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P98160

- PGBM_HUMAN

UniProt

P98160 - PGBM_HUMAN

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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

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 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
Complete GO annotation...

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_267654. Defective EXT2 causes exostoses 2.
REACT_267659. Defective B3GAT3 causes JDSSDHD.
REACT_267674. Defective EXT1 causes exostoses 1, TRPS2 and CHDS.
REACT_267711. Defective B4GALT7 causes EDS, progeroid type.
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 matrix Source: UniProtKB
  3. extracellular region Source: Reactome
  4. extracellular space Source: BHF-UCL
  5. extracellular vesicular exosome Source: UniProtKB
  6. focal adhesion Source: UniProtKB
  7. Golgi lumen Source: Reactome
  8. lysosomal lumen Source: Reactome
  9. plasma membrane Source: Reactome
Complete GO annotation...

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...)1 Publication
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...)1 Publication
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...)2 Publications
Glycosylationi2121 – 21211N-linked (GlcNAc...)1 Publication
Glycosylationi2995 – 29951O-linked (Xyl...) (chondroitin sulfate)Sequence Analysis
Glycosylationi3072 – 30721N-linked (GlcNAc...)1 Publication
Glycosylationi3105 – 31051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3279 – 32791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3780 – 37801N-linked (GlcNAc...)1 Publication
Disulfide bondi3819 ↔ 3845By similarity
Glycosylationi3836 – 38361N-linked (GlcNAc...)1 Publication
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...)1 Publication
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

BgeeiP98160.
CleanExiHS_HSPG2.
ExpressionAtlasiP98160. baseline and differential.
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
FLT1P17948-22EBI-6896259,EBI-6530464
KDRP359685EBI-947664,EBI-1005487

Protein-protein interaction databases

BioGridi109571. 18 interactions.
IntActiP98160. 16 interactions.
MINTiMINT-123304.
STRINGi9606.ENSP00000363827.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000063501.
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.
InterProiIPR013320. ConA-like_dom.
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

