dbPTM

COPD_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	COPD_ARATH
UniProt AC	Q93Y22
Protein Name	Coatomer subunit delta
Gene Name	At5g05010
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	527
Subcellular Localization	Cytoplasm. Golgi apparatus membrane Peripheral membrane protein Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane Peripheral membrane protein Cytoplasmic side. The coatomer is cytoplasmic or polymerized on the cytoplasmic side o
Protein Description	The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity)..
Protein Sequence	MVVLAAAIVVKSGKVIVSRHYVDMSRIRIEGLLAAFPKLVGMGKQHTYIETENVRYVYQPIEALFLLLVTTKQSNILEDLATLTLLSKLVPEYSMSLDEEGISRASFELIFAFDEVISLGHKESVTVAQVKQYCEMESHEEKLHKLVMQSKINDTKDVMKRKANEIDKSKIEKNKPGGFSSMGSMGSGRLESGFNELSISSGGGGGYGSGSGFGMISDVDPINTKPKDRSRSSVTAPPKSSGMKLGKSGKNQLMESLKAEGEDVIEDVKPTGQSKAAAPPPTDPFTLTVEEKLNVALRRDGGLSSFDMQGTLSLQILNQEDGFVQVQIATGENPEILFKTHPNINRDMFNNENILGLKRPDQPFPTGQGGDGVGLLRWRMQRADESMVPLTINCWPSVSGNETYVSLEYEASSMFDLTNVIISVPLPALREAPSVRQCDGEWRYDPRNSVLEWSILLIDNSNRSGSMEFVVPPVDSSVFFPISVQFAATSTYSGLKVTGMIPLRGGGGATPRFVQRTQLIAQNYQVI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
180	Phosphorylation	KNKPGGFSSMGSMGS HCCCCCCCCCCCCCC	23.77	23776212
181	Phosphorylation	NKPGGFSSMGSMGSG CCCCCCCCCCCCCCC	25.54	23776212
184	Phosphorylation	GGFSSMGSMGSGRLE CCCCCCCCCCCCCCC	16.01	30291188
187	Phosphorylation	SSMGSMGSGRLESGF CCCCCCCCCCCCCCC	16.46	23776212
230	Phosphorylation	NTKPKDRSRSSVTAP CCCCCCCCCCCCCCC	46.80	25561503
232	Phosphorylation	KPKDRSRSSVTAPPK CCCCCCCCCCCCCCC	30.33	23111157
233	Phosphorylation	PKDRSRSSVTAPPKS CCCCCCCCCCCCCCC	23.52	19880383
510	Phosphorylation	LRGGGGATPRFVQRT CCCCCCCCHHHHHHH	20.47	29654922

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 COPD_ARATH !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SUMO3_ARATH	SUMO3	physical	20855607
SUMO1_ARATH	SUMO1	physical	20855607

Drug and Disease Associations

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

Regulatory Network of COPD_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-184, AND MASSSPECTROMETRY.	19376835 [Abstract]