H2B6_ARATH - dbPTM
H2B6_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID H2B6_ARATH
UniProt AC O23629
Protein Name Histone H2B.6
Gene Name H2B
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 150
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 MAPRAEKKPAEKKPAAEKPVEEKSKAEKAPAEKKPKAGKKLPKEAGAGGDKKKKMKKKSVETYKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLASESSKLARYNKKPTITSREIQTAVRLVLPGELAKHAVSEGTKAVTKFTSS
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 Orthologous
Protein Cluster
2Methylation------MAPRAEKKP
------CCCHHHCCC
11.4217691833
2"N,N-dimethylalanine"------MAPRAEKKP
------CCCHHHCCC
11.42-
7Acetylation-MAPRAEKKPAEKKP
-CCCHHHCCCCCCCC
64.1717691833
12AcetylationAEKKPAEKKPAAEKP
HHCCCCCCCCCCCCC
67.1917691833
13"N6,N6-dimethyllysine"EKKPAEKKPAAEKPV
HCCCCCCCCCCCCCH
31.24-
13MethylationEKKPAEKKPAAEKPV
HCCCCCCCCCCCCCH
31.24-
28AcetylationEEKSKAEKAPAEKKP
HHHHHHHCCCHHHCC
65.6117691833
33AcetylationAEKAPAEKKPKAGKK
HHCCCHHHCCCCCCC
76.2017691833
34AcetylationEKAPAEKKPKAGKKL
HCCCHHHCCCCCCCC
43.1621311031
39AcetylationEKKPKAGKKLPKEAG
HHCCCCCCCCCHHHC
56.8717691833
40AcetylationKKPKAGKKLPKEAGA
HCCCCCCCCCHHHCC
69.9317691833
72MethylationIYIFKVLKQVHPDIG
HHHHHHHHHHCCCCC
53.9423161681
81PhosphorylationVHPDIGISSKAMGIM
HCCCCCCCHHHHHHH
22.1525561503
82PhosphorylationHPDIGISSKAMGIMN
CCCCCCCHHHHHHHH
23.6325561503
83MethylationPDIGISSKAMGIMNS
CCCCCCHHHHHHHHH
35.2923161681
116PhosphorylationYNKKPTITSREIQTA
HCCCCCCCHHHHHHH
24.9825561503
117PhosphorylationNKKPTITSREIQTAV
CCCCCCCHHHHHHHH
24.8625561503
134MethylationVLPGELAKHAVSEGT
HCCHHHHHHHHHHHC
44.7323161681
138PhosphorylationELAKHAVSEGTKAVT
HHHHHHHHHHCHHHH
30.9625561503

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
-KUbiquitinationE3 ubiquitin ligaseHUB1Q8RXD6
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseHUB2Q9C895
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of H2B6_ARATH !!

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 H2B6_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of H2B6_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of H2B6_ARATH

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-28; LYS-33; LYS-39 AND LYS-40,METHYLATION AT ALA-2, UBIQUITINATION AT LYS-146, AND MASSSPECTROMETRY.
Methylation
ReferencePubMed
"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-28; LYS-33; LYS-39 AND LYS-40,METHYLATION AT ALA-2, UBIQUITINATION AT LYS-146, AND MASSSPECTROMETRY.

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