dbPTM

HDT2_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HDT2_ARATH
UniProt AC	Q56WH4
Protein Name	Histone deacetylase HDT2
Gene Name	HDT2
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	306
Subcellular Localization	Nucleus, nucleolus .
Protein Description	Probably mediates the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events..
Protein Sequence	MEFWGVAVTPKNATKVTPEEDSLVHISQASLDCTVKSGESVVLSVTVGGAKLVIGTLSQDKFPQISFDLVFDKEFELSHSGTKANVHFIGYKSPNIEQDDFTSSDDEDVPEAVPAPAPTAVTANGNAGAAVVKADTKPKAKPAEVKPAEEKPESDEEDESDDEDESEEDDDSEKGMDVDEDDSDDDEEEDSEDEEEEETPKKPEPINKKRPNESVSKTPVSGKKAKPAAAPASTPQKTEEKKKGGHTATPHPAKKGGKSPVNANQSPKSGGQSSGGNNNKKPFNSGKQFGGSNNKGSNKGKGKGRA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEFWGVAV -------CCEEEEEE	9.64	22223895
93	Phosphorylation	VHFIGYKSPNIEQDD EEEEEECCCCCCCCC	18.07	23776212
102	Phosphorylation	NIEQDDFTSSDDEDV CCCCCCCCCCCCCCC	34.02	23776212
103	Phosphorylation	IEQDDFTSSDDEDVP CCCCCCCCCCCCCCC	31.59	23776212
104	Phosphorylation	EQDDFTSSDDEDVPE CCCCCCCCCCCCCCC	46.13	23776212
119	Phosphorylation	AVPAPAPTAVTANGN CCCCCCCCEEECCCC	35.55	23776212
122	Phosphorylation	APAPTAVTANGNAGA CCCCCEEECCCCCCE	16.37	23776212
154	Phosphorylation	PAEEKPESDEEDESD CCCCCCCCCCCCCCC	59.87	27531888
160	Phosphorylation	ESDEEDESDDEDESE CCCCCCCCCCCCCCC	63.78	27531888
166	Phosphorylation	ESDDEDESEEDDDSE CCCCCCCCCCCCCHH	59.62	27531888
172	Phosphorylation	ESEEDDDSEKGMDVD CCCCCCCHHCCCCCC	48.48	27531888
183	Phosphorylation	MDVDEDDSDDDEEED CCCCCCCCCCCCCCC	56.09	23776212
191	Phosphorylation	DDDEEEDSEDEEEEE CCCCCCCCCCHHHHH	50.67	23776212
199	Phosphorylation	EDEEEEETPKKPEPI CCHHHHHCCCCCCCC	43.62	23776212
233	Phosphorylation	KPAAAPASTPQKTEE CCCCCCCCCCCCCCH	39.29	18433157
234	Phosphorylation	PAAAPASTPQKTEEK CCCCCCCCCCCCCHH	31.67	26658240
247	Phosphorylation	EKKKGGHTATPHPAK HHHCCCCCCCCCCCC	35.19	25561503
249	Phosphorylation	KKGGHTATPHPAKKG HCCCCCCCCCCCCCC	24.24	25561503
259	Phosphorylation	PAKKGGKSPVNANQS CCCCCCCCCCCCCCC	37.04	23776212
266	Phosphorylation	SPVNANQSPKSGGQS CCCCCCCCCCCCCCC	33.82	19880383

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 HDT2_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HDT2_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 HDT2_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
HDT2_ARATH	HD2B	physical	25813344

Drug and Disease Associations

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

Regulatory Network of HDT2_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; SER-259 ANDSER-266, AND MASS SPECTROMETRY.	19376835 [Abstract]
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis."; de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.; J. Proteome Res. 7:2458-2470(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND MASSSPECTROMETRY.	18433157 [Abstract]