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P98160 (PGBM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Endorepellin
  2. LG3 peptide
Gene names
Name:HSPG2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length4391 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10 Ref.17 Ref.18 Ref.19

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. Ref.9 Ref.10 Ref.17 Ref.18 Ref.19

The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity. Ref.9 Ref.10 Ref.17 Ref.18 Ref.19

Subunit structure

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). Ref.11 Ref.13 Ref.14

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane.

Tissue specificity

Found in the basement membranes.

Post-translational modification

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. Ref.9 Ref.15 Ref.21

Involvement in disease

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. Ref.5

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. Ref.12

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.

Sequence similarities

Contains 4 EGF-like domains.

Contains 22 Ig-like C2-type (immunoglobulin-like) domains.

Contains 11 laminin EGF-like domains.

Contains 3 laminin G-like domains.

Contains 3 laminin IV type A domains.

Contains 4 LDL-receptor class A domains.

Contains 1 SEA domain.

Ontologies

Keywords
   Biological processAngiogenesis
   Cellular componentBasement membrane
Extracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainEGF-like domain
Immunoglobulin domain
Laminin EGF-like domain
Repeat
Signal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
Heparan sulfate
Proteoglycan
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

brain development

Inferred from electronic annotation. Source: Ensembl

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cardiac muscle tissue development

Inferred from electronic annotation. Source: Ensembl

cartilage development involved in endochondral bone morphogenesis

Inferred from electronic annotation. Source: Ensembl

chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

chondroitin sulfate metabolic process

Traceable author statement. Source: Reactome

embryonic skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

endochondral ossification

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

glycosaminoglycan biosynthetic process

Traceable author statement. Source: Reactome

glycosaminoglycan catabolic process

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

lipoprotein metabolic process

Traceable author statement. Source: Reactome

phototransduction, visible light

Traceable author statement. Source: Reactome

protein localization

Inferred from electronic annotation. Source: Ensembl

retinoid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

basal lamina

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

lysosomal lumen

Traceable author statement. Source: Reactome

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein C-terminus binding

Inferred from physical interaction Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KDRP359684EBI-947664,EBI-1005487

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 43914370Basement membrane-specific heparan sulfate proteoglycan core protein
PRO_0000026696
Chain3687 – 4391705Endorepellin
PRO_0000391621
Chain4197 – 4391195LG3 peptide
PRO_0000391622

Regions

Domain80 – 191112SEA
Domain198 – 23538LDL-receptor class A 1
Domain284 – 32037LDL-receptor class A 2
Domain324 – 36037LDL-receptor class A 3
Domain367 – 40438LDL-receptor class A 4
Domain405 – 504100Ig-like C2-type 1
Domain521 – 53010Laminin EGF-like 1; first part
Domain538 – 730193Laminin IV type A 1
Domain731 – 76333Laminin EGF-like 1; second part
Domain764 – 81350Laminin EGF-like 2
Domain814 – 87158Laminin EGF-like 3
Domain879 – 92345Laminin EGF-like 4; truncated
Domain924 – 93310Laminin EGF-like 5; first part
Domain941 – 1125185Laminin IV type A 2
Domain1126 – 115833Laminin EGF-like 5; second part
Domain1159 – 120850Laminin EGF-like 6
Domain1209 – 126557Laminin EGF-like 7
Domain1275 – 132450Laminin EGF-like 8
Domain1325 – 133410Laminin EGF-like 9; first part
Domain1344 – 1529186Laminin IV type A 3
Domain1530 – 156233Laminin EGF-like 9; second part
Domain1563 – 161250Laminin EGF-like 10
Domain1613 – 167058Laminin EGF-like 11
Domain1677 – 177195Ig-like C2-type 2
Domain1772 – 186594Ig-like C2-type 3
Domain1866 – 195590Ig-like C2-type 4
Domain1956 – 205196Ig-like C2-type 5
Domain2052 – 2151100Ig-like C2-type 6
Domain2152 – 224493Ig-like C2-type 7
Domain2245 – 234096Ig-like C2-type 8
Domain2341 – 243696Ig-like C2-type 9
Domain2437 – 253397Ig-like C2-type 10
Domain2534 – 262996Ig-like C2-type 11
Domain2630 – 272697Ig-like C2-type 12
Domain2727 – 2826100Ig-like C2-type 13
Domain2827 – 292498Ig-like C2-type 14
Domain2925 – 302197Ig-like C2-type 15
Domain3022 – 311291Ig-like C2-type 16
Domain3113 – 321199Ig-like C2-type 17
Domain3212 – 329887Ig-like C2-type 18
Domain3299 – 3399101Ig-like C2-type 19
Domain3400 – 348889Ig-like C2-type 20
Domain3489 – 357486Ig-like C2-type 21
Domain3575 – 366288Ig-like C2-type 22
Domain3663 – 3843181Laminin G-like 1
Domain3844 – 388138EGF-like 1
Domain3884 – 392239EGF-like 2
Domain3928 – 4103176Laminin G-like 2
Domain4104 – 414138EGF-like 3
Domain4143 – 417634EGF-like 4
Domain4201 – 4389189Laminin G-like 3
Region4149 – 41513Mediates motor neuron attachment Potential
Region4299 – 43013Mediates motor neuron attachment Potential

