylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
10	Succinylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
10	Crotonylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
10	Other	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
10	"N6,N6,N6-trimethyllysine"	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
10	Methylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	4735580
10	Acetylation	RTKQTARKSTGGKAP CCCHHHHHCCCCCCC	50.32	-
11	Phosphorylation	TKQTARKSTGGKAPR CCHHHHHCCCCCCCH	27.08	10464286
11	ADP-ribosylation	TKQTARKSTGGKAPR CCHHHHHCCCCCCCH	27.08	-
12	Phosphorylation	KQTARKSTGGKAPRK CHHHHHCCCCCCCHH	53.65	-
15	Glutarylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
15	Lactoylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
15	Succinylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
15	Other	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	-
15	Acetylation	ARKSTGGKAPRKQLA HHHCCCCCCCHHHHH	57.47	4735580
18	Citrullination	STGGKAPRKQLATKA CCCCCCCHHHHHHHH	44.18	-
18	Methylation	STGGKAPRKQLATKA CCCCCCCHHHHHHHH	44.18	-
18	Asymmetric dimethylarginine	STGGKAPRKQLATKA CCCCCCCHHHHHHHH	44.18	-
19	Glutarylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Other	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Butyrylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Crotonylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	N6-crotonyl-L-lysine	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Acetylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Methylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
19	Lactoylation	TGGKAPRKQLATKAA CCCCCCHHHHHHHHH	48.91	-
24	N6-crotonyl-L-lysine	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Acetylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	4735580
24	Glutarylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Crotonylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Lactoylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Butyrylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Other	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
24	Methylation	PRKQLATKAARKSAP CHHHHHHHHHHHHCC	34.15	-
27	Citrullination	QLATKAARKSAPATG HHHHHHHHHHCCCCC	38.02	-
27	Citrullination	QLATKAARKSAPATG HHHHHHHHHHCCCCC	38.02	-
28	Methylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	4735580
28	"N6,N6,N6-trimethyllysine"	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	-
28	Crotonylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	-
28	Glutarylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	-
28	Other	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	-
28	Lactoylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	-
28	Acetylation	LATKAARKSAPATGG HHHHHHHHHCCCCCC	46.36	-
29	ADP-ribosylation	ATKAARKSAPATGGV HHHHHHHHCCCCCCC	33.65	-
29	Phosphorylation	ATKAARKSAPATGGV HHHHHHHHCCCCCCC	33.65	10464286
37	"N6,N6,N6-trimethyllysine"	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	-
37	Acetylation	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	-
37	Methylation	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	-
37	Other	APATGGVKKPHRYRP CCCCCCCCCCCCCCC	64.95	-
38	Methylation	PATGGVKKPHRYRPG CCCCCCCCCCCCCCC	43.58	-
42	Phosphorylation	GVKKPHRYRPGTVAL CCCCCCCCCCCCHHH	20.37	-
57	"N6,N6,N6-trimethyllysine"	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Acetylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Methylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Succinylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Lactoylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Other	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Glutarylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
57	Crotonylation	REIRRYQKSTELLIR HHHHHHHHCHHHHHH	50.87	-
58	Phosphorylation	EIRRYQKSTELLIRK HHHHHHHCHHHHHHH	16.16	-
65	Other	STELLIRKLPFQRLV CHHHHHHHCCHHHHH	54.22	-
65	Methylation	STELLIRKLPFQRLV CHHHHHHHCCHHHHH	54.22	-
80	Lactoylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	-
80	"N6,N6,N6-trimethyllysine"	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	-
80	Glutarylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	-
80	Acetylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	-
80	Other	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	-
80	Succinylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	-
80	Methylation	REIAQDFKTDLRFQS HHHHHHHCCCHHHHH	49.79	-
81	Phosphorylation	EIAQDFKTDLRFQSS HHHHHHCCCHHHHHH	40.01	29541418
87	Phosphorylation	KTDLRFQSSAVMALQ CCCHHHHHHHHHHHH	19.97	-
108	Phosphorylation	LVGLFEDTNLCAIHA HHHHHCCCCEEEEEE	23.93	-
116	Acetylation	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	-
116	Glutarylation	NLCAIHAKRVTIMPK CEEEEEEEECEECHH	32.99	-
123	Succinylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	Methylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	Glutarylation	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	Other	KRVTIMPKDIQLARR EECEECHHHHHHHHH	50.51	-
123	Acetylation	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
7	T	Phosphorylation	Kinase	PKC	-	Uniprot
11	S	Phosphorylation	Kinase	RPS6KA3	F1MZW8	GPS
11	S	Phosphorylation	Kinase	RPS6KA5	E1BN61	GPS
11	S	Phosphorylation	Kinase	RPS6KA4	F1MQE1	GPS
11	S	Phosphorylation	Kinase	AURKC	F1MY86	GPS
11	S	Phosphorylation	Kinase	AURKB	Q08DN4	GPS
11	S	Phosphorylation	Kinase	ALTERNATE	-	Uniprot
12	T	Phosphorylation	Kinase	PKC	-	Uniprot
12	T	Phosphorylation	Kinase	CHEK1	-	Uniprot
29	S	Phosphorylation	Kinase	RPS6KA5	E1BN61	GPS
29	S	Phosphorylation	Kinase	AURKC	F1MY86	GPS
29	S	Phosphorylation	Kinase	AURKB	Q08DN4	GPS
29	S	Phosphorylation	Kinase	ALTERNATE	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of H31_BOVIN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of H31_BOVIN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of H31_BOVIN !!

Drug and Disease Associations

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

Regulatory Network of H31_BOVIN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Histone 3. 3. Sequence studies on the cyanogen bromide peptides;complete amino acid sequence of calf thymus histone 3."; Delange R.J., Hooper J.A., Smith E.L.; J. Biol. Chem. 248:3261-3274(1973). Cited for: PROTEIN SEQUENCE OF 2-136, DISULFIDE BONDS, ACETYLATION AT LYS-15 ANDLYS-24, AND METHYLATION AT LYS-10 AND LYS-28.	4735580 [Abstract]
Methylation
Reference	PubMed
"Histone 3. 3. Sequence studies on the cyanogen bromide peptides;complete amino acid sequence of calf thymus histone 3."; Delange R.J., Hooper J.A., Smith E.L.; J. Biol. Chem. 248:3261-3274(1973). Cited for: PROTEIN SEQUENCE OF 2-136, DISULFIDE BONDS, ACETYLATION AT LYS-15 ANDLYS-24, AND METHYLATION AT LYS-10 AND LYS-28.	4735580 [Abstract]
Phosphorylation
Reference	PubMed
"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.	10464286 [Abstract]