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P35052

- GPC1_HUMAN

UniProt

P35052 - GPC1_HUMAN

Protein

Glypican-1

Gene

GPC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (23 Mar 2010)
      Previous versions | rss
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    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

    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-SubCell
    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

    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

    ArrayExpressiP35052.
    BgeeiP35052.
    CleanExiHS_GPC1.
    GenevestigatoriP35052.

    Organism-specific databases

    HPAiHPA030571.

    Interactioni

    Protein-protein interaction databases

    BioGridi109079. 4 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.
    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

    MELRARGWWL LCAAAALVAC ARGDPASKSR SCGEVRQIYG AKGFSLSDVP    50
    QAEISGEHLR ICPQGYTCCT SEMEENLANR SHAELETALR DSSRVLQAML 100
    ATQLRSFDDH FQHLLNDSER TLQATFPGAF GELYTQNARA FRDLYSELRL 150
    YYRGANLHLE ETLAEFWARL LERLFKQLHP QLLLPDDYLD CLGKQAEALR 200
    PFGEAPRELR LRATRAFVAA RSFVQGLGVA SDVVRKVAQV PLGPECSRAV 250
    MKLVYCAHCL GVPGARPCPD YCRNVLKGCL ANQADLDAEW RNLLDSMVLI 300
    TDKFWGTSGV ESVIGSVHTW LAEAINALQD NRDTLTAKVI QGCGNPKVNP 350
    QGPGPEEKRR RGKLAPRERP PSGTLEKLVS EAKAQLRDVQ DFWISLPGTL 400
    CSEKMALSTA SDDRCWNGMA RGRYLPEVMG DGLANQINNP EVEVDITKPD 450
    MTIRQQIMQL KIMTNRLRSA YNGNDVDFQD ASDDGSGSGS GDGCLDDLCS 500
    RKVSRKSSSS RTPLTHALPG LSEQEGQKTS AASCPQPPTF LLPLLLFLAL 550
    TVARPRWR 558
    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.
    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.
    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. 4 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.
    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

    ArrayExpressi P35052.
    Bgeei P35052.
    CleanExi HS_GPC1.
    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

    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 1, 2014
    This is version 122 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