Sites

Metal binding42581Calcium
Metal binding42751Calcium; via carbonyl oxygen
Metal binding43251Calcium; via carbonyl oxygen
Metal binding43271Calcium
Site4196 – 41972Cleavage; by BMP1

Amino acid modifications

Glycosylation421O-linked (GalNAc...) Ref.21
Glycosylation651O-linked (Xyl...) (heparan sulfate) Potential
Glycosylation711O-linked (Xyl...) (heparan sulfate) Potential
Glycosylation761O-linked (Xyl...) (heparan sulfate) Potential
Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation5541N-linked (GlcNAc...) Ref.20
Glycosylation17551N-linked (GlcNAc...) Ref.16 Ref.20
Glycosylation21211N-linked (GlcNAc...) Ref.15
Glycosylation29951O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation30721N-linked (GlcNAc...) Ref.20
Glycosylation31051N-linked (GlcNAc...) Potential
Glycosylation32791N-linked (GlcNAc...) Potential
Glycosylation37801N-linked (GlcNAc...) Ref.20
Glycosylation38361N-linked (GlcNAc...) Ref.20
Glycosylation39331O-linked (Xyl...) (chondroitin sulfate) Potential
Glycosylation40681N-linked (GlcNAc...) Ref.20
Glycosylation41791O-linked (Xyl...) (chondroitin sulfate) Potential
Disulfide bond199 ↔ 212 By similarity
Disulfide bond206 ↔ 225 By similarity
Disulfide bond219 ↔ 234 By similarity
Disulfide bond285 ↔ 297 By similarity
Disulfide bond292 ↔ 310 By similarity
Disulfide bond304 ↔ 319 By similarity
Disulfide bond325 ↔ 337 By similarity
Disulfide bond332 ↔ 350 By similarity
Disulfide bond344 ↔ 359 By similarity
Disulfide bond368 ↔ 381 By similarity
Disulfide bond375 ↔ 394 By similarity
Disulfide bond388 ↔ 403 By similarity
Disulfide bond764 ↔ 773 By similarity
Disulfide bond766 ↔ 780 By similarity
Disulfide bond783 ↔ 792 By similarity
Disulfide bond795 ↔ 811 By similarity
Disulfide bond814 ↔ 829 By similarity
Disulfide bond816 ↔ 839 By similarity
Disulfide bond842 ↔ 851 By similarity
Disulfide bond854 ↔ 869 By similarity
Disulfide bond879 ↔ 892 By similarity
Disulfide bond894 ↔ 903 By similarity
Disulfide bond906 ↔ 921 By similarity
Disulfide bond1159 ↔ 1168 By similarity
Disulfide bond1161 ↔ 1175 By similarity
Disulfide bond1178 ↔ 1187 By similarity
Disulfide bond1190 ↔ 1206 By similarity
Disulfide bond1209 ↔ 1224 By similarity
Disulfide bond1211 ↔ 1234 By similarity
Disulfide bond1237 ↔ 1246 By similarity
Disulfide bond1249 ↔ 1263 By similarity
Disulfide bond1275 ↔ 1287 By similarity
Disulfide bond1277 ↔ 1293 By similarity
Disulfide bond1295 ↔ 1304 By similarity
Disulfide bond1307 ↔ 1322 By similarity
Disulfide bond1563 ↔ 1572 By similarity
Disulfide bond1565 ↔ 1579 By similarity
Disulfide bond1582 ↔ 1591 By similarity
Disulfide bond1594 ↔ 1610 By similarity
Disulfide bond1613 ↔ 1628 By similarity
Disulfide bond1615 ↔ 1638 By similarity
Disulfide bond1641 ↔ 1650 By similarity
Disulfide bond1653 ↔ 1668 By similarity
Disulfide bond3819 ↔ 3845 By similarity
Disulfide bond3848 ↔ 3859 By similarity
Disulfide bond3853 ↔ 3869 By similarity
Disulfide bond3871 ↔ 3880 By similarity
Disulfide bond3888 ↔ 3899 By similarity
Disulfide bond3893 ↔ 3910 By similarity
Disulfide bond3912 ↔ 3921 By similarity
Disulfide bond4076 ↔ 4102 By similarity
Disulfide bond4108 ↔ 4119 By similarity
Disulfide bond4113 ↔ 4129 By similarity
Disulfide bond4131 ↔ 4140 By similarity
Disulfide bond4147 ↔ 4159 By similarity
Disulfide bond4153 ↔ 4164 By similarity
Disulfide bond4166 ↔ 4175 By similarity
Disulfide bond4355 ↔ 4389 Ref.22

