H2B1_BOVIN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2B1_BOVIN
• UniProt AC: P62808
• Protein Name: Histone H2B type 1
• Organism: Bos taurus (Bovine).
• Sequence Length: 126
• 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: MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK

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
2	Acetylation	------MPEPAKSAP ------CCCCCCCCC	57.17	-
6	Acetylation	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	-
6	Other	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	-
6	Butyrylation	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	-
6	Crotonylation	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	-
6	Lactoylation	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	-
6	N6-crotonyl-L-lysine	--MPEPAKSAPAPKK --CCCCCCCCCCCCC	58.84	-
12	Other	AKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	-
12	Acetylation	AKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	-
12	N6-crotonyl-L-lysine	AKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	-
12	Lactoylation	AKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	-
12	Crotonylation	AKSAPAPKKGSKKAV CCCCCCCCCCCHHHH	72.39	-
13	N6-crotonyl-L-lysine	KSAPAPKKGSKKAVT CCCCCCCCCCHHHHH	68.32	-
13	Crotonylation	KSAPAPKKGSKKAVT CCCCCCCCCCHHHHH	68.32	-
13	Acetylation	KSAPAPKKGSKKAVT CCCCCCCCCCHHHHH	68.32	-
13	Other	KSAPAPKKGSKKAVT CCCCCCCCCCHHHHH	68.32	-
15	Phosphorylation	APAPKKGSKKAVTKA CCCCCCCCHHHHHHH	39.60	-
16	Crotonylation	PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH	54.11	-
16	Acetylation	PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH	54.11	-
16	N6-crotonyl-L-lysine	PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH	54.11	-
16	Lactoylation	PAPKKGSKKAVTKAQ CCCCCCCHHHHHHHH	54.11	-
17	N6-crotonyl-L-lysine	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	-
17	Crotonylation	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	-
17	Lactoylation	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	-
17	Glutarylation	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	-
17	Acetylation	APKKGSKKAVTKAQK CCCCCCHHHHHHHHH	50.19	-
21	Acetylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	-
21	N6-crotonyl-L-lysine	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	-
21	Butyrylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	-
21	Other	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	-
21	Crotonylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	-
21	Lactoylation	GSKKAVTKAQKKDGK CCHHHHHHHHHHCCC	42.07	-
24	Lactoylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	-
24	Crotonylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	-
24	Other	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	-
24	Acetylation	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	-
24	N6-crotonyl-L-lysine	KAVTKAQKKDGKKRK HHHHHHHHHCCCCCC	58.66	-
25	Other	AVTKAQKKDGKKRKR HHHHHHHHCCCCCCC	60.68	-
35	Glutarylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	-
35	Succinylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	-
35	Crotonylation	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	-
35	Other	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	-
35	N6-crotonyl-L-lysine	KKRKRSRKESYSVYV CCCCCCCHHHHHHHH	52.86	-
37	Phosphorylation	RKRSRKESYSVYVYK CCCCCHHHHHHHHHH	26.24	-
44	Other	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	-
44	Lactoylation	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	-
44	Glutarylation	SYSVYVYKVLKQVHP HHHHHHHHHHHHHCC	30.92	-
47	Methylation	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	-
47	Glutarylation	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	-
47	Other	VYVYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	-
56	Phosphorylation	VHPDTGISSKAMGIM HCCCCCCCHHHHHHH	27.42	29541418
57	Phosphorylation	HPDTGISSKAMGIMN CCCCCCCHHHHHHHH	23.63	29541418
58	"N6,N6-dimethyllysine"	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	-
58	Methylation	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	-
58	Other	PDTGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	-
80	Methylation	RIAGEASRLAHYNKR HHHHHHHHHHHHCCC	42.83	-
86	"N6,N6,N6-trimethyllysine"	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	-
86	Acetylation	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	-
86	Other	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	-
86	Methylation	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	-
86	Lactoylation	SRLAHYNKRSTITSR HHHHHHCCCCCCCHH	40.33	-
87	Methylation	RLAHYNKRSTITSRE HHHHHCCCCCCCHHH	35.08	-
93	Methylation	KRSTITSREIQTAVR CCCCCCHHHHHHHHH	36.07	-
109	Lactoylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	-
109	Glutarylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	-
109	Other	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	-
109	Methylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	-
113	Phosphorylation	ELAKHAVSEGTKAVT HHHHHHHHHHHHHHH	30.96	29541418
113	O-linked_Glycosylation	ELAKHAVSEGTKAVT HHHHHHHHHHHHHHH	30.96	-
116	Phosphorylation	KHAVSEGTKAVTKYT HHHHHHHHHHHHHHC	16.27	-
117	Methylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	-
117	Lactoylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	-
117	Other	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	-
117	Glutarylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	-
117	Succinylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	-
121	Lactoylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	-
121	Glutarylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	-
121	Other	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	-
121	Succinylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	-
121	Ubiquitination	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	2713375

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
15	S	Phosphorylation	Kinase	MST1	Q24K22	Uniprot
37	S	Phosphorylation	Kinase	AMPK	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of H2B1_BOVIN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of H2B1_BOVIN !!

Protein-Protein Interaction

Oops, there are no PPI records of H2B1_BOVIN !!

Drug and Disease Associations

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