« Hide

        10         20         30         40         50
MGWRAAGALL LALLLHGRLL AVTHGLRAYD GLSLPEDIET VTASQMRWTH
60 70 80 90 100
SYLSDDEDML ADSISGDDLG SGDLGSGDFQ MVYFRALVNF TRSIEYSPQL
110 120 130 140 150
EDAGSREFRE VSEAVVDTLE SEYLKIPGDQ VVSVVFIKEL DGWVFVELDV
160 170 180 190 200
GSEGNADGAQ IQEMLLRVIS SGSVASYVTS PQGFQFRRLG TVPQFPRACT
210 220 230 240 250
EAEFACHSYN ECVALEYRCD RRPDCRDMSD ELNCEEPVLG ISPTFSLLVE
260 270 280 290 300
TTSLPPRPET TIMRQPPVTH APQPLLPGSV RPLPCGPQEA ACRNGHCIPR
310 320 330 340 350
DYLCDGQEDC EDGSDELDCG PPPPCEPNEF PCGNGHCALK LWRCDGDFDC
360 370 380 390 400
EDRTDEANCP TKRPEEVCGP TQFRCVSTNM CIPASFHCDE ESDCPDRSDE
410 420 430 440 450
FGCMPPQVVT PPRESIQASR GQTVTFTCVA IGVPTPIINW RLNWGHIPSH
460 470 480 490 500
PRVTVTSEGG RGTLIIRDVK ESDQGAYTCE AMNARGMVFG IPDGVLELVP
510 520 530 540 550
QRGPCPDGHF YLEHSAACLP CFCFGITSVC QSTRRFRDQI RLRFDQPDDF
560 570 580 590 600
KGVNVTMPAQ PGTPPLSSTQ LQIDPSLHEF QLVDLSRRFL VHDSFWALPE
610 620 630 640 650
QFLGNKVDSY GGSLRYNVRY ELARGMLEPV QRPDVVLMGA GYRLLSRGHT
660 670 680 690 700
PTQPGALNQR QVQFSEEHWV HESGRPVQRA ELLQVLQSLE AVLIQTVYNT
710 720 730 740 750
KMASVGLSDI AMDTTVTHAT SHGRAHSVEE CRCPIGYSGL SCESCDAHFT
760 770 780 790 800
RVPGGPYLGT CSGCNCNGHA SSCDPVYGHC LNCQHNTEGP QCNKCKAGFF
810 820 830 840 850
GDAMKATATS CRPCPCPYID ASRRFSDTCF LDTDGQATCD ACAPGYTGRR
860 870 880 890 900
CESCAPGYEG NPIQPGGKCR PVNQEIVRCD ERGSMGTSGE ACRCKNNVVG
910 920 930 940 950
RLCNECADGS FHLSTRNPDG CLKCFCMGVS RHCTSSSWSR AQLHGASEEP
960 970 980 990 1000
GHFSLTNAAS THTTNEGIFS PTPGELGFSS FHRLLSGPYF WSLPSRFLGD
1010 1020 1030 1040 1050
KVTSYGGELR FTVTQRSQPG STPLHGQPLV VLQGNNIILE HHVAQEPSPG
1060 1070 1080 1090 1100
QPSTFIVPFR EQAWQRPDGQ PATREHLLMA LAGIDTLLIR ASYAQQPAES
1110 1120 1130 1140 1150
RVSGISMDVA VPEETGQDPA LEVEQCSCPP GYRGPSCQDC DTGYTRTPSG
1160 1170 1180 1190 1200
LYLGTCERCS CHGHSEACEP ETGACQGCQH HTEGPRCEQC QPGYYGDAQR
1210 1220 1230 1240 1250
GTPQDCQLCP CYGDPAAGQA AHTCFLDTDG HPTCDACSPG HSGRHCERCA
1260 1270 1280 1290 1300
PGYYGNPSQG QPCQRDSQVP GPIGCNCDPQ GSVSSQCDAA GQCQCKAQVE
1310 1320 1330 1340 1350
GLTCSHCRPH HFHLSASNPD GCLPCFCMGI TQQCASSAYT RHLISTHFAP
1360 1370 1380 1390 1400
GDFQGFALVN PQRNSRLTGE FTVEPVPEGA QLSFGNFAQL GHESFYWQLP
1410 1420 1430 1440 1450
ETYQGDKVAA YGGKLRYTLS YTAGPQGSPL SDPDVQITGN NIMLVASQPA
1460 1470 1480 1490 1500
LQGPERRSYE IMFREEFWRR PDGQPATREH LLMALADLDE LLIRATFSSV
1510 1520 1530 1540 1550
PLAASISAVS LEVAQPGPSN RPRALEVEEC RCPPGYIGLS CQDCAPGYTR
1560 1570 1580 1590 1600
TGSGLYLGHC ELCECNGHSD LCHPETGACS QCQHNAAGEF CELCAPGYYG
1610 1620 1630 1640 1650
DATAGTPEDC QPCACPLTNP ENMFSRTCES LGAGGYRCTA CEPGYTGQYC
1660 1670 1680 1690 1700
