H2B7_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2B7_ARATH
• UniProt AC: Q9LZT0
• Protein Name: Histone H2B.7
• Gene Name: At3g46030
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 145
• 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: MAPKAEKKPAEKKPVEEKSKAEKAPAEKKPKAGKKLPKEAGAGGDKKKKMKKKSVETYKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLASESSKLARYNKKPTITSREIQTAVRLVLPGELAKHAVSEGTKAVTKFTSS

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	Methylation	------MAPKAEKKP ------CCCHHHCCC	17.82	17691833
2	"N,N-dimethylalanine"	------MAPKAEKKP ------CCCHHHCCC	17.82	-
4	Methylation	----MAPKAEKKPAE ----CCCHHHCCCCC	60.69	17691833
7	Acetylation	-MAPKAEKKPAEKKP -CCCHHHCCCCCCCC	69.76	17691833
12	Acetylation	AEKKPAEKKPVEEKS HHCCCCCCCCHHHHH	65.56	17691833
13	Methylation	EKKPAEKKPVEEKSK HCCCCCCCCHHHHHH	45.89	-
13	"N6,N6-dimethyllysine"	EKKPAEKKPVEEKSK HCCCCCCCCHHHHHH	45.89	-
23	Acetylation	EEKSKAEKAPAEKKP HHHHHHHCCCHHHCC	65.61	17691833
28	Acetylation	AEKAPAEKKPKAGKK HHCCCHHHCCCCCCC	76.20	17691833
29	Acetylation	EKAPAEKKPKAGKKL HCCCHHHCCCCCCCC	43.16	-
34	Acetylation	EKKPKAGKKLPKEAG HHCCCCCCCCCHHHC	56.87	17691833
35	Acetylation	KKPKAGKKLPKEAGA HCCCCCCCCCHHHCC	69.93	17691833
76	Phosphorylation	VHPDIGISSKAMGIM HCCCCCCCHHHHHHH	22.15	25561503
77	Phosphorylation	HPDIGISSKAMGIMN CCCCCCCHHHHHHHH	23.63	25561503
111	Phosphorylation	YNKKPTITSREIQTA HCCCCCCCHHHHHHH	24.98	25561503
112	Phosphorylation	NKKPTITSREIQTAV CCCCCCCHHHHHHHH	24.86	25561503
133	Phosphorylation	ELAKHAVSEGTKAVT HHHHHHHHHHCHHHH	30.96	25561503

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of H2B7_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of H2B7_ARATH !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of H2B7_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of H2B7_ARATH !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"Characterization of post-translational modifications of histone H2B-variants isolated from Arabidopsis thaliana.";
Bergmueller E., Gehrig P.M., Gruissem W.;
J. Proteome Res. 6:3655-3668(2007).
Cited for: ACETYLATION AT LYS-7; LYS-12; LYS-23; LYS-28; LYS-34 AND LYS-35,METHYLATION AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 17691833

Methylation

"Characterization of post-translational modifications of histone H2B-variants isolated from Arabidopsis thaliana.";
Bergmueller E., Gehrig P.M., Gruissem W.;
J. Proteome Res. 6:3655-3668(2007).
Cited for: ACETYLATION AT LYS-7; LYS-12; LYS-23; LYS-28; LYS-34 AND LYS-35,METHYLATION AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 17691833