Natural variations

Natural variant681D → E.
Corresponds to variant rs1869780 [ dbSNP | Ensembl ].
VAR_047979
Natural variant3031L → H.
Corresponds to variant rs17460381 [ dbSNP | Ensembl ].
VAR_057051
Natural variant6381M → V. Ref.1 Ref.2 Ref.5
Corresponds to variant rs1874792 [ dbSNP | Ensembl ].
VAR_047980
Natural variant7651N → S. Ref.1 Ref.2 Ref.5
Corresponds to variant rs989994 [ dbSNP | Ensembl ].
VAR_047981
Natural variant11861R → Q.
Corresponds to variant rs2229481 [ dbSNP | Ensembl ].
VAR_047982
Natural variant13231L → V.
Corresponds to variant rs10917058 [ dbSNP | Ensembl ].
VAR_057052
Natural variant15031A → V. Ref.1 Ref.2 Ref.5
Corresponds to variant rs897471 [ dbSNP | Ensembl ].
VAR_047983
Natural variant15321C → Y in SJS1. Ref.5
VAR_014122
Natural variant17581R → Q.
Corresponds to variant rs2229483 [ dbSNP | Ensembl ].
VAR_047984
Natural variant19191R → C.
Corresponds to variant rs2229474 [ dbSNP | Ensembl ].
VAR_047985
Natural variant19671V → I.
Corresponds to variant rs2229475 [ dbSNP | Ensembl ].
VAR_047986
Natural variant29801L → H. Ref.2
Corresponds to variant rs2229489 [ dbSNP | Ensembl ].
VAR_047987
Natural variant29811V → I.
Corresponds to variant rs2229490 [ dbSNP | Ensembl ].
VAR_047988
Natural variant29951S → G. Ref.2
Corresponds to variant rs2229491 [ dbSNP | Ensembl ].
VAR_047989
Natural variant31681A → T. Ref.2
Corresponds to variant rs2228349 [ dbSNP | Ensembl ].
VAR_047990
Natural variant32561H → Y.
Corresponds to variant rs2291827 [ dbSNP | Ensembl ].
VAR_047991
Natural variant35301R → W.
Corresponds to variant rs2270699 [ dbSNP | Ensembl ].
VAR_047992
Natural variant36321R → Q. Ref.2
Corresponds to variant rs2229493 [ dbSNP | Ensembl ].
VAR_047993
Natural variant36401V → I.
Corresponds to variant rs17459097 [ dbSNP | Ensembl ].
VAR_047994
Natural variant43311S → N.
Corresponds to variant rs3736360 [ dbSNP | Ensembl ].
VAR_047995

Experimental info

Mutagenesis41971D → I: Abolishes BMP1-mediated cleavage of endorepellin. Ref.9
Mutagenesis42581D → A: Retains proper folding. Reduced calcium ion binding. Ref.9
Mutagenesis43271N → A: Retains proper folding. Reduced calcium ion binding. Ref.9
Sequence conflict61A → P in CAA44373. Ref.2
Sequence conflict61A → P in AAA52700. Ref.1
Sequence conflict581D → Y in AAA52700. Ref.1
Sequence conflict435 – 4373TPI → APFL in CAA44373. Ref.2
Sequence conflict4501H → Q in CAA44373. Ref.2
Sequence conflict5021R → RA in CAA44373. Ref.2
Sequence conflict7931N → K in CAA44373. Ref.2
Sequence conflict890 – 8912EA → RT in AAB21121. Ref.6
Sequence conflict9091G → R in CAA44373. Ref.2
Sequence conflict9091G → R in AAB21121. Ref.6
Sequence conflict11021V → L in AAB21121. Ref.6
Sequence conflict11331R → L in AAB21121. Ref.6
Sequence conflict12221H → L in AAB21121. Ref.6
Sequence conflict14061D → G in AAA52699. Ref.7
Sequence conflict14101A → G in AAA52699. Ref.7
Sequence conflict1466 – 14705EFWRR → LNLRQ in AAA52699. Ref.7
Sequence conflict1703 – 17042SP → RG in CAA44373. Ref.2
Sequence conflict17531Q → R in CAA44373. Ref.2
Sequence conflict20381I → M in AAA52700. Ref.1
Sequence conflict20501P → Q in CAA44373. Ref.2
Sequence conflict20521P → G in AAA52700. Ref.1
Sequence conflict20931P → H in CAA44373. Ref.2
Sequence conflict26271S → R in CAA44373. Ref.2
Sequence conflict27701H → Y in CAA44373. Ref.2
Sequence conflict32411P → R in CAA44373. Ref.2
Sequence conflict34271R → Q in AAA52700. Ref.1
Sequence conflict40041S → T in CAA44373. Ref.2
Sequence conflict41351F → I in CAA44373. Ref.2
Sequence conflict43321V → I in CAA44373. Ref.2

Secondary structure

....................................... 4391
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P98160 [UniParc].

Last modified January 11, 2011. Version 4.
Checksum: C587660E24C83324

FASTA4,391468,830
        10         20         30         40         50         60 
MGWRAAGALL LALLLHGRLL AVTHGLRAYD GLSLPEDIET VTASQMRWTH SYLSDDEDML 

        70         80         90        100        110        120 
ADSISGDDLG SGDLGSGDFQ MVYFRALVNF TRSIEYSPQL EDAGSREFRE VSEAVVDTLE 

       130        140        150        160        170        180 
SEYLKIPGDQ VVSVVFIKEL DGWVFVELDV GSEGNADGAQ IQEMLLRVIS SGSVASYVTS 

       190        200        210        220        230        240 
PQGFQFRRLG TVPQFPRACT EAEFACHSYN ECVALEYRCD RRPDCRDMSD ELNCEEPVLG 

       250        260        270        280        290        300 
ISPTFSLLVE TTSLPPRPET TIMRQPPVTH APQPLLPGSV RPLPCGPQEA ACRNGHCIPR 

       310        320        330        340        350        360 
DYLCDGQEDC EDGSDELDCG PPPPCEPNEF PCGNGHCALK LWRCDGDFDC EDRTDEANCP 

