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P98160

- PGBM_HUMAN

UniProt

P98160 - PGBM_HUMAN

Protein

Basement membrane-specific heparan sulfate proteoglycan core protein

Gene

HSPG2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 4 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Integral component of basement membranes. Component of the glomerular basement membrane (GBM), responsible for the fixed negative electrostatic membrane charge, and which provides a barrier which is both size- and charge-selective. It serves as an attachment substrate for cells. Plays essential roles in vascularization. Critical for normal heart development and for regulating the vascular response to injury. Also required for avascular cartilage development.
    Endorepellin in an anti-angiogenic and anti-tumor peptide that inhibits endothelial cell migration, collagen-induced endothelial tube morphogenesis and blood vessel growth in the chorioallantoic membrane. Blocks endothelial cell adhesion to fibronectin and type I collagen. Anti-tumor agent in neovascularization. Interaction with its ligand, integrin alpha2/beta1, is required for the anti-angiogenic properties. Evokes a reduction in phosphorylation of receptor tyrosine kinases via alpha2/beta1 integrin-mediated activation of the tyrosine phosphatase, PTPN6.
    The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei4196 – 41972Cleavage; by BMP1
    Metal bindingi4258 – 42581Calcium
    Metal bindingi4275 – 42751Calcium; via carbonyl oxygen
    Metal bindingi4325 – 43251Calcium; via carbonyl oxygen
    Metal bindingi4327 – 43271Calcium

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein C-terminus binding Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. brain development Source: Ensembl
    3. carbohydrate metabolic process Source: Reactome
    4. cardiac muscle tissue development Source: Ensembl
    5. cartilage development involved in endochondral bone morphogenesis Source: Ensembl
    6. chondrocyte differentiation Source: Ensembl
    7. chondroitin sulfate metabolic process Source: Reactome
    8. embryonic skeletal system morphogenesis Source: Ensembl
    9. endochondral ossification Source: Ensembl
    10. extracellular matrix disassembly Source: Reactome
    11. extracellular matrix organization Source: Reactome
    12. glycosaminoglycan biosynthetic process Source: Reactome
    13. glycosaminoglycan catabolic process Source: Reactome
    14. glycosaminoglycan metabolic process Source: Reactome
    15. lipoprotein metabolic process Source: Reactome
    16. phototransduction, visible light Source: Reactome
    17. protein localization Source: Ensembl
    18. retinoid metabolic process Source: Reactome
    19. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    Angiogenesis

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_120752. HS-GAG degradation.
    REACT_121248. HS-GAG biosynthesis.
    REACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.
    REACT_13552. Integrin cell surface interactions.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_169262. Laminin interactions.
    REACT_24968. Retinoid metabolism and transport.
    REACT_6841. Chylomicron-mediated lipid transport.
    REACT_75925. Amyloids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Basement membrane-specific heparan sulfate proteoglycan core protein
    Short name:
    HSPG
    Alternative name(s):
    Perlecan
    Short name:
    PLC
    Cleaved into the following 2 chains:
    Gene namesi
    Name:HSPG2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:5273. HSPG2.

