GPVI_HUMAN - dbPTM
GPVI_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPVI_HUMAN
UniProt AC Q9HCN6
Protein Name Platelet glycoprotein VI {ECO:0000305}
Gene Name GP6 {ECO:0000312|HGNC:HGNC:14388}
Organism Homo sapiens (Human).
Sequence Length 339
Subcellular Localization Isoform 1: Cell membrane
Single-pass membrane protein.
Isoform 2: Cell membrane
Single-pass membrane protein.
Protein Description 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 or LYN) and SYK, the adapter protein LAT and leads to the activation of PLCG2..
Protein Sequence MSPSPTALFCLGLCLGRVPAQSGPLPKPSLQALPSSLVPLEKPVTLRCQGPPGVDLYRLEKLSSSRYQDQAVLFIPAMKRSLAGRYRCSYQNGSLWSLPSDQLELVATGVFAKPSLSAQPGPAVSSGGDVTLQCQTRYGFDQFALYKEGDPAPYKNPERWYRASFPIITVTAAHSGTYRCYSFSSRDPYLWSAPSDPLELVVTGTSVTPSRLPTEPPSPVAEFSEATAELTVSFTNEVFTTETSRSITASPKESDSPAGPARQYYTKGNLVRICLGAVILIILAGFLAEDWHSRRKRLRHRGRAVQRPLPPLPPLPLTRKSNGGQDGGRQDVHSRGLCS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
22PhosphorylationLGRVPAQSGPLPKPS
HCCCCCCCCCCCCCH
44.4729449344
45PhosphorylationVPLEKPVTLRCQGPP
CCCCCCEEEEECCCC
19.6027251275
63PhosphorylationLYRLEKLSSSRYQDQ
EEEEEECCCCCCCCC
37.0227251275
64PhosphorylationYRLEKLSSSRYQDQA
EEEEECCCCCCCCCE
29.3027251275
65PhosphorylationRLEKLSSSRYQDQAV
EEEECCCCCCCCCEE
31.4727251275
67PhosphorylationEKLSSSRYQDQAVLF
EECCCCCCCCCEEEE
20.5618083107
92N-linked_GlycosylationRYRCSYQNGSLWSLP
CEEEEECCCCCEECC
33.5116014566
331 (in isoform 3)Phosphorylation-38.4425921289
342 (in isoform 3)Phosphorylation-25921289
380 (in isoform 3)Ubiquitination--

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of GPVI_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
92NGlycosylation

16014566

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of GPVI_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LYN_HUMANLYNphysical
11943772
FYN_HUMANFYNphysical
11943772
LYN_HUMANLYNphysical
12594225
FCERG_HUMANFCER1Gphysical
12594225
TRAF4_HUMANTRAF4physical
20946164
TGFI1_HUMANTGFB1I1physical
20946164
NCF1_HUMANNCF1physical
20946164
FAK2_HUMANPTK2Bphysical
20946164
LYN_HUMANLYNphysical
20946164

Drug and Disease Associations
Kegg Disease
H01235 Bleeding disorder platelet-type
OMIM Disease
614201Bleeding disorder, platelet-type 11 (BDPLT11)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GPVI_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"The influence of N-linked glycosylation on the function of plateletglycoprotein VI.";
Kunicki T.J., Cheli Y., Moroi M., Furihata K.;
Blood 106:2744-2749(2005).
Cited for: GLYCOSYLATION AT ASN-92, AND MUTAGENESIS OF ASN-92; SER-94 AND LEU-95.

TOP