HDA6_ARATH - dbPTM
HDA6_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HDA6_ARATH
UniProt AC Q9FML2
Protein Name Histone deacetylase 6
Gene Name HDA6
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 471
Subcellular Localization Nucleus, nucleolus . Nucleus .
Protein Description Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Might remove acetyl residues only from specific targets, such as rDNA repeats or complex transgenes. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Required for rRNA gene silencing in nucleolar dominance. Plays a role in transgene silencing, but this effect seems to bee independent of the histone deacetylase activity. [PubMed: 11340181]
Protein Sequence MEADESGISLPSGPDGRKRRVSYFYEPTIGDYYYGQGHPMKPHRIRMAHSLIIHYHLHRRLEISRPSLADASDIGRFHSPEYVDFLASVSPESMGDPSAARNLRRFNVGEDCPVFDGLFDFCRASAGGSIGAAVKLNRQDADIAINWGGGLHHAKKSEASGFCYVNDIVLGILELLKMFKRVLYIDIDVHHGDGVEEAFYTTDRVMTVSFHKFGDFFPGTGHIRDVGAEKGKYYALNVPLNDGMDDESFRSLFRPLIQKVMEVYQPEAVVLQCGADSLSGDRLGCFNLSVKGHADCLRFLRSYNVPLMVLGGGGYTIRNVARCWCYETAVAVGVEPDNKLPYNEYFEYFGPDYTLHVDPSPMENLNTPKDMERIRNTLLEQLSGLIHAPSVQFQHTPPVNRVLDEPEDDMETRPKPRIWSGTATYESDSDDDDKPLHGYSCRGGATTDRDSTGEDEMDDDNPEPDVNPPSS
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
1Acetylation-------MEADESGI
-------CCCCCCCC
9.6322223895
420PhosphorylationRPKPRIWSGTATYES
CCCCCEEEEEEEEEC
24.7223776212
422PhosphorylationKPRIWSGTATYESDS
CCCEEEEEEEEECCC
15.4323776212
424PhosphorylationRIWSGTATYESDSDD
CEEEEEEEEECCCCC
27.8823776212
425PhosphorylationIWSGTATYESDSDDD
EEEEEEEEECCCCCC
15.8023776212
427PhosphorylationSGTATYESDSDDDDK
EEEEEEECCCCCCCC
31.8123776212
429PhosphorylationTATYESDSDDDDKPL
EEEEECCCCCCCCCC
52.8223776212
440PhosphorylationDKPLHGYSCRGGATT
CCCCCCEECCCCCCC
11.2623776212
446PhosphorylationYSCRGGATTDRDSTG
EECCCCCCCCCCCCC
32.2923776212
447PhosphorylationSCRGGATTDRDSTGE
ECCCCCCCCCCCCCC
28.6223776212
451PhosphorylationGATTDRDSTGEDEMD
CCCCCCCCCCCCCCC
38.9223776212
452PhosphorylationATTDRDSTGEDEMDD
CCCCCCCCCCCCCCC
49.2123776212
470PhosphorylationEPDVNPPSS------
CCCCCCCCC------
50.3523776212
471PhosphorylationPDVNPPSS-------
CCCCCCCC-------
50.4423776212

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

Oops, there are no upstream regulatory protein records of HDA6_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HDA6_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 HDA6_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H2A3_ARATHHTA2physical
16648464
H2B10_ARATHHTB2physical
16648464
H33_ARATHAT4G40030physical
16648464
SAP18_ARATHSAP18physical
17999645
FLD_ARATHFLDphysical
21398257
EIN3_ARATHEIN3physical
21737749
EIL1_ARATHEIL1physical
21737749
DNMT1_ARATHMET1physical
21994348
MSI5_ARATHNFC5physical
22102827
MSI4_ARATHFVEphysical
22102827
HDT3_ARATHHD2Cphysical
22368268
AS1_ARATHAS1physical
23271976
TPL_ARATHTPLphysical
23267111

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HDA6_ARATH

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Related Literatures of Post-Translational Modification

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