       370        380        390        400        410        420 
TKRPEEVCGP TQFRCVSTNM CIPASFHCDE ESDCPDRSDE FGCMPPQVVT PPRESIQASR 

       430        440        450        460        470        480 
GQTVTFTCVA IGVPTPIINW RLNWGHIPSH PRVTVTSEGG RGTLIIRDVK ESDQGAYTCE 

       490        500        510        520        530        540 
AMNARGMVFG IPDGVLELVP QRGPCPDGHF YLEHSAACLP CFCFGITSVC QSTRRFRDQI 

       550        560        570        580        590        600 
RLRFDQPDDF KGVNVTMPAQ PGTPPLSSTQ LQIDPSLHEF QLVDLSRRFL VHDSFWALPE 

       610        620        630        640        650        660 
QFLGNKVDSY GGSLRYNVRY ELARGMLEPV QRPDVVLMGA GYRLLSRGHT PTQPGALNQR 

       670        680        690        700        710        720 
QVQFSEEHWV HESGRPVQRA ELLQVLQSLE AVLIQTVYNT KMASVGLSDI AMDTTVTHAT 

       730        740        750        760        770        780 
SHGRAHSVEE CRCPIGYSGL SCESCDAHFT RVPGGPYLGT CSGCNCNGHA SSCDPVYGHC 

       790        800        810        820        830        840 
LNCQHNTEGP QCNKCKAGFF GDAMKATATS CRPCPCPYID ASRRFSDTCF LDTDGQATCD 

       850        860        870        880        890        900 
ACAPGYTGRR CESCAPGYEG NPIQPGGKCR PVNQEIVRCD ERGSMGTSGE ACRCKNNVVG 

       910        920        930        940        950        960 
RLCNECADGS FHLSTRNPDG CLKCFCMGVS RHCTSSSWSR AQLHGASEEP GHFSLTNAAS 

       970        980        990       1000       1010       1020 
THTTNEGIFS PTPGELGFSS FHRLLSGPYF WSLPSRFLGD KVTSYGGELR FTVTQRSQPG 

      1030       1040       1050       1060       1070       1080 
STPLHGQPLV VLQGNNIILE HHVAQEPSPG QPSTFIVPFR EQAWQRPDGQ PATREHLLMA 

      1090       1100       1110       1120       1130       1140 
LAGIDTLLIR ASYAQQPAES RVSGISMDVA VPEETGQDPA LEVEQCSCPP GYRGPSCQDC 

      1150       1160       1170       1180       1190       1200 
DTGYTRTPSG LYLGTCERCS CHGHSEACEP ETGACQGCQH HTEGPRCEQC QPGYYGDAQR 

      1210       1220       1230       1240       1250       1260 
GTPQDCQLCP CYGDPAAGQA AHTCFLDTDG HPTCDACSPG HSGRHCERCA PGYYGNPSQG 

      1270       1280       1290       1300       1310       1320 
QPCQRDSQVP GPIGCNCDPQ GSVSSQCDAA GQCQCKAQVE GLTCSHCRPH HFHLSASNPD 

      1330       1340       1350       1360       1370       1380 
GCLPCFCMGI TQQCASSAYT RHLISTHFAP GDFQGFALVN PQRNSRLTGE FTVEPVPEGA 

      1390       1400       1410       1420       1430       1440 
QLSFGNFAQL GHESFYWQLP ETYQGDKVAA YGGKLRYTLS YTAGPQGSPL SDPDVQITGN 

      1450       1460       1470       1480       1490       1500 
NIMLVASQPA LQGPERRSYE IMFREEFWRR PDGQPATREH LLMALADLDE LLIRATFSSV 

      1510       1520       1530       1540       1550       1560 
PLAASISAVS LEVAQPGPSN RPRALEVEEC RCPPGYIGLS CQDCAPGYTR TGSGLYLGHC 

