H2B10_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: H2B10_ARATH
• UniProt AC: Q9FFC0
• Protein Name: Histone H2B.10
• Gene Name: At5g22880
• 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: MAKADKKPAEKKPAEKTPAAEPAAAAEKKPKAGKKLPKEPAGAGDKKKKRSKKNVETYKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLAGESSKLARYNKKPTITSREIQTAVRLVLPGELAKHAVSEGTKAVTKFTSS

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
3	Methylation	-----MAKADKKPAE -----CCCCCCCCCC	56.68	-
6	Acetylation	--MAKADKKPAEKKP --CCCCCCCCCCCCC	66.57	17691833
11	Acetylation	ADKKPAEKKPAEKTP CCCCCCCCCCCCCCC	67.19	17691833
12	"N6,N6-dimethyllysine"	DKKPAEKKPAEKTPA CCCCCCCCCCCCCCC	40.75	-
12	Methylation	DKKPAEKKPAEKTPA CCCCCCCCCCCCCCC	40.75	17691833
16	Acetylation	AEKKPAEKTPAAEPA CCCCCCCCCCCCCHH	63.01	17691833
17	Phosphorylation	EKKPAEKTPAAEPAA CCCCCCCCCCCCHHH	15.07	25561503
28	Acetylation	EPAAAAEKKPKAGKK CHHHHHHHCCCCCCC	70.42	17691833
34	Acetylation	EKKPKAGKKLPKEPA HHCCCCCCCCCCCCC	56.87	17691833
35	Acetylation	KKPKAGKKLPKEPAG HCCCCCCCCCCCCCC	69.93	17691833
67	Methylation	IYIFKVLKQVHPDIG HHHHHHHHHHCCCCC	53.94	-
76	Phosphorylation	VHPDIGISSKAMGIM HCCCCCCCHHHHHHH	22.15	25561503
77	Phosphorylation	HPDIGISSKAMGIMN CCCCCCCHHHHHHHH	23.63	25561503
78	Methylation	PDIGISSKAMGIMNS CCCCCCHHHHHHHHH	35.29	-
111	Phosphorylation	YNKKPTITSREIQTA HCCCCCCCHHHHHHH	24.98	25561503
112	Phosphorylation	NKKPTITSREIQTAV CCCCCCCHHHHHHHH	24.86	25561503
129	Methylation	VLPGELAKHAVSEGT HCCHHHHHHHHHHHC	44.73	-
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 H2B10_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of H2B10_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 H2B10_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HTR12_ARATH	HTR12	physical	23154417

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-6; LYS-11; LYS-16; LYS-28; LYS-34 AND LYS-35,METHYLATION AT LYS-12, 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-6; LYS-11; LYS-16; LYS-28; LYS-34 AND LYS-35,METHYLATION AT LYS-12, AND MASS SPECTROMETRY.
PubMed: 17691833