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P53621

- COPA_HUMAN

UniProt

P53621 - COPA_HUMAN

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Protein

Coatomer subunit alpha

Gene

COPA

Organism
Homo sapiens (Human)
Status
Reviewed - 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. 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).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.

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. COPI coating of Golgi vesicle Source: Reactome
  2. intracellular protein transport Source: InterPro
  3. membrane organization Source: Reactome
  4. pancreatic juice secretion Source: MGI
  5. retrograde vesicle-mediated transport, Golgi to ER Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hormone

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_11096. COPI Mediated Transport.
SignaLinkiP53621.

Names & Taxonomyi

Protein namesi
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:
Alternative name(s):
Xenopsin-related peptide
Gene namesi
Name:COPA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2230. COPA.

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
Peptide Xenin : Secreted By similarity

GO - Cellular componenti

  1. COPI vesicle coat Source: UniProtKB
  2. cytoplasm Source: MGI
  3. cytosol Source: Reactome
  4. extracellular space Source: MGI
  5. extracellular vesicular exosome Source: UniProt
  6. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26746.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12241224Coatomer subunit alphaPRO_0000223307Add
BLAST
Peptidei1 – 3535ProxeninPRO_0000041400Add
BLAST
Peptidei1 – 2525XeninPRO_0000041401Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei173 – 1731Phosphoserine7 Publications
Modified residuei185 – 1851Phosphothreonine1 Publication
Modified residuei402 – 4021Phosphoserine2 Publications
Modified residuei895 – 8951Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53621.
PaxDbiP53621.
PRIDEiP53621.

PTM databases

PhosphoSiteiP53621.

Expressioni

Tissue specificityi

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 stagei

Xenin is released into the circulation after a meal.

Gene expression databases

BgeeiP53621.
CleanExiHS_COPA.
GenevestigatoriP53621.

Organism-specific databases

HPAiHPA028024.

Interactioni

Subunit structurei

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). Interacts with JAGN1.By similarity1 Publication

Protein-protein interaction databases

BioGridi107709. 49 interactions.
IntActiP53621. 23 interactions.
MINTiMINT-1144184.
STRINGi9606.ENSP00000357048.

Structurei

3D structure databases

ProteinModelPortaliP53621.
SMRiP53621. Positions 1-320, 905-1224.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati7 – 3731WD 1Add
BLAST
Repeati49 – 7931WD 2Add
BLAST
Repeati91 – 12131WD 3Add
BLAST
Repeati133 – 16331WD 4Add
BLAST
Repeati203 – 23331WD 5Add
BLAST
Repeati247 – 27731WD 6Add
BLAST

