Reviewed,
UniProtKB/Swiss-Prot Q9Y678 (COPG_HUMAN)
Last modified
July 7, 2009.
Version 69.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Coatomer subunit gamma Alternative name(s): Gamma-coat protein Short name=Gamma-COP | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 874 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| 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 By similarity. |
| Subunit structure | Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts with ZNF289/ARFGAP2 through its C-terminal appendage domain. Ref.4 |
| Subcellular location | Cytoplasm By similarity. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmic vesicle › COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it By similarity. |
| Sequence similarities | Belongs to the COPG family. Contains 4 HEAT repeats. |
Ontologies
| Keywords | |
|---|---|
| Biological process | ER-Golgi transport Protein transport Transport |
| Cellular component | Cytoplasm Cytoplasmic vesicle Golgi apparatus Membrane |
| Coding sequence diversity | Polymorphism |
| Domain | Repeat |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | COPI coating of Golgi vesicle Inferred from Experiment. Source: Reactome intracellular protein transportInferred from electronic annotation. Source: InterPro retrograde vesicle-mediated transport, Golgi to ERInferred from Experiment. Source: Reactome |
| Cellular component | COPI vesicle coat Inferred from sequence or structural similarity. Source: UniProtKB cytosolInferred from Experiment. Source: Reactome |
| Molecular function | protein binding Inferred from physical interaction. Source: IntAct structural molecule activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| BRF2 | Q9HAW0 | 1 | EBI-1049127,EBI-1055224 | |
| ILK | Q13418 | 1 | EBI-1049127,EBI-747644 | |
| MAGED1 | Q9Y5V3 | 1 | EBI-1049127,EBI-716006 | |
| PHB2 | Q99623 | 1 | EBI-1049127,EBI-358348 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 874 | 874 | Coatomer subunit gamma | PRO_0000193858 | |||||||||||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Repeat | 64 – 101 | 38 | HEAT 1 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Repeat | 283 – 320 | 38 | HEAT 2 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Repeat | 322 – 355 | 34 | HEAT 3 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Repeat | 356 – 392 | 37 | HEAT 4 | ||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 609 – 874 | 266 | Interaction with ZNF289/ARFGAP2 | ||||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 681 | 1 | M → T: dbSNP rs15648. | VAR_054039 | |||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 776 | 1 | W → S: Loss of interaction with ZNF289/ARFGAP2. Ref.4 | ||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 609 – 618 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 621 – 623 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 644 – 654 | 11 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 656 – 667 | 12 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 672 – 686 | 15 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 688 – 693 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 695 – 698 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 704 – 711 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 714 – 716 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 722 – 735 | 14 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 737 – 739 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 747 – 752 | 6 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 756 – 758 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 760 – 763 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 764 – 766 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 772 – 779 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 785 – 791 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 797 – 808 | 12 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 814 – 817 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 824 – 834 | 11 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 835 – 837 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 838 – 862 | 25 | |||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 863 – 872 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. Chen J.-L.Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed: 10931946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pituitary. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin. |
| [3] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [4] | "Gamma-COP appendage domain -- structure and function." Watson P.J., Frigerio G., Collins B.M., Duden R., Owen D.J. Traffic 5:79-88(2004) [PubMed: 14690497] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 608-874, INTERACTION WITH ZNF289, MUTAGENESIS OF TRP-776. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AF100756 mRNA. Translation: AAD43020.1. BC066650 mRNA. Translation: AAH66650.1. | |||||||||||||
| IPI | IPI00783982. | ||||||||||||
| RefSeq | NP_057212.1. | ||||||||||||
| UniGene | Hs.518250 | ||||||||||||
3D structure databases | |||||||||||||
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| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q9Y678. 10 interactions. | ||||||||||||
Proteomic databases | |||||||||||||
| PeptideAtlas | Q9Y678. | ||||||||||||
| PRIDE | Q9Y678. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSG00000181789. Homo sapiens. [Contig view] | ||||||||||||
| GeneID | 22820. | ||||||||||||
| KEGG | hsa:22820. | ||||||||||||
| UCSC | uc003els.1. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| GeneCards | GC03P130451. | ||||||||||||
| H-InvDB | HIX0023057. | ||||||||||||
| HGNC | HGNC:2236. COPG. | ||||||||||||
| PharmGKB | PA26752. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOVERGEN | Q9Y678. | ||||||||||||
| OMA | Q9Y678. LNFEAAW. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| Reactome | REACT_11123. Membrane Trafficking. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q9Y678. | ||||||||||||
| Bgee | Q9Y678. | ||||||||||||
| CleanEx | HS_COPG. | ||||||||||||
| GermOnline | ENSG00000181789. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR011989. ARM-like. IPR002553. Clathrin/coatomer_adapt-like_N. IPR015873. Clathrin_a/coatomer_app_sub_C. IPR017106. Coatomer_gamma_subunit. IPR014863. Coatomer_gsu_app. IPR013040. Coatomer_gsu_app_Ig-like-sub. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.30.310.30. AP2_A_adaptin_C. 1 hit. G3DSA:1.25.10.10. ARM-like. 1 hit. G3DSA:2.60.40.1480. Coatomer_gsu_app_Ig-like-sub. 1 hit. | ||||||||||||
| Pfam | PF01602. Adaptin_N. 1 hit. PF08752. Gamma-COP. 1 hit. [Graphical view] | ||||||||||||
| PIRSF | PIRSF037093. Coatomer_gamma_subunit. 1 hit. | ||||||||||||
| PROSITE | PS50077. HEAT_REPEAT. False negative. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| NextBio | 43212. | ||||||||||||
Entry information
| Entry name | COPG_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9Y678 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 3 Human chromosome 3: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


