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Protein

Platelet glycoprotein VI

Gene

GP6

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

Functioni

Collagen receptor involved in collagen-induced platelet adhesion and activation. Plays a key role in platelet procoagulant activity and subsequent thrombin and fibrin formation. This procoagulant function may contribute to arterial and venous thrombus formation. The signaling pathway involves the FcR gamma-chain, the Src kinases (likely Fyn/Lyn), the adapter protein LAT and leads to the activation of phospholipase C gamma2.1 Publication

GO - Molecular functioni

  • collagen binding Source: UniProtKB
  • receptor activity Source: UniProtKB
  • transmembrane signaling receptor activity Source: ProtInc

GO - Biological processi

  • blood coagulation Source: Reactome
  • enzyme linked receptor protein signaling pathway Source: ProtInc
  • leukocyte migration Source: Reactome
  • platelet activation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Blood coagulation, Hemostasis

Enzyme and pathway databases

ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
REACT_1230. Platelet Adhesion to exposed collagen.
REACT_1695. GPVI-mediated activation cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet glycoprotein VI
Short name:
GPVI
Alternative name(s):
Glycoprotein 6
Gene namesi
Name:GP6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:14388. GP6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 267247ExtracellularSequence AnalysisAdd
BLAST
Transmembranei268 – 28821HelicalSequence AnalysisAdd
BLAST
Topological domaini289 – 33951CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
  • tetraspanin-enriched microdomain Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Bleeding disorder, platelet-type 11 (BDPLT11)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA mild to moderate bleeding disorder caused by defective platelet activation and aggregation in response to collagen.

See also OMIM:614201
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti58 – 581R → C in BDPLT11; results in abnormal protein migration and a loss of collagen binding. 1 Publication
VAR_066590
Natural varianti175 – 1751S → N in BDPLT11; shows strongly reduced membrane expression and decreased interaction with the snake toxin convulxin. 1 Publication
VAR_066591

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi61 – 611K → A: Increases collagen binding. 1 Publication
Mutagenesisi79 – 791K → E: Dramatically reduces collagen binding. 1 Publication
Mutagenesisi80 – 801R → A: Reduces collagen binding. 1 Publication
Mutagenesisi92 – 921N → A: Reduces collagen binding (65 to 70%). 1 Publication
Mutagenesisi94 – 941S → A: Reduces collagen binding (65 to 70%). 1 Publication
Mutagenesisi95 – 951L → H: No effect on collagen binding. 1 Publication
Mutagenesisi186 – 1861R → A: Reduces collagen binding. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614201. phenotype.
Orphaneti98885. Bleeding diathesis due to glycoprotein VI deficiency.
PharmGKBiPA28824.

Polymorphism and mutation databases

BioMutaiGP6.
DMDMi327478600.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 339319Platelet glycoprotein VIPRO_0000232383Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi48 ↔ 881 Publication
Glycosylationi92 – 921N-linked (GlcNAc...)1 Publication
Disulfide bondi134 ↔ 1801 Publication

Post-translational modificationi

N-linked glycosylation at Asn-92 is not required for the cell surface expression, but contributes to maximal adhesion to type I collagen, collagen-related peptide (CRP), and, to a lesser extent, to the snake venom C-type lectin convulxin (CVX).1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9HCN6.
PRIDEiQ9HCN6.

PTM databases

PhosphoSiteiQ9HCN6.

Expressioni

Tissue specificityi

Megakaryocytes and platelets.1 Publication

Gene expression databases

BgeeiQ9HCN6.
CleanExiHS_GP6.
ExpressionAtlasiQ9HCN6. baseline.
GenevisibleiQ9HCN6. HS.

Organism-specific databases

HPAiHPA066482.

Interactioni

Subunit structurei

Associated with Fc receptor gamma chain. The GPVI-FcRgamma complex is associated with the Src kinase family Fyn and Lyn.

