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GPC1 (glypican 1)

Written2013-11Wael Awad, Derek T Logan, Katrin Mani
Dept. of Biochemistry & Structural Biology, Lund University, Box 124, S-221 00 Lund, Sweden (WA,DTL); Glycobiology, Dept. of Experimental Medical Science, BMC A13, S-221 84 Lund, Sweden (KM)

(Note : for Links provided by Atlas : click)

Identity

Alias_symbol (synonym)glypican
Other alias
HGNC (Hugo) GPC1
LocusID (NCBI) 2817
Atlas_Id 44301
Location 2q37.3  [Link to chromosome band 2q37]
Location_base_pair Starts at 240435698 and ends at 240468078 bp from pter ( according to hg19-Feb_2009)  [Mapping GPC1.png]
Fusion genes
(updated 2016)
GPC1 (2q37.3) / ANKFN1 (17q22)GPC1 (2q37.3) / GPC1 (2q37.3)GPC1 (2q37.3) / MFN1 (3q26.33)

DNA/RNA

Description The gene spans 32381 pb of DNA, comprising 9 exons.
Transcription 1676 bp open reading frame.

Protein

 
  Crystal structure of the N-glycosylated human Gpc-1 core protein (PDB entry 4ACR). Cartoon diagram of Gpc-1 in which the body of the structure is coloured light blue, the N-terminal helix and loop in dark blue and the C-terminal helix in red. Important loops (L1:L3) and all of the α-helices (α1:α14) are labelled. The seven disulphide bonds common to all glypicans are indicated in yellow. The assignment of different lobes in the Gpc-1 structure (Svensson et al., 2011) is displayed on the bottom line.
Description The glypican-1 gene codes for a protein of 558 amino acids with a predicted molecular weight of 62 kDa. It is a cell surface, lipid-raft-associated heparan sulfate proteoglycan (HSPG), composed of a glycosylphosphatidylinositol (GPI)-anchored core protein substituted with a three chains of heparan sulfate near its C-terminus. It shares, along with all other glypicans, an N-terminal secretory signal, heparan sulfate attachment sites, 14 evolutionary conserved cysteine residues and hydrophobic domain near the C-terminus for the addition of the glycosylphosphatidylinositol (GPI) anchor. Also, the glypican-1 core protein contains two N-glycosylation sites at Asn79 & Asn116, which are found to be invariably occupied. The N-linked glycans at these sites affect Gpc-1 protein expression and heparan sulfate substitution. Nevertheless the protein is folded correctly even in the absence of N-linked glycans (Svensson et al., 2011). Recently, the structure of C-terminally truncated human N-glycosylated Gpc-1 core protein was determined at 2.55 Å resolution (Svensson et al., 2012; Awad et al., 2013), which revealed a highly extended, cylindrical (dimensions 120 x 30 x 30 Å), stable all-α-helical fold. Its structural similarity to the Dally-like protein from Drosophila (Kim et al., 2011) confirmed a conserved overall fold for the glypican family. The Gpc-1 structure consists of 14 α-helices (α1- α14) and three major loops (L1-L3). The extended helix α2 (83Å) traverses the whole protein, carrying two N-linked glycans close to its ends. The Gpc-1 structure revealed the complete arrangement of the 14 Cys residues conserved across the glypican family, in 7 disulfide bonds, 6 of them located near the molecule N terminus at a region termed "Cys-rich lobe". This lobe is followed by a region forms the heart of the structure called the "central lobe". This lobe is stabilized by evolutionary conserved hydrophobic centers. The last region of the Gpc-1 molecule is termed the "protease site lobe" because of the presence of a protease site in this part. No additional electron density was observed in the electron density maps from crystals of non-truncated glypican-1 containing the HS attachment region near the C-terminus, which suggests that this part is highly disordered. This extended long C terminus (50 residues) might thus give the core protein a freedom in its orientation when Gpc-1 is anchored to the cell membrane (Svensson et al., 2012).
Expression GPC1 is expressed mainly in the central nervous system (CNS) and skeletal system during development but also in many other tissues in the adult.
Localisation GPC1 is a cell surface HSPG that can be internalized via a caveolin-1 associated pathway. GPC1 undergoes a recycling from cell surface to endosomes and back to the cell surface via Golgi. During recycling, the HS chains of GPC1 are degraded by heparanase and further on by a novel copper, nitric oxide and vitamin C-dependent deaminative cleavage. New HS chains are synthesized on the stubs remaining on the core protein (Cheng et al., 2002; Fransson and Mani, 2007).
Function Many of the functions of GPC1 are dependent on the HS side chains, which are capable of binding and/or activating and/or transporting a variety of growth factors (FGF2), cytokines, enzymes, viral proteins, and polyamines. It is known that both the core protein and the HS chains of GPC1 are important for brain function, as knock-out of GPC1 gene expression results in reduction of brain size by 30% (Jen et al., 2009) and errors in HS metabolism result in neurodegeneration and mental retardation accompanied by accumulation of amyloid β in human brain (Ohmi et al., 2011). A role for GPC1 in axonal guidance and regeneration via Slit has been proposed (Bloechlinger et al., 2004; Lau and Margolis, 2010). Several studies indicate involvement of Gpc1 in prion conversion and scrapie infection (Löfgren et al., 2008; Taylor et al., 2009; Hooper, 2011).
Homology GPC1 belongs to the glypican family. To date, six different glypicans have been identified in vertebrates (GPC1, GPC2, GPC3, GPC4, GPC5, and GPC6), two in Drosophila melanogaster (Dally and Dally-like protein), two in C. elegans (Gpn-1 and Lon-2) and one in zebrafish (knypek). Based on sequence comparisons, vertebrate glypicans fall into two subfamilies: glypicans 1, 2, 4, 6 and glypicans 3 and 5, with approximately 25% amino acid identity between the groups.

