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P35052

- GPC1_HUMAN

UniProt

P35052 - GPC1_HUMAN

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Protein

Glypican-1

Gene

GPC1

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

Functioni

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.By similarity2 Publications

GO - Molecular functioni

  1. copper ion binding Source: UniProtKB
  2. fibroblast growth factor binding Source: UniProtKB
  3. laminin binding Source: UniProtKB

GO - Biological processi

  1. axon guidance Source: Reactome
  2. carbohydrate metabolic process Source: Reactome
  3. chondroitin sulfate metabolic process Source: Reactome
  4. glycosaminoglycan biosynthetic process Source: Reactome
  5. glycosaminoglycan catabolic process Source: Reactome
  6. glycosaminoglycan metabolic process Source: Reactome
  7. heparan sulfate proteoglycan catabolic process Source: UniProtKB
  8. myelin assembly Source: UniProtKB
  9. negative regulation of fibroblast growth factor receptor signaling pathway Source: UniProtKB
  10. phototransduction, visible light Source: Reactome
  11. positive regulation of skeletal muscle cell differentiation Source: UniProtKB
  12. retinoid metabolic process Source: Reactome
  13. Schwann cell differentiation Source: UniProtKB
  14. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Ligandi

Copper, Zinc

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_19226. Activation of Rac.
REACT_19230. Role of Abl in Robo-Slit signaling.
REACT_19342. Inactivation of Cdc42 and Rac.
REACT_19351. Signaling by Robo receptor.
REACT_24968. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Glypican-1
Cleaved into the following chain:
Gene namesi
Name:GPC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:4449. GPC1.

Subcellular locationi

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.

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. endosome Source: UniProtKB-KW
  3. extracellular space Source: ProtInc
  4. extracellular vesicular exosome Source: UniProt
  5. Golgi lumen Source: Reactome
  6. integral component of plasma membrane Source: ProtInc
  7. lysosomal lumen Source: Reactome
  8. membrane raft Source: UniProtKB
  9. plasma membrane Source: Reactome
  10. proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

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.
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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi79 – 791N → 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. 1 Publication
Mutagenesisi116 – 1161N → 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. 1 Publication

Organism-specific databases

Orphaneti30391. Biliary atresia.
PharmGKBiPA28830.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 530507Glypican-1PRO_0000012295Add
BLAST
Chaini24 – ?Secreted glypican-1PRO_0000333837
Propeptidei531 – 55828Removed in mature formCuratedPRO_0000012296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 681 Publication
Disulfide bondi62 ↔ 2561 Publication
Disulfide bondi69 ↔ 2591 Publication
Glycosylationi79 – 791N-linked (GlcNAc...)2 Publications
Glycosylationi116 – 1161N-linked (GlcNAc...)3 Publications
Disulfide bondi191 ↔ 3431 Publication
Disulfide bondi246 ↔ 2791 Publication
Disulfide bondi268 ↔ 4151 Publication
Disulfide bondi272 ↔ 4011 Publication
Glycosylationi486 – 4861O-linked (Xyl...) (heparan sulfate)Curated
Glycosylationi488 – 4881O-linked (Xyl...) (heparan sulfate)Curated
Glycosylationi490 – 4901O-linked (Xyl...) (heparan sulfate)Curated
Lipidationi530 – 5301GPI-anchor amidated serine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Heparan sulfate, Lipoprotein, Proteoglycan, S-nitrosylation

Proteomic databases

MaxQBiP35052.
PaxDbiP35052.
PRIDEiP35052.

PTM databases

PhosphoSiteiP35052.

Expressioni

Gene expression databases

BgeeiP35052.
CleanExiHS_GPC1.
ExpressionAtlasiP35052. baseline and differential.
GenevestigatoriP35052.

Organism-specific databases

HPAiHPA030571.

Interactioni

Protein-protein interaction databases

BioGridi109079. 6 interactions.
IntActiP35052. 2 interactions.
STRINGi9606.ENSP00000264039.

Structurei

Secondary structure

1
558
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 419
Helixi46 – 483
Helixi56 – 583
Beta strandi60 – 623
Beta strandi64 – 685
Helixi71 – 13060
Helixi132 – 15221
Helixi159 – 17820
Turni201 – 2044
Helixi205 – 23733
Helixi244 – 25411
Helixi256 – 2594
Helixi269 – 27911
Helixi281 – 2844
Helixi287 – 30014
Helixi301 – 3044
Helixi313 – 33018
Turni332 – 3365
Helixi374 – 38916
Helixi392 – 40312
Beta strandi418 – 4225
Beta strandi431 – 4333
Helixi434 – 4363
Beta strandi440 – 4423
Helixi451 – 47121

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ACRX-ray2.55A/B/C/D24-479[»]
4AD7X-ray2.94A/B/C/D24-529[»]
4BWEX-ray2.46A/B/C/D24-479[»]
ProteinModelPortaliP35052.
SMRiP35052. Positions 29-475.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glypican family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG235988.
GeneTreeiENSGT00550000074430.
HOGENOMiHOG000253003.
HOVERGENiHBG003464.
InParanoidiP35052.
KOiK08107.
OrthoDBiEOG761BTG.
PhylomeDBiP35052.
TreeFamiTF105317.

Family and domain databases

InterProiIPR001863. Glypican.
IPR015502. Glypican-1.
IPR019803. Glypican_CS.
[Graphical view]
PANTHERiPTHR10822. PTHR10822. 1 hit.
PTHR10822:SF8. PTHR10822:SF8. 1 hit.
PfamiPF01153. Glypican. 1 hit.
[Graphical view]
PROSITEiPS01207. GLYPICAN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P35052-1) [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
MELRARGWWL LCAAAALVAC ARGDPASKSR SCGEVRQIYG AKGFSLSDVP
60 70 80 90 100
QAEISGEHLR ICPQGYTCCT SEMEENLANR SHAELETALR DSSRVLQAML
110 120 130 140 150
ATQLRSFDDH FQHLLNDSER TLQATFPGAF GELYTQNARA FRDLYSELRL
160 170 180 190 200
YYRGANLHLE ETLAEFWARL LERLFKQLHP QLLLPDDYLD CLGKQAEALR
210 220 230 240 250
PFGEAPRELR LRATRAFVAA RSFVQGLGVA SDVVRKVAQV PLGPECSRAV
260 270 280 290 300
MKLVYCAHCL GVPGARPCPD YCRNVLKGCL ANQADLDAEW RNLLDSMVLI
310 320 330 340 350
TDKFWGTSGV ESVIGSVHTW LAEAINALQD NRDTLTAKVI QGCGNPKVNP
360 370 380 390 400
QGPGPEEKRR RGKLAPRERP PSGTLEKLVS EAKAQLRDVQ DFWISLPGTL
410 420 430 440 450
CSEKMALSTA SDDRCWNGMA RGRYLPEVMG DGLANQINNP EVEVDITKPD
460 470 480 490 500
MTIRQQIMQL KIMTNRLRSA YNGNDVDFQD ASDDGSGSGS GDGCLDDLCS
510 520 530 540 550
RKVSRKSSSS RTPLTHALPG LSEQEGQKTS AASCPQPPTF LLPLLLFLAL

TVARPRWR
Length:558
Mass (Da):61,680
Last modified:March 23, 2010 - v2
Checksum:i16553B56080A83C8
GO
Isoform 2 (identifier: P35052-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:287
Mass (Da):31,931
Checksum:iD986658ECFD5AA92
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti337 – 3371A → D in a breast cancer sample; somatic mutation. 1 Publication
VAR_036044
Natural varianti500 – 5001S → G.2 Publications
Corresponds to variant rs2228331 [ dbSNP | Ensembl ].
VAR_033977

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7272Missing in isoform 2. 1 PublicationVSP_055225Add
BLAST
Alternative sequencei295 – 35965DSMVL…PEEKR → GEPPPARAAWNCLGECTTGG PGGRVVPSLELGPRDLIRDA LTRARSGWCCRVEGPGCLLN VLSDV in isoform 2. 1 PublicationVSP_055226Add
BLAST
Alternative sequencei360 – 558199Missing in isoform 2. 1 PublicationVSP_055227Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2534.1. [P35052-1]
PIRiA36347.
RefSeqiNP_002072.2. NM_002081.2. [P35052-1]
UniGeneiHs.328232.

Genome annotation databases

EnsembliENST00000264039; ENSP00000264039; ENSG00000063660. [P35052-1]
GeneIDi2817.
KEGGihsa:2817.
UCSCiuc002vyw.4. human. [P35052-1]

Polymorphism databases

DMDMi292495012.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS2534.1. [P35052-1 ]
PIRi A36347.
RefSeqi NP_002072.2. NM_002081.2. [P35052-1 ]
UniGenei Hs.328232.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4ACR X-ray 2.55 A/B/C/D 24-479 [» ]
4AD7 X-ray 2.94 A/B/C/D 24-529 [» ]
4BWE X-ray 2.46 A/B/C/D 24-479 [» ]
ProteinModelPortali P35052.
SMRi P35052. Positions 29-475.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109079. 6 interactions.
IntActi P35052. 2 interactions.
STRINGi 9606.ENSP00000264039.

PTM databases

PhosphoSitei P35052.

Polymorphism databases

DMDMi 292495012.

Proteomic databases

MaxQBi P35052.
PaxDbi P35052.
PRIDEi P35052.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264039 ; ENSP00000264039 ; ENSG00000063660 . [P35052-1 ]
GeneIDi 2817.
KEGGi hsa:2817.
UCSCi uc002vyw.4. human. [P35052-1 ]

Organism-specific databases

CTDi 2817.
GeneCardsi GC02P241378.
H-InvDB HIX0002996.
HGNCi HGNC:4449. GPC1.
HPAi HPA030571.
MIMi 600395. gene.
neXtProti NX_P35052.
Orphaneti 30391. Biliary atresia.
PharmGKBi PA28830.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG235988.
GeneTreei ENSGT00550000074430.
HOGENOMi HOG000253003.
HOVERGENi HBG003464.
InParanoidi P35052.
KOi K08107.
OrthoDBi EOG761BTG.
PhylomeDBi P35052.
TreeFami TF105317.

Enzyme and pathway databases

Reactomei REACT_120752. HS-GAG degradation.
REACT_121248. HS-GAG biosynthesis.
REACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.
REACT_19226. Activation of Rac.
REACT_19230. Role of Abl in Robo-Slit signaling.
REACT_19342. Inactivation of Cdc42 and Rac.
REACT_19351. Signaling by Robo receptor.
REACT_24968. Retinoid metabolism and transport.

Miscellaneous databases

GeneWikii Glypican_1.
GenomeRNAii 2817.
NextBioi 11103.
PROi P35052.
SOURCEi Search...

Gene expression databases

Bgeei P35052.
CleanExi HS_GPC1.
ExpressionAtlasi P35052. baseline and differential.
Genevestigatori P35052.

Family and domain databases

InterProi IPR001863. Glypican.
IPR015502. Glypican-1.
IPR019803. Glypican_CS.
[Graphical view ]
PANTHERi PTHR10822. PTHR10822. 1 hit.
PTHR10822:SF8. PTHR10822:SF8. 1 hit.
Pfami PF01153. Glypican. 1 hit.
[Graphical view ]
PROSITEi PS01207. GLYPICAN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-337.

Entry informationi

Entry nameiGPC1_HUMAN
AccessioniPrimary (citable) accession number: P35052
Secondary accession number(s): B3KTD1, Q53QM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: March 23, 2010
Last modified: October 29, 2014
This is version 123 of the entry and version 2 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 2
    Human chromosome 2: 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