dbPTM

H2B_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	H2B_DROME
UniProt AC	P02283
Protein Name	Histone H2B
Gene Name	His2B
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	123
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	MPPKTSGKAAKKAGKAQKNITKTDKKKKRKRKESYAIYIYKVLKQVHPDTGISSKAMSIMNSFVNDIFERIAAEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Methylation	------MPPKTSGKA ------CCCCCCHHH	38.81	3127388
8	Acetylation	MPPKTSGKAAKKAGK CCCCCCHHHHHHHHH	44.96	21791702
11	Acetylation	KTSGKAAKKAGKAQK CCCHHHHHHHHHHHH	48.27	21791702
12	Acetylation	TSGKAAKKAGKAQKN CCHHHHHHHHHHHHC	58.61	21791702
15	Acetylation	KAAKKAGKAQKNITK HHHHHHHHHHHCCCC	53.13	21791702
18	Acetylation	KKAGKAQKNITKTDK HHHHHHHHCCCCCCH	56.00	21791702
21	Phosphorylation	GKAQKNITKTDKKKK HHHHHCCCCCCHHHH	36.97	22817900
22	Acetylation	KAQKNITKTDKKKKR HHHHCCCCCCHHHHH	51.43	21791702
34	Phosphorylation	KKRKRKESYAIYIYK HHHHHHHHHHHHHHH	23.93	22817900
44	Succinylation	IYIYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	22389435
44	Acetylation	IYIYKVLKQVHPDTG HHHHHHHHHHCCCCC	53.94	21791702
54	Phosphorylation	HPDTGISSKAMSIMN CCCCCCCHHHHHHHH	23.63	27794539
85	Phosphorylation	LAHYNKRSTITSREI HHHHCCCCCCCHHHH	26.27	27626673
88	Phosphorylation	YNKRSTITSREIQTA HCCCCCCCHHHHHHH	23.09	27626673
106	Acetylation	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	21791702
106	Ubiquitination	LLPGELAKHAVSEGT HCCHHHHHHHHHHHH	44.73	31113955
110	O-linked_Glycosylation	ELAKHAVSEGTKAVT HHHHHHHHHHHHHHH	30.96	-
114	Succinylation	HAVSEGTKAVTKYTS HHHHHHHHHHHHHCC	52.28	22389435
118	Succinylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	22389435
118	Acetylation	EGTKAVTKYTSSK-- HHHHHHHHHCCCC--	39.67	21791702

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
34	S	Phosphorylation	Kinase	TAF1	P51123	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	Bre1	Q9VRP9	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of H2B_DROME !!

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 H2B_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of H2B_DROME !!

Drug and Disease Associations

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

Regulatory Network of H2B_DROME

Related Literatures of Post-Translational Modification

Methylation
Reference	PubMed
"Methylation of Drosophila histones at proline, lysine, and arginineresidues during heat shock."; Desrosiers R., Tanguay R.M.; J. Biol. Chem. 263:4686-4692(1988). Cited for: METHYLATION AT PRO-2.	3127388 [Abstract]
Phosphorylation
Reference	PubMed
"TAF1 activates transcription by phosphorylation of serine 33 inhistone H2B."; Maile T., Kwoczynski S., Katzenberger R.J., Wassarman D.A., Sauer F.; Science 304:1010-1014(2004). Cited for: PHOSPHORYLATION AT SER-34.	15143281 [Abstract]