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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.5 Publications
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, PTPN6.5 Publications
The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity.5 Publications

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
  3. protein 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_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. Golgi lumen Source: Reactome
  2. basal lamina Source: Ensembl
  3. extracellular region Source: Reactome
  4. extracellular space Source: BHF-UCL
  5. extracellular vesicular exosome Source: UniProtKB
  6. lysosomal lumen Source: Reactome
  7. 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

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 – 2121 Reviewed prediction
Add
BLAST
Chaini22 – 43914370Basement membrane-specific heparan sulfate proteoglycan core protein
PRO_0000026696Add
BLAST
Chaini3687 – 4391705Endorepellin
PRO_0000391621Add
BLAST
Chaini4197 – 4391195LG3 peptide
PRO_0000391622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421O-linked (GalNAc...)1 Publication
Glycosylationi65 – 651O-linked (Xyl...) (heparan sulfate) Reviewed prediction
Glycosylationi71 – 711O-linked (Xyl...) (heparan sulfate) Reviewed prediction
Glycosylationi76 – 761O-linked (Xyl...) (heparan sulfate) Reviewed prediction
Glycosylationi89 – 891N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi199 ↔ 212 By similarity
Disulfide bondi206 ↔ 225 By similarity
Disulfide bondi219 ↔ 234 By similarity
Disulfide bondi285 ↔ 297 By similarity
Disulfide bondi292 ↔ 310 By similarity
Disulfide bondi304 ↔ 319 By similarity
Disulfide bondi325 ↔ 337 By similarity
Disulfide bondi332 ↔ 350 By similarity
Disulfide bondi344 ↔ 359 By similarity
Disulfide bondi368 ↔ 381 By similarity
Disulfide bondi375 ↔ 394 By similarity
Disulfide bondi388 ↔ 403 By similarity
Glycosylationi554 – 5541N-linked (GlcNAc...)1 Publication
Disulfide bondi764 ↔ 773 By similarity
Disulfide bondi766 ↔ 780 By similarity
Disulfide bondi783 ↔ 792 By similarity
Disulfide bondi795 ↔ 811 By similarity
Disulfide bondi814 ↔ 829 By similarity
Disulfide bondi816 ↔ 839 By similarity
Disulfide bondi842 ↔ 851 By similarity
Disulfide bondi854 ↔ 869 By similarity
Disulfide bondi879 ↔ 892 By similarity
Disulfide bondi894 ↔ 903 By similarity
Disulfide bondi906 ↔ 921 By similarity
Disulfide bondi1159 ↔ 1168 By similarity
Disulfide bondi1161 ↔ 1175 By similarity
Disulfide bondi1178 ↔ 1187 By similarity
Disulfide bondi1190 ↔ 1206 By similarity
Disulfide bondi1209 ↔ 1224 By similarity
Disulfide bondi1211 ↔ 1234 By similarity
Disulfide bondi1237 ↔ 1246 By similarity
Disulfide bondi1249 ↔ 1263 By similarity
Disulfide bondi1275 ↔ 1287 By similarity
Disulfide bondi1277 ↔ 1293 By similarity
Disulfide bondi1295 ↔ 1304 By similarity
Disulfide bondi1307 ↔ 1322 By similarity
Disulfide bondi1563 ↔ 1572 By similarity
Disulfide bondi1565 ↔ 1579 By similarity
Disulfide bondi1582 ↔ 1591 By similarity
Disulfide bondi1594 ↔ 1610 By similarity
Disulfide bondi1613 ↔ 1628 By similarity
Disulfide bondi1615 ↔ 1638 By similarity
Disulfide bondi1641 ↔ 1650 By similarity
Disulfide bondi1653 ↔ 1668 By similarity
Glycosylationi1755 – 17551N-linked (GlcNAc...)2 Publications
Glycosylationi2121 – 21211N-linked (GlcNAc...)1 Publication
Glycosylationi2995 – 29951O-linked (Xyl...) (chondroitin sulfate) Reviewed prediction
Glycosylationi3072 – 30721N-linked (GlcNAc...)1 Publication
Glycosylationi3105 – 31051N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3279 – 32791N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3780 – 37801N-linked (GlcNAc...)1 Publication
Disulfide bondi3819 ↔ 3845 By similarity
Glycosylationi3836 – 38361N-linked (GlcNAc...)1 Publication
Disulfide bondi3848 ↔ 3859 By similarity
Disulfide bondi3853 ↔ 3869 By similarity
Disulfide bondi3871 ↔ 3880 By similarity
Disulfide bondi3888 ↔ 3899 By similarity
Disulfide bondi3893 ↔ 3910 By similarity
Disulfide bondi3912 ↔ 3921 By similarity
Glycosylationi3933 – 39331O-linked (Xyl...) (chondroitin sulfate) Reviewed prediction
Glycosylationi4068 – 40681N-linked (GlcNAc...)1 Publication
Disulfide bondi4076 ↔ 4102 By similarity
Disulfide bondi4108 ↔ 4119 By similarity
Disulfide bondi4113 ↔ 4129 By similarity
Disulfide bondi4131 ↔ 4140 By similarity
Disulfide bondi4147 ↔ 4159 By similarity
Disulfide bondi4153 ↔ 4164 By similarity
Disulfide bondi4166 ↔ 4175 By similarity
Glycosylationi4179 – 41791O-linked (Xyl...) (chondroitin sulfate) Reviewed prediction
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.
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.3 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