Sequence similaritiesi

Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00520000055597.
HOGENOMiHOG000195913.
HOVERGENiHBG005379.
InParanoidiP53621.
KOiK05236.
OMAiFWVLGAH.
OrthoDBiEOG78WKQX.
PhylomeDBiP53621.
TreeFamiTF105693.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR016391. Coatomer_asu.
IPR010714. Coatomer_asu_C.
IPR006692. Coatomer_WD-assoc_reg.
IPR020472. G-protein_beta_WD-40_rep.
IPR011048. Haem_d1.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF04053. Coatomer_WDAD. 1 hit.
PF06957. COPI_C. 1 hit.
PF00400. WD40. 6 hits.
[Graphical view]
PIRSFiPIRSF003354. Coatomer_alpha_subunit. 1 hit.
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
SSF51004. SSF51004. 3 hits.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P53621-1) [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
MLTKFETKSA RVKGLSFHPK RPWILTSLHN GVIQLWDYRM CTLIDKFDEH
60 70 80 90 100
DGPVRGIDFH KQQPLFVSGG DDYKIKVWNY KLRRCLFTLL GHLDYIRTTF
110 120 130 140 150
FHHEYPWILS ASDDQTIRVW NWQSRTCVCV LTGHNHYVMC AQFHPTEDLV
160 170 180 190 200
VSASLDQTVR VWDISGLRKK NLSPGAVESD VRGITGVDLF GTTDAVVKHV
210 220 230 240 250
LEGHDRGVNW AAFHPTMPLI VSGADDRQVK IWRMNESKAW EVDTCRGHYN
260 270 280 290 300
NVSCAVFHPR QELILSNSED KSIRVWDMSK RTGVQTFRRD HDRFWVLAAH
310 320 330 340 350
PNLNLFAAGH DGGMIVFKLE RERPAYAVHG NMLHYVKDRF LRQLDFNSSK
360 370 380 390 400
DVAVMQLRSG SKFPVFNMSY NPAENAVLLC TRASNLENST YDLYTIPKDA
410 420 430 440 450
DSQNPDAPEG KRSSGLTAVW VARNRFAVLD RMHSLLIKNL KNEITKKVQV
460 470 480 490 500
PNCDEIFYAG TGNLLLRDAD SITLFDVQQK RTLASVKISK VKYVIWSADM
510 520 530 540 550
SHVALLAKHA IVICNRKLDA LCNIHENIRV KSGAWDESGV FIYTTSNHIK
560 570 580 590 600
YAVTTGDHGI IRTLDLPIYV TRVKGNNVYC LDRECRPRVL TIDPTEFKFK
610 620 630 640 650
LALINRKYDE VLHMVRNAKL VGQSIIAYLQ KKGYPEVALH FVKDEKTRFS
660 670 680 690 700
LALECGNIEI ALEAAKALDD KNCWEKLGEV ALLQGNHQIV EMCYQRTKNF
710 720 730 740 750
DKLSFLYLIT GNLEKLRKMM KIAEIRKDMS GHYQNALYLG DVSERVRILK
760 770 780 790 800
NCGQKSLAYL TAATHGLDEE AESLKETFDP EKETIPDIDP NAKLLQPPAP
810 820 830 840 850
IMPLDTNWPL LTVSKGFFEG TIASKGKGGA LAADIDIDTV GTEGWGEDAE
860 870 880 890 900
LQLDEDGFVE ATEGLGDDAL GKGQEEGGGW DVEEDLELPP ELDISPGAAG
910 920 930 940 950
GAEDGFFVPP TKGTSPTQIW CNNSQLPVDH ILAGSFETAM RLLHDQVGVI
960 970 980 990 1000
QFGPYKQLFL QTYARGRTTY QALPCLPSMY GYPNRNWKDA GLKNGVPAVG
1010 1020 1030 1040 1050
LKLNDLIQRL QLCYQLTTVG KFEEAVEKFR SILLSVPLLV VDNKQEIAEA
1060 1070 1080 1090 1100
QQLITICREY IVGLSVETER KKLPKETLEQ QKRICEMAAY FTHSNLQPVH
1110 1120 1130 1140 1150
MILVLRTALN LFFKLKNFKT AATFARRLLE LGPKPEVAQQ TRKILSACEK
1160 1170 1180 1190 1200
NPTDAYQLNY DMHNPFDICA ASYRPIYRGK PVEKCPLSGA CYSPEFKGQI
1210 1220
CRVTTVTEIG KDVIGLRISP LQFR
Length:1,224
Mass (Da):138,346
Last modified:September 2, 2008 - v2
Checksum:i5A8BC35CE78F155D
GO
Isoform 2 (identifier: P53621-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,233
Mass (Da):139,324
Checksum:iF43D084894C9AD98
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti703 – 7031L → V in AAB70879. (PubMed:8647451)Curated

RNA editingi

Edited at about 31%.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti164 – 1641I → V in RNA edited version.
VAR_066525
Natural varianti1040 – 10401V → G.
Corresponds to variant rs34997807 [ dbSNP | Ensembl ].
VAR_033803

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei509 – 5091H → HEHSCPLPLT in isoform 2. 1 PublicationVSP_035043

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1202.1. [P53621-1]
CCDS41424.1. [P53621-2]
PIRiJC4668. ERHUAH.
RefSeqiNP_001091868.1. NM_001098398.1. [P53621-2]
NP_004362.2. NM_004371.3. [P53621-1]
UniGeneiHs.162121.
Hs.685025.

Genome annotation databases

EnsembliENST00000241704; ENSP00000241704; ENSG00000122218. [P53621-1]
ENST00000368069; ENSP00000357048; ENSG00000122218. [P53621-2]
GeneIDi1314.
KEGGihsa:1314.
UCSCiuc001fvv.4. human. [P53621-2]
uc009wti.3. human. [P53621-1]

Polymorphism databases

DMDMi205371746.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, RNA editing

Cross-referencesi

Web resourcesi

Wikipedia

Xenin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1202.1. [P53621-1 ]
CCDS41424.1. [P53621-2 ]
PIRi JC4668. ERHUAH.
RefSeqi NP_001091868.1. NM_001098398.1. [P53621-2 ]
NP_004362.2. NM_004371.3. [P53621-1 ]
UniGenei Hs.162121.
Hs.685025.

3D structure databases

ProteinModelPortali P53621.
SMRi P53621. Positions 1-320, 905-1224.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107709. 49 interactions.
IntActi P53621. 23 interactions.
MINTi MINT-1144184.
STRINGi 9606.ENSP00000357048.

PTM databases

PhosphoSitei P53621.

Polymorphism databases

DMDMi 205371746.

Proteomic databases

MaxQBi P53621.
PaxDbi P53621.
PRIDEi P53621.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000241704 ; ENSP00000241704 ; ENSG00000122218 . [P53621-1 ]
ENST00000368069 ; ENSP00000357048 ; ENSG00000122218 . [P53621-2 ]
GeneIDi 1314.
KEGGi hsa:1314.
UCSCi uc001fvv.4. human. [P53621-2 ]
uc009wti.3. human. [P53621-1 ]

Organism-specific databases

CTDi 1314.
GeneCardsi GC01M160258.
HGNCi HGNC:2230. COPA.
HPAi HPA028024.
MIMi 601924. gene.
neXtProti NX_P53621.
PharmGKBi PA26746.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00520000055597.
HOGENOMi HOG000195913.
HOVERGENi HBG005379.
InParanoidi P53621.
KOi K05236.
OMAi FWVLGAH.
OrthoDBi EOG78WKQX.
PhylomeDBi P53621.
TreeFami TF105693.

Enzyme and pathway databases

Reactomei REACT_11096. COPI Mediated Transport.
SignaLinki P53621.

Miscellaneous databases

ChiTaRSi COPA. human.
GeneWikii COPA_(gene).
GenomeRNAii 1314.
NextBioi 5373.
PROi P53621.
SOURCEi Search...

Gene expression databases

Bgeei P53621.
CleanExi HS_COPA.
Genevestigatori P53621.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR016391. Coatomer_asu.
IPR010714. Coatomer_asu_C.
IPR006692. Coatomer_WD-assoc_reg.
IPR020472. G-protein_beta_WD-40_rep.
IPR011048. Haem_d1.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF04053. Coatomer_WDAD. 1 hit.
PF06957. COPI_C. 1 hit.
PF00400. WD40. 6 hits.
[Graphical view ]
PIRSFi PIRSF003354. Coatomer_alpha_subunit. 1 hit.
PRINTSi PR00320. GPROTEINBRPT.
SMARTi SM00320. WD40. 7 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 2 hits.
SSF51004. SSF51004. 3 hits.
PROSITEi PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF COPA TO PRODUCE XENIN.
  7. Cited for: REVIEW ON XENIN.
  8. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-895, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND THR-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: RNA EDITING OF POSITION 164.
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-402, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: INTERACTION WITH JAGN1.

Entry informationi

Entry nameiCOPA_HUMAN
AccessioniPrimary (citable) accession number: P53621
Secondary accession number(s): Q5T201, Q8IXZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 2, 2008
Last modified: October 29, 2014
This is version 153 of the entry and version 2 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 1
    Human chromosome 1: 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