Binary interactionsi

WithEntry#Exp.IntActNotes
LYNP079482EBI-515278,EBI-79452

Protein-protein interaction databases

BioGridi119379. 8 interactions.
DIPiDIP-33875N.
IntActiQ9HCN6. 4 interactions.
MINTiMINT-258007.

Structurei

Secondary structure

1
339
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 346Combined sources
Beta strandi36 – 394Combined sources
Beta strandi44 – 496Combined sources
Beta strandi55 – 617Combined sources
Turni62 – 643Combined sources
Beta strandi67 – 7711Combined sources
Helixi80 – 823Combined sources
Beta strandi84 – 929Combined sources
Beta strandi95 – 973Combined sources
Beta strandi103 – 1119Combined sources
Beta strandi115 – 1195Combined sources
Beta strandi130 – 1356Combined sources
Beta strandi142 – 1476Combined sources
Beta strandi159 – 17012Combined sources
Beta strandi175 – 1839Combined sources
Beta strandi198 – 2025Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GI7X-ray2.40A/B21-203[»]
ProteinModelPortaliQ9HCN6.
SMRiQ9HCN6. Positions 22-261.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HCN6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 10479Ig-like C2-type 1Add
BLAST
Domaini114 – 19683Ig-like C2-type 2Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG79029.
GeneTreeiENSGT00760000119033.
HOGENOMiHOG000234395.
HOVERGENiHBG074353.
InParanoidiQ9HCN6.
KOiK06264.
OMAiASSWCSI.
PhylomeDBiQ9HCN6.
TreeFamiTF336644.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
[Graphical view]

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. AlignAdd to basket

Isoform 1 (identifier: Q9HCN6-1) [UniParc]FASTAAdd to basket

Also known as: VI-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.

« Hide

        10         20         30         40         50
MSPSPTALFC LGLCLGRVPA QSGPLPKPSL QALPSSLVPL EKPVTLRCQG
60 70 80 90 100
PPGVDLYRLE KLSSSRYQDQ AVLFIPAMKR SLAGRYRCSY QNGSLWSLPS
110 120 130 140 150
DQLELVATGV FAKPSLSAQP GPAVSSGGDV TLQCQTRYGF DQFALYKEGD
160 170 180 190 200
PAPYKNPERW YRASFPIITV TAAHSGTYRC YSFSSRDPYL WSAPSDPLEL
210 220 230 240 250
VVTGTSVTPS RLPTEPPSPV AEFSEATAEL TVSFTNEVFT TETSRSITAS
260 270 280 290 300
PKESDSPAGP ARQYYTKGNL VRICLGAVIL IILAGFLAED WHSRRKRLRH
310 320 330
RGRAVQRPLP PLPPLPLTRK SNGGQDGGRQ DVHSRGLCS
Length:339
Mass (Da):36,866
Last modified:April 5, 2011 - v4
Checksum:i3EFE2DD0E1676BA8
GO
Isoform 2 (identifier: Q9HCN6-2) [UniParc]FASTAAdd to basket

Also known as: VI-2

The sequence of this isoform differs from the canonical sequence as follows:
     204-221: Missing.

Show »
Length:321
Mass (Da):35,091
Checksum:iEEE281373112DB21
GO
Isoform 3 (identifier: Q9HCN6-3) [UniParc]FASTAAdd to basket

Also known as: VI-3

The sequence of this isoform differs from the canonical sequence as follows:
     260-339: PARQYYTKGN...QDVHSRGLCS → ESCPPVLHQG...TGMNMSITLI