Implicated in

Note
  
Entity Various cancers
Note Many studies have shown that GPC1 is crucial for efficient cancer cell growth, metastasis, and angiogenesis of many human and mouse cancer cell types (Ding et al., 2005; Kayed et al., 2006; Aikawa et al., 2008; Whipple et al., 2012). GPC1 is up-regulated in human cancer cells such as glioma, pancreatic and breast cancers and supports and maintains the mitogenic effect of several HS-binding growth factors (Matsuda et al., 2001; Kayed et al., 2006; Su et al., 2006). Downregulation of GPC1 results in prolonged doubling times and decreased growth of cancer cells in vitro, as well as attenuated tumor growth, angiogenesis, and metastasis in vivo.
  
  
Entity Neurodegenerative diseases
Note A number of studies indicate involvement of GPC1 in the pathogenesis of several neurodegenerative diseases including Alzheimer's disease (van Horssen et al., 2001; Watanabe et al., 2004; Cappai et al., 2005; O'Callaghan et al., 2008; Timmer et al., 2009; Cheng et al., 2011), prion disease (Cheng et al., 2006; Löfgren et al., 2008; Taylor et al., 2009; Hooper, 2011), and Niemann-Pick type C1 disease (Mani et al., 2006). GPC1 has been localized to the amyloid plaques of Alzheimer's disease. Both nitric oxide- and heparanase-induced degraded GPC1 HS have found to be associated with amyloid deposits, including the toxic amyloid β peptide aggregates in brain of human Alzheimer's patients and transgenic Alzheimer's mice (Sandwall et al., 2010; Cheng et al., 2011). Further, it has been shown that the HS oligosaccharides released from GPC1 by Cu/NO-vitamin C form conjugates with amyloid β peptides, thereby modulating and suppressing oligomerization of amyloid β and dissolving toxic amyloid β oligomers in hippocampal slices from Alzheimer's mice (Cheng et al., 2011). Other studies have shown that amyloid β toxicity is attenuated in cells overexpressing heparanase, suggesting that HS oligosaccharides generated by cleavage with heparanase could also have a protective effect (Sandwall et al., 2010; Zhang et al., 2012).
  

Bibliography

Glypican-1 modulates the angiogenic and metastatic potential of human and mouse cancer cells.
Aikawa T, Whipple CA, Lopez ME, Gunn J, Young A, Lander AD, Korc M.
J Clin Invest. 2008 Jan;118(1):89-99.
PMID 18064304
 
Improvements in the order, isotropy and electron density of glypican-1 crystals by controlled dehydration.
Awad W, Svensson Birkedal G, Thunnissen MM, Mani K, Logan DT.
Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2524-33. doi: 10.1107/S0907444913025250. Epub 2013 Nov 19.
PMID 24311593
 
Dynamic changes in glypican-1 expression in dorsal root ganglion neurons after peripheral and central axonal injury.
Bloechlinger S, Karchewski LA, Woolf CJ.
Eur J Neurosci. 2004 Mar;19(5):1119-32.
PMID 15016071
 
The amyloid precursor protein (APP) of Alzheimer disease and its paralog, APLP2, modulate the Cu/Zn-Nitric Oxide-catalyzed degradation of glypican-1 heparan sulfate in vivo.
Cappai R, Cheng F, Ciccotosto GD, Needham BE, Masters CL, Multhaup G, Fransson LA, Mani K.
J Biol Chem. 2005 Apr 8;280(14):13913-20. Epub 2005 Jan 27.
PMID 15677459
 
Suppression of amyloid beta A11 antibody immunoreactivity by vitamin C: possible role of heparan sulfate oligosaccharides derived from glypican-1 by ascorbate-induced, nitric oxide (NO)-catalyzed degradation.
Cheng F, Cappai R, Ciccotosto GD, Svensson G, Multhaup G, Fransson LA, Mani K.
J Biol Chem. 2011 Aug 5;286(31):27559-72. doi: 10.1074/jbc.M111.243345. Epub 2011 Jun 3.
PMID 21642435
 
Copper-dependent co-internalization of the prion protein and glypican-1.
Cheng F, Lindqvist J, Haigh CL, Brown DR, Mani K.
J Neurochem. 2006 Sep;98(5):1445-57.
PMID 16923158
 
Nitric oxide-dependent processing of heparan sulfate in recycling S-nitrosylated glypican-1 takes place in caveolin-1-containing endosomes.
Cheng F, Mani K, van den Born J, Ding K, Belting M, Fransson LA.
J Biol Chem. 2002 Nov 15;277(46):44431-9. Epub 2002 Sep 10.
PMID 12226079
 
Growth factor-induced shedding of syndecan-1 confers glypican-1 dependence on mitogenic responses of cancer cells.
Ding K, Lopez-Burks M, Sanchez-Duran JA, Korc M, Lander AD.
J Cell Biol. 2005 Nov 21;171(4):729-38. Epub 2005 Nov 14.
PMID 16286510
 
Novel aspects of vitamin C: how important is glypican-1 recycling?
Fransson LA, Mani K.
Trends Mol Med. 2007 Apr;13(4):143-9. Epub 2007 Mar 6.
PMID 17344097
 
Glypican-1 facilitates prion conversion in lipid rafts.
Hooper NM.
J Neurochem. 2011 Mar;116(5):721-5. doi: 10.1111/j.1471-4159.2010.06936.x. (REVIEW)
PMID 20681952
 
Glypican-1 controls brain size through regulation of fibroblast growth factor signaling in early neurogenesis.
Jen YH, Musacchio M, Lander AD.
Neural Dev. 2009 Sep 4;4:33. doi: 10.1186/1749-8104-4-33.
PMID 19732411
 
Correlation of glypican-1 expression with TGF-beta, BMP, and activin receptors in pancreatic ductal adenocarcinoma.
Kayed H, Kleeff J, Keleg S, Jiang X, Penzel R, Giese T, Zentgraf H, Buchler MW, Korc M, Friess H.
Int J Oncol. 2006 Nov;29(5):1139-48.
PMID 17016645
 
Structure of the protein core of the glypican Dally-like and localization of a region important for hedgehog signaling.
Kim MS, Saunders AM, Hamaoka BY, Beachy PA, Leahy DJ.
Proc Natl Acad Sci U S A. 2011 Aug 9;108(32):13112-7. doi: 10.1073/pnas.1109877108. Epub 2011 Jul 26.
PMID 21828006
 
Inhibitors of slit protein interactions with the heparan sulphate proteoglycan glypican-1: potential agents for the treatment of spinal cord injury.
Lau E, Margolis RU.
Clin Exp Pharmacol Physiol. 2010 Apr;37(4):417-21. doi: 10.1111/j.1440-1681.2009.05318.x. Epub 2009 Oct 16.
PMID 19843094
 
Involvement of glypican-1 autoprocessing in scrapie infection.
Lofgren K, Cheng F, Fransson LA, Bedecs K, Mani K.
Eur J Neurosci. 2008 Sep;28(5):964-72. doi: 10.1111/j.1460-9568.2008.06386.x. Epub 2008 Aug 20.
PMID 18717736
 
Defective nitric oxide-dependent, deaminative cleavage of glypican-1 heparan sulfate in Niemann-Pick C1 fibroblasts.
Mani K1, Cheng F, Fransson LA.
Glycobiology. 2006 Aug;16(8):711-8. Epub 2006 Apr 27.
PMID 16645004
 
Glypican-1 is overexpressed in human breast cancer and modulates the mitogenic effects of multiple heparin-binding growth factors in breast cancer cells.
Matsuda K, Maruyama H, Guo F, Kleeff J, Itakura J, Matsumoto Y, Lander AD, Korc M.
Cancer Res. 2001 Jul 15;61(14):5562-9.
PMID 11454708
 
Heparan sulfate accumulation with Abeta deposits in Alzheimer's disease and Tg2576 mice is contributed by glial cells.
O'Callaghan P, Sandwall E, Li JP, Yu H, Ravid R, Guan ZZ, van Kuppevelt TH, Nilsson LN, Ingelsson M, Hyman BT, Kalimo H, Lindahl U, Lannfelt L, Zhang X.
Brain Pathol. 2008 Oct;18(4):548-61. doi: 10.1111/j.1750-3639.2008.00152.x. Epub 2008 Apr 11.
PMID 18422760
 
Defects in the medial entorhinal cortex and dentate gyrus in the mouse model of Sanfilippo syndrome type B.
Ohmi K, Zhao HZ, Neufeld EF.
PLoS One. 2011;6(11):e27461. doi: 10.1371/journal.pone.0027461. Epub 2011 Nov 9.
PMID 22096577
 
Heparan sulfate mediates amyloid-beta internalization and cytotoxicity.
Sandwall E, O'Callaghan P, Zhang X, Lindahl U, Lannfelt L, Li JP.
Glycobiology. 2010 May;20(5):533-41. doi: 10.1093/glycob/cwp205. Epub 2010 Jan 5.
PMID 20053627
 
Glypican-1 is frequently overexpressed in human gliomas and enhances FGF-2 signaling in glioma cells.
Su G, Meyer K, Nandini CD, Qiao D, Salamat S, Friedl A.
Am J Pathol. 2006 Jun;168(6):2014-26.
PMID 16723715
 
Crystal structure of N-glycosylated human glypican-1 core protein: structure of two loops evolutionarily conserved in vertebrate glypican-1.
Svensson G, Awad W, Hakansson M, Mani K, Logan DT.
J Biol Chem. 2012 Apr 20;287(17):14040-51. doi: 10.1074/jbc.M111.322487. Epub 2012 Feb 20.
PMID 22351761
 
Glypican-1 mediates both prion protein lipid raft association and disease isoform formation.
Taylor DR, Whitehouse IJ, Hooper NM.
PLoS Pathog. 2009 Nov;5(11):e1000666. doi: 10.1371/journal.ppat.1000666. Epub 2009 Nov 20.
PMID 19936054
 
Amyloid beta induces cellular relocalization and production of agrin and glypican-1.
Timmer NM, van Horssen J, Otte-Holler I, Wilhelmus MM, David G, van Beers J, de Waal RM, Verbeek MM.
Brain Res. 2009 Mar 13;1260:38-46. doi: 10.1016/j.brainres.2008.12.063. Epub 2009 Jan 7.
PMID 19166823
 
Glypican-1 as an Abeta binding HSPG in the human brain: its localization in DIG domains and possible roles in the pathogenesis of Alzheimer's disease.
Watanabe N, Araki W, Chui DH, Makifuchi T, Ihara Y, Tabira T.
FASEB J. 2004 Jun;18(9):1013-5. Epub 2004 Apr 14.
PMID 15084524
 
A KrasG12D-driven genetic mouse model of pancreatic cancer requires glypican-1 for efficient proliferation and angiogenesis.
Whipple CA, Young AL, Korc M.
Oncogene. 2012 May 17;31(20):2535-44. doi: 10.1038/onc.2011.430. Epub 2011 Sep 26.
PMID 21996748
 
Heparanase overexpression impairs inflammatory response and macrophage-mediated clearance of amyloid-beta in murine brain.
Zhang X, Wang B, O'Callaghan P, Hjertstrom E, Jia J, Gong F, Zcharia E, Nilsson LN, Lannfelt L, Vlodavsky I, Lindahl U, Li JP.
Acta Neuropathol. 2012 Oct;124(4):465-78. doi: 10.1007/s00401-012-0997-1. Epub 2012 Jun 13.
PMID 22692572
 
Heparan sulfate proteoglycan expression in cerebrovascular amyloid beta deposits in Alzheimer's disease and hereditary cerebral hemorrhage with amyloidosis (Dutch) brains.
van Horssen J, Otte-Holler I, David G, Maat-Schieman ML, van den Heuvel LP, Wesseling P, de Waal RM, Verbeek MM.
Acta Neuropathol. 2001 Dec;102(6):604-14.
PMID 11761721
 

Citation

This paper should be referenced as such :
Awad, W ; Logan, DT ; Mani, K
GPC1 (glypican 1)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(7):461-464.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/GPC1ID44301ch2q37.html


Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 1 ]
  Bone: Osteochondroma


External links

Nomenclature
HGNC (Hugo)GPC1   4449
Cards
AtlasGPC1ID44301ch2q37
Entrez_Gene (NCBI)GPC1  2817  glypican 1
Aliasesglypican
GeneCards (Weizmann)GPC1
Ensembl hg19 (Hinxton)ENSG00000063660 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000063660 [Gene_View]  chr2:240435698-240468078 [Contig_View]  GPC1 [Vega]
ICGC DataPortalENSG00000063660
TCGA cBioPortalGPC1
AceView (NCBI)GPC1
Genatlas (Paris)GPC1
WikiGenes2817
SOURCE (Princeton)GPC1
Genetics Home Reference (NIH)GPC1
Genomic and cartography
GoldenPath hg38 (UCSC)GPC1  -     chr2:240435698-240468078 +  2q37.3   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)GPC1  -     2q37.3   [Description]    (hg19-Feb_2009)
EnsemblGPC1 - 2q37.3 [CytoView hg19]  GPC1 - 2q37.3 [CytoView hg38]
Mapping of homologs : NCBIGPC1 [Mapview hg19]  GPC1 [Mapview hg38]
OMIM600395   
Gene and transcription
Genbank (Entrez)AB209122 AK095397 AK096638 AK223516 BC008123
RefSeq transcript (Entrez)NM_002081
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)GPC1
Cluster EST : UnigeneHs.328232 [ NCBI ]
CGAP (NCI)Hs.328232
Alternative Splicing GalleryENSG00000063660
Gene ExpressionGPC1 [ NCBI-GEO ]   GPC1 [ EBI - ARRAY_EXPRESS ]   GPC1 [ SEEK ]   GPC1 [ MEM ]
Gene Expression Viewer (FireBrowse)GPC1 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)2817
GTEX Portal (Tissue expression)GPC1
Protein : pattern, domain, 3D structure
UniProt/SwissProtP35052   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP35052  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP35052
Splice isoforms : SwissVarP35052
PhosPhoSitePlusP35052
Domaine pattern : Prosite (Expaxy)GLYPICAN (PS01207)   
Domains : Interpro (EBI)Glypican    Glypican-1    Glypican_CS   
Domain families : Pfam (Sanger)Glypican (PF01153)   
Domain families : Pfam (NCBI)pfam01153   
Conserved Domain (NCBI)GPC1
DMDM Disease mutations2817
Blocks (Seattle)GPC1
PDB (SRS)4ACR    4AD7    4BWE    4YWT   
PDB (PDBSum)4ACR    4AD7    4BWE    4YWT   
PDB (IMB)4ACR    4AD7    4BWE    4YWT   
PDB (RSDB)4ACR    4AD7    4BWE    4YWT   
Structural Biology KnowledgeBase4ACR    4AD7    4BWE    4YWT   
SCOP (Structural Classification of Proteins)4ACR    4AD7    4BWE    4YWT   
CATH (Classification of proteins structures)4ACR    4AD7    4BWE    4YWT   
SuperfamilyP35052
Human Protein AtlasENSG00000063660
Peptide AtlasP35052
HPRD02671
IPIIPI00015688   IPI00952744   IPI00893155   IPI00556267   IPI00892905   IPI00892532   IPI00892648   
Protein Interaction databases
DIP (DOE-UCLA)P35052
IntAct (EBI)P35052
FunCoupENSG00000063660
BioGRIDGPC1
STRING (EMBL)GPC1
ZODIACGPC1
Ontologies - Pathways
QuickGOP35052
Ontology : AmiGOretinoid metabolic process  copper ion binding  proteinaceous extracellular matrix  extracellular space  nucleoplasm  endosome  Golgi lumen  cytosol  plasma membrane  plasma membrane  integral component of plasma membrane  glycosaminoglycan biosynthetic process  glycosaminoglycan catabolic process  axon guidance  Schwann cell differentiation  fibroblast growth factor binding  heparan sulfate proteoglycan catabolic process  glycosaminoglycan metabolic process  anchored component of membrane  myelin assembly  negative regulation of fibroblast growth factor receptor signaling pathway  lysosomal lumen  laminin binding  heparan sulfate proteoglycan binding  membrane raft  membrane raft  leukocyte migration  extracellular exosome  positive regulation of skeletal muscle cell differentiation  
Ontology : EGO-EBIretinoid metabolic process  copper ion binding  proteinaceous extracellular matrix  extracellular space  nucleoplasm  endosome  Golgi lumen  cytosol  plasma membrane  plasma membrane  integral component of plasma membrane  glycosaminoglycan biosynthetic process  glycosaminoglycan catabolic process  axon guidance  Schwann cell differentiation  fibroblast growth factor binding  heparan sulfate proteoglycan catabolic process  glycosaminoglycan metabolic process  anchored component of membrane  myelin assembly  negative regulation of fibroblast growth factor receptor signaling pathway  lysosomal lumen  laminin binding  heparan sulfate proteoglycan binding  membrane raft  membrane raft  leukocyte migration  extracellular exosome  positive regulation of skeletal muscle cell differentiation  
Pathways : KEGGProteoglycans in cancer   
REACTOMEP35052 [protein]
REACTOME PathwaysR-HSA-975634 [pathway]   
NDEx NetworkGPC1
Atlas of Cancer Signalling NetworkGPC1
Wikipedia pathwaysGPC1
Orthology - Evolution
OrthoDB2817
GeneTree (enSembl)ENSG00000063660
Phylogenetic Trees/Animal Genes : TreeFamGPC1
HOVERGENP35052
HOGENOMP35052
Homologs : HomoloGeneGPC1
Homology/Alignments : Family Browser (UCSC)GPC1
Gene fusions - Rearrangements
Fusion : MitelmanGPC1/ANKFN1 [2q37.3/17q22]  
Fusion : MitelmanGPC1/MFN1 [2q37.3/3q26.33]  [t(2;3)(q37;q26)]  
Fusion: TCGAGPC1 2q37.3 ANKFN1 17q22 LUSC
Fusion: TCGAGPC1 2q37.3 MFN1 3q26.33 LUSC
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerGPC1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)GPC1
dbVarGPC1
ClinVarGPC1
1000_GenomesGPC1 
Exome Variant ServerGPC1
ExAC (Exome Aggregation Consortium)GPC1 (select the gene name)
Genetic variants : HAPMAP2817
Genomic Variants (DGV)GPC1 [DGVbeta]
DECIPHERGPC1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisGPC1 
Mutations
ICGC Data PortalGPC1 
TCGA Data PortalGPC1 
Broad Tumor PortalGPC1
OASIS PortalGPC1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICGPC1  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDGPC1
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch GPC1
DgiDB (Drug Gene Interaction Database)GPC1
DoCM (Curated mutations)GPC1 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)GPC1 (select a term)
intoGenGPC1
NCG5 (London)GPC1
Cancer3DGPC1(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM600395   
Orphanet8781   
MedgenGPC1
Genetic Testing Registry GPC1
NextProtP35052 [Medical]
TSGene2817
GENETestsGPC1
Target ValidationGPC1
Huge Navigator GPC1 [HugePedia]
snp3D : Map Gene to Disease2817
BioCentury BCIQGPC1
ClinGenGPC1
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD2817
Chemical/Pharm GKB GenePA28830
Clinical trialGPC1
Miscellaneous
canSAR (ICR)GPC1 (select the gene name)
Probes
Litterature
PubMed49 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineGPC1
EVEXGPC1
GoPubMedGPC1
iHOPGPC1
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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