P53621 (COPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Coatomer subunit alpha

Alternative name(s):
Alpha-coat protein
Short name=Alpha-COP
HEP-COP
Short name=HEPCOP

Cleaved into the following 2 chains:

1. Xenin
   Alternative name(s):
   Xenopsin-related peptide
2. Proxenin

Gene names

Name:

COPA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1224 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor.
Subunit structure	Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Probably interacts with PEX11A. Interacts with SCYL1 By similarity.
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. Xenin: Secreted By similarity.
Tissue specificity	Uniformly expressed in a wide range of adult and fetal tissues. Xenin is found in gastric, duodenal and jejunal mucosa. Circulates in the blood. Seems to be confined to specific endocrine cells.
Developmental stage	Xenin is released into the circulation after a meal.
Sequence similarities	Contains 6 WD repeats.
RNA editing	Edited at position 164. Edited at about 31%. Ref.19

Ontologies

Keywords
Biological process	ER-Golgi transport Protein transport Transport
Cellular component	Cytoplasm Cytoplasmic vesicle Golgi apparatus Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism RNA editing
Domain	Repeat WD repeat
Molecular function	Hormone
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	COPI coating of Golgi vesicle Traceable author statement. Source: Reactome intracellular protein transport Inferred from electronic annotation. Source: InterPro pancreatic juice secretion Inferred from direct assay Ref.5. Source: MGI retrograde vesicle-mediated transport, Golgi to ER Traceable author statement. Source: Reactome
Cellular component	COPI vesicle coat Inferred from sequence or structural similarity. Source: UniProtKB cytosol Traceable author statement. Source: Reactome extracellular space Inferred from direct assay Ref.5. Source: MGI microsome Inferred from direct assay. Source: MGI soluble fraction Inferred from direct assay. Source: MGI
Molecular function	hormone activity Inferred from electronic annotation. Source: UniProtKB-KW structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P53621-1)

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: P53621-2)

The sequence of this isoform differs from the canonical sequence as follows:
     509-509: H → HEHSCPLPLT