      1570       1580       1590       1600       1610       1620 
ELCECNGHSD LCHPETGACS QCQHNAAGEF CELCAPGYYG DATAGTPEDC QPCACPLTNP 

      1630       1640       1650       1660       1670       1680 
ENMFSRTCES LGAGGYRCTA CEPGYTGQYC EQCGPGYVGN PSVQGGQCLP ETNQAPLVVE 

      1690       1700       1710       1720       1730       1740 
VHPARSIVPQ GGSHSLRCQV SGSPPHYFYW SREDGRPVPS GTQQRHQGSE LHFPSVQPSD 

      1750       1760       1770       1780       1790       1800 
AGVYICTCRN LHQSNTSRAE LLVTEAPSKP ITVTVEEQRS QSVRPGADVT FICTAKSKSP 

      1810       1820       1830       1840       1850       1860 
AYTLVWTRLH NGKLPTRAMD FNGILTIRNV QLSDAGTYVC TGSNMFAMDQ GTATLHVQAS 

      1870       1880       1890       1900       1910       1920 
GTLSAPVVSI HPPQLTVQPG QLAEFRCSAT GSPTPTLEWT GGPGGQLPAK AQIHGGILRL 

      1930       1940       1950       1960       1970       1980 
PAVEPTDQAQ YLCRAHSSAG QQVARAVLHV HGGGGPRVQV SPERTQVHAG RTVRLYCRAA 

      1990       2000       2010       2020       2030       2040 
GVPSATITWR KEGGSLPPQA RSERTDIATL LIPAITTADA GFYLCVATSP AGTAQARIQV 

      2050       2060       2070       2080       2090       2100 
VVLSASDASP PPVKIESSSP SVTEGQTLDL NCVVAGSAHA QVTWYRRGGS LPPHTQVHGS 

      2110       2120       2130       2140       2150       2160 
RLRLPQVSPA DSGEYVCRVE NGSGPKEASI TVSVLHGTHS GPSYTPVPGS TRPIRIEPSS 

      2170       2180       2190       2200       2210       2220 
SHVAEGQTLD LNCVVPGQAH AQVTWHKRGG SLPARHQTHG SLLRLHQVTP ADSGEYVCHV 

      2230       2240       2250       2260       2270       2280 
VGTSGPLEAS VLVTIEASVI PGPIPPVRIE SSSSTVAEGQ TLDLSCVVAG QAHAQVTWYK 

      2290       2300       2310       2320       2330       2340 
RGGSLPARHQ VRGSRLYIFQ ASPADAGQYV CRASNGMEAS ITVTVTGTQG ANLAYPAGST 

      2350       2360       2370       2380       2390       2400 
QPIRIEPSSS QVAEGQTLDL NCVVPGQSHA QVTWHKRGGS LPVRHQTHGS LLRLYQASPA 

      2410       2420       2430       2440       2450       2460 
DSGEYVCRVL GSSVPLEASV LVTIEPAGSV PALGVTPTVR IESSSSQVAE GQTLDLNCLV 

      2470       2480       2490       2500       2510       2520 
AGQAHAQVTW HKRGGSLPAR HQVHGSRLRL LQVTPADSGE YVCRVVGSSG TQEASVLVTI 

      2530       2540       2550       2560       2570       2580 
QQRLSGSHSQ GVAYPVRIES SSASLANGHT LDLNCLVASQ APHTITWYKR GGSLPSRHQI 

      2590       2600       2610       2620       2630       2640 
VGSRLRIPQV TPADSGEYVC HVSNGAGSRE TSLIVTIQGS GSSHVPSVSP PIRIESSSPT 

      2650       2660       2670       2680       2690       2700 
VVEGQTLDLN CVVARQPQAI ITWYKRGGSL PSRHQTHGSH LRLHQMSVAD SGEYVCRANN 

      2710       2720       2730       2740       2750       2760 
NIDALEASIV ISVSPSAGSP SAPGSSMPIR IESSSSHVAE GETLDLNCVV PGQAHAQVTW 

