H2B1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2B1_ARATH
• UniProt AC: Q9LQQ4
• Protein Name: Histone H2B.1
• Gene Name: At1g07790
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 148
• 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: MAPRAEKKPAEKKTAAERPVEENKAAEKAPAEKKPKAGKKLPPKEAGDKKKKRSKKNVETYKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLAQESSKLARYNKKPTITSREIQTAVRLVLPGELAKHAVSEGTKAVTKFTSS

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	------MAPRAEKKP ------CCCHHHCCH	11.42	17691833
2	"N,N-dimethylalanine"	------MAPRAEKKP ------CCCHHHCCH	11.42	-
7	Acetylation	-MAPRAEKKPAEKKT -CCCHHHCCHHHHCC	64.17	17691833
12	Acetylation	AEKKPAEKKTAAERP HHCCHHHHCCCCCCC	58.49	-
13	Methylation	EKKPAEKKTAAERPV HCCHHHHCCCCCCCH	34.60	-
13	"N6,N6-dimethyllysine"	EKKPAEKKTAAERPV HCCHHHHCCCCCCCH	34.60	-
28	Acetylation	EENKAAEKAPAEKKP HHCHHHHHCCCCCCC	55.75	-
33	Acetylation	AEKAPAEKKPKAGKK HHHCCCCCCCCCCCC	76.20	-
39	Acetylation	EKKPKAGKKLPPKEA CCCCCCCCCCCCHHH	56.87	17691833
40	Acetylation	KKPKAGKKLPPKEAG CCCCCCCCCCCHHHC	66.37	17691833
79	Phosphorylation	VHPDIGISSKAMGIM HCCCCCCCHHHHHHH	22.15	25561503
80	Phosphorylation	HPDIGISSKAMGIMN CCCCCCCHHHHHHHH	23.63	25561503
83	Sulfoxidation	IGISSKAMGIMNSFI CCCCHHHHHHHHHHH	4.26	23289948
86	Sulfoxidation	SSKAMGIMNSFINDI CHHHHHHHHHHHHHH	2.59	23289948
114	Phosphorylation	YNKKPTITSREIQTA HCCCCCCCHHHHHHH	24.98	25561503
115	Phosphorylation	NKKPTITSREIQTAV CCCCCCCHHHHHHHH	24.86	25561503
136	Phosphorylation	ELAKHAVSEGTKAVT HHHHHHHHHHCHHHH	30.96	25561503
144	Ubiquitination	EGTKAVTKFTSS--- HHCHHHHHHCCC---	39.79	17554311

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

Oops, there are no upstream regulatory protein records of H2B1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of H2B1_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 H2B1_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of H2B1_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-39 AND LYS-40, METHYLATION AT ALA-2, ANDMASS 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-39 AND LYS-40, METHYLATION AT ALA-2, ANDMASS SPECTROMETRY.
PubMed: 17691833

Ubiquitylation

"Control of DNA methylation and heterochromatic silencing by histoneH2B deubiquitination.";
Sridhar V.V., Kapoor A., Zhang K., Zhu J., Zhou T., Hasegawa P.M.,Bressan R.A., Zhu J.-K.;
Nature 447:735-738(2007).
Cited for: UBIQUITINATION AT LYS-144, AND MASS SPECTROMETRY.
PubMed: 17554311