COPG_DROME - dbPTM
COPG_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COPG_DROME
UniProt AC Q8I0G5
Protein Name Coatomer subunit gamma {ECO:0000250|UniProtKB:P53620, ECO:0000312|EMBL:AAN14275.1}
Gene Name gammaCOP {ECO:0000312|FlyBase:FBgn0028968}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 883
Subcellular Localization Cytoplasm . Golgi apparatus membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasmic vesicle, COPI-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side . Endoplasmic reticulum . The coatomer is cytoplasmic or polyme
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. Required for limiting lipid storage in lipid droplets. Involved in the expansion of luminal extracellular matrices and apical membrane during tubulogenesis. Required in the tracheal epithelium for luminal protein secretion and diametric tube growth. In salivary glands, required for deposition of O-glycans and luminal extracellular matrix assembly. Required for epidermal morphogenesis and cuticle development..
Protein Sequence MNYFSLTSHKKHRGHPSAGPSNAYQNLEKTSVLQETRTFNETPVNPRKCIHILTKILYLINQGEQLVAREATDCFFAMTKLFQSKDVVLRRMVYLGIKELSSIAEDVIIVTSSLTKDMTGKEDLYRAAAIRALCSITDNTMLQAVERYMKQCIVDKNAAVSCAALVSSLRLANTAGDVVKRWANEAQEALNSDNIMVQYHALGLLYHIRKSDRLAVSKLVNKLTRGSLKSPYAVCMLIRIACKLIEEEDIPSEELSDSPLFTFIESCLRHKSEMVIYEAAHAIVNLKNTNPRMLSPAFSILQLFCSSPKATLRFAAVRTLNKVAMTHPAAVTTCNLDLEGLITDSNRSVATLAITTLLKTGAESSVERLMKQISTFVAEISDEFKVVVVQAICALCTKYPRKHTVLMNFLSGMLREEGGLEYKTSIVDTIITIIEENADAKESGLSHLCEFIEDCEHVSLAVRILHLLGKEGPFAATPSKYIRFIYNRVILESPIVRAAAVTAMAQFGASCPALLSNILVLLGRCQMDPDDEVRDRATYYLSILNSERPELYKNYIIERENCSLALLEKSLVEHLNGDVDTRFDISIVPKAAIVKPVIANDVMLVTSSAPRPPKITREEESAARLAQLPGIQVLGPIHRSTAPIQLTESETEYTVQCIKHIFGQHVVFQFDCLNTLSDQILENVRVELTLPEGFTTRAVIPCPKLPYNDLQTTFVIVEFPPDAANSIATFGATLRFVVKDCDPNTGEPESEEGYDDEYMLEDLELTVADQIQKTRKNNFQVSWDAADSEEWLQAEDTFVLSAVTTLQDAVNTIVKILGLGAANLSENVPEGTHLHTLLCSGTFRGGAEILVRAKLALSEGVTLNLTVRSTDQDVAELITAAIG
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
7Phosphorylation-MNYFSLTSHKKHRG
-CCCCCCCCCCCCCC
27.8222817900
606PhosphorylationANDVMLVTSSAPRPP
ECCEEEEECCCCCCC
17.0121082442
607PhosphorylationNDVMLVTSSAPRPPK
CCEEEEECCCCCCCC
19.6121082442
608PhosphorylationDVMLVTSSAPRPPKI
CEEEEECCCCCCCCC
32.6921082442

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_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COPG_DROME !!

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_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

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

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Related Literatures of Post-Translational Modification

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