COPE_MOUSE - dbPTM
COPE_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COPE_MOUSE
UniProt AC O89079
Protein Name Coatomer subunit epsilon
Gene Name Cope
Organism Mus musculus (Mouse).
Sequence Length 308
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. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated with ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity)..
Protein Sequence MAPPVPGAVSGGSGEVDELFDVKNAFYIGSYQQCINEAQRVKLSSPEREVERDVFLYRAYLAQRKYGVVLDEIKPSSAPELQAVRMFAEYLASENQRDSIVLELDREMSRSVDVTNTTFLLMAASIYFHDQNPDAALRTLHQGDGLECMAMTIQILLKLDRLDLARKELKKMQDQDEDATLTQLATAWVNLAVGGEKLQEAYYIFQELADKCSPTLLLLNGQAACHSAQGRWETAEGVLQEALDKDSGHPETLINLIVLSQHLGKPPEVTNRYLSQLKDAHRAHPFIKEYQAKENDFDRLAMQYAPSA
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
10PhosphorylationPPVPGAVSGGSGEVD
CCCCCCCCCCCCCCC
36.5824925903
13PhosphorylationPGAVSGGSGEVDELF
CCCCCCCCCCCCHHH
34.9924925903
42UbiquitinationINEAQRVKLSSPERE
HHHHHCCCCCCCCHH
44.8627667366
44PhosphorylationEAQRVKLSSPEREVE
HHHCCCCCCCCHHHH
37.8226060331
45PhosphorylationAQRVKLSSPEREVER
HHCCCCCCCCHHHHH
41.0125338131
65AcetylationRAYLAQRKYGVVLDE
HHHHHHHHHCEEECC
33.9922826441
99PhosphorylationASENQRDSIVLELDR
HCCCCCCCEEHHHCH
19.45-
265UbiquitinationVLSQHLGKPPEVTNR
HHHHHCCCCHHHHHH
64.8522790023
278AcetylationNRYLSQLKDAHRAHP
HHHHHHHHHHHHHCH
45.2722902405
278UbiquitinationNRYLSQLKDAHRAHP
HHHHHHHHHHHHHCH
45.2722790023
307PhosphorylationLAMQYAPSA------
HHHHHCCCC------
38.1430482847

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 COPE_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 COPE_MOUSE !!

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

Oops, there are no PPI records of COPE_MOUSE !!

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

loading...

Related Literatures of Post-Translational Modification

TOP