      2770       2780       2790       2800       2810       2820 
HKRGGSLPSH HQTRGSRLRL HHVSPADSGE YVCRVMGSSG PLEASVLVTI EASGSSAVHV 

      2830       2840       2850       2860       2870       2880 
PAPGGAPPIR IEPSSSRVAE GQTLDLKCVV PGQAHAQVTW HKRGGNLPAR HQVHGPLLRL 

      2890       2900       2910       2920       2930       2940 
NQVSPADSGE YSCQVTGSSG TLEASVLVTI EPSSPGPIPA PGLAQPIYIE ASSSHVTEGQ 

      2950       2960       2970       2980       2990       3000 
TLDLNCVVPG QAHAQVTWYK RGGSLPARHQ THGSQLRLHL VSPADSGEYV CRAASGPGPE 

      3010       3020       3030       3040       3050       3060 
QEASFTVTVP PSEGSSYRLR SPVISIDPPS STVQQGQDAS FKCLIHDGAA PISLEWKTRN 

      3070       3080       3090       3100       3110       3120 
QELEDNVHIS PNGSIITIVG TRPSNHGTYR CVASNAYGVA QSVVNLSVHG PPTVSVLPEG 

      3130       3140       3150       3160       3170       3180 
PVWVKVGKAV TLECVSAGEP RSSARWTRIS STPAKLEQRT YGLMDSHAVL QISSAKPSDA 

      3190       3200       3210       3220       3230       3240 
GTYVCLAQNA LGTAQKQVEV IVDTGAMAPG APQVQAEEAE LTVEAGHTAT LRCSATGSPA 

      3250       3260       3270       3280       3290       3300 
PTIHWSKLRS PLPWQHRLEG DTLIIPRVAQ QDSGQYICNA TSPAGHAEAT IILHVESPPY 

      3310       3320       3330       3340       3350       3360 
ATTVPEHASV QAGETVQLQC LAHGTPPLTF QWSRVGSSLP GRATARNELL HFERAAPEDS 

      3370       3380       3390       3400       3410       3420 
GRYRCRVTNK VGSAEAFAQL LVQGPPGSLP ATSIPAGSTP TVQVTPQLET KSIGASVEFH 

      3430       3440       3450       3460       3470       3480 
CAVPSDRGTQ LRWFKEGGQL PPGHSVQDGV LRIQNLDQSC QGTYICQAHG PWGKAQASAQ 

      3490       3500       3510       3520       3530       3540 
LVIQALPSVL INIRTSVQTV VVGHAVEFEC LALGDPKPQV TWSKVGGHLR PGIVQSGGVV 

      3550       3560       3570       3580       3590       3600 
RIAHVELADA GQYRCTATNA AGTTQSHVLL LVQALPQISM PQEVRVPAGS AAVFPCIASG 

      3610       3620       3630       3640       3650       3660 
YPTPDISWSK LDGSLPPDSR LENNMLMLPS VRPQDAGTYV CTATNRQGKV KAFAHLQVPE 

      3670       3680       3690       3700       3710       3720 
RVVPYFTQTP YSFLPLPTIK DAYRKFEIKI TFRPDSADGM LLYNGQKRVP GSPTNLANRQ 

      3730       3740       3750       3760       3770       3780 
PDFISFGLVG GRPEFRFDAG SGMATIRHPT PLALGHFHTV TLLRSLTQGS LIVGDLAPVN 

      3790       3800       3810       3820       3830       3840 
GTSQGKFQGL DLNEELYLGG YPDYGAIPKA GLSSGFIGCV RELRIQGEEI VFHDLNLTAH 

      3850       3860       3870       3880       3890       3900 
GISHCPTCRD RPCQNGGQCH DSESSSYVCV CPAGFTGSRC EHSQALHCHP EACGPDATCV 

      3910       3920       3930       3940       3950       3960 
NRPDGRGYTC RCHLGRSGLR CEEGVTVTTP SLSGAGSYLA LPALTNTHHE LRLDVEFKPL 

