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Protein

Glypican-3

Gene

GPC3

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

Functioni

Cell surface proteoglycan that bears heparan sulfate. Inhibits the dipeptidyl peptidase activity of DPP4. May be involved in the suppression/modulation of growth in the predominantly mesodermal tissues and organs. May play a role in the modulation of IGF2 interactions with its receptor and thereby modulate its function. May regulate growth and tumor predisposition.1 Publication

GO - Molecular functioni

  1. peptidyl-dipeptidase inhibitor activity Source: UniProtKB

GO - Biological processi

  1. anatomical structure morphogenesis Source: ProtInc
  2. anterior/posterior axis specification Source: Ensembl
  3. body morphogenesis Source: Ensembl
  4. bone mineralization Source: Ensembl
  5. branching involved in ureteric bud morphogenesis Source: Ensembl
  6. carbohydrate metabolic process Source: Reactome
  7. cell proliferation involved in metanephros development Source: Ensembl
  8. chondroitin sulfate metabolic process Source: Reactome
  9. coronary vasculature development Source: Ensembl
  10. embryonic hindlimb morphogenesis Source: Ensembl
  11. glycosaminoglycan biosynthetic process Source: Reactome
  12. glycosaminoglycan catabolic process Source: Reactome
  13. glycosaminoglycan metabolic process Source: Reactome
  14. lung development Source: Ensembl
  15. mesenchymal cell proliferation involved in ureteric bud development Source: UniProtKB
  16. mesonephric duct morphogenesis Source: Ensembl
  17. negative regulation of canonical Wnt signaling pathway Source: Ensembl
  18. negative regulation of epithelial cell proliferation Source: Ensembl
  19. negative regulation of growth Source: Ensembl
  20. negative regulation of smoothened signaling pathway Source: Ensembl
  21. osteoclast differentiation Source: Ensembl
  22. pathogenesis Source: Reactome
  23. phototransduction, visible light Source: Reactome
  24. positive regulation of BMP signaling pathway Source: Ensembl
  25. positive regulation of endocytosis Source: Ensembl
  26. positive regulation of glucose import Source: Ensembl
  27. positive regulation of protein catabolic process Source: Ensembl
  28. positive regulation of smoothened signaling pathway Source: Ensembl
  29. positive regulation of Wnt signaling pathway, planar cell polarity pathway Source: Ensembl
  30. retinoid metabolic process Source: Reactome
  31. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor

Enzyme and pathway databases

ReactomeiREACT_120752. HS-GAG degradation.
REACT_121248. HS-GAG biosynthesis.
REACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.
REACT_24968. Retinoid metabolism and transport.
REACT_267741. Defective EXT2 causes exostoses 2.
REACT_267942. Defective EXT1 causes exostoses 1, TRPS2 and CHDS.
REACT_268678. Defective B3GAT3 causes JDSSDHD.
REACT_268749. Defective B4GALT7 causes EDS, progeroid type.
SignaLinkiP51654.

Names & Taxonomyi

Protein namesi
Recommended name:
Glypican-3
Alternative name(s):
GTR2-2
Intestinal protein OCI-5
MXR7
Cleaved into the following chain:
Gene namesi
Name:GPC3
Synonyms:OCI5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:4451. GPC3.

Subcellular locationi

Cell membrane By similarity; Lipid-anchorGPI-anchor By similarity; Extracellular side By similarity

GO - Cellular componenti

  1. anchored component of plasma membrane Source: Ensembl
  2. extracellular space Source: UniProtKB-SubCell
  3. extracellular vesicular exosome Source: UniProtKB
  4. Golgi lumen Source: Reactome
  5. integral component of plasma membrane Source: ProtInc
  6. lysosomal lumen Source: Reactome
  7. plasma membrane Source: Reactome
  8. proteinaceous extracellular matrix Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Simpson-Golabi-Behmel syndrome 1 (SGBS1)1 Publication

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

Disease descriptionA condition characterized by pre- and postnatal overgrowth (gigantism), facial dysmorphism and a variety of inconstant visceral and skeletal malformations. Characteristic dysmorphic features include macrocephaly with coarse, distinctive facies with a large protruding jaw, broad nasal bridge and cleft palate. Cardiac defects are frequent.

See also OMIM:312870
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti296 – 2961W → R in SGBS1. 1 Publication
VAR_021385

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi312870. phenotype.
Orphaneti373. Simpson-Golabi-Behmel syndrome.
PharmGKBiPA28832.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 580Removed in mature formSequence AnalysisPRO_0000012310
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – ?Glypican-3PRO_0000012309
Chaini25 – ?Secreted glypican-3PRO_0000333844

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi418 – 4181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi495 – 4951O-linked (Xyl...) (heparan sulfate)Sequence Analysis
Glycosylationi509 – 5091O-linked (Xyl...) (heparan sulfate)Sequence Analysis

Keywords - PTMi

Glycoprotein, GPI-anchor, Heparan sulfate, Lipoprotein, Proteoglycan

Proteomic databases

MaxQBiP51654.
PaxDbiP51654.
PRIDEiP51654.

PTM databases

PhosphoSiteiP51654.

Expressioni

Tissue specificityi

Highly expressed in lung, liver and kidney.

Gene expression databases

BgeeiP51654.
CleanExiHS_GPC3.
ExpressionAtlasiP51654. baseline and differential.
GenevestigatoriP51654.

Organism-specific databases

HPAiCAB017784.
HPA006316.

Interactioni

Subunit structurei

Interacts with DPP4.1 Publication

Protein-protein interaction databases

BioGridi108983. 7 interactions.
IntActiP51654. 1 interaction.
STRINGi9606.ENSP00000359854.

Structurei

3D structure databases

ProteinModelPortaliP51654.
SMRiP51654. Positions 34-475.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glypican family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG281821.
GeneTreeiENSGT00550000074430.
HOGENOMiHOG000049177.
HOVERGENiHBG005896.
InParanoidiP51654.
KOiK08109.
OMAiCWNGQEL.
OrthoDBiEOG761BTG.
PhylomeDBiP51654.
TreeFamiTF105317.

Family and domain databases

InterProiIPR001863. Glypican.
IPR015501. Glypican-3.
IPR019803. Glypican_CS.
[Graphical view]
PANTHERiPTHR10822. PTHR10822. 1 hit.
PTHR10822:SF4. PTHR10822:SF4. 1 hit.
PfamiPF01153. Glypican. 1 hit.
[Graphical view]
PROSITEiPS01207. GLYPICAN. 1 hit.
[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: P51654-1) [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
MAGTVRTACL VVAMLLSLDF PGQAQPPPPP PDATCHQVRS FFQRLQPGLK
60 70 80 90 100
WVPETPVPGS DLQVCLPKGP TCCSRKMEEK YQLTARLNME QLLQSASMEL
110 120 130 140 150
KFLIIQNAAV FQEAFEIVVR HAKNYTNAMF KNNYPSLTPQ AFEFVGEFFT
160 170 180 190 200
DVSLYILGSD INVDDMVNEL FDSLFPVIYT QLMNPGLPDS ALDINECLRG
210 220 230 240 250
ARRDLKVFGN FPKLIMTQVS KSLQVTRIFL QALNLGIEVI NTTDHLKFSK
260 270 280 290 300
DCGRMLTRMW YCSYCQGLMM VKPCGGYCNV VMQGCMAGVV EIDKYWREYI
310 320 330 340 350
LSLEELVNGM YRIYDMENVL LGLFSTIHDS IQYVQKNAGK LTTTIGKLCA
360 370 380 390 400
HSQQRQYRSA YYPEDLFIDK KVLKVAHVEH EETLSSRRRE LIQKLKSFIS
410 420 430 440 450
FYSALPGYIC SHSPVAENDT LCWNGQELVE RYSQKAARNG MKNQFNLHEL
460 470 480 490 500
KMKGPEPVVS QIIDKLKHIN QLLRTMSMPK GRVLDKNLDE EGFESGDCGD
510 520 530 540 550
DEDECIGGSG DGMIKVKNQL RFLAELAYDL DVDDAPGNSQ QATPKDNEIS
560 570 580
TFHNLGNVHS PLKLLTSMAI SVVCFFFLVH
Length:580
Mass (Da):65,563
Last modified:September 30, 1996 - v1
Checksum:i19485B76D3CE15FC
GO
Isoform 2 (identifier: P51654-2) [UniParc]FASTAAdd to basket

Also known as: Variant B

The sequence of this isoform differs from the canonical sequence as follows:
     59-112: Missing.

Show »
Length:526
Mass (Da):59,475
Checksum:iA0858770AF739C17
GO
Isoform 3 (identifier: P51654-3) [UniParc]FASTAAdd to basket

Also known as: Variant C

The sequence of this isoform differs from the canonical sequence as follows:
     344-344: T → TETEKKIWHFKYPIFFLCIGLDLQ

Show »
Length:603
Mass (Da):68,414
Checksum:i1930C0382E91AF60
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti296 – 2961W → R in SGBS1. 1 Publication
VAR_021385
Natural varianti429 – 4291V → M.1 Publication
Corresponds to variant rs413112608 [ dbSNP | Ensembl ].
VAR_069139

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei59 – 11254Missing in isoform 2. 1 PublicationVSP_046117Add
BLAST
Alternative sequencei344 – 3441T → TETEKKIWHFKYPIFFLCIG LDLQ in isoform 3. 1 PublicationVSP_046703

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50410 mRNA. Translation: AAA93471.1.
L47124 Genomic DNA. Translation: AAA98131.1.
L47125 mRNA. Translation: AAA98132.1.
L47176 mRNA. Translation: AAB58806.1.
Z37987 mRNA. Translation: CAA86069.1.
DQ349136 mRNA. Translation: ABC72125.1.
DQ349138 mRNA. Translation: ABC72127.1.
AL008712
, AC002420, AF003529, AL009174, Z99570 Genomic DNA. Translation: CAI43110.1.
AL009174
, AC002420, AF003529, AL008712, Z99570 Genomic DNA. Translation: CAI42761.1.
Z99570
, AC002420, AF003529, AL008712, AL009174 Genomic DNA. Translation: CAI42277.1.
AL034401 Genomic DNA. No translation available.
AL662851 Genomic DNA. No translation available.
Z97196 Genomic DNA. No translation available.
CH471107 Genomic DNA. Translation: EAX11771.1.
AF003529 Genomic DNA. Translation: AAB87062.1.
CCDSiCCDS14638.1. [P51654-1]
CCDS55496.1. [P51654-3]
RefSeqiNP_001158089.1. NM_001164617.1. [P51654-3]
NP_001158091.1. NM_001164619.1. [P51654-2]
NP_004475.1. NM_004484.3. [P51654-1]
UniGeneiHs.644108.

Genome annotation databases

EnsembliENST00000370818; ENSP00000359854; ENSG00000147257. [P51654-1]
ENST00000394299; ENSP00000377836; ENSG00000147257. [P51654-3]
GeneIDi2719.
KEGGihsa:2719.
UCSCiuc004exe.2. human. [P51654-1]
uc010nro.2. human.

Polymorphism databases

DMDMi1708022.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50410 mRNA. Translation: AAA93471.1.
L47124 Genomic DNA. Translation: AAA98131.1.
L47125 mRNA. Translation: AAA98132.1.
L47176 mRNA. Translation: AAB58806.1.
Z37987 mRNA. Translation: CAA86069.1.
DQ349136 mRNA. Translation: ABC72125.1.
DQ349138 mRNA. Translation: ABC72127.1.
AL008712
, AC002420, AF003529, AL009174, Z99570 Genomic DNA. Translation: CAI43110.1.
AL009174
, AC002420, AF003529, AL008712, Z99570 Genomic DNA. Translation: CAI42761.1.
Z99570
, AC002420, AF003529, AL008712, AL009174 Genomic DNA. Translation: CAI42277.1.
AL034401 Genomic DNA. No translation available.
AL662851 Genomic DNA. No translation available.
Z97196 Genomic DNA. No translation available.
CH471107 Genomic DNA. Translation: EAX11771.1.
AF003529 Genomic DNA. Translation: AAB87062.1.
CCDSiCCDS14638.1. [P51654-1]
CCDS55496.1. [P51654-3]
RefSeqiNP_001158089.1. NM_001164617.1. [P51654-3]
NP_001158091.1. NM_001164619.1. [P51654-2]
NP_004475.1. NM_004484.3. [P51654-1]
UniGeneiHs.644108.

3D structure databases

ProteinModelPortaliP51654.
SMRiP51654. Positions 34-475.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108983. 7 interactions.
IntActiP51654. 1 interaction.
STRINGi9606.ENSP00000359854.

PTM databases

PhosphoSiteiP51654.

Polymorphism databases

DMDMi1708022.

Proteomic databases

MaxQBiP51654.
PaxDbiP51654.
PRIDEiP51654.

Protocols and materials databases

DNASUi2719.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370818; ENSP00000359854; ENSG00000147257. [P51654-1]
ENST00000394299; ENSP00000377836; ENSG00000147257. [P51654-3]
GeneIDi2719.
KEGGihsa:2719.
UCSCiuc004exe.2. human. [P51654-1]
uc010nro.2. human.

Organism-specific databases

CTDi2719.
GeneCardsiGC0XM132669.
GeneReviewsiGPC3.
HGNCiHGNC:4451. GPC3.
HPAiCAB017784.
HPA006316.
MIMi300037. gene.
312870. phenotype.
neXtProtiNX_P51654.
Orphaneti373. Simpson-Golabi-Behmel syndrome.
PharmGKBiPA28832.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG281821.
GeneTreeiENSGT00550000074430.
HOGENOMiHOG000049177.
HOVERGENiHBG005896.
InParanoidiP51654.
KOiK08109.
OMAiCWNGQEL.
OrthoDBiEOG761BTG.
PhylomeDBiP51654.
TreeFamiTF105317.

Enzyme and pathway databases

ReactomeiREACT_120752. HS-GAG degradation.
REACT_121248. HS-GAG biosynthesis.
REACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.
REACT_24968. Retinoid metabolism and transport.
REACT_267741. Defective EXT2 causes exostoses 2.
REACT_267942. Defective EXT1 causes exostoses 1, TRPS2 and CHDS.
REACT_268678. Defective B3GAT3 causes JDSSDHD.
REACT_268749. Defective B4GALT7 causes EDS, progeroid type.
SignaLinkiP51654.

Miscellaneous databases

ChiTaRSiGPC3. human.
GeneWikiiGlypican_3.
GenomeRNAii2719.
NextBioi10734.
PROiP51654.
SOURCEiSearch...

Gene expression databases

BgeeiP51654.
CleanExiHS_GPC3.
ExpressionAtlasiP51654. baseline and differential.
GenevestigatoriP51654.

Family and domain databases

InterProiIPR001863. Glypican.
IPR015501. Glypican-3.
IPR019803. Glypican_CS.
[Graphical view]
PANTHERiPTHR10822. PTHR10822. 1 hit.
PTHR10822:SF4. PTHR10822:SF4. 1 hit.
PfamiPF01153. Glypican. 1 hit.
[Graphical view]
PROSITEiPS01207. GLYPICAN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mapping of the Simpson-Golabi-Behmel overgrowth syndrome gene (GPC3) to chromosome X in human and rat by fluorescence in situ hybridization."
    Shen T., Sonoda G., Hamid J., Li M., Filmus J., Buick R.N., Testa J.R.
    Mamm. Genome 8:72-72(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Mutations in GPC3, a glypican gene, cause the Simpson-Golabi-Behmel overgrowth syndrome."
    Pilia G., Hughes-Benzie R.M., Mackenzie A., Baybayan P., Chen E.Y., Huber R., Neri G., Cao A., Forabosco A., Schlessinger D.
    Nat. Genet. 12:241-247(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), DISEASE.
    Tissue: Embryo.
  3. "Cloning and characterization of human cDNAs encoding a protein with high homology to rat intestinal development protein OCI-5."
    Lage H., Dietel M.
    Gene 188:151-156(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Expression of the Glypican-3 protein in hepatoma cells."
    Grozdanov P.N., Yovchev M.I., Dabeva M.D.
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), VARIANT MET-429.
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "Analysis of exon/intron structure and 400 kb of genomic sequence surrounding the 5'-promoter and 3'-terminal ends of the human glypican 3 (GPC3) gene."
    Huber R., Crisponi L., Mazzarella R., Chen C.N., Su Y., Shizuya H., Chen E.Y., Cao A., Pilia G.
    Genomics 45:48-58(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
  8. "The Simpson-Golabi-Behmel syndrome causative glypican-3, binds to and inhibits the dipeptidyl peptidase activity of CD26."
    Davoodi J., Kelly J., Gendron N.H., MacKenzie A.E.
    Proteomics 7:2300-2310(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DPP4.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Mutational analysis of the GPC3/GPC4 glypican gene cluster on Xq26 in patients with Simpson-Golabi-Behmel syndrome: identification of loss-of-function mutations in the GPC3 gene."
    Veugelers M., Cat B.D., Muyldermans S.Y., Reekmans G., Delande N., Frints S., Legius E., Fryns J.-P., Schrander-Stumpel C., Weidle B., Magdalena N., David G.
    Hum. Mol. Genet. 9:1321-1328(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SGBS1 ARG-296.

Entry informationi

Entry nameiGPC3_HUMAN
AccessioniPrimary (citable) accession number: P51654
Secondary accession number(s): C9JLE3
, G3V1R0, Q2L880, Q2L882
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1996
Last sequence update: September 30, 1996
Last modified: March 31, 2015
This is version 140 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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

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.