Note: Has no transmembrane domain. Does not interact with Fc receptor gamma chain. Does not bind to collagen-like peptides.Curated
Show »
Length:620
Mass (Da):67,476
Checksum:iF6DBAE2547664D7A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 3 (identifier: Q9HCN6-3)
Sequence conflicti314 – 3141P → A in BAB12247 (PubMed:11027634).Curated
Sequence conflicti323 – 3231K → T in BAB12247 (PubMed:11027634).Curated
Sequence conflicti573 – 5731R → G in BAB12247 (PubMed:11027634).Curated
Sequence conflicti606 – 6061F → L in BAB12247 (PubMed:11027634).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti58 – 581R → C in BDPLT11; results in abnormal protein migration and a loss of collagen binding. 1 Publication
VAR_066590
Natural varianti175 – 1751S → N in BDPLT11; shows strongly reduced membrane expression and decreased interaction with the snake toxin convulxin. 1 Publication
VAR_066591
Natural varianti219 – 2191P → S.3 Publications
Corresponds to variant rs1613662 [ dbSNP | Ensembl ].
VAR_060352
Natural varianti237 – 2371E → K.3 Publications
Corresponds to variant rs1654416 [ dbSNP | Ensembl ].
VAR_060353
Natural varianti249 – 2491A → T.3 Publications
Corresponds to variant rs2304167 [ dbSNP | Ensembl ].
VAR_060354
Natural varianti317 – 3171L → Q.3 Publications
Corresponds to variant rs1654413 [ dbSNP | Ensembl ].
VAR_059389
Natural varianti322 – 3221N → H.3 Publications
Corresponds to variant rs1671152 [ dbSNP | Ensembl ].
VAR_059390
Natural varianti335 – 3351R → G.
Corresponds to variant rs1654412 [ dbSNP | Ensembl ].
VAR_060355

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei204 – 22118Missing in isoform 2. 1 PublicationVSP_017879Add
BLAST
Alternative sequencei260 – 33980PARQY…RGLCS → ESCPPVLHQGQPGPDMPRGC DPNNPGGVSGRGLAQPEEAP AAQGQGCAEAASAPPAPPAD PEIKRGSGWRPTGCSQPRVM FMTAEPQARSYPREGSWHGR RLKDWRVWSVEAGGQRLQLW KRGHAASSWCSIREPFGQCL SVCLPLCLRAPSIWDGRNLW RPHPPPCTLWMTWYPGWTTY WPLSSTSLIWAPDGSLRFPA LRVDSVPSSVQNPPVLPFGP LCSCLVFPRNSHPHSISHCG LTNLLSSLRTGLAGSLGMSF IFLSVKLARCPLPFTLENKI SLCNMVKPHLYQQNKKTQKL ARCGGASLYSQQLRGLRWEN GLSLGGRGCSELRSHHCTLA RVTKPDFVSKNTGMNMSITL I in isoform 3. 1 PublicationVSP_017880Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB043819 mRNA. Translation: BAB12245.1.
AB043820 mRNA. Translation: BAB12246.1.
AB043821 mRNA. Translation: BAB12247.1.
AB035073 mRNA. Translation: BAA89353.1.
AC011476 Genomic DNA. No translation available.
BC104832 mRNA. Translation: AAI04833.1.
BC111963 mRNA. Translation: AAI11964.1.
CCDSiCCDS42626.1. [Q9HCN6-3]
CCDS46184.1. [Q9HCN6-1]
CCDS58678.1. [Q9HCN6-2]
PIRiJC7509.
RefSeqiNP_001077368.2. NM_001083899.2. [Q9HCN6-3]
NP_001242946.2. NM_001256017.2. [Q9HCN6-2]
NP_057447.5. NM_016363.5. [Q9HCN6-1]
UniGeneiHs.661752.

Genome annotation databases

EnsembliENST00000310373; ENSP00000308782; ENSG00000088053. [Q9HCN6-3]
ENST00000333884; ENSP00000334552; ENSG00000088053. [Q9HCN6-2]
ENST00000417454; ENSP00000394922; ENSG00000088053.
ENST00000612096; ENSP00000481583; ENSG00000276065. [Q9HCN6-2]
ENST00000612184; ENSP00000479873; ENSG00000277439. [Q9HCN6-2]
ENST00000613801; ENSP00000478918; ENSG00000278670. [Q9HCN6-2]
ENST00000614662; ENSP00000478025; ENSG00000276065. [Q9HCN6-3]
ENST00000615407; ENSP00000481524; ENSG00000278670. [Q9HCN6-3]
ENST00000616319; ENSP00000481125; ENSG00000278316. [Q9HCN6-2]
ENST00000616456; ENSP00000483314; ENSG00000277439.
ENST00000619136; ENSP00000479034; ENSG00000278316. [Q9HCN6-3]
ENST00000622279; ENSP00000484029; ENSG00000277439. [Q9HCN6-3]
GeneIDi51206.
KEGGihsa:51206.
UCSCiuc002qik.3. human. [Q9HCN6-1]
uc002qil.3. human. [Q9HCN6-3]
uc010esq.3. human. [Q9HCN6-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB043819 mRNA. Translation: BAB12245.1.
AB043820 mRNA. Translation: BAB12246.1.
AB043821 mRNA. Translation: BAB12247.1.
AB035073 mRNA. Translation: BAA89353.1.
AC011476 Genomic DNA. No translation available.
BC104832 mRNA. Translation: AAI04833.1.
BC111963 mRNA. Translation: AAI11964.1.
CCDSiCCDS42626.1. [Q9HCN6-3]
CCDS46184.1. [Q9HCN6-1]
CCDS58678.1. [Q9HCN6-2]
PIRiJC7509.
RefSeqiNP_001077368.2. NM_001083899.2. [Q9HCN6-3]
NP_001242946.2. NM_001256017.2. [Q9HCN6-2]
NP_057447.5. NM_016363.5. [Q9HCN6-1]
UniGeneiHs.661752.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GI7X-ray2.40A/B21-203[»]
ProteinModelPortaliQ9HCN6.
SMRiQ9HCN6. Positions 22-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119379. 8 interactions.
DIPiDIP-33875N.
IntActiQ9HCN6. 4 interactions.
MINTiMINT-258007.

PTM databases

PhosphoSiteiQ9HCN6.

Polymorphism and mutation databases

BioMutaiGP6.
DMDMi327478600.

Proteomic databases

PaxDbiQ9HCN6.
PRIDEiQ9HCN6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000310373; ENSP00000308782; ENSG00000088053. [Q9HCN6-3]
ENST00000333884; ENSP00000334552; ENSG00000088053. [Q9HCN6-2]
ENST00000417454; ENSP00000394922; ENSG00000088053.
ENST00000612096; ENSP00000481583; ENSG00000276065. [Q9HCN6-2]
ENST00000612184; ENSP00000479873; ENSG00000277439. [Q9HCN6-2]
ENST00000613801; ENSP00000478918; ENSG00000278670. [Q9HCN6-2]
ENST00000614662; ENSP00000478025; ENSG00000276065. [Q9HCN6-3]
ENST00000615407; ENSP00000481524; ENSG00000278670. [Q9HCN6-3]
ENST00000616319; ENSP00000481125; ENSG00000278316. [Q9HCN6-2]
ENST00000616456; ENSP00000483314; ENSG00000277439.
ENST00000619136; ENSP00000479034; ENSG00000278316. [Q9HCN6-3]
ENST00000622279; ENSP00000484029; ENSG00000277439. [Q9HCN6-3]
GeneIDi51206.
KEGGihsa:51206.
UCSCiuc002qik.3. human. [Q9HCN6-1]
uc002qil.3. human. [Q9HCN6-3]
uc010esq.3. human. [Q9HCN6-2]

Organism-specific databases

CTDi51206.
GeneCardsiGC19M055525.
HGNCiHGNC:14388. GP6.
HPAiHPA066482.
MIMi605546. gene.
614201. phenotype.
neXtProtiNX_Q9HCN6.
Orphaneti98885. Bleeding diathesis due to glycoprotein VI deficiency.
PharmGKBiPA28824.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG79029.
GeneTreeiENSGT00760000119033.
HOGENOMiHOG000234395.
HOVERGENiHBG074353.
InParanoidiQ9HCN6.
KOiK06264.
OMAiASSWCSI.
PhylomeDBiQ9HCN6.
TreeFamiTF336644.

Enzyme and pathway databases

ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
REACT_1230. Platelet Adhesion to exposed collagen.
REACT_1695. GPVI-mediated activation cascade.

Miscellaneous databases

EvolutionaryTraceiQ9HCN6.
GeneWikiiGPVI.
GenomeRNAii51206.
NextBioi54258.
PROiQ9HCN6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HCN6.
CleanExiHS_GP6.
ExpressionAtlasiQ9HCN6. baseline.
GenevisibleiQ9HCN6. HS.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, genomic structure, chromosomal localization, and alternative splice forms of the platelet collagen receptor glycoprotein VI."
    Ezumi Y., Uchiyama T., Takayama H.
    Biochem. Biophys. Res. Commun. 277:27-36(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), PROTEIN SEQUENCE OF 28-41; 62-79 AND 114-142, VARIANTS SER-219; LYS-237; THR-249; GLN-317 AND HIS-322.
  2. "Cloning, characterization, and functional studies of human and mouse glycoprotein VI: a platelet-specific collagen receptor from the immunoglobulin superfamily."
    Jandrot-Perrus M., Busfield S., Lagrue A.-H., Xiong X., Debili N., Chickering T., Le Couedic J.-P., Goodearl A., Dussault B., Fraser C., Vainchenker W., Villeval J.-L.
    Blood 96:1798-1807(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH FC RECEPTOR GAMMA CHAIN, TISSUE SPECIFICITY.
    Tissue: Megakaryocyte.
  3. "Platelet glycoprotein VI."
    Miura Y.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-219; LYS-237; THR-249; GLN-317 AND HIS-322.
  4. "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].
  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] (ISOFORM 1), VARIANTS SER-219; LYS-237; THR-249; GLN-317 AND HIS-322.
  6. "A novel association of Fc receptor gamma-chain with glycoprotein VI and their co-expression as a collagen receptor in human platelets."
    Tsuji M., Ezumi Y., Arai M., Takayama H.
    J. Biol. Chem. 272:23528-23531(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FC RECEPTOR GAMMA CHAIN.
  7. "The influence of N-linked glycosylation on the function of platelet glycoprotein VI."
    Kunicki T.J., Cheli Y., Moroi M., Furihata K.
    Blood 106:2744-2749(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-92, MUTAGENESIS OF ASN-92; SER-94 AND LEU-95.
  8. "Gain- and loss-of-function mutants confirm the importance of apical residues to the primary interaction of human glycoprotein VI with collagen."
    O'connor M.N., Smethurst P.A., Farndale R.W., Ouwehand W.H.
    J. Thromb. Haemost. 4:869-873(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-61; LYS-79; ARG-80 AND ARG-186.
  9. "Structural basis for platelet collagen responses by the immune-type receptor glycoprotein VI."
    Horii K., Kahn M.L., Herr A.B.
    Blood 108:936-942(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-203, DISULFIDE BONDS.
  10. "Absence of collagen-induced platelet activation caused by compound heterozygous GPVI mutations."
    Dumont B., Lasne D., Rothschild C., Bouabdelli M., Ollivier V., Oudin C., Ajzenberg N., Grandchamp B., Jandrot-Perrus M.
    Blood 114:1900-1903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BDPLT11 CYS-58, CHARACTERIZATION OF VARIANT BDPLT11 CYS-58.
  11. "A compound heterozygous mutation in glycoprotein VI in a patient with a bleeding disorder."
    Hermans C., Wittevrongel C., Thys C., Smethurst P.A., Van Geet C., Freson K.
    J. Thromb. Haemost. 7:1356-1363(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BDPLT11 ASN-175, CHARACTERIZATION OF VARIANT BDPLT11 ASN-175.

Entry informationi

Entry nameiGPVI_HUMAN
AccessioniPrimary (citable) accession number: Q9HCN6
Secondary accession number(s): Q9HCN7, Q9UIF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: April 5, 2011
Last modified: July 22, 2015
This is version 122 of the entry and version 4 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.