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Identification
HMDB Protein ID HMDBP08333
Secondary Accession Numbers
  • 14045
Name Coatomer subunit epsilon
Synonyms
  1. Epsilon-COP
  2. Epsilon-coat protein
Gene Name COPE
Protein Type Unknown
Biological Properties
General Function Involved in structural molecule activity
Specific Function 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. In mammals, the coatomer can only be recruited by membranes associated to 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
Pathways Not Available
Reactions Not Available
GO Classification
Component
membrane coat
macromolecular complex
protein complex
vesicle coat
copi vesicle coat
Function
binding
structural molecule activity
protein binding
Process
establishment of localization
transport
golgi vesicle transport
retrograde vesicle-mediated transport, golgi to er
vesicle-mediated transport
Cellular Location
  1. Cytoplasm
  2. Golgi apparatus membrane
  3. Peripheral membrane protein
  4. Peripheral membrane protein
  5. Cytoplasmic vesicle
  6. Cytoplasmic side
  7. Cytoplasmic side
  8. COPI-coated vesicle membrane
Gene Properties
Chromosome Location Chromosome:1
Locus 19p13.11
SNPs COPE
Gene Sequence
>927 bp
ATGGCGCCTCCGGCCCCCGGCCCGGCCTCCGGCGGCTCCGGGGAGGTAGACGAGCTGTTC
GACGTAAAGAACGCCTTCTACATCGGCAGCTACCAGCAGTGCATAAACGAGGCGCAGCGG
GTGAAGCTATCAAGCCCAGAGAGAGACGTGGAGAGGGACGTCTTCCTGTATAGAGCGTAC
CTGGCGCAGAGGAAGTTCGGTGTGGTCCTGGATGAGATCAAGCCCTCCTCGGCCCCTGAG
CTCCAGGCCGTGCGCATGTTTGCTGACTACCTCGCCCACGAGAGTCGGAGGGACAGCATC
GTGGCCGAGCTGGACCGAGAGATGAGCAGGAGCGTGGACGTGACCAACACCACCTTCCTG
CTCATGGCCGCCTCCATCTATCTCCACGACCAGAACCCGGATGCCGCCCTGCGTGCGCTG
CACCAGGGGGACAGCCTGGAGTGCACAGCCATGACAGTGCAGATCCTGCTGAAGCTGGAC
CGCCTGGACCTCGCCCGGAAGGAGCTGAAGAGAATGCAGGACCTGGACGAGGATGCCACC
CTCACCCAGCTCGCCACTGCCTGGGTCAGCCTGGCCACGGGTGGTGAGAAGCTGCAGGAT
GCCTACTACATCTTCCAGGAGATGGCTGACAAGTGCTCGCCCACCCTGCTGCTGCTCAAT
GGGCAGGCGGCCTGCCACATGGCCCAGGGCCGCTGGGAGGCCGCTGAGGGCCTGCTGCAG
GAGGCGCTAGACAAGGATAGTGGCTACCCAGAGACGCTGGTCAACCTCATCGTCCTGTCC
CAGCACCTGGGCAAGCCCCCTGAGGTGACAAACCGATACCTGTCCCAGCTGAAGGATGCC
CACAGGTCCCATCCCTTCATCAAGGAGTACCAGGCCAAGGAGAACGACTTTGACAGGCTG
GTGCTACAGTACGCTCCCAGCGCCTGA
Protein Properties
Number of Residues 308
Molecular Weight 34481.6
Theoretical pI 4.75
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Coatomer subunit epsilon
MAPPAPGPASGGSGEVDELFDVKNAFYIGSYQQCINEAQRVKLSSPERDVERDVFLYRAY
LAQRKFGVVLDEIKPSSAPELQAVRMFADYLAHESRRDSIVAELDREMSRSVDVTNTTFL
LMAASIYLHDQNPDAALRALHQGDSLECTAMTVQILLKLDRLDLARKELKRMQDLDEDAT
LTQLATAWVSLATGGEKLQDAYYIFQEMADKCSPTLLLLNGQAACHMAQGRWEAAEGLLQ
EALDKDSGYPETLVNLIVLSQHLGKPPEVTNRYLSQLKDAHRSHPFIKEYQAKENDFDRL
VLQYAPSA
GenBank ID Protein 31542319
UniProtKB/Swiss-Prot ID O14579
UniProtKB/Swiss-Prot Entry Name COPE_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_007263.3
GeneCard ID COPE
GenAtlas ID COPE
HGNC ID HGNC:2234
References
General References
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  2. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  3. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  4. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
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