Y2766_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: Y2766_ARATH
• UniProt AC: O80934
• Protein Name: Uncharacterized protein At2g37660, chloroplastic
• Gene Name: At2g37660
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 325
• Subcellular Localization: Plastid, chloroplast .
• Protein Sequence: MAMMTTTTTTFFHPLLPANTYKSGAVASSFVSVPRSSSLQFRSLVSDSTSICGPSKFTGKNRRVSVTVSAAATTEPLTVLVTGAGGRTGQIVYKKLKERSEQFVARGLVRTKESKEKINGEDEVFIGDIRDTASIAPAVEGIDALVILTSAVPQMKPGFDPSKGGRPEFFFDDGAYPEQVDWIGQKNQIDAAKAAGVKQIVLVGSMGGTNINHPLNSIGNANILVWKRKAEQYLADSGIPYTIIRAGGLQDKDGGIRELLVGKDDELLETETRTIARADVAEVCVQALQLEEAKFKALDLASKPEGTGTPTKDFKALFTQVTTKF

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
70	Acetylation	RVSVTVSAAATTEPL EEEEEEEECCCCCCE	9.22	22223895
74	Phosphorylation	TVSAAATTEPLTVLV EEEECCCCCCEEEEE	30.77	29654922
94	Acetylation	RTGQIVYKKLKERSE CCHHHHHHHHHHHHH	40.51	21311031
270	Phosphorylation	KDDELLETETRTIAR CCHHHHHHHCHHHHH	42.50	25561503
302	Phosphorylation	FKALDLASKPEGTGT HHHHHHCCCCCCCCC	56.92	23776212
307	Phosphorylation	LASKPEGTGTPTKDF HCCCCCCCCCCCHHH	35.90	23776212
309	Phosphorylation	SKPEGTGTPTKDFKA CCCCCCCCCCHHHHH	27.85	23776212
311	Phosphorylation	PEGTGTPTKDFKALF CCCCCCCCHHHHHHH	42.98	23776212
319	Phosphorylation	KDFKALFTQVTTKF- HHHHHHHHHHHCCC-	23.99	24299221

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

Oops, there are no upstream regulatory protein records of Y2766_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of Y2766_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 Y2766_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of Y2766_ARATH !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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 THR-309, AND MASSSPECTROMETRY.
PubMed: 19376835