    Subcellular locationi

    GO - Cellular componenti

    1. basal lamina Source: Ensembl
    2. extracellular region Source: Reactome
    3. extracellular space Source: BHF-UCL
    4. extracellular vesicular exosome Source: UniProtKB
    5. Golgi lumen Source: Reactome
    6. lysosomal lumen Source: Reactome
    7. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Schwartz-Jampel syndrome (SJS1) [MIM:255800]: Rare autosomal recessive disorder characterized by permanent myotonia (prolonged failure of muscle relaxation) and skeletal dysplasia, resulting in reduced stature, kyphoscoliosis, bowing of the diaphyses and irregular epiphyses.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1532 – 15321C → Y in SJS1. 1 Publication
    VAR_014122
    Dyssegmental dysplasia Silverman-Handmaker type (DDSH) [MIM:224410]: The dyssegmental dysplasias are rare, autosomal recessive skeletal dysplasias with anisospondyly and micromelia. There are two recognized types: the severe, lethal DDSH and the milder Rolland-Desbuquois form. Individuals with DDSH also have a flat face, micrognathia, cleft palate and reduced joint mobility, and frequently have an encephalocoele. The endochondral growth plate is short, the calcospherites (which are spherical calcium-phosphorus crystals produced by hypertrophic chondrocytes) are unfused, and there is mucoid degeneration of the resting cartilage.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi4197 – 41971D → I: Abolishes BMP1-mediated cleavage of endorepellin. 1 Publication
    Mutagenesisi4258 – 42581D → A: Retains proper folding. Reduced calcium ion binding. 1 Publication
    Mutagenesisi4327 – 43271N → A: Retains proper folding. Reduced calcium ion binding. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi224410. phenotype.
    255800. phenotype.
    Orphaneti1865. Dyssegmental dysplasia, Silverman-Handmaker type.
    800. Schwartz-Jampel syndrome.
    PharmGKBiPA29537.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 43914370Basement membrane-specific heparan sulfate proteoglycan core proteinPRO_0000026696Add
    BLAST
    Chaini3687 – 4391705EndorepellinPRO_0000391621Add
    BLAST
    Chaini4197 – 4391195LG3 peptidePRO_0000391622Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi42 – 421O-linked (GalNAc...)2 Publications
    Glycosylationi65 – 651O-linked (Xyl...) (heparan sulfate)Sequence Analysis
    Glycosylationi71 – 711O-linked (Xyl...) (heparan sulfate)Sequence Analysis
    Glycosylationi76 – 761O-linked (Xyl...) (heparan sulfate)Sequence Analysis
    Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi199 ↔ 212By similarity
    Disulfide bondi206 ↔ 225By similarity
    Disulfide bondi219 ↔ 234By similarity
    Disulfide bondi285 ↔ 297By similarity
    Disulfide bondi292 ↔ 310By similarity
    Disulfide bondi304 ↔ 319By similarity
    Disulfide bondi325 ↔ 337By similarity
    Disulfide bondi332 ↔ 350By similarity
    Disulfide bondi344 ↔ 359By similarity
    Disulfide bondi368 ↔ 381By similarity
    Disulfide bondi375 ↔ 394By similarity
    Disulfide bondi388 ↔ 403By similarity
    Glycosylationi554 – 5541N-linked (GlcNAc...)2 Publications
    Disulfide bondi764 ↔ 773By similarity
    Disulfide bondi766 ↔ 780By similarity
    Disulfide bondi783 ↔ 792By similarity
    Disulfide bondi795 ↔ 811By similarity
    Disulfide bondi814 ↔ 829By similarity
    Disulfide bondi816 ↔ 839By similarity
    Disulfide bondi842 ↔ 851By similarity
    Disulfide bondi854 ↔ 869By similarity
    Disulfide bondi879 ↔ 892By similarity
    Disulfide bondi894 ↔ 903By similarity
    Disulfide bondi906 ↔ 921By similarity
    Disulfide bondi1159 ↔ 1168By similarity
    Disulfide bondi1161 ↔ 1175By similarity
    Disulfide bondi1178 ↔ 1187By similarity
    Disulfide bondi1190 ↔ 1206By similarity
    Disulfide bondi1209 ↔ 1224By similarity
    Disulfide bondi1211 ↔ 1234By similarity
    Disulfide bondi1237 ↔ 1246By similarity
    Disulfide bondi1249 ↔ 1263By similarity
    Disulfide bondi1275 ↔ 1287By similarity
    Disulfide bondi1277 ↔ 1293By similarity
    Disulfide bondi1295 ↔ 1304By similarity
    Disulfide bondi1307 ↔ 1322By similarity
    Disulfide bondi1563 ↔ 1572By similarity
    Disulfide bondi1565 ↔ 1579By similarity
    Disulfide bondi1582 ↔ 1591By similarity
    Disulfide bondi1594 ↔ 1610By similarity
    Disulfide bondi1613 ↔ 1628By similarity
    Disulfide bondi1615 ↔ 1638By similarity
    Disulfide bondi1641 ↔ 1650By similarity
    Disulfide bondi1653 ↔ 1668By similarity
    Glycosylationi1755 – 17551N-linked (GlcNAc...)3 Publications
    Glycosylationi2121 – 21211N-linked (GlcNAc...)2 Publications
    Glycosylationi2995 – 29951O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Glycosylationi3072 – 30721N-linked (GlcNAc...)2 Publications
    Glycosylationi3105 – 31051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3279 – 32791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3780 – 37801N-linked (GlcNAc...)2 Publications
    Disulfide bondi3819 ↔ 3845By similarity
    Glycosylationi3836 – 38361N-linked (GlcNAc...)2 Publications
    Disulfide bondi3848 ↔ 3859By similarity
    Disulfide bondi3853 ↔ 3869By similarity
    Disulfide bondi3871 ↔ 3880By similarity
    Disulfide bondi3888 ↔ 3899By similarity
    Disulfide bondi3893 ↔ 3910By similarity
    Disulfide bondi3912 ↔ 3921By similarity
    Glycosylationi3933 – 39331O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Glycosylationi4068 – 40681N-linked (GlcNAc...)2 Publications
    Disulfide bondi4076 ↔ 4102By similarity
    Disulfide bondi4108 ↔ 4119By similarity
    Disulfide bondi4113 ↔ 4129By similarity
    Disulfide bondi4131 ↔ 4140By similarity
    Disulfide bondi4147 ↔ 4159By similarity
    Disulfide bondi4153 ↔ 4164By similarity
    Disulfide bondi4166 ↔ 4175By similarity
    Glycosylationi4179 – 41791O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
    Disulfide bondi4355 ↔ 43891 Publication

    Post-translational modificationi

    Proteolytic processing produces the C-terminal angiogenic peptide, endorepellin. This peptide can be further processed to produce the LG3 peptide.2 Publications
    N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. Perlecan contains three heparan sulfate chains. The LG3 peptide contains at least three and up to five potential O-glycosylation sites but no N-glycosylation.5 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Heparan sulfate, Proteoglycan

    Proteomic databases

    MaxQBiP98160.
    PaxDbiP98160.
    PRIDEiP98160.

    2D gel databases

    DOSAC-COBS-2DPAGEP98160.

    PTM databases

    PhosphoSiteiP98160.

    Expressioni

    Tissue specificityi

    Found in the basement membranes.

    Gene expression databases

    ArrayExpressiP98160.
    BgeeiP98160.
    CleanExiHS_HSPG2.
    GenevestigatoriP98160.

    Organism-specific databases

    HPAiCAB009820.
    CAB020718.
    HPA018892.

    Interactioni

    Subunit structurei

    Purified perlecan has a strong tendency to aggregate in dimers or stellate structures. It interacts with other basement membrane components such as laminin, prolargin and collagen type IV. Interacts with COL13A1, FGFBP1 and VWA1. Interacts (via C-terminus) with ECM1 (via C-terminus).3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KDRP359684EBI-947664,EBI-1005487

    Protein-protein interaction databases

    BioGridi109571. 17 interactions.
    IntActiP98160. 10 interactions.
    MINTiMINT-123304.
    STRINGi9606.ENSP00000363827.

    Structurei

    Secondary structure

    1
    4391
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni4199 – 42024
    Beta strandi4203 – 421412
    Helixi4216 – 42194
    Beta strandi4228 – 42369
    Beta strandi4239 – 42468
    Beta strandi4259 – 42657
    Beta strandi4268 – 42747
    Beta strandi4279 – 42835
    Beta strandi4290 – 42923
    Beta strandi4294 – 43018
    Beta strandi4304 – 43096
    Beta strandi4315 – 43184
    Beta strandi4320 – 43223
    Beta strandi4332 – 43354
    Helixi4340 – 43434
    Turni4344 – 43463
    Beta strandi4353 – 436311
    Beta strandi4366 – 43683
    Turni4376 – 43783
    Beta strandi4381 – 43888

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3SH4X-ray1.50A4197-4391[»]
    3SH5X-ray2.80A4197-4391[»]
    ProteinModelPortaliP98160.
    SMRiP98160. Positions 1770-1858, 4197-4391.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini80 – 191112SEAPROSITE-ProRule annotationAdd
    BLAST
    Domaini198 – 23538LDL-receptor class A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini284 – 32037LDL-receptor class A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini324 – 36037LDL-receptor class A 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini367 – 40438LDL-receptor class A 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini405 – 504100Ig-like C2-type 1Add
    BLAST
    Domaini521 – 53010Laminin EGF-like 1; first partPROSITE-ProRule annotation
    Domaini538 – 730193Laminin IV type A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini731 – 76333Laminin EGF-like 1; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini764 – 81350Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini814 – 87158Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini879 – 92345Laminin EGF-like 4; truncatedPROSITE-ProRule annotationAdd
    BLAST
    Domaini924 – 93310Laminin EGF-like 5; first partPROSITE-ProRule annotation
    Domaini941 – 1125185Laminin IV type A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1126 – 115833Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini1159 – 120850Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1209 – 126557Laminin EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1275 – 132450Laminin EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1325 – 133410Laminin EGF-like 9; first partPROSITE-ProRule annotation
    Domaini1344 – 1529186Laminin IV type A 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1530 – 156233Laminin EGF-like 9; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini1563 – 161250Laminin EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1613 – 167058Laminin EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1677 – 177195Ig-like C2-type 2Add
    BLAST
    Domaini1772 – 186594Ig-like C2-type 3Add
    BLAST
    Domaini1866 – 195590Ig-like C2-type 4Add
    BLAST
    Domaini1956 – 205196Ig-like C2-type 5Add
    BLAST
    Domaini2052 – 2151100Ig-like C2-type 6Add
    BLAST
    Domaini2152 – 224493Ig-like C2-type 7Add
    BLAST
    Domaini2245 – 234096Ig-like C2-type 8Add
    BLAST
    Domaini2341 – 243696Ig-like C2-type 9Add
    BLAST
    Domaini2437 – 253397Ig-like C2-type 10Add
    BLAST
    Domaini2534 – 262996Ig-like C2-type 11Add
    BLAST
    Domaini2630 – 272697Ig-like C2-type 12Add
    BLAST
    Domaini2727 – 2826100Ig-like C2-type 13Add
    BLAST
    Domaini2827 – 292498Ig-like C2-type 14Add
    BLAST
    Domaini2925 – 302197Ig-like C2-type 15Add
    BLAST
    Domaini3022 – 311291Ig-like C2-type 16Add
    BLAST
    Domaini3113 – 321199Ig-like C2-type 17Add
    BLAST
    Domaini3212 – 329887Ig-like C2-type 18Add
    BLAST
    Domaini3299 – 3399101Ig-like C2-type 19Add
    BLAST
    Domaini3400 – 348889Ig-like C2-type 20Add
    BLAST
    Domaini3489 – 357486Ig-like C2-type 21Add
    BLAST
    Domaini3575 – 366288Ig-like C2-type 22Add
    BLAST
    Domaini3663 – 3843181Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini3844 – 388138EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini3884 – 392239EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini3928 – 4103176Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini4104 – 414138EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini4143 – 417634EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini4201 – 4389189Laminin G-like 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni4149 – 41513Mediates motor neuron attachmentSequence Analysis
    Regioni4299 – 43013Mediates motor neuron attachmentSequence Analysis

    Sequence similaritiesi

    Contains 4 EGF-like domains.PROSITE-ProRule annotation
    Contains 11 laminin EGF-like domains.PROSITE-ProRule annotation
    Contains 3 laminin G-like domains.PROSITE-ProRule annotation
    Contains 3 laminin IV type A domains.PROSITE-ProRule annotation
    Contains 4 LDL-receptor class A domains.PROSITE-ProRule annotation
    Contains 1 SEA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Immunoglobulin domain, Laminin EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG258321.
    HOGENOMiHOG000049276.
    HOVERGENiHBG008174.
    InParanoidiP98160.
    KOiK06255.
    OMAiRQCTSSS.
    OrthoDBiEOG7BGHJZ.
    PhylomeDBiP98160.
    TreeFamiTF326548.

    Family and domain databases

    Gene3Di2.60.120.200. 3 hits.
    2.60.40.10. 22 hits.
    4.10.400.10. 4 hits.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR002049. EGF_laminin.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR018031. Laminin_B_subgr.
    IPR000034. Laminin_B_type_IV.
    IPR001791. Laminin_G.
    IPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR000082. SEA_dom.
    [Graphical view]
    PfamiPF00008. EGF. 2 hits.
    PF07679. I-set. 19 hits.
    PF00052. Laminin_B. 3 hits.
    PF00053. Laminin_EGF. 9 hits.
    PF00054. Laminin_G_1. 1 hit.
    PF02210. Laminin_G_2. 2 hits.
    PF00057. Ldl_recept_a. 4 hits.
    [Graphical view]
    PRINTSiPR00261. LDLRECEPTOR.
    SMARTiSM00181. EGF. 4 hits.
    SM00180. EGF_Lam. 8 hits.
    SM00408. IGc2. 22 hits.
    SM00281. LamB. 3 hits.
    SM00282. LamG. 3 hits.
    SM00192. LDLa. 4 hits.
    SM00200. SEA. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 3 hits.
    SSF57424. SSF57424. 4 hits.
    PROSITEiPS00022. EGF_1. 9 hits.
    PS01186. EGF_2. 6 hits.
    PS50026. EGF_3. 4 hits.
    PS01248. EGF_LAM_1. 11 hits.
    PS50027. EGF_LAM_2. 8 hits.
    PS50835. IG_LIKE. 22 hits.
    PS50025. LAM_G_DOMAIN. 3 hits.
    PS51115. LAMININ_IVA. 3 hits.
    PS01209. LDLRA_1. 4 hits.
    PS50068. LDLRA_2. 4 hits.
    PS50024. SEA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P98160-1 [UniParc]FASTAAdd to Basket

