dbPTM

COPG_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	COPG_ARATH
UniProt AC	Q0WW26
Protein Name	Coatomer subunit gamma
Gene Name	At4g34450
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	886
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	MAQPLVKKDDDHDDELEYSPFMGIEKGAVLQEARVFNDPQVDPRRCSQVITKLLYLLNQGESFTKVEATEVFFSVTKLFQSKDTGLRRMVYLIIKELSPSSDEVIIVTSSLMKDMNSKIDMYRANAIRVLCRIIDGTLLTQIERYLKQAIVDKNPVVSSAALVSGLHLLKTNPEIVKRWSNEVQEGIQSRSALVQFHALALLHQIRQNDRLAVSKLVGSLTRGSVRSPLAQCLLIRYTSQVIRDMANHGQSGERPFYEFLESCLRHKAEMVILEAARAITELDGVTSRELTPAITVLQLFLSSPRPVLRFAAVRTLNKVAMTHPMAVTNCNIDMESLISDQNRSIATLAITTLLKTGNESSVERLMKQITNFMSDIADEFKIVVVDAIRSLCVKFPLKYRSLMTFLSNILREEGGFEYKRAIVDSIVTIIRDIPDAKESGLLHLCEFIEDCEFTYLSTQILHFLGIEGPNTSDPSKYIRYIYNRVHLENATVRAAAVSTLAKFGFMVESLKPRITVLLKRCIYDSDDEVRDRATLYLSVLGGDGTVDTDKESKDFLFGSLEVPLVNMETSLKNYEPSEEAFDINSVPKEVKSQPLAEKKAQGKKPTGLGAPPAAPASGFDGYERLLSSIPEFAAFGKLFKSSLPVELTEAETEYAVNVVKHIFDSHVVFQYNCTNTIPEQLLERVNVIVDASEAEEFSEVTSKALNSLPYDSPGQAFVVFEKPAGVPAVGKFSNTLTFVVKEVDPSTGEAEDDGVEDEYQLEDLEVVAGDYMVKVGVSNFRNAWESMDEEDERVDEYGLGQRESLGEAVKAVMDLLGMQTCEGTETIPLNARSHTCLLSGVYIGNVKVLVRAQFGMDSSKDIAMKLTVRAEDVSVAEAIHEIVASG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
214	Phosphorylation	QNDRLAVSKLVGSLT HCCHHHHHHHHHHCC	18.05	19376835
525	Phosphorylation	LKRCIYDSDDEVRDR HHHHHCCCCCHHHHH	29.95	30291188
577	Phosphorylation	SLKNYEPSEEAFDIN HHCCCCCCCCCCCCC	35.81	30291188
786	Phosphorylation	NFRNAWESMDEEDER CCHHHHHCCCHHHHH	22.34	23776212
797	Phosphorylation	EDERVDEYGLGQRES HHHHHHHHCCCCHHH	17.12	23776212

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 COPG_ARATH !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of COPG_ARATH !!

Drug and Disease Associations

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

Regulatory Network of COPG_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-214, AND MASSSPECTROMETRY.	19376835 [Abstract]