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.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4149 – 41513Mediates motor neuron attachment Reviewed prediction
Regioni4299 – 43013Mediates motor neuron attachment Reviewed prediction

Sequence similaritiesi

Contains 4 EGF-like domains.
Contains 1 SEA domain.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61A → P in CAA44373. 1 Publication
Sequence conflicti6 – 61A → P in AAA52700. 1 Publication
Sequence conflicti58 – 581D → Y in AAA52700. 1 Publication
Sequence conflicti435 – 4373TPI → APFL in CAA44373. 1 Publication
Sequence conflicti450 – 4501H → Q in CAA44373. 1 Publication
Sequence conflicti502 – 5021R → RA in CAA44373. 1 Publication
Sequence conflicti793 – 7931N → K in CAA44373. 1 Publication
Sequence conflicti890 – 8912EA → RT in AAB21121. 1 Publication
Sequence conflicti909 – 9091G → R in CAA44373. 1 Publication
Sequence conflicti909 – 9091G → R in AAB21121. 1 Publication
Sequence conflicti1102 – 11021V → L in AAB21121. 1 Publication
Sequence conflicti1133 – 11331R → L in AAB21121. 1 Publication
Sequence conflicti1222 – 12221H → L in AAB21121. 1 Publication
Sequence conflicti1406 – 14061D → G in AAA52699. 1 Publication
Sequence conflicti1410 – 14101A → G in AAA52699. 1 Publication
Sequence conflicti1466 – 14705EFWRR → LNLRQ in AAA52699. 1 Publication
Sequence conflicti1703 – 17042SP → RG in CAA44373. 1 Publication
Sequence conflicti1753 – 17531Q → R in CAA44373. 1 Publication
Sequence conflicti2038 – 20381I → M in AAA52700. 1 Publication
Sequence conflicti2050 – 20501P → Q in CAA44373. 1 Publication
Sequence conflicti2052 – 20521P → G in AAA52700. 1 Publication
Sequence conflicti2093 – 20931P → H in CAA44373. 1 Publication
Sequence conflicti2627 – 26271S → R in CAA44373. 1 Publication
Sequence conflicti2770 – 27701H → Y in CAA44373. 1 Publication
Sequence conflicti3241 – 32411P → R in CAA44373. 1 Publication
Sequence conflicti3427 – 34271R → Q in AAA52700. 1 Publication
Sequence conflicti4004 – 40041S → T in CAA44373. 1 Publication
Sequence conflicti4135 – 41351F → I in CAA44373. 1 Publication
Sequence conflicti4332 – 43321V → I in CAA44373. 1 Publication

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

« 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: September 3, 2014
This is version 169 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

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