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    MGWRAAGALL LALLLHGRLL AVTHGLRAYD GLSLPEDIET VTASQMRWTH     50
    SYLSDDEDML ADSISGDDLG SGDLGSGDFQ MVYFRALVNF TRSIEYSPQL 100
    EDAGSREFRE VSEAVVDTLE SEYLKIPGDQ VVSVVFIKEL DGWVFVELDV 150
    GSEGNADGAQ IQEMLLRVIS SGSVASYVTS PQGFQFRRLG TVPQFPRACT 200
    EAEFACHSYN ECVALEYRCD RRPDCRDMSD ELNCEEPVLG ISPTFSLLVE 250
    TTSLPPRPET TIMRQPPVTH APQPLLPGSV RPLPCGPQEA ACRNGHCIPR 300
    DYLCDGQEDC EDGSDELDCG PPPPCEPNEF PCGNGHCALK LWRCDGDFDC 350
    EDRTDEANCP TKRPEEVCGP TQFRCVSTNM CIPASFHCDE ESDCPDRSDE 400
    FGCMPPQVVT PPRESIQASR GQTVTFTCVA IGVPTPIINW RLNWGHIPSH 450
    PRVTVTSEGG RGTLIIRDVK ESDQGAYTCE AMNARGMVFG IPDGVLELVP 500
    QRGPCPDGHF YLEHSAACLP CFCFGITSVC QSTRRFRDQI RLRFDQPDDF 550
    KGVNVTMPAQ PGTPPLSSTQ LQIDPSLHEF QLVDLSRRFL VHDSFWALPE 600
    QFLGNKVDSY GGSLRYNVRY ELARGMLEPV QRPDVVLMGA GYRLLSRGHT 650
    PTQPGALNQR QVQFSEEHWV HESGRPVQRA ELLQVLQSLE AVLIQTVYNT 700
    KMASVGLSDI AMDTTVTHAT SHGRAHSVEE CRCPIGYSGL SCESCDAHFT 750
    RVPGGPYLGT CSGCNCNGHA SSCDPVYGHC LNCQHNTEGP QCNKCKAGFF 800
    GDAMKATATS CRPCPCPYID ASRRFSDTCF LDTDGQATCD ACAPGYTGRR 850
    CESCAPGYEG NPIQPGGKCR PVNQEIVRCD ERGSMGTSGE ACRCKNNVVG 900
    RLCNECADGS FHLSTRNPDG CLKCFCMGVS RHCTSSSWSR AQLHGASEEP 950
    GHFSLTNAAS THTTNEGIFS PTPGELGFSS FHRLLSGPYF WSLPSRFLGD 1000
    KVTSYGGELR FTVTQRSQPG STPLHGQPLV VLQGNNIILE HHVAQEPSPG 1050
    QPSTFIVPFR EQAWQRPDGQ PATREHLLMA LAGIDTLLIR ASYAQQPAES 1100
    RVSGISMDVA VPEETGQDPA LEVEQCSCPP GYRGPSCQDC DTGYTRTPSG 1150
    LYLGTCERCS CHGHSEACEP ETGACQGCQH HTEGPRCEQC QPGYYGDAQR 1200
    GTPQDCQLCP CYGDPAAGQA AHTCFLDTDG HPTCDACSPG HSGRHCERCA 1250
    PGYYGNPSQG QPCQRDSQVP GPIGCNCDPQ GSVSSQCDAA GQCQCKAQVE 1300
    GLTCSHCRPH HFHLSASNPD GCLPCFCMGI TQQCASSAYT RHLISTHFAP 1350
    GDFQGFALVN PQRNSRLTGE FTVEPVPEGA QLSFGNFAQL GHESFYWQLP 1400
    ETYQGDKVAA YGGKLRYTLS YTAGPQGSPL SDPDVQITGN NIMLVASQPA 1450
    LQGPERRSYE IMFREEFWRR PDGQPATREH LLMALADLDE LLIRATFSSV 1500
    PLAASISAVS LEVAQPGPSN RPRALEVEEC RCPPGYIGLS CQDCAPGYTR 1550
    TGSGLYLGHC ELCECNGHSD LCHPETGACS QCQHNAAGEF CELCAPGYYG 1600
    DATAGTPEDC QPCACPLTNP ENMFSRTCES LGAGGYRCTA CEPGYTGQYC 1650
    EQCGPGYVGN PSVQGGQCLP ETNQAPLVVE VHPARSIVPQ GGSHSLRCQV 1700
    SGSPPHYFYW SREDGRPVPS GTQQRHQGSE LHFPSVQPSD AGVYICTCRN 1750
    LHQSNTSRAE LLVTEAPSKP ITVTVEEQRS QSVRPGADVT FICTAKSKSP 1800
    AYTLVWTRLH NGKLPTRAMD FNGILTIRNV QLSDAGTYVC TGSNMFAMDQ 1850
    GTATLHVQAS GTLSAPVVSI HPPQLTVQPG QLAEFRCSAT GSPTPTLEWT 1900
    GGPGGQLPAK AQIHGGILRL PAVEPTDQAQ YLCRAHSSAG QQVARAVLHV 1950
    HGGGGPRVQV SPERTQVHAG RTVRLYCRAA GVPSATITWR KEGGSLPPQA 2000
    RSERTDIATL LIPAITTADA GFYLCVATSP AGTAQARIQV VVLSASDASP 2050
    PPVKIESSSP SVTEGQTLDL NCVVAGSAHA QVTWYRRGGS LPPHTQVHGS 2100
    RLRLPQVSPA DSGEYVCRVE NGSGPKEASI TVSVLHGTHS GPSYTPVPGS 2150
    TRPIRIEPSS SHVAEGQTLD LNCVVPGQAH AQVTWHKRGG SLPARHQTHG 2200
    SLLRLHQVTP ADSGEYVCHV VGTSGPLEAS VLVTIEASVI PGPIPPVRIE 2250
    SSSSTVAEGQ TLDLSCVVAG QAHAQVTWYK RGGSLPARHQ VRGSRLYIFQ 2300
    ASPADAGQYV CRASNGMEAS ITVTVTGTQG ANLAYPAGST QPIRIEPSSS 2350
    QVAEGQTLDL NCVVPGQSHA QVTWHKRGGS LPVRHQTHGS LLRLYQASPA 2400
    DSGEYVCRVL GSSVPLEASV LVTIEPAGSV PALGVTPTVR IESSSSQVAE 2450
    GQTLDLNCLV AGQAHAQVTW HKRGGSLPAR HQVHGSRLRL LQVTPADSGE 2500
    YVCRVVGSSG TQEASVLVTI QQRLSGSHSQ GVAYPVRIES SSASLANGHT 2550
    LDLNCLVASQ APHTITWYKR GGSLPSRHQI VGSRLRIPQV TPADSGEYVC 2600
    HVSNGAGSRE TSLIVTIQGS GSSHVPSVSP PIRIESSSPT VVEGQTLDLN 2650
    CVVARQPQAI ITWYKRGGSL PSRHQTHGSH LRLHQMSVAD SGEYVCRANN 2700
    NIDALEASIV ISVSPSAGSP SAPGSSMPIR IESSSSHVAE GETLDLNCVV 2750
    PGQAHAQVTW HKRGGSLPSH HQTRGSRLRL HHVSPADSGE YVCRVMGSSG 2800
    PLEASVLVTI EASGSSAVHV PAPGGAPPIR IEPSSSRVAE GQTLDLKCVV 2850
    PGQAHAQVTW HKRGGNLPAR HQVHGPLLRL NQVSPADSGE YSCQVTGSSG 2900
    TLEASVLVTI EPSSPGPIPA PGLAQPIYIE ASSSHVTEGQ TLDLNCVVPG 2950
    QAHAQVTWYK RGGSLPARHQ THGSQLRLHL VSPADSGEYV CRAASGPGPE 3000
    QEASFTVTVP PSEGSSYRLR SPVISIDPPS STVQQGQDAS FKCLIHDGAA 3050
    PISLEWKTRN QELEDNVHIS PNGSIITIVG TRPSNHGTYR CVASNAYGVA 3100
    QSVVNLSVHG PPTVSVLPEG PVWVKVGKAV TLECVSAGEP RSSARWTRIS 3150
    STPAKLEQRT YGLMDSHAVL QISSAKPSDA GTYVCLAQNA LGTAQKQVEV 3200
    IVDTGAMAPG APQVQAEEAE LTVEAGHTAT LRCSATGSPA PTIHWSKLRS 3250
    PLPWQHRLEG DTLIIPRVAQ QDSGQYICNA TSPAGHAEAT IILHVESPPY 3300
    ATTVPEHASV QAGETVQLQC LAHGTPPLTF QWSRVGSSLP GRATARNELL 3350
    HFERAAPEDS GRYRCRVTNK VGSAEAFAQL LVQGPPGSLP ATSIPAGSTP 3400
    TVQVTPQLET KSIGASVEFH CAVPSDRGTQ LRWFKEGGQL PPGHSVQDGV 3450
    LRIQNLDQSC QGTYICQAHG PWGKAQASAQ LVIQALPSVL INIRTSVQTV 3500
    VVGHAVEFEC LALGDPKPQV TWSKVGGHLR PGIVQSGGVV RIAHVELADA 3550
    GQYRCTATNA AGTTQSHVLL LVQALPQISM PQEVRVPAGS AAVFPCIASG 3600
    YPTPDISWSK LDGSLPPDSR LENNMLMLPS VRPQDAGTYV CTATNRQGKV 3650
    KAFAHLQVPE RVVPYFTQTP YSFLPLPTIK DAYRKFEIKI TFRPDSADGM 3700
    LLYNGQKRVP GSPTNLANRQ PDFISFGLVG GRPEFRFDAG SGMATIRHPT 3750
    PLALGHFHTV TLLRSLTQGS LIVGDLAPVN GTSQGKFQGL DLNEELYLGG 3800
    YPDYGAIPKA GLSSGFIGCV RELRIQGEEI VFHDLNLTAH GISHCPTCRD 3850
    RPCQNGGQCH DSESSSYVCV CPAGFTGSRC EHSQALHCHP EACGPDATCV 3900
    NRPDGRGYTC RCHLGRSGLR CEEGVTVTTP SLSGAGSYLA LPALTNTHHE 3950
    LRLDVEFKPL APDGVLLFSG GKSGPVEDFV SLAMVGGHLE FRYELGSGLA 4000
    VLRSAEPLAL GRWHRVSAER LNKDGSLRVN GGRPVLRSSP GKSQGLNLHT 4050
    LLYLGGVEPS VPLSPATNMS AHFRGCVGEV SVNGKRLDLT YSFLGSQGIG 4100
    QCYDSSPCER QPCQHGATCM PAGEYEFQCL CRDGFKGDLC EHEENPCQLR 4150
    EPCLHGGTCQ GTRCLCLPGF SGPRCQQGSG HGIAESDWHL EGSGGNDAPG 4200
    QYGAYFHDDG FLAFPGHVFS RSLPEVPETI ELEVRTSTAS GLLLWQGVEV 4250
    GEAGQGKDFI SLGLQDGHLV FRYQLGSGEA RLVSEDPIND GEWHRVTALR 4300
    EGRRGSIQVD GEELVSGRSP GPNVAVNAKG SVYIGGAPDV ATLTGGRFSS 4350
    GITGCVKNLV LHSARPGAPP PQPLDLQHRA QAGANTRPCP S 4391
    Length:4,391
    Mass (Da):468,830
    Last modified:January 11, 2011 - v4
    Checksum:iC587660E24C83324
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61A → P in CAA44373. (PubMed:1730768)Curated
    Sequence conflicti6 – 61A → P in AAA52700. (PubMed:1569102)Curated
    Sequence conflicti58 – 581D → Y in AAA52700. (PubMed:1569102)Curated
    Sequence conflicti435 – 4373TPI → APFL in CAA44373. (PubMed:1730768)Curated
    Sequence conflicti450 – 4501H → Q in CAA44373. (PubMed:1730768)Curated
    Sequence conflicti502 – 5021R → RA in CAA44373. (PubMed:1730768)Curated
    Sequence conflicti793 – 7931N → K in CAA44373. (PubMed:1730768)Curated
    Sequence conflicti890 – 8912EA → RT in AAB21121. (PubMed:1685141)Curated
    Sequence conflicti909 – 9091G → R in CAA44373. (PubMed:1730768)Curated
    Sequence conflicti909 – 9091G → R in AAB21121. (PubMed:1685141)Curated
    Sequence conflicti1102 – 11021V → L in AAB21121. (PubMed:1685141)Curated
    Sequence conflicti1133 – 11331R → L in AAB21121. (PubMed:1685141)Curated
    Sequence conflicti1222 – 12221H → L in AAB21121. (PubMed:1685141)Curated
    Sequence conflicti1406 – 14061D → G in AAA52699. (PubMed:1679749)Curated
    Sequence conflicti1410 – 14101A → G in AAA52699. (PubMed:1679749)Curated
    Sequence conflicti1466 – 14705EFWRR → LNLRQ in AAA52699. (PubMed:1679749)Curated
    Sequence conflicti1703 – 17042SP → RG in CAA44373. (PubMed:1730768)Curated
    Sequence conflicti1753 – 17531Q → R in CAA44373. (PubMed:1730768)Curated
    Sequence conflicti2038 – 20381I → M in AAA52700. (PubMed:1569102)Curated
    Sequence conflicti2050 – 20501P → Q in CAA44373. (PubMed:1730768)Curated
    Sequence conflicti2052 – 20521P → G in AAA52700. (PubMed:1569102)Curated
    Sequence conflicti2093 – 20931P → H in CAA44373. (PubMed:1730768)Curated
    Sequence conflicti2627 – 26271S → R in CAA44373. (PubMed:1730768)Curated
    Sequence conflicti2770 – 27701H → Y in CAA44373. (PubMed:1730768)Curated
    Sequence conflicti3241 – 32411P → R in CAA44373. (PubMed:1730768)Curated
    Sequence conflicti3427 – 34271R → Q in AAA52700. (PubMed:1569102)Curated
    Sequence conflicti4004 – 40041S → T in CAA44373. (PubMed:1730768)Curated
    Sequence conflicti4135 – 41351F → I in CAA44373. (PubMed:1730768)Curated
    Sequence conflicti4332 – 43321V → I in CAA44373. (PubMed:1730768)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti68 – 681D → E.
    Corresponds to variant rs1869780 [ dbSNP | Ensembl ].
    VAR_047979
    Natural varianti303 – 3031L → H.
    Corresponds to variant rs17460381 [ dbSNP | Ensembl ].
    VAR_057051
    Natural varianti638 – 6381M → V.3 Publications
    Corresponds to variant rs1874792 [ dbSNP | Ensembl ].
    VAR_047980
    Natural varianti765 – 7651N → S.3 Publications
    Corresponds to variant rs989994 [ dbSNP | Ensembl ].
    VAR_047981
    Natural varianti1186 – 11861R → Q.
    Corresponds to variant rs2229481 [ dbSNP | Ensembl ].
    VAR_047982
    Natural varianti1323 – 13231L → V.
    Corresponds to variant rs10917058 [ dbSNP | Ensembl ].
    VAR_057052
    Natural varianti1503 – 15031A → V.3 Publications
    Corresponds to variant rs897471 [ dbSNP | Ensembl ].
    VAR_047983
    Natural varianti1532 – 15321C → Y in SJS1. 1 Publication
    VAR_014122
    Natural varianti1758 – 17581R → Q.
    Corresponds to variant rs2229483 [ dbSNP | Ensembl ].
    VAR_047984
    Natural varianti1919 – 19191R → C.
    Corresponds to variant rs2229474 [ dbSNP | Ensembl ].
    VAR_047985
    Natural varianti1967 – 19671V → I.
    Corresponds to variant rs2229475 [ dbSNP | Ensembl ].
    VAR_047986
    Natural varianti2980 – 29801L → H.1 Publication
    Corresponds to variant rs2229489 [ dbSNP | Ensembl ].
    VAR_047987
    Natural varianti2981 – 29811V → I.
    Corresponds to variant rs2229490 [ dbSNP | Ensembl ].
    VAR_047988
    Natural varianti2995 – 29951S → G.1 Publication
    Corresponds to variant rs2229491 [ dbSNP | Ensembl ].
    VAR_047989
    Natural varianti3168 – 31681A → T.1 Publication
    Corresponds to variant rs2228349 [ dbSNP | Ensembl ].
    VAR_047990
    Natural varianti3256 – 32561H → Y.
    Corresponds to variant rs2291827 [ dbSNP | Ensembl ].
    VAR_047991
    Natural varianti3530 – 35301R → W.
    Corresponds to variant rs2270699 [ dbSNP | Ensembl ].
    VAR_047992
    Natural varianti3632 – 36321R → Q.1 Publication
    Corresponds to variant rs2229493 [ dbSNP | Ensembl ].
    VAR_047993
    Natural varianti3640 – 36401V → I.
    Corresponds to variant rs17459097 [ dbSNP | Ensembl ].
    VAR_047994
    Natural varianti4331 – 43311S → N.
    Corresponds to variant rs3736360 [ dbSNP | Ensembl ].
    VAR_047995

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M85289 mRNA. Translation: AAA52700.1.
    X62515 mRNA. Translation: CAA44373.1.
    AL590556, AL590103 Genomic DNA. Translation: CAH71870.1.
    AL590103, AL590556 Genomic DNA. Translation: CAI12125.1.
    L22078 Genomic DNA. No translation available.
    AL445795 Genomic DNA. Translation: CAC18534.1.
    S76436 mRNA. Translation: AAB21121.2.
    M64283 mRNA. Translation: AAA52699.1.
    CCDSiCCDS30625.1.
    PIRiA38096.
    RefSeqiNP_001278789.1. NM_001291860.1.
    NP_005520.4. NM_005529.6.
    UniGeneiHs.562227.

    Genome annotation databases

    EnsembliENST00000374695; ENSP00000363827; ENSG00000142798.
    GeneIDi3339.
    KEGGihsa:3339.
    UCSCiuc001bfj.3. human.

    Polymorphism databases

    DMDMi317373536.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Wikipedia

    Perlecan entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M85289 mRNA. Translation: AAA52700.1 .
    X62515 mRNA. Translation: CAA44373.1 .
    AL590556 , AL590103 Genomic DNA. Translation: CAH71870.1 .
    AL590103 , AL590556 Genomic DNA. Translation: CAI12125.1 .
    L22078 Genomic DNA. No translation available.
    AL445795 Genomic DNA. Translation: CAC18534.1 .
    S76436 mRNA. Translation: AAB21121.2 .
    M64283 mRNA. Translation: AAA52699.1 .
    CCDSi CCDS30625.1.
    PIRi A38096.
    RefSeqi NP_001278789.1. NM_001291860.1.
    NP_005520.4. NM_005529.6.
    UniGenei Hs.562227.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3SH4 X-ray 1.50 A 4197-4391 [» ]
    3SH5 X-ray 2.80 A 4197-4391 [» ]
    ProteinModelPortali P98160.
    SMRi P98160. Positions 1770-1858, 4197-4391.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109571. 17 interactions.
    IntActi P98160. 10 interactions.
    MINTi MINT-123304.
    STRINGi 9606.ENSP00000363827.

    Chemistry

    DrugBanki DB00102. Becaplermin.
    DB00039. Palifermin.

    PTM databases

    PhosphoSitei P98160.

    Polymorphism databases

    DMDMi 317373536.

    2D gel databases

    DOSAC-COBS-2DPAGE P98160.

    Proteomic databases

    MaxQBi P98160.
    PaxDbi P98160.
    PRIDEi P98160.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374695 ; ENSP00000363827 ; ENSG00000142798 .
    GeneIDi 3339.
    KEGGi hsa:3339.
    UCSCi uc001bfj.3. human.

    Organism-specific databases

    CTDi 3339.
    GeneCardsi GC01M022148.
    H-InvDB HIX0023554.
    HIX0023598.
    HGNCi HGNC:5273. HSPG2.
    HPAi CAB009820.
    CAB020718.
    HPA018892.
    MIMi 142461. gene.
    224410. phenotype.
    255800. phenotype.
    neXtProti NX_P98160.
    Orphaneti 1865. Dyssegmental dysplasia, Silverman-Handmaker type.
    800. Schwartz-Jampel syndrome.
    PharmGKBi PA29537.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG258321.
    HOGENOMi HOG000049276.
    HOVERGENi HBG008174.
    InParanoidi P98160.
    KOi K06255.
    OMAi RQCTSSS.
    OrthoDBi EOG7BGHJZ.
    PhylomeDBi P98160.
    TreeFami TF326548.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_120752. HS-GAG degradation.
    REACT_121248. HS-GAG biosynthesis.
    REACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.
    REACT_13552. Integrin cell surface interactions.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_169262. Laminin interactions.
    REACT_24968. Retinoid metabolism and transport.
    REACT_6841. Chylomicron-mediated lipid transport.
    REACT_75925. Amyloids.

    Miscellaneous databases

    ChiTaRSi HSPG2. human.
    GeneWikii Perlecan.
    GenomeRNAii 3339.
    NextBioi 13216.
    PROi P98160.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P98160.
    Bgeei P98160.
    CleanExi HS_HSPG2.
    Genevestigatori P98160.

    Family and domain databases

    Gene3Di 2.60.120.200. 3 hits.
    2.60.40.10. 22 hits.
    4.10.400.10. 4 hits.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR002049. EGF_laminin.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR018031. Laminin_B_subgr.
    IPR000034. Laminin_B_type_IV.
    IPR001791. Laminin_G.
    IPR023415. LDLR_class-A_CS.
    IPR002172. LDrepeatLR_classA_rpt.
    IPR000082. SEA_dom.
    [Graphical view ]
    Pfami PF00008. EGF. 2 hits.
    PF07679. I-set. 19 hits.
    PF00052. Laminin_B. 3 hits.
    PF00053. Laminin_EGF. 9 hits.
    PF00054. Laminin_G_1. 1 hit.
    PF02210. Laminin_G_2. 2 hits.
    PF00057. Ldl_recept_a. 4 hits.
    [Graphical view ]
    PRINTSi PR00261. LDLRECEPTOR.
    SMARTi SM00181. EGF. 4 hits.
    SM00180. EGF_Lam. 8 hits.
    SM00408. IGc2. 22 hits.
    SM00281. LamB. 3 hits.
    SM00282. LamG. 3 hits.
    SM00192. LDLa. 4 hits.
    SM00200. SEA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 3 hits.
    SSF57424. SSF57424. 4 hits.
    PROSITEi PS00022. EGF_1. 9 hits.
    PS01186. EGF_2. 6 hits.
    PS50026. EGF_3. 4 hits.
    PS01248. EGF_LAM_1. 11 hits.
    PS50027. EGF_LAM_2. 8 hits.
    PS50835. IG_LIKE. 22 hits.
    PS50025. LAM_G_DOMAIN. 3 hits.
    PS51115. LAMININ_IVA. 3 hits.
    PS01209. LDLRA_1. 4 hits.
    PS50068. LDLRA_2. 4 hits.
    PS50024. SEA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the human heparan sulfate proteoglycan from basement membrane (HSPG2/perlecan). A chimeric molecule with multiple domains homologous to the low density lipoprotein receptor, laminin, neural cell adhesion molecules, and epidermal growth factor."
      Murdoch A.D., Dodge G.R., Cohen I., Tuan R.S., Iozzo R.V.
      J. Biol. Chem. 267:8544-8557(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-638; SER-765 AND VAL-1503.
      Tissue: Colon and Skin.
    2. "Human basement membrane heparan sulfate proteoglycan core protein: a 467-kD protein containing multiple domains resembling elements of the low density lipoprotein receptor, laminin, neural cell adhesion molecules, and epidermal growth factor."
      Kallunki P., Tryggvason K.
      J. Cell Biol. 116:559-571(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-638; SER-765; VAL-1503; HIS-2980; GLY-2995; THR-3168 AND GLN-3632.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Structural characterization of the complete human perlecan gene and its promoter."
      Cohen I.R., Graessel S., Murdoch A.D., Iozzo R.V.
      Proc. Natl. Acad. Sci. U.S.A. 90:10404-10408(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
    5. "Perlecan, the major proteoglycan of basement membranes, is altered in patients with Schwartz-Jampel syndrome (chondrodystrophic myotonia)."
      Nicole S., Davoine C.-S., Topaloglu H., Cattolico L., Barral D., Beighton P., Ben-Hamida C., Hammouda H., Cruaud C., White P.S., Samson D., Urtizberea J.A., Lehmann-Horn F., Weissenbach J., Hentati F., Fontaine B.
      Nat. Genet. 26:480-483(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-4391, VARIANTS VAL-638 AND SJS1 TYR-1532, VARIANTS SER-765 AND VAL-1503.
    6. "Cloning of human heparan sulfate proteoglycan core protein, assignment of the gene (HSPG2) to 1p36.1-->p35 and identification of a BamHI restriction fragment length polymorphism."
      Kallunki P., Eddy R.L., Byers M.G., Kestila M., Shows T.B., Tryggvason K.
      Genomics 11:389-396(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 890-1396.
      Tissue: Fibrosarcoma.
    7. "Heparan sulfate proteoglycan of human colon: partial molecular cloning, cellular expression, and mapping of the gene (HSPG2) to the short arm of human chromosome 1."
      Dodge G.R., Kovalszky I., Chu M.-L., Hassell J.R., McBride O.W., Yi H.F., Iozzo R.V.
      Genomics 10:673-680(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1016-1470.
      Tissue: Colon.
    8. "Matrix-associated heparan sulfate proteoglycan: core protein-specific monoclonal antibodies decorate the pericellular matrix of connective tissue cells and the stromal side of basement membranes."
      Heremans A., van der Schueren B., de Cock B., Paulsson M., Cassiman J.-J., van den Berghe H., David G.
      J. Cell Biol. 109:3199-3211(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1379-1398 AND 2259-2278.
    9. "BMP-1/Tolloid-like metalloproteases process endorepellin, the angiostatic C-terminal fragment of perlecan."
      Gonzalez E.M., Reed C.C., Bix G., Fu J., Zhang Y., Gopalakrishnan B., Greenspan D.S., Iozzo R.V.
      J. Biol. Chem. 280:7080-7087(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 4197-4208, PROTEOLYTIC PROCESSING AT ASN-4196, FUNCTION OF LG3 PEPTIDE, GLYCOSYLATION, MUTAGENESIS OF ASP-4197; ASP-4258 AND ASN-4327.
    10. "Endorepellin, a novel inhibitor of angiogenesis derived from the C terminus of perlecan."
      Mongiat M., Sweeney S.M., San Antonio J.D., Fu J., Iozzo R.V.
      J. Biol. Chem. 278:4238-4249(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 4197-4203, PROTEOLYTIC PROCESSING AT ASN-4196, FUNCTION OF ENDOREPELLIN AND LG3 PEPTIDE.
    11. "Fibroblast growth factor-binding protein is a novel partner for perlecan protein core."
      Mongiat M., Otto J., Oldershaw R., Ferrer F., Sato J.D., Iozzo R.V.
      J. Biol. Chem. 276:10263-10271(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FGFBP1.
    12. "Dyssegmental dysplasia, Silverman-Handmaker type, is caused by functional null mutations of the perlecan gene."
      Arikawa-Hirasawa E., Wilcox W.R., Le A.H., Silverman N., Govindraj P., Hassell J.R., Yamada Y.
      Nat. Genet. 27:431-434(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN DDSH.
    13. "The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparin."
      Tu H., Sasaki T., Snellman A., Gohring W., Pirila P., Timpl R., Pihlajaniemi T.
      J. Biol. Chem. 277:23092-23099(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COL13A1.
    14. "Perlecan protein core interacts with extracellular matrix protein 1 (ECM1), a glycoprotein involved in bone formation and angiogenesis."
      Mongiat M., Fu J., Oldershaw R., Greenhalgh R., Gown A.M., Iozzo R.V.
      J. Biol. Chem. 278:17491-17499(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ECM1.
    15. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
      Zhang H., Li X.-J., Martin D.B., Aebersold R.
      Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-2121.
    16. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1755.
      Tissue: Plasma.
    17. "Endorepellin in vivo: targeting the tumor vasculature and retarding cancer growth and metabolism."
      Bix G., Castello R., Burrows M., Zoeller J.J., Weech M., Iozzo R.A., Cardi C., Thakur M.L., Barker C.A., Camphausen K., Iozzo R.V.
      J. Natl. Cancer Inst. 98:1634-1646(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF ENDOREPELLIN.
    18. "Integrin alpha2beta1 is the required receptor for endorepellin angiostatic activity."
      Woodall B.P., Nystroem A., Iozzo R.A., Eble J.A., Niland S., Krieg T., Eckes B., Pozzi A., Iozzo R.V.
      J. Biol. Chem. 283:2335-2343(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF ENDOREPELLIN, IDENTIFICATION OF RECEPTOR.
    19. "Role of tyrosine phosphatase SHP-1 in the mechanism of endorepellin angiostatic activity."
      Nystrom A., Shaik Z.P., Gullberg D., Krieg T., Eckes B., Zent R., Pozzi A., Iozzo R.V.
      Blood 114:4897-4906(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-554; ASN-1755; ASN-3072; ASN-3780; ASN-3836 AND ASN-4068.
      Tissue: Liver.
    21. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
      Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-42, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
    22. "Crystal structure of the LG3 domain of endorepellin, an angiogenesis inhibitor."
      Le B.V., Kim H., Choi J., Kim J.H., Hahn M.J., Lee C., Kim K.K., Hwang H.Y.
      J. Mol. Biol. 414:231-242(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 4197-4391, DISULFIDE BOND, CALCIUM-BINDING SITES.

    Entry informationi

    Entry nameiPGBM_HUMAN
    AccessioniPrimary (citable) accession number: P98160
    Secondary accession number(s): Q16287, Q5SZI3, Q9H3V5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 170 of the entry and version 4 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

    Miscellaneous

    The LG3 peptide has been found in the urine of patients with end-stage renal disease and in the amniotic fluid of pregnant women with premature rupture of fetal membranes.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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