Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Coatomer subunit epsilon

Gene

COPE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. COPI coating of Golgi vesicle Source: Reactome
  2. ER to Golgi vesicle-mediated transport Source: GO_Central
  3. intra-Golgi vesicle-mediated transport Source: UniProtKB
  4. membrane organization Source: Reactome
  5. protein transport Source: UniProtKB-KW
  6. retrograde vesicle-mediated transport, Golgi to ER Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_11096. COPI Mediated Transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Coatomer subunit epsilon
Alternative name(s):
Epsilon-coat protein
Short name:
Epsilon-COP
Gene namesi
Name:COPE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:2234. COPE.

Subcellular locationi

Cytoplasm By similarity. Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmic vesicleCOPI-coated vesicle membrane By similarity; Peripheral membrane protein By similarity; 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

GO - Cellular componenti

  1. COPI vesicle coat Source: UniProtKB
  2. cytosol Source: Reactome
  3. Golgi apparatus Source: LIFEdb
  4. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26750.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 308307Coatomer subunit epsilonPRO_0000193851Add
BLAST

Post-translational modificationi

Phosphorylated by PKA.
Polyubiquitinated by RCHY1 in the presence of androgen, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO14579.
PaxDbiO14579.
PRIDEiO14579.

2D gel databases

OGPiO14579.

PTM databases

PhosphoSiteiO14579.

Expressioni

Gene expression databases

BgeeiO14579.
CleanExiHS_COPE.
ExpressionAtlasiO14579. baseline and differential.
GenevestigatoriO14579.

Organism-specific databases

HPAiCAB034345.
HPA041605.
HPA043576.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi116447. 29 interactions.
IntActiO14579. 8 interactions.
MINTiMINT-5000768.
STRINGi9606.ENSP00000262812.

Structurei

3D structure databases

ProteinModelPortaliO14579.
SMRiO14579. Positions 17-307.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the COPE family.Curated

Phylogenomic databases

eggNOGiNOG289253.
GeneTreeiENSGT00390000003478.
HOGENOMiHOG000205825.
HOVERGENiHBG002201.
InParanoidiO14579.
KOiK17268.
OrthoDBiEOG7QK0CC.
PhylomeDBiO14579.
TreeFamiTF313390.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR006822. Coatomer_esu.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR10805. PTHR10805. 1 hit.
PfamiPF04733. Coatomer_E. 1 hit.
[Graphical view]
PIRSFiPIRSF016478. Coatomer_esu. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O14579-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAPPAPGPAS GGSGEVDELF DVKNAFYIGS YQQCINEAQR VKLSSPERDV
60 70 80 90 100
ERDVFLYRAY LAQRKFGVVL DEIKPSSAPE LQAVRMFADY LAHESRRDSI
110 120 130 140 150
VAELDREMSR SVDVTNTTFL LMAASIYLHD QNPDAALRAL HQGDSLECTA
160 170 180 190 200
MTVQILLKLD RLDLARKELK RMQDLDEDAT LTQLATAWVS LATGGEKLQD
210 220 230 240 250
AYYIFQEMAD KCSPTLLLLN GQAACHMAQG RWEAAEGLLQ EALDKDSGYP
260 270 280 290 300
ETLVNLIVLS QHLGKPPEVT NRYLSQLKDA HRSHPFIKEY QAKENDFDRL

VLQYAPSA
Length:308
Mass (Da):34,482
Last modified:January 23, 2007 - v3
Checksum:iA71146F3332F6BA9
GO
Isoform 2 (identifier: O14579-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     97-97: R → S
     98-148: Missing.

Note: No experimental confirmation available.

Show »
Length:257
Mass (Da):28,797
Checksum:i0F26BDC0A83D65BF
GO
Isoform 3 (identifier: O14579-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     194-245: Missing.

Note: No experimental confirmation available.

Show »
Length:256
Mass (Da):28,773
Checksum:i4B35360D41136F1A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131S → C.
Corresponds to variant rs2231987 [ dbSNP | Ensembl ].
VAR_054032
Natural varianti117 – 1171T → I.2 Publications
Corresponds to variant rs10330 [ dbSNP | Ensembl ].
VAR_054033

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei97 – 971R → S in isoform 2. 1 PublicationVSP_042770
Alternative sequencei98 – 14851Missing in isoform 2. 1 PublicationVSP_042771Add
BLAST
Alternative sequencei194 – 24552Missing in isoform 3. 1 PublicationVSP_045070Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12387.1. [O14579-1]
CCDS12388.1. [O14579-2]
CCDS12389.1. [O14579-3]
RefSeqiNP_009194.2. NM_007263.3. [O14579-1]
NP_955474.1. NM_199442.1. [O14579-2]
NP_955476.1. NM_199444.1. [O14579-3]
UniGeneiHs.10326.

Genome annotation databases

EnsembliENST00000262812; ENSP00000262812; ENSG00000105669. [O14579-1]
ENST00000349893; ENSP00000343134; ENSG00000105669. [O14579-3]
ENST00000351079; ENSP00000345674; ENSG00000105669. [O14579-2]
GeneIDi11316.
KEGGihsa:11316.
UCSCiuc002nkk.3. human. [O14579-1]
uc002nkl.3. human. [O14579-2]
uc002nkm.3. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12387.1. [O14579-1]
CCDS12388.1. [O14579-2]
CCDS12389.1. [O14579-3]
RefSeqiNP_009194.2. NM_007263.3. [O14579-1]
NP_955474.1. NM_199442.1. [O14579-2]
NP_955476.1. NM_199444.1. [O14579-3]
UniGeneiHs.10326.

3D structure databases

ProteinModelPortaliO14579.
SMRiO14579. Positions 17-307.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116447. 29 interactions.
IntActiO14579. 8 interactions.
MINTiMINT-5000768.
STRINGi9606.ENSP00000262812.

PTM databases

PhosphoSiteiO14579.

2D gel databases

OGPiO14579.

Proteomic databases

MaxQBiO14579.
PaxDbiO14579.
PRIDEiO14579.

Protocols and materials databases

DNASUi11316.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262812; ENSP00000262812; ENSG00000105669. [O14579-1]
ENST00000349893; ENSP00000343134; ENSG00000105669. [O14579-3]
ENST00000351079; ENSP00000345674; ENSG00000105669. [O14579-2]
GeneIDi11316.
KEGGihsa:11316.
UCSCiuc002nkk.3. human. [O14579-1]
uc002nkl.3. human. [O14579-2]
uc002nkm.3. human.

Organism-specific databases

CTDi11316.
GeneCardsiGC19M019010.
HGNCiHGNC:2234. COPE.
HPAiCAB034345.
HPA041605.
HPA043576.
MIMi606942. gene.
neXtProtiNX_O14579.
PharmGKBiPA26750.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG289253.
GeneTreeiENSGT00390000003478.
HOGENOMiHOG000205825.
HOVERGENiHBG002201.
InParanoidiO14579.
KOiK17268.
OrthoDBiEOG7QK0CC.
PhylomeDBiO14579.
TreeFamiTF313390.

Enzyme and pathway databases

ReactomeiREACT_11096. COPI Mediated Transport.

Miscellaneous databases

ChiTaRSiCOPE. human.
GeneWikiiCOPE_(gene).
GenomeRNAii11316.
NextBioi42987.
PROiO14579.
SOURCEiSearch...

Gene expression databases

BgeeiO14579.
CleanExiHS_COPE.
ExpressionAtlasiO14579. baseline and differential.
GenevestigatoriO14579.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR006822. Coatomer_esu.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR10805. PTHR10805. 1 hit.
PfamiPF04733. Coatomer_E. 1 hit.
[Graphical view]
PIRSFiPIRSF016478. Coatomer_esu. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCOPE_HUMAN
AccessioniPrimary (citable) accession number: O14579
Secondary accession number(s): A6NE29
, A6NKA3, O76097, Q6IBB8, Q9UGP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.