Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O14579 (COPE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coatomer subunit epsilon
Alternative name(s):
Epsilon-coat protein
Short name=Epsilon-COP
Gene names
Name:COPE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length308 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 By similarity.

Subunit structure

Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits.

Subcellular location

Cytoplasm By similarity. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. 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.

Post-translational modification

Phosphorylated by PKA.

Polyubiquitinated by RCHY1 in the presence of androgen, leading to proteasomal degradation.

Sequence similarities

Belongs to the COPE family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14579-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O14579-2)

The sequence of this isoform differs from the canonical sequence as follows:
     97-97: R → S
     98-148: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O14579-3)

The sequence of this isoform differs from the canonical sequence as follows:
     194-245: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 308307Coatomer subunit epsilon
PRO_0000193851

Natural variations

Alternative sequence971R → S in isoform 2.
VSP_042770
Alternative sequence98 – 14851Missing in isoform 2.
VSP_042771
Alternative sequence194 – 24552Missing in isoform 3.
VSP_045070
Natural variant131S → C.
Corresponds to variant rs2231987 [ dbSNP | Ensembl ].
VAR_054032
Natural variant1171T → I. Ref.1 Ref.4
Corresponds to variant rs10330 [ dbSNP | Ensembl ].
VAR_054033

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A71146F3332F6BA9

FASTA30834,482
        10         20         30         40         50         60 
MAPPAPGPAS GGSGEVDELF DVKNAFYIGS YQQCINEAQR VKLSSPERDV ERDVFLYRAY 

        70         80         90        100        110        120 
LAQRKFGVVL DEIKPSSAPE LQAVRMFADY LAHESRRDSI VAELDREMSR SVDVTNTTFL 

       130        140        150        160        170        180 
LMAASIYLHD QNPDAALRAL HQGDSLECTA MTVQILLKLD RLDLARKELK RMQDLDEDAT 

       190        200        210        220        230        240 
LTQLATAWVS LATGGEKLQD AYYIFQEMAD KCSPTLLLLN GQAACHMAQG RWEAAEGLLQ 

       250        260        270        280        290        300 
EALDKDSGYP ETLVNLIVLS QHLGKPPEVT NRYLSQLKDA HRSHPFIKEY QAKENDFDRL 


VLQYAPSA 

« Hide

Isoform 2 [UniParc].

Checksum: 0F26BDC0A83D65BF
Show »

FASTA25728,797
Isoform 3 [UniParc].

Checksum: 4B35360D41136F1A
Show »

FASTA25628,773

References

« Hide 'large scale' references
[1]"Segregation of COPI-rich and anterograde-cargo-rich domains in endoplasmic-reticulum-to-Golgi transport complexes."
Shima D.T., Scales S.J., Kreis T.E., Pepperkok R.
Curr. Biol. 9:821-824(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-117.
Tissue: Brain.
[2]"Cloning, expression, and phosphorylation by protein kinase A of human epsilon-COP."
Baehr C., Herzog A., Haeussermann S., Marks F., Gschwendt M.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[4]"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] (ISOFORMS 1 AND 2), VARIANT ILE-117.
Tissue: Testis and Uterus.
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORMS 1 AND 3).
Tissue: Brain, Embryonic carcinoma, Lymph and Skin.
[9]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-23; 66-85 AND 172-211, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA."
Maruyama S., Miyajima N., Bohgaki M., Tsukiyama T., Shigemura M., Nonomura K., Hatakeyama S.
Mol. Cell. Biochem. 307:73-82(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY RCHY1.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ131182 mRNA. Translation: CAA10316.1.
AJ249366 mRNA. Translation: CAB55628.1.
AL136928 mRNA. Translation: CAB66862.1.
AK126476 mRNA. Translation: BAG54333.1.
AK315281 mRNA. Translation: BAG37690.1.
CR456886 mRNA. Translation: CAG33167.1.
AC002985 Genomic DNA. Translation: AAB81543.1.
AC005197 Genomic DNA. Translation: AAC24612.1.
CH471106 Genomic DNA. Translation: EAW84749.1.
CH471106 Genomic DNA. Translation: EAW84752.1.
CH471106 Genomic DNA. Translation: EAW84756.1.
BC003155 mRNA. Translation: AAH03155.1.
BC007250 mRNA. Translation: AAH07250.1.
BC017285 mRNA. Translation: AAH17285.1.
BM454494 mRNA. No translation available.
RefSeqNP_009194.2. NM_007263.3.
NP_955474.1. NM_199442.1.
NP_955476.1. NM_199444.1.
UniGeneHs.10326.

3D structure databases

ProteinModelPortalO14579.
SMRO14579. Positions 17-307.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116447. 25 interactions.
IntActO14579. 6 interactions.
MINTMINT-5000768.
STRING9606.ENSP00000262812.

PTM databases

PhosphoSiteO14579.

2D gel databases

OGPO14579.

Proteomic databases

PaxDbO14579.
PRIDEO14579.

Protocols and materials databases

DNASU11316.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262812; ENSP00000262812; ENSG00000105669. [O14579-1]
ENST00000349893; ENSP00000343134; ENSG00000105669. [O14579-3]
ENST00000351079; ENSP00000345674; ENSG00000105669. [O14579-2]
GeneID11316.
KEGGhsa:11316.
UCSCuc002nkk.3. human. [O14579-1]
uc002nkl.3. human. [O14579-2]
uc002nkm.3. human.

Organism-specific databases

CTD11316.
GeneCardsGC19M019010.
HGNCHGNC:2234. COPE.
HPACAB034345.
HPA041605.
HPA043576.
MIM606942. gene.
neXtProtNX_O14579.
PharmGKBPA26750.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG289253.
HOGENOMHOG000205825.
HOVERGENHBG002201.
InParanoidO14579.
KOK17268.
OrthoDBEOG7QK0CC.
PhylomeDBO14579.
TreeFamTF313390.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressO14579.
BgeeO14579.
CleanExHS_COPE.
GenevestigatorO14579.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR006822. Coatomer_esu.
IPR011990. TPR-like_helical.
[Graphical view]
PANTHERPTHR10805. PTHR10805. 1 hit.
PfamPF04733. Coatomer_E. 1 hit.
[Graphical view]
PIRSFPIRSF016478. Coatomer_esu. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCOPE. human.
GeneWikiCOPE_(gene).
GenomeRNAi11316.
NextBio42987.
PROO14579.
SOURCESearch...

Entry information

Entry nameCOPE_HUMAN
AccessionPrimary (citable) accession number: O14579
Secondary accession number(s): A6NE29 expand/collapse secondary AC list , A6NKA3, O76097, Q6IBB8, Q9UGP6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 122 of the entry and version 3 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

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 19

Human chromosome 19: entries, gene names and cross-references to MIM