EQCGPGYVGN PSVQGGQCLP ETNQAPLVVE VHPARSIVPQ GGSHSLRCQV
1710 1720 1730 1740 1750
SGSPPHYFYW SREDGRPVPS GTQQRHQGSE LHFPSVQPSD AGVYICTCRN
1760 1770 1780 1790 1800
LHQSNTSRAE LLVTEAPSKP ITVTVEEQRS QSVRPGADVT FICTAKSKSP
1810 1820 1830 1840 1850
AYTLVWTRLH NGKLPTRAMD FNGILTIRNV QLSDAGTYVC TGSNMFAMDQ
1860 1870 1880 1890 1900
GTATLHVQAS GTLSAPVVSI HPPQLTVQPG QLAEFRCSAT GSPTPTLEWT
1910 1920 1930 1940 1950
GGPGGQLPAK AQIHGGILRL PAVEPTDQAQ YLCRAHSSAG QQVARAVLHV
1960 1970 1980 1990 2000
HGGGGPRVQV SPERTQVHAG RTVRLYCRAA GVPSATITWR KEGGSLPPQA
2010 2020 2030 2040 2050
RSERTDIATL LIPAITTADA GFYLCVATSP AGTAQARIQV VVLSASDASP
2060 2070 2080 2090 2100
PPVKIESSSP SVTEGQTLDL NCVVAGSAHA QVTWYRRGGS LPPHTQVHGS
2110 2120 2130 2140 2150
RLRLPQVSPA DSGEYVCRVE NGSGPKEASI TVSVLHGTHS GPSYTPVPGS
2160 2170 2180 2190 2200
TRPIRIEPSS SHVAEGQTLD LNCVVPGQAH AQVTWHKRGG SLPARHQTHG
2210 2220 2230 2240 2250
SLLRLHQVTP ADSGEYVCHV VGTSGPLEAS VLVTIEASVI PGPIPPVRIE
2260 2270 2280 2290 2300
SSSSTVAEGQ TLDLSCVVAG QAHAQVTWYK RGGSLPARHQ VRGSRLYIFQ
2310 2320 2330 2340 2350
ASPADAGQYV CRASNGMEAS ITVTVTGTQG ANLAYPAGST QPIRIEPSSS
2360 2370 2380 2390 2400
QVAEGQTLDL NCVVPGQSHA QVTWHKRGGS LPVRHQTHGS LLRLYQASPA
2410 2420 2430 2440 2450
DSGEYVCRVL GSSVPLEASV LVTIEPAGSV PALGVTPTVR IESSSSQVAE
2460 2470 2480 2490 2500
GQTLDLNCLV AGQAHAQVTW HKRGGSLPAR HQVHGSRLRL LQVTPADSGE
2510 2520 2530 2540 2550
YVCRVVGSSG TQEASVLVTI QQRLSGSHSQ GVAYPVRIES SSASLANGHT
2560 2570 2580 2590 2600
LDLNCLVASQ APHTITWYKR GGSLPSRHQI VGSRLRIPQV TPADSGEYVC
2610 2620 2630 2640 2650
HVSNGAGSRE TSLIVTIQGS GSSHVPSVSP PIRIESSSPT VVEGQTLDLN
2660 2670 2680 2690 2700
CVVARQPQAI ITWYKRGGSL PSRHQTHGSH LRLHQMSVAD SGEYVCRANN
2710 2720 2730 2740 2750
NIDALEASIV ISVSPSAGSP SAPGSSMPIR IESSSSHVAE GETLDLNCVV
2760 2770 2780 2790 2800
PGQAHAQVTW HKRGGSLPSH HQTRGSRLRL HHVSPADSGE YVCRVMGSSG
2810 2820 2830 2840 2850
PLEASVLVTI EASGSSAVHV PAPGGAPPIR IEPSSSRVAE GQTLDLKCVV
2860 2870 2880 2890 2900
PGQAHAQVTW HKRGGNLPAR HQVHGPLLRL NQVSPADSGE YSCQVTGSSG
2910 2920 2930 2940 2950
TLEASVLVTI EPSSPGPIPA PGLAQPIYIE ASSSHVTEGQ TLDLNCVVPG
2960 2970 2980 2990 3000
QAHAQVTWYK RGGSLPARHQ THGSQLRLHL VSPADSGEYV CRAASGPGPE
3010 3020 3030 3040 3050
QEASFTVTVP PSEGSSYRLR SPVISIDPPS STVQQGQDAS FKCLIHDGAA
3060 3070 3080 3090 3100
PISLEWKTRN QELEDNVHIS PNGSIITIVG TRPSNHGTYR CVASNAYGVA
3110 3120 3130 3140 3150
QSVVNLSVHG PPTVSVLPEG PVWVKVGKAV TLECVSAGEP RSSARWTRIS
3160 3170 3180 3190 3200
STPAKLEQRT YGLMDSHAVL QISSAKPSDA GTYVCLAQNA LGTAQKQVEV
3210 3220 3230 3240 3250
IVDTGAMAPG APQVQAEEAE LTVEAGHTAT LRCSATGSPA PTIHWSKLRS
3260 3270 3280 3290 3300
PLPWQHRLEG DTLIIPRVAQ QDSGQYICNA TSPAGHAEAT IILHVESPPY
3310 3320 3330 3340 3350
ATTVPEHASV QAGETVQLQC LAHGTPPLTF QWSRVGSSLP GRATARNELL
3360 3370 3380 3390 3400
HFERAAPEDS GRYRCRVTNK VGSAEAFAQL LVQGPPGSLP ATSIPAGSTP
3410 3420 3430 3440 3450
TVQVTPQLET KSIGASVEFH CAVPSDRGTQ LRWFKEGGQL PPGHSVQDGV
3460 3470 3480 3490 3500
LRIQNLDQSC QGTYICQAHG PWGKAQASAQ LVIQALPSVL INIRTSVQTV
3510 3520 3530 3540 3550
VVGHAVEFEC LALGDPKPQV TWSKVGGHLR PGIVQSGGVV RIAHVELADA
3560 3570 3580 3590 3600
GQYRCTATNA AGTTQSHVLL LVQALPQISM PQEVRVPAGS AAVFPCIASG
3610 3620 3630 3640 3650
YPTPDISWSK LDGSLPPDSR LENNMLMLPS VRPQDAGTYV CTATNRQGKV
3660 3670 3680 3690 3700
KAFAHLQVPE RVVPYFTQTP YSFLPLPTIK DAYRKFEIKI TFRPDSADGM
3710 3720 3730 3740 3750
LLYNGQKRVP GSPTNLANRQ PDFISFGLVG GRPEFRFDAG SGMATIRHPT
3760 3770 3780 3790 3800
PLALGHFHTV TLLRSLTQGS LIVGDLAPVN GTSQGKFQGL DLNEELYLGG
3810 3820 3830 3840 3850
YPDYGAIPKA GLSSGFIGCV RELRIQGEEI VFHDLNLTAH GISHCPTCRD
3860 3870 3880 3890 3900
RPCQNGGQCH DSESSSYVCV CPAGFTGSRC EHSQALHCHP EACGPDATCV
3910 3920 3930 3940 3950
NRPDGRGYTC RCHLGRSGLR CEEGVTVTTP SLSGAGSYLA LPALTNTHHE
3960 3970 3980 3990 4000
LRLDVEFKPL APDGVLLFSG GKSGPVEDFV SLAMVGGHLE FRYELGSGLA
4010 4020 4030 4040 4050
VLRSAEPLAL GRWHRVSAER LNKDGSLRVN GGRPVLRSSP GKSQGLNLHT
4060 4070 4080 4090 4100
LLYLGGVEPS VPLSPATNMS AHFRGCVGEV SVNGKRLDLT YSFLGSQGIG
4110 4120 4130 4140 4150
QCYDSSPCER QPCQHGATCM PAGEYEFQCL CRDGFKGDLC EHEENPCQLR
4160 4170 4180 4190 4200
EPCLHGGTCQ GTRCLCLPGF SGPRCQQGSG HGIAESDWHL EGSGGNDAPG
4210 4220 4230 4240 4250
QYGAYFHDDG FLAFPGHVFS RSLPEVPETI ELEVRTSTAS GLLLWQGVEV
4260 4270 4280 4290 4300
GEAGQGKDFI SLGLQDGHLV FRYQLGSGEA RLVSEDPIND GEWHRVTALR
4310 4320 4330 4340 4350
EGRRGSIQVD GEELVSGRSP GPNVAVNAKG SVYIGGAPDV ATLTGGRFSS
4360 4370 4380 4390
GITGCVKNLV LHSARPGAPP PQPLDLQHRA QAGANTRPCP S
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 18 interactions.
IntActi P98160. 16 interactions.
MINTi MINT-123304.
STRINGi 9606.ENSP00000363827.

Chemistry

DrugBanki 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.
GeneTreei ENSGT00530000063501.
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_267654. Defective EXT2 causes exostoses 2.
REACT_267659. Defective B3GAT3 causes JDSSDHD.
REACT_267674. Defective EXT1 causes exostoses 1, TRPS2 and CHDS.
REACT_267711. Defective B4GALT7 causes EDS, progeroid type.
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

Bgeei P98160.
CleanExi HS_HSPG2.
ExpressionAtlasi P98160. baseline and differential.
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 IPR013320. ConA-like_dom.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 172 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