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1224	1224	Coatomer subunit alpha		PRO_0000223307
	Peptide	1 – 35	35	Proxenin		PRO_0000041400
	Peptide	1 – 25	25	Xenin Ref.5		PRO_0000041401
Regions
	Repeat	7 – 37	31	WD 1
	Repeat	49 – 79	31	WD 2
	Repeat	91 – 121	31	WD 3
	Repeat	133 – 163	31	WD 4
	Repeat	203 – 233	31	WD 5
	Repeat	247 – 277	31	WD 6
Amino acid modifications
	Modified residue	173	1	Phosphoserine Ref.7 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
	Modified residue	249	1	Phosphotyrosine Ref.9
	Modified residue	402	1	Phosphoserine Ref.7 Ref.15
	Modified residue	895	1	Phosphoserine Ref.14
	Modified residue	1035	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	509	1	H → HEHSCPLPLT in isoform 2.		VSP_035043
	Natural variant	164	1	I → V in RNA edited version.		VAR_066525
	Natural variant	1040	1	V → G. Corresponds to variant rs34997807 [ dbSNP | Ensembl ].		VAR_033803
Experimental info
	Sequence conflict	703	1	L → V in AAB70879. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 2, 2008. Version 2. Checksum: 5A8BC35CE78F155D	FASTA	1,224	138,346
	10 20 30 40 50 60 MLTKFETKSA RVKGLSFHPK RPWILTSLHN GVIQLWDYRM CTLIDKFDEH DGPVRGIDFH 70 80 90 100 110 120 KQQPLFVSGG DDYKIKVWNY KLRRCLFTLL GHLDYIRTTF FHHEYPWILS ASDDQTIRVW 130 140 150 160 170 180 NWQSRTCVCV LTGHNHYVMC AQFHPTEDLV VSASLDQTVR VWDISGLRKK NLSPGAVESD 190 200 210 220 230 240 VRGITGVDLF GTTDAVVKHV LEGHDRGVNW AAFHPTMPLI VSGADDRQVK IWRMNESKAW 250 260 270 280 290 300 EVDTCRGHYN NVSCAVFHPR QELILSNSED KSIRVWDMSK RTGVQTFRRD HDRFWVLAAH 310 320 330 340 350 360 PNLNLFAAGH DGGMIVFKLE RERPAYAVHG NMLHYVKDRF LRQLDFNSSK DVAVMQLRSG 370 380 390 400 410 420 SKFPVFNMSY NPAENAVLLC TRASNLENST YDLYTIPKDA DSQNPDAPEG KRSSGLTAVW 430 440 450 460 470 480 VARNRFAVLD RMHSLLIKNL KNEITKKVQV PNCDEIFYAG TGNLLLRDAD SITLFDVQQK 490 500 510 520 530 540 RTLASVKISK VKYVIWSADM SHVALLAKHA IVICNRKLDA LCNIHENIRV KSGAWDESGV 550 560 570 580 590 600 FIYTTSNHIK YAVTTGDHGI IRTLDLPIYV TRVKGNNVYC LDRECRPRVL TIDPTEFKFK 610 620 630 640 650 660 LALINRKYDE VLHMVRNAKL VGQSIIAYLQ KKGYPEVALH FVKDEKTRFS LALECGNIEI 670 680 690 700 710 720 ALEAAKALDD KNCWEKLGEV ALLQGNHQIV EMCYQRTKNF DKLSFLYLIT GNLEKLRKMM 730 740 750 760 770 780 KIAEIRKDMS GHYQNALYLG DVSERVRILK NCGQKSLAYL TAATHGLDEE AESLKETFDP 790 800 810 820 830 840 EKETIPDIDP NAKLLQPPAP IMPLDTNWPL LTVSKGFFEG TIASKGKGGA LAADIDIDTV 850 860 870 880 890 900 GTEGWGEDAE LQLDEDGFVE ATEGLGDDAL GKGQEEGGGW DVEEDLELPP ELDISPGAAG 910 920 930 940 950 960 GAEDGFFVPP TKGTSPTQIW CNNSQLPVDH ILAGSFETAM RLLHDQVGVI QFGPYKQLFL 970 980 990 1000 1010 1020 QTYARGRTTY QALPCLPSMY GYPNRNWKDA GLKNGVPAVG LKLNDLIQRL QLCYQLTTVG 1030 1040 1050 1060 1070 1080 KFEEAVEKFR SILLSVPLLV VDNKQEIAEA QQLITICREY IVGLSVETER KKLPKETLEQ 1090 1100 1110 1120 1130 1140 QKRICEMAAY FTHSNLQPVH MILVLRTALN LFFKLKNFKT AATFARRLLE LGPKPEVAQQ 1150 1160 1170 1180 1190 1200 TRKILSACEK NPTDAYQLNY DMHNPFDICA ASYRPIYRGK PVEKCPLSGA CYSPEFKGQI 1210 1220 CRVTTVTEIG KDVIGLRISP LQFR
	Isoform 2 [UniParc]. Checksum: F43D084894C9AD98	FASTA	1,233	139,324
	10 20 30 40 50 60 MLTKFETKSA RVKGLSFHPK RPWILTSLHN GVIQLWDYRM CTLIDKFDEH DGPVRGIDFH 70 80 90 100 110 120 KQQPLFVSGG DDYKIKVWNY KLRRCLFTLL GHLDYIRTTF FHHEYPWILS ASDDQTIRVW 130 140 150 160 170 180 NWQSRTCVCV LTGHNHYVMC AQFHPTEDLV VSASLDQTVR VWDISGLRKK NLSPGAVESD 190 200 210 220 230 240 VRGITGVDLF GTTDAVVKHV LEGHDRGVNW AAFHPTMPLI VSGADDRQVK IWRMNESKAW 250 260 270 280 290 300 EVDTCRGHYN NVSCAVFHPR QELILSNSED KSIRVWDMSK RTGVQTFRRD HDRFWVLAAH 310 320 330 340 350 360 PNLNLFAAGH DGGMIVFKLE RERPAYAVHG NMLHYVKDRF LRQLDFNSSK DVAVMQLRSG 370 380 390 400 410 420 SKFPVFNMSY NPAENAVLLC TRASNLENST YDLYTIPKDA DSQNPDAPEG KRSSGLTAVW 430 440 450 460 470 480 VARNRFAVLD RMHSLLIKNL KNEITKKVQV PNCDEIFYAG TGNLLLRDAD SITLFDVQQK 490 500 510 520 530 540 RTLASVKISK VKYVIWSADM SHVALLAKHE HSCPLPLTAI VICNRKLDAL CNIHENIRVK 550 560 570 580 590 600 SGAWDESGVF IYTTSNHIKY AVTTGDHGII RTLDLPIYVT RVKGNNVYCL DRECRPRVLT 610 620 630 640 650 660 IDPTEFKFKL ALINRKYDEV LHMVRNAKLV GQSIIAYLQK KGYPEVALHF VKDEKTRFSL 670 680 690 700 710 720 ALECGNIEIA LEAAKALDDK NCWEKLGEVA LLQGNHQIVE MCYQRTKNFD KLSFLYLITG 730 740 750 760 770 780 NLEKLRKMMK IAEIRKDMSG HYQNALYLGD VSERVRILKN CGQKSLAYLT AATHGLDEEA 790 800 810 820 830 840 ESLKETFDPE KETIPDIDPN AKLLQPPAPI MPLDTNWPLL TVSKGFFEGT IASKGKGGAL 850 860 870 880 890 900 AADIDIDTVG TEGWGEDAEL QLDEDGFVEA TEGLGDDALG KGQEEGGGWD VEEDLELPPE 910 920 930 940 950 960 LDISPGAAGG AEDGFFVPPT KGTSPTQIWC NNSQLPVDHI LAGSFETAMR LLHDQVGVIQ 970 980 990 1000 1010 1020 FGPYKQLFLQ TYARGRTTYQ ALPCLPSMYG YPNRNWKDAG LKNGVPAVGL KLNDLIQRLQ 1030 1040 1050 1060 1070 1080 LCYQLTTVGK FEEAVEKFRS ILLSVPLLVV DNKQEIAEAQ QLITICREYI VGLSVETERK 1090 1100 1110 1120 1130 1140 KLPKETLEQQ KRICEMAAYF THSNLQPVHM ILVLRTALNL FFKLKNFKTA ATFARRLLEL 1150 1160 1170 1180 1190 1200 GPKPEVAQQT RKILSACEKN PTDAYQLNYD MHNPFDICAA SYRPIYRGKP VEKCPLSGAC 1210 1220 1230 YSPEFKGQIC RVTTVTEIGK DVIGLRISPL QFR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"HEP-COP, a novel human gene whose product is highly homologous to the alpha-subunit of the yeast coatomer protein complex." Chow V.T.K., Quek H.H. Gene 169:223-227(1996) [PubMed: 8647451] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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. , 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].
[4]	"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] (ISOFORM 2). Tissue: Uterus.
[5]	"Identification of xenin, a xenopsin-related peptide, in the human gastric mucosa and its effect on exocrine pancreatic secretion." Feurle G.E., Hamscher G., Kusiek R., Meyer H.E., Metzger J.W. J. Biol. Chem. 267:22305-22309(1992) [PubMed: 1429581] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-25 (XENIN). Tissue: Gastric mucosa.
[6]	"Alpha coat protein COPA (HEP-COP): presence of an Alu repeat in cDNA and identity of the amino terminus to xenin." Chow V.T.K., Quek H.H. Ann. Hum. Genet. 61:369-373(1997) [PubMed: 9365789] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF COPA TO PRODUCE XENIN.
[7]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-402, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Xenin -- a review." Feurle G.E. Peptides 19:609-615(1998) [PubMed: 9533652] [Abstract] Cited for: REVIEW ON XENIN.
[9]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-249, MASS SPECTROMETRY.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-895, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-402, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"Genome-wide evaluation and discovery of vertebrate A-to-I RNA editing sites." Maas S., Godfried Sie C.P., Stoev I., Dupuis D.E., Latona J., Porman A.M., Evans B., Rekawek P., Kluempers V., Mutter M., Gommans W.M., Lopresti D. Biochem. Biophys. Res. Commun. 412:407-412(2011) [PubMed: 21835166] [Abstract] Cited for: RNA EDITING OF POSITION 164.
+	Additional computationally mapped references.

Web resources

Wikipedia

Xenin entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	U24105 mRNA. Translation: AAB70879.1. AL513282, AL445230 Genomic DNA. Translation: CAI12454.1. AL513282, AL445230 Genomic DNA. Translation: CAI12455.1. AL445230, AL513282 Genomic DNA. Translation: CAI15004.1. AL445230, AL513282 Genomic DNA. Translation: CAI15005.1. CH471121 Genomic DNA. Translation: EAW52723.1. CH471121 Genomic DNA. Translation: EAW52725.1. BC038447 mRNA. Translation: AAH38447.1.
IPI	IPI00295857. IPI00646493.
PIR	ERHUAH. JC4668.
RefSeq	NP_001091868.1. NM_001098398.1. NP_004362.2. NM_004371.3.
UniGene	Hs.162121. Hs.685025.
3D structure databases
ProteinModelPortal	P53621.
SMR	P53621. Positions 1-812, 905-1224.
ModBase	Search...
Protein-protein interaction databases
IntAct	P53621. 13 interactions.
MINT	MINT-1144184.
STRING	P53621.
PTM databases
PhosphoSite	P53621.
Polymorphism databases
DMDM	205371746.
Proteomic databases
PRIDE	P53621.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000241704; ENSP00000241704; ENSG00000122218.
GeneID	1314.
KEGG	hsa:1314.
Organism-specific databases
CTD	1314.
GeneCards	GC01M160258.
H-InvDB	HIX0023608.
HGNC	HGNC:2230. COPA.
HPA	HPA028024.
MIM	601924. gene.
neXtProt	NX_P53621.
PharmGKB	PA26746.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08148.
GeneTree	ENSGT00600000084501.
HOVERGEN	HBG005379.
OMA	LSGACYC.
PhylomeDB	P53621.
Enzyme and pathway databases
Pathway_Interaction_DB	arf_3pathway. Arf1 pathway.
Reactome	REACT_11123. Membrane Trafficking.
Gene expression databases
ArrayExpress	P53621.
Bgee	P53621.
CleanEx	HS_COPA.
Genevestigator	P53621.
GermOnline	ENSG00000122218. Homo sapiens.
Family and domain databases
InterPro	IPR016391. Coatomer_asu. IPR010714. Coatomer_asu_C. IPR006692. Coatomer_WD-assoc_reg. IPR020472. G-protein_beta_WD-40_rep. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR011046. WD40_repeat-like_dom. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_dom. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
KO	K05236.
Pfam	PF04053. Coatomer_WDAD. 1 hit. PF06957. COPI_C. 1 hit. PF00400. WD40. 6 hits. [Graphical view]
PIRSF	PIRSF003354. Coatomer_alpha_subunit. 1 hit.
PRINTS	PR00320. GPROTEINBRPT.
SMART	SM00320. WD40. 7 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. 1 hit. PS50082. WD_REPEATS_2. 6 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	5373.
SOURCE	Search...

Entry information

Entry name

COPA_HUMAN

Accession

Primary (citable) accession number: P53621
Secondary accession number(s): Q5T201, Q8IXZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	September 2, 2008
Last modified:	January 25, 2012
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.