      3970       3980       3990       4000       4010       4020 
APDGVLLFSG GKSGPVEDFV SLAMVGGHLE FRYELGSGLA VLRSAEPLAL GRWHRVSAER 

      4030       4040       4050       4060       4070       4080 
LNKDGSLRVN GGRPVLRSSP GKSQGLNLHT LLYLGGVEPS VPLSPATNMS AHFRGCVGEV 

      4090       4100       4110       4120       4130       4140 
SVNGKRLDLT YSFLGSQGIG QCYDSSPCER QPCQHGATCM PAGEYEFQCL CRDGFKGDLC 

      4150       4160       4170       4180       4190       4200 
EHEENPCQLR EPCLHGGTCQ GTRCLCLPGF SGPRCQQGSG HGIAESDWHL EGSGGNDAPG 

      4210       4220       4230       4240       4250       4260 
QYGAYFHDDG FLAFPGHVFS RSLPEVPETI ELEVRTSTAS GLLLWQGVEV GEAGQGKDFI 

      4270       4280       4290       4300       4310       4320 
SLGLQDGHLV FRYQLGSGEA RLVSEDPIND GEWHRVTALR EGRRGSIQVD GEELVSGRSP 

      4330       4340       4350       4360       4370       4380 
GPNVAVNAKG SVYIGGAPDV ATLTGGRFSS GITGCVKNLV LHSARPGAPP PQPLDLQHRA 

      4390 
QAGANTRPCP S 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA38096.
RefSeqNP_005520.4. NM_005529.5.
UniGeneHs.562227.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3SH4X-ray1.50A4197-4391[»]
3SH5X-ray2.80A4197-4391[»]
ProteinModelPortalP98160.
SMRP98160. Positions 1770-1858, 4197-4391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109571. 17 interactions.
IntActP98160. 10 interactions.
MINTMINT-123304.
STRING9606.ENSP00000363827.

Chemistry

DrugBankDB00102. Becaplermin.
DB00039. Palifermin.

PTM databases

PhosphoSiteP98160.

Polymorphism databases

DMDM317373536.

2D gel databases

DOSAC-COBS-2DPAGEP98160.

Proteomic databases

PaxDbP98160.
PRIDEP98160.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374695; ENSP00000363827; ENSG00000142798.
GeneID3339.
KEGGhsa:3339.
UCSCuc001bfj.3. human.

Organism-specific databases

CTD3339.
GeneCardsGC01M022148.
H-InvDBHIX0023554.
HIX0023598.
HGNCHGNC:5273. HSPG2.
HPACAB009820.
CAB020718.
HPA018892.
MIM142461. gene.
224410. phenotype.
255800. phenotype.
neXtProtNX_P98160.
Orphanet1865. Dyssegmental dysplasia, Silverman-Handmaker type.
800. Schwartz-Jampel syndrome.
PharmGKBPA29537.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258321.
HOGENOMHOG000049276.
HOVERGENHBG008174.
InParanoidP98160.
KOK06255.
OMARQCTSSS.
OrthoDBEOG7BGHJZ.
PhylomeDBP98160.
TreeFamTF326548.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP98160.
BgeeP98160.
CleanExHS_HSPG2.
GenevestigatorP98160.

Family and domain databases

Gene3D2.60.120.200. 3 hits.
2.60.40.10. 22 hits.
4.10.400.10. 4 hits.
InterProIPR008985. 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]
PfamPF00008. 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]
PRINTSPR00261. LDLRECEPTOR.
SMARTSM00181. 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]
SUPFAMSSF49899. SSF49899. 3 hits.
SSF57424. SSF57424. 4 hits.
PROSITEPS00022. 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]
ProtoNetSearch...

Other

ChiTaRSHSPG2. human.
GeneWikiPerlecan.
GenomeRNAi3339.
NextBio13216.
PROP98160.
SOURCESearch...

Entry information

Entry namePGBM_HUMAN
AccessionPrimary (citable) accession number: P98160
Secondary accession number(s): Q16287, Q5SZI3, Q9H3V5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 165 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM