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Q9Y678 (COPG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coatomer subunit gamma-1
Alternative name(s):
Gamma-1-coat protein
Short name=Gamma-1-COP
Gene names
Name:COPG1
Synonyms:COPG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length874 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis By similarity. Ref.6

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. Interacts with EGFR upon EGF treatment; interaction is essential for regulation of EGF-dependent nuclear transport of EGFR by retrograde trafficking from the Golgi to the ER. Interacts with COPB1. Interacts with TMED10 (via C-terminus). Interacts with TMED2, TMED3, TMED7 and TMED9. Ref.1 Ref.6 Ref.8

Subcellular location

Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicleCOPI-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. Predominantly located in the cis-Golgi apparatus By similarity. Ref.1

Sequence similarities

Belongs to the COPG family.

Contains 4 HEAT repeats.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 874874Coatomer subunit gamma-1
PRO_0000193858

Regions

Repeat64 – 10138HEAT 1
Repeat283 – 32038HEAT 2
Repeat322 – 35534HEAT 3
Repeat356 – 39237HEAT 4
Region609 – 874266Interaction with ZNF289/ARFGAP2

Natural variations

Natural variant6811M → T.
Corresponds to variant rs15648 [ dbSNP | Ensembl ].
VAR_054039

Experimental info

Mutagenesis7761W → S: Loss of interaction with ZNF289/ARFGAP2. Ref.8
Sequence conflict6221E → V in BAG50968. Ref.3
Sequence conflict7861E → G in BAG50968. Ref.3
Sequence conflict8421V → M in BAG50968. Ref.3
Sequence conflict8541M → T in BAF84382. Ref.3
Sequence conflict8541M → T in BAG50968. Ref.3

Secondary structure

........................................... 874
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y678 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: A2FAB492C598EC98

FASTA87497,718
        10         20         30         40         50         60 
MLKKFDKKDE ESGGGSNPFQ HLEKSAVLQE ARVFNETPIN PRKCAHILTK ILYLINQGEH 

        70         80         90        100        110        120 
LGTTEATEAF FAMTKLFQSN DPTLRRMCYL TIKEMSCIAE DVIIVTSSLT KDMTGKEDNY 

       130        140        150        160        170        180 
RGPAVRALCQ ITDSTMLQAI ERYMKQAIVD KVPSVSSSAL VSSLHLLKCS FDVVKRWVNE 

       190        200        210        220        230        240 
AQEAASSDNI MVQYHALGLL YHVRKNDRLA VNKMISKVTR HGLKSPFAYC MMIRVASKQL 

       250        260        270        280        290        300 
EEEDGSRDSP LFDFIESCLR NKHEMVVYEA ASAIVNLPGC SAKELAPAVS VLQLFCSSPK 

       310        320        330        340        350        360 
AALRYAAVRT LNKVAMKHPS AVTACNLDLE NLVTDSNRSI ATLAITTLLK TGSESSIDRL 

       370        380        390        400        410        420 
MKQISSFMSE ISDEFKVVVV QAISALCQKY PRKHAVLMNF LFTMLREEGG FEYKRAIVDC 

       430        440        450        460        470        480 
IISIIEENSE SKETGLSHLC EFIEDCEFTV LATRILHLLG QEGPKTTNPS KYIRFIYNRV 

       490        500        510        520        530        540 
VLEHEEVRAG AVSALAKFGA QNEEMLPSIL VLLKRCVMDD DNEVRDRATF YLNVLEQKQK 

       550        560        570        580        590        600 
ALNAGYILNG LTVSIPGLER ALQQYTLEPS EKPFDLKSVP LATAPMAEQR TESTPITAVK 

       610        620        630        640        650        660 
QPEKVAATRQ EIFQEQLAAV PEFRGLGPLF KSSPEPVALT ESETEYVIRC TKHTFTNHMV 

       670        680        690        700        710        720 
FQFDCTNTLN DQTLENVTVQ MEPTEAYEVL CYVPARSLPY NQPGTCYTLV ALPKEDPTAV 

       730        740        750        760        770        780 
ACTFSCMMKF TVKDCDPTTG ETDDEGYEDE YVLEDLEVTV ADHIQKVMKL NFEAAWDEVG 

       790        800        810        820        830        840 
DEFEKEETFT LSTIKTLEEA VGNIVKFLGM HPCERSDKVP DNKNTHTLLL AGVFRGGHDI 

       850        860        870 
LVRSRLLLLD TVTMQVTARS LEELPVDIIL ASVG 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of novel isoforms of COP I subunits."
Futatsumori M., Kasai K., Takatsu H., Shin H.-W., Nakayama K.
J. Biochem. 128:793-801(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH COPB1 AND TMED10, SUBCELLULAR LOCATION.
[2]"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. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pituitary.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta and Teratocarcinoma.
[4]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[6]"COPI-mediated retrograde trafficking from the Golgi to the ER regulates EGFR nuclear transport."
Wang Y.N., Wang H., Yamaguchi H., Lee H.J., Lee H.H., Hung M.C.
Biochem. Biophys. Res. Commun. 399:498-504(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EGFR.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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] [Europe PMC] [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

EMBL
GenBank
DDBJ
AB047846 mRNA. Translation: BAB17657.1.
AF100756 mRNA. Translation: AAD43020.1.
AK001724 mRNA. Translation: BAG50968.1.
AK291693 mRNA. Translation: BAF84382.1.
CH471052 Genomic DNA. Translation: EAW79267.1.
BC066650 mRNA. Translation: AAH66650.1.
RefSeqNP_057212.1. NM_016128.3.
UniGeneHs.518250.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1R4XX-ray1.90A608-874[»]
ProteinModelPortalQ9Y678.
SMRQ9Y678. Positions 20-311, 452-502, 608-873.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116496. 45 interactions.
DIPDIP-29872N.
IntActQ9Y678. 14 interactions.
MINTMINT-4657598.
STRING9606.ENSP00000325002.

PTM databases

PhosphoSiteQ9Y678.

Polymorphism databases

DMDM12229771.

Proteomic databases

PaxDbQ9Y678.
PeptideAtlasQ9Y678.
PRIDEQ9Y678.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314797; ENSP00000325002; ENSG00000181789.
GeneID22820.
KEGGhsa:22820.
UCSCuc003els.3. human.

Organism-specific databases

CTD22820.
GeneCardsGC03P128970.
HGNCHGNC:2236. COPG1.
HPAHPA037867.
MIM615525. gene.
neXtProtNX_Q9Y678.
PharmGKBPA26752.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5240.
HOGENOMHOG000184434.
HOVERGENHBG004368.
InParanoidQ9Y678.
KOK17267.
OMAEYVVRCT.
OrthoDBEOG75XGK5.
PhylomeDBQ9Y678.
TreeFamTF300324.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressQ9Y678.
BgeeQ9Y678.
CleanExHS_COPG.
GenevestigatorQ9Y678.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
2.60.40.1480. 1 hit.
3.30.310.30. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002553. Clathrin/coatomer_adapt-like_N.
IPR015873. Clathrin_a/coatomer_app_sub_C.
IPR009028. Coatomer/calthrin_app_sub_C.
IPR013041. Coatomer/clathrin_app_Ig-like.
IPR017106. Coatomer_gsu.
IPR013040. Coatomer_gsu_app_Ig-like-sub.
[Graphical view]
PANTHERPTHR10261. PTHR10261. 1 hit.
PfamPF01602. Adaptin_N. 1 hit.
PF08752. COP-gamma_platf. 1 hit.
[Graphical view]
PIRSFPIRSF037093. Coatomer_gamma_subunit. 1 hit.
SUPFAMSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCOPG1. human.
EvolutionaryTraceQ9Y678.
GeneWikiCOPG.
GenomeRNAi22820.
NextBio43212.
PROQ9Y678.
SOURCESearch...

Entry information

Entry nameCOPG1_HUMAN
AccessionPrimary (citable) accession number: Q9Y678
Secondary accession number(s): A8K6M8, B3KMF6, Q54AC4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM