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P35052 (GPC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glypican-1

Cleaved into the following chain:

  1. Secreted glypican-1
Gene names
Name:GPC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination By similarity. May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling. Ref.12 Ref.14

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor; Extracellular side. Endosome. Note: S-nitrosylated form recycled in endosomes. Localizes to CAV1-containing vesicles close to the cell surface. Cleavage of heparan sulfate side chains takes place mainly in late endosomes. Associates with both forms of PRNP in lipid rafts. Colocalizes with APP in perinuclear compartments and with CP in intracellular compartments. Associates with fibrillar APP Abeta peptides in lipid rafts in Alzheimer disease brains. Ref.1 Ref.7 Ref.9 Ref.11 Ref.12

Secreted glypican-1: Secretedextracellular space Ref.7 Ref.9 Ref.11 Ref.12.

Post-translational modification

S-nitrosylated in a Cu2+-dependent manner. Nitric acid (NO) is released from the nitrosylated cysteines by ascorbate or by some other reducing agent, in a Cu2+ or Zn2+ dependent manner. This free nitric oxide is then capable of cleaving the heparan sulfate side chains.

N- and O-glycosylated. N-glycosylation is mainly of the complex type containing sialic acid. O-glycosylated with heparan sulfate. The heparan sulfate chains can be cleaved either by the action of heparanase or, degraded by a deaminative process that uses nitric oxide (NO) released from the S-nitrosylated cysteines. This process is triggered by ascorbate, or by some other reducing agent, in a Cu2+- or Zn2+ dependent manner. Cu2+ ions are provided by ceruloproteins such as APP, PRNP or CP which associate with GCP1 in intracellular compartments or lipid rafts. Ref.1 Ref.6 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15

This cell-associated glypican is further processed to give rise to a medium-released species.

Involvement in disease

Associates (via the heparan sulfate side chains) with fibrillar APP-beta amyloid peptides in primitive and classic amyloid plaques and may be involved in the deposition of these senile plaques in the Alzheimer disease (AD) brain. Ref.7 Ref.8

Misprocessing of GPC1 is found in fibroblasts of patients with Niemann-Pick Type C1 disease. This is due to the defective deaminative degradation of heparan sulfate chains. Ref.7 Ref.8

Sequence similarities

Belongs to the glypican family.

Ontologies

Keywords
   Cellular componentCell membrane
Endosome
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   LigandCopper
Zinc
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Heparan sulfate
Lipoprotein
Proteoglycan
S-nitrosylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processSchwann cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

axon guidance

Traceable author statement. Source: Reactome

carbohydrate metabolic process

Traceable author statement. Source: Reactome

chondroitin sulfate metabolic process

Traceable author statement. Source: Reactome

glycosaminoglycan biosynthetic process

Traceable author statement. Source: Reactome

glycosaminoglycan catabolic process

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

heparan sulfate proteoglycan catabolic process

Inferred from direct assay Ref.6. Source: UniProtKB

myelin assembly

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of fibroblast growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

phototransduction, visible light

Traceable author statement. Source: Reactome

positive regulation of skeletal muscle cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

retinoid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

anchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Traceable author statement Ref.1. Source: ProtInc

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708PubMed 23376485. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

lysosomal lumen

Traceable author statement. Source: Reactome

membrane raft

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

proteinaceous extracellular matrix

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncopper ion binding

Inferred from direct assay Ref.6. Source: UniProtKB

fibroblast growth factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

laminin binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35052-1)

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.
Isoform 2 (identifier: P35052-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.
     295-359: DSMVLITDKF...PQGPGPEEKR → GEPPPARAAW...GCLLNVLSDV
     360-558: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.1
Chain24 – 530507Glypican-1
PRO_0000012295
Chain24 – ?Secreted glypican-1PRO_0000333837
Propeptide531 – 55828Removed in mature form Probable
PRO_0000012296

Amino acid modifications

Lipidation5301GPI-anchor amidated serine Probable
Glycosylation791N-linked (GlcNAc...) Ref.13 Ref.15
Glycosylation1161N-linked (GlcNAc...) Ref.1 Ref.13 Ref.15
Glycosylation4861O-linked (Xyl...) (heparan sulfate) Probable
Glycosylation4881O-linked (Xyl...) (heparan sulfate) Probable
Glycosylation4901O-linked (Xyl...) (heparan sulfate) Probable
Disulfide bond32 ↔ 68 Ref.15
Disulfide bond62 ↔ 256 Ref.15
Disulfide bond69 ↔ 259 Ref.15
Disulfide bond191 ↔ 343 Ref.15
Disulfide bond246 ↔ 279 Ref.15
Disulfide bond268 ↔ 415 Ref.15
Disulfide bond272 ↔ 401 Ref.15

Natural variations

Alternative sequence1 – 7272Missing in isoform 2.
VSP_055225
Alternative sequence295 – 35965DSMVL…PEEKR → GEPPPARAAWNCLGECTTGG PGGRVVPSLELGPRDLIRDA LTRARSGWCCRVEGPGCLLN VLSDV in isoform 2.
VSP_055226
Alternative sequence360 – 558199Missing in isoform 2.
VSP_055227
Natural variant3371A → D in a breast cancer sample; somatic mutation. Ref.16
VAR_036044
Natural variant5001S → G. Ref.1 Ref.5
Corresponds to variant rs2228331 [ dbSNP | Ensembl ].
VAR_033977

Experimental info

Mutagenesis791N → Q: Protein yield reduced by half. Protein yield reduced by 90%, abolishes N-glycosylation but no effect on secondary structure; when associated with Q-116. Ref.13
Mutagenesis1161N → Q: No effect on protein yield. Protein yield reduced by 90%, abolishes N-glycosylation but no effect on secondary structure; when associated with Q-79. Ref.13

Secondary structure

................................................ 558
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 23, 2010. Version 2.
Checksum: 16553B56080A83C8

FASTA55861,680
        10         20         30         40         50         60 
MELRARGWWL LCAAAALVAC ARGDPASKSR SCGEVRQIYG AKGFSLSDVP QAEISGEHLR 

        70         80         90        100        110        120 
ICPQGYTCCT SEMEENLANR SHAELETALR DSSRVLQAML ATQLRSFDDH FQHLLNDSER 

       130        140        150        160        170        180 
TLQATFPGAF GELYTQNARA FRDLYSELRL YYRGANLHLE ETLAEFWARL LERLFKQLHP 

       190        200        210        220        230        240 
QLLLPDDYLD CLGKQAEALR PFGEAPRELR LRATRAFVAA RSFVQGLGVA SDVVRKVAQV 

       250        260        270        280        290        300 
PLGPECSRAV MKLVYCAHCL GVPGARPCPD YCRNVLKGCL ANQADLDAEW RNLLDSMVLI 

       310        320        330        340        350        360 
TDKFWGTSGV ESVIGSVHTW LAEAINALQD NRDTLTAKVI QGCGNPKVNP QGPGPEEKRR 

       370        380        390        400        410        420 
RGKLAPRERP PSGTLEKLVS EAKAQLRDVQ DFWISLPGTL CSEKMALSTA SDDRCWNGMA 

       430        440        450        460        470        480 
RGRYLPEVMG DGLANQINNP EVEVDITKPD MTIRQQIMQL KIMTNRLRSA YNGNDVDFQD 

       490        500        510        520        530        540 
ASDDGSGSGS GDGCLDDLCS RKVSRKSSSS RTPLTHALPG LSEQEGQKTS AASCPQPPTF 

       550 
LLPLLLFLAL TVARPRWR 

« Hide

Isoform 2 [UniParc].

Checksum: D986658ECFD5AA92
Show »

FASTA28731,931

References

« Hide 'large scale' references
[1]"Molecular cloning of a phosphatidylinositol-anchored membrane heparan sulfate proteoglycan from human lung fibroblasts."
David G., Lories V., Decock B., Marynen P., Cassiman J.-J., van den Berghe H.
J. Cell Biol. 111:3165-3176(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 24-53; 100-118 AND 298-317, GPI-ANCHOR AT SER-530, GLYCOSYLATION AT ASN-116, VARIANT GLY-500.
Tissue: Lung fibroblast.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain and Tongue.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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), VARIANT GLY-500.
Tissue: Salivary gland.
[6]"Prion, amyloid beta-derived Cu(II) ions, or free Zn(II) ions support S-nitroso-dependent autocleavage of glypican-1 heparan sulfate."
Mani K., Cheng F., Havsmark B., Jonsson M., Belting M., Fransson L.A.
J. Biol. Chem. 278:38956-38965(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: COPPER-BINDING, S-NITROSYLATION, GLYCOSYLATION.
[7]"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 D.H., Makifuchi T., Ihara Y., Tabira T.
FASEB J. 18:1013-1015(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, POSSIBLE ASSOCIATION WITH ALZHEIMER DISEASE.
[8]"Defective nitric oxide-dependent, deaminative cleavage of glypican-1 heparan sulfate in Niemann-Pick C1 fibroblasts."
Mani K., Cheng F., Fransson L.A.
Glycobiology 16:711-718(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: S-NITROSYLATION, ASSOCIATION WITH NIEMANN-PICK TYPE C1 DISEASE.
[9]"Constitutive and vitamin C-induced, NO-catalyzed release of heparan sulfate from recycling glypican-1 in late endosomes."
Mani K., Cheng F., Fransson L.A.
Glycobiology 16:1251-1261(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, S-NITROSYLATION, GLYCOSYLATION.
[10]"Chemical and thermal unfolding of glypican-1: protective effect of heparan sulfate against heat-induced irreversible aggregation."
Svensson G., Linse S., Mani K.
Biochemistry 48:9994-10004(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, ABSENCE OF GLYCOSYLATION AT SER-55.
[11]"S-Nitrosylation of secreted recombinant human glypican-1."
Svensson G., Mani K.
Glycoconj. J. 26:1247-1257(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: S-NITROSYLATION, SUBCELLULAR LOCATION, GLYCOSYLATION.
[12]"Glypican-1 mediates both prion protein lipid raft association and disease isoform formation."
Taylor D.R., Whitehouse I.J., Hooper N.M.
PLoS Pathog. 5:E1000666-E1000666(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]"The structural role of N-linked glycans on human glypican-1."
Svensson G., Hyrenius Wittsten A., Linse S., Mani K.
Biochemistry 50:9377-9387(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-79 AND ASN-116, MUTAGENESIS OF ASN-79 AND ASN-116.
[14]"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 G.D., Svensson G., Multhaup G., Fransson L.A., Mani K.
J. Biol. Chem. 286:27559-27572(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: S-NITROSYLATION, GLYCOSYLATION, FUNCTION.
[15]"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 D.T.
J. Biol. Chem. 287:14040-14051(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), DISULFIDE BONDS, LACK OF GLYCOSYLATION AT SER-55, GLYCOSYLATION AT ASN-79 AND ASN-116.
[16]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-337.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54232 mRNA. Translation: CAA38139.1.
AK095397 mRNA. Translation: BAG53043.1.
AK096638 mRNA. Translation: BAG53345.1.
AC110619 Genomic DNA. Translation: AAY24160.1.
CH471063 Genomic DNA. Translation: EAW71180.1.
CH471063 Genomic DNA. Translation: EAW71183.1.
BC051279 mRNA. Translation: AAH51279.1.
CCDSCCDS2534.1.
PIRA36347.
RefSeqNP_002072.2. NM_002081.2.
UniGeneHs.328232.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4ACRX-ray2.55A/B/C/D24-479[»]
4AD7X-ray2.94A/B/C/D24-529[»]
4BWEX-ray2.46A/B/C/D24-479[»]
ProteinModelPortalP35052.
SMRP35052. Positions 29-475.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109079. 4 interactions.
IntActP35052. 2 interactions.
STRING9606.ENSP00000264039.

PTM databases

PhosphoSiteP35052.

Polymorphism databases

DMDM292495012.

Proteomic databases

MaxQBP35052.
PaxDbP35052.
PRIDEP35052.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264039; ENSP00000264039; ENSG00000063660.
GeneID2817.
KEGGhsa:2817.
UCSCuc002vyw.4. human.

Organism-specific databases

CTD2817.
GeneCardsGC02P241378.
H-InvDBHIX0002996.
HGNCHGNC:4449. GPC1.
HPAHPA030571.
MIM600395. gene.
neXtProtNX_P35052.
Orphanet30391. Biliary atresia.
PharmGKBPA28830.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG235988.
HOGENOMHOG000253003.
HOVERGENHBG003464.
InParanoidP35052.
KOK08107.
OrthoDBEOG761BTG.
PhylomeDBP35052.
TreeFamTF105317.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP35052.
BgeeP35052.
CleanExHS_GPC1.
GenevestigatorP35052.

Family and domain databases

InterProIPR001863. Glypican.
IPR015502. Glypican-1.
IPR019803. Glypican_CS.
[Graphical view]
PANTHERPTHR10822. PTHR10822. 1 hit.
PTHR10822:SF8. PTHR10822:SF8. 1 hit.
PfamPF01153. Glypican. 1 hit.
[Graphical view]
PROSITEPS01207. GLYPICAN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiGlypican_1.
GenomeRNAi2817.
NextBio11103.
PROP35052.
SOURCESearch...

Entry information

Entry nameGPC1_HUMAN
AccessionPrimary (citable) accession number: P35052
Secondary accession number(s): B3KTD1, Q53QM4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: March 23, 2010
Last modified: July 9, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM