UniProtKB - P98160 (PGBM_HUMAN)
Protein
Basement membrane-specific heparan sulfate proteoglycan core protein
Gene
HSPG2
Organism
Homo sapiens (Human)
Status
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.
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.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 4258 | Calcium | 1 | |
Metal bindingi | 4275 | Calcium; via carbonyl oxygen | 1 | |
Metal bindingi | 4325 | Calcium; via carbonyl oxygen | 1 | |
Metal bindingi | 4327 | Calcium | 1 |
GO - Molecular functioni
- amyloid-beta binding Source: ARUK-UCL
- calcium ion binding Source: InterPro
- extracellular matrix structural constituent conferring compression resistance Source: BHF-UCL
- integrin binding Source: ARUK-UCL
- low-density lipoprotein particle receptor binding Source: ARUK-UCL
- protein C-terminus binding Source: UniProtKB
GO - Biological processi
- angiogenesis Source: UniProtKB-KW
- animal organ morphogenesis Source: GO_Central
- brain development Source: ARUK-UCL
- cell differentiation Source: ARUK-UCL
- cellular protein metabolic process Source: Reactome
- circulatory system development Source: ARUK-UCL
- extracellular matrix organization Source: Reactome
- glycosaminoglycan biosynthetic process Source: Reactome
- glycosaminoglycan catabolic process Source: Reactome
- inflammatory response Source: ARUK-UCL
- lipid metabolic process Source: ARUK-UCL
- negative regulation of amyloid fibril formation Source: ARUK-UCL
- negative regulation of angiogenesis Source: ARUK-UCL
- negative regulation of cell death Source: ARUK-UCL
- receptor-mediated endocytosis Source: ARUK-UCL
- retinoid metabolic process Source: Reactome
- tissue development Source: GO_Central
Keywordsi
Biological process | Angiogenesis |
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
PathwayCommonsi | P98160 |
Reactomei | R-HSA-1474228, Degradation of the extracellular matrix R-HSA-1971475, A tetrasaccharide linker sequence is required for GAG synthesis R-HSA-2022928, HS-GAG biosynthesis R-HSA-2024096, HS-GAG degradation R-HSA-216083, Integrin cell surface interactions R-HSA-3000157, Laminin interactions R-HSA-3000171, Non-integrin membrane-ECM interactions R-HSA-3000178, ECM proteoglycans R-HSA-3560783, Defective B4GALT7 causes EDS, progeroid type R-HSA-3560801, Defective B3GAT3 causes JDSSDHD R-HSA-3656237, Defective EXT2 causes exostoses 2 R-HSA-3656253, Defective EXT1 causes exostoses 1, TRPS2 and CHDS R-HSA-4420332, Defective B3GALT6 causes EDSP2 and SEMDJL1 R-HSA-975634, Retinoid metabolism and transport R-HSA-977225, Amyloid fiber formation |
SIGNORi | P98160 |
Names & Taxonomyi
Protein namesi | Recommended name: Basement membrane-specific heparan sulfate proteoglycan core proteinShort name: HSPG Alternative name(s): Perlecan Short name: PLC Cleaved into the following 2 chains: |
Gene namesi | Name:HSPG2 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:5273, HSPG2 |
MIMi | 142461, gene |
neXtProti | NX_P98160 |
VEuPathDBi | HostDB:ENSG00000142798.17 |
Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- basement membrane Source: GO_Central
- collagen-containing extracellular matrix Source: UniProtKB
- extracellular exosome Source: UniProtKB
- extracellular region Source: BHF-UCL
- extracellular space Source: UniProtKB
Golgi apparatus
- Golgi lumen Source: Reactome
Lysosome
- lysosomal lumen Source: Reactome
Plasma Membrane
- plasma membrane Source: Reactome
- plasma membrane protein complex Source: ARUK-UCL
Other locations
- focal adhesion Source: UniProtKB
Keywords - Cellular componenti
Basement membrane, Extracellular matrix, SecretedPathology & Biotechi
Involvement in diseasei
Schwartz-Jampel syndrome (SJS1)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionRare 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.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_014122 | 1532 | C → Y in SJS1. 1 PublicationCorresponds to variant dbSNP:rs137853248EnsemblClinVar. | 1 |
Dyssegmental dysplasia Silverman-Handmaker type (DDSH)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionThe 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.
Related information in OMIMMutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 4197 | D → I: Abolishes BMP1-mediated cleavage of endorepellin. 1 Publication | 1 | |
Mutagenesisi | 4258 | D → A: Retains proper folding. Reduced calcium ion binding. 1 Publication | 1 | |
Mutagenesisi | 4327 | N → A: Retains proper folding. Reduced calcium ion binding. 1 Publication | 1 |
Keywords - Diseasei
Disease variantOrganism-specific databases
DisGeNETi | 3339 |
MalaCardsi | HSPG2 |
MIMi | 224410, phenotype 255800, phenotype |
OpenTargetsi | ENSG00000142798 |
Orphaneti | 1865, Dyssegmental dysplasia, Silverman-Handmaker type 800, Schwartz-Jampel syndrome |
PharmGKBi | PA29537 |
Miscellaneous databases
Pharosi | P98160, Tbio |
Chemistry databases
DrugBanki | DB00039, Palifermin |
Genetic variation databases
BioMutai | HSPG2 |
DMDMi | 317373536 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 21 | Sequence analysisAdd BLAST | 21 | |
ChainiPRO_0000026696 | 22 – 4391 | Basement membrane-specific heparan sulfate proteoglycan core proteinAdd BLAST | 4370 | |
ChainiPRO_0000391621 | 3687 – 4391 | EndorepellinAdd BLAST | 705 | |
ChainiPRO_0000391622 | 4197 – 4391 | LG3 peptideAdd BLAST | 195 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 42 | O-linked (GalNAc...) threonine1 Publication | 1 | |
Glycosylationi | 65 | O-linked (Xyl...) (heparan sulfate) serineSequence analysis | 1 | |
Glycosylationi | 71 | O-linked (Xyl...) (heparan sulfate) serineSequence analysis | 1 | |
Glycosylationi | 76 | O-linked (Xyl...) (heparan sulfate) serineSequence analysis | 1 | |
Glycosylationi | 89 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 199 ↔ 212 | By similarity | ||
Disulfide bondi | 206 ↔ 225 | By similarity | ||
Disulfide bondi | 219 ↔ 234 | By similarity | ||
Disulfide bondi | 285 ↔ 297 | By similarity | ||
Disulfide bondi | 292 ↔ 310 | By similarity | ||
Disulfide bondi | 304 ↔ 319 | By similarity | ||
Disulfide bondi | 325 ↔ 337 | By similarity | ||
Disulfide bondi | 332 ↔ 350 | By similarity | ||
Disulfide bondi | 344 ↔ 359 | By similarity | ||
Disulfide bondi | 368 ↔ 381 | By similarity | ||
Disulfide bondi | 375 ↔ 394 | By similarity | ||
Disulfide bondi | 388 ↔ 403 | By similarity | ||
Glycosylationi | 554 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 764 ↔ 773 | By similarity | ||
Disulfide bondi | 766 ↔ 780 | By similarity | ||
Disulfide bondi | 783 ↔ 792 | By similarity | ||
Disulfide bondi | 795 ↔ 811 | By similarity | ||
Disulfide bondi | 814 ↔ 829 | By similarity | ||
Disulfide bondi | 816 ↔ 839 | By similarity | ||
Disulfide bondi | 842 ↔ 851 | By similarity | ||
Disulfide bondi | 854 ↔ 869 | By similarity | ||
Disulfide bondi | 879 ↔ 892 | By similarity | ||
Disulfide bondi | 894 ↔ 903 | By similarity | ||
Disulfide bondi | 906 ↔ 921 | By similarity | ||
Disulfide bondi | 1159 ↔ 1168 | By similarity | ||
Disulfide bondi | 1161 ↔ 1175 | By similarity | ||
Disulfide bondi | 1178 ↔ 1187 | By similarity | ||
Disulfide bondi | 1190 ↔ 1206 | By similarity | ||
Disulfide bondi | 1209 ↔ 1224 | By similarity | ||
Disulfide bondi | 1211 ↔ 1234 | By similarity | ||
Disulfide bondi | 1237 ↔ 1246 | By similarity | ||
Disulfide bondi | 1249 ↔ 1263 | By similarity | ||
Disulfide bondi | 1275 ↔ 1287 | By similarity | ||
Disulfide bondi | 1277 ↔ 1293 | By similarity | ||
Disulfide bondi | 1295 ↔ 1304 | By similarity | ||
Disulfide bondi | 1307 ↔ 1322 | By similarity | ||
Disulfide bondi | 1563 ↔ 1572 | By similarity | ||
Disulfide bondi | 1565 ↔ 1579 | By similarity | ||
Disulfide bondi | 1582 ↔ 1591 | By similarity | ||
Disulfide bondi | 1594 ↔ 1610 | By similarity | ||
Disulfide bondi | 1613 ↔ 1628 | By similarity | ||
Disulfide bondi | 1615 ↔ 1638 | By similarity | ||
Disulfide bondi | 1641 ↔ 1650 | By similarity | ||
Disulfide bondi | 1653 ↔ 1668 | By similarity | ||
Glycosylationi | 1755 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Glycosylationi | 2121 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 2995 | O-linked (Xyl...) (chondroitin sulfate) serineSequence analysis | 1 | |
Glycosylationi | 3072 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 3105 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3279 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3780 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 3819 ↔ 3845 | By similarity | ||
Glycosylationi | 3836 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 3848 ↔ 3859 | By similarity | ||
Disulfide bondi | 3853 ↔ 3869 | By similarity | ||
Disulfide bondi | 3871 ↔ 3880 | By similarity | ||
Disulfide bondi | 3888 ↔ 3899 | By similarity | ||
Disulfide bondi | 3893 ↔ 3910 | By similarity | ||
Disulfide bondi | 3912 ↔ 3921 | By similarity | ||
Glycosylationi | 3933 | O-linked (Xyl...) (chondroitin sulfate) serineSequence analysis | 1 | |
Glycosylationi | 4068 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 4076 ↔ 4102 | By similarity | ||
Disulfide bondi | 4108 ↔ 4119 | By similarity | ||
Disulfide bondi | 4113 ↔ 4129 | By similarity | ||
Disulfide bondi | 4131 ↔ 4140 | By similarity | ||
Disulfide bondi | 4147 ↔ 4159 | By similarity | ||
Disulfide bondi | 4153 ↔ 4164 | By similarity | ||
Disulfide bondi | 4166 ↔ 4175 | By similarity | ||
Glycosylationi | 4179 | O-linked (Xyl...) (chondroitin sulfate) serineSequence analysis | 1 | |
Disulfide bondi | 4355 ↔ 4389 | 1 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
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 4196 – 4197 | Cleavage; by BMP1 | 2 |
Keywords - PTMi
Disulfide bond, Glycoprotein, Heparan sulfate, ProteoglycanProteomic databases
EPDi | P98160 |
jPOSTi | P98160 |
MassIVEi | P98160 |
MaxQBi | P98160 |
PaxDbi | P98160 |
PeptideAtlasi | P98160 |
PRIDEi | P98160 |
ProteomicsDBi | 57796 |
2D gel databases
DOSAC-COBS-2DPAGEi | P98160 |
PTM databases
CarbonylDBi | P98160 |
GlyConnecti | 653, 43 N-Linked glycans (5 sites), 2 O-Linked glycans (2 sites) |
GlyGeni | P98160, 54 sites, 1 N-linked glycan (1 site), 7 O-linked glycans (35 sites) |
iPTMneti | P98160 |
PhosphoSitePlusi | P98160 |
Expressioni
Tissue specificityi
Found in the basement membranes.
Gene expression databases
Bgeei | ENSG00000142798, Expressed in fundus of stomach and 231 other tissues |
ExpressionAtlasi | P98160, baseline and differential |
Genevisiblei | P98160, HS |
Organism-specific databases
HPAi | ENSG00000142798, Tissue enhanced (smooth) |
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 PublicationsBinary interactionsi
Hide detailsP98160
With | #Exp. | IntAct |
---|---|---|
KDR [P35968] | 5 | EBI-947664,EBI-1005487 |
Endorepellin (PRO_0000391621)
With | #Exp. | IntAct |
---|---|---|
FLT1 - isoform 2 [P17948-2] | 2 | EBI-6896259,EBI-6530464 |
KDR [P35968] | 2 | EBI-6896259,EBI-1005487 |
LG3 peptide (PRO_0000391622)
With | #Exp. | IntAct |
---|---|---|
FLT1 - isoform 2 [P17948-2] | 2 | EBI-6896607,EBI-6530464 |
KDR [P35968] | 2 | EBI-6896607,EBI-1005487 |
GO - Molecular functioni
- integrin binding Source: ARUK-UCL
- low-density lipoprotein particle receptor binding Source: ARUK-UCL
- protein C-terminus binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 109571, 43 interactors |
IntActi | P98160, 35 interactors |
MINTi | P98160 |
STRINGi | 9606.ENSP00000363827 |
Miscellaneous databases
RNActi | P98160, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P98160 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 80 – 191 | SEAPROSITE-ProRule annotationAdd BLAST | 112 | |
Domaini | 198 – 235 | LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 284 – 320 | LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 324 – 360 | LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 367 – 404 | LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 405 – 504 | Ig-like C2-type 1Add BLAST | 100 | |
Domaini | 521 – 530 | Laminin EGF-like 1; first partPROSITE-ProRule annotation | 10 | |
Domaini | 538 – 730 | Laminin IV type A 1PROSITE-ProRule annotationAdd BLAST | 193 | |
Domaini | 731 – 763 | Laminin EGF-like 1; second partPROSITE-ProRule annotationAdd BLAST | 33 | |
Domaini | 764 – 813 | Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST | 50 | |
Domaini | 814 – 871 | Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST | 58 | |
Domaini | 879 – 923 | Laminin EGF-like 4; truncatedPROSITE-ProRule annotationAdd BLAST | 45 | |
Domaini | 924 – 933 | Laminin EGF-like 5; first partPROSITE-ProRule annotation | 10 | |
Domaini | 941 – 1125 | Laminin IV type A 2PROSITE-ProRule annotationAdd BLAST | 185 | |
Domaini | 1126 – 1158 | Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd BLAST | 33 | |
Domaini | 1159 – 1208 | Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST | 50 | |
Domaini | 1209 – 1265 | Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST | 57 | |
Domaini | 1275 – 1324 | Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST | 50 | |
Domaini | 1325 – 1334 | Laminin EGF-like 9; first partPROSITE-ProRule annotation | 10 | |
Domaini | 1344 – 1529 | Laminin IV type A 3PROSITE-ProRule annotationAdd BLAST | 186 | |
Domaini | 1530 – 1562 | Laminin EGF-like 9; second partPROSITE-ProRule annotationAdd BLAST | 33 | |
Domaini | 1563 – 1612 | Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST | 50 | |
Domaini | 1613 – 1670 | Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST | 58 | |
Domaini | 1677 – 1771 | Ig-like C2-type 2Add BLAST | 95 | |
Domaini | 1772 – 1865 | Ig-like C2-type 3Add BLAST | 94 | |
Domaini | 1866 – 1955 | Ig-like C2-type 4Add BLAST | 90 | |
Domaini | 1956 – 2051 | Ig-like C2-type 5Add BLAST | 96 | |
Domaini | 2052 – 2151 | Ig-like C2-type 6Add BLAST | 100 | |
Domaini | 2152 – 2244 | Ig-like C2-type 7Add BLAST | 93 | |
Domaini | 2245 – 2340 | Ig-like C2-type 8Add BLAST | 96 | |
Domaini | 2341 – 2436 | Ig-like C2-type 9Add BLAST | 96 | |
Domaini | 2437 – 2533 | Ig-like C2-type 10Add BLAST | 97 | |
Domaini | 2534 – 2629 | Ig-like C2-type 11Add BLAST | 96 | |
Domaini | 2630 – 2726 | Ig-like C2-type 12Add BLAST | 97 | |
Domaini | 2727 – 2826 | Ig-like C2-type 13Add BLAST | 100 | |
Domaini | 2827 – 2924 | Ig-like C2-type 14Add BLAST | 98 | |
Domaini | 2925 – 3021 | Ig-like C2-type 15Add BLAST | 97 | |
Domaini | 3022 – 3112 | Ig-like C2-type 16Add BLAST | 91 | |
Domaini | 3113 – 3211 | Ig-like C2-type 17Add BLAST | 99 | |
Domaini | 3212 – 3298 | Ig-like C2-type 18Add BLAST | 87 | |
Domaini | 3299 – 3399 | Ig-like C2-type 19Add BLAST | 101 | |
Domaini | 3400 – 3488 | Ig-like C2-type 20Add BLAST | 89 | |
Domaini | 3489 – 3574 | Ig-like C2-type 21Add BLAST | 86 | |
Domaini | 3575 – 3662 | Ig-like C2-type 22Add BLAST | 88 | |
Domaini | 3663 – 3843 | Laminin G-like 1PROSITE-ProRule annotationAdd BLAST | 181 | |
Domaini | 3844 – 3881 | EGF-like 1PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 3884 – 3922 | EGF-like 2PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 3928 – 4103 | Laminin G-like 2PROSITE-ProRule annotationAdd BLAST | 176 | |
Domaini | 4104 – 4141 | EGF-like 3PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 4143 – 4176 | EGF-like 4PROSITE-ProRule annotationAdd BLAST | 34 | |
Domaini | 4201 – 4389 | Laminin G-like 3PROSITE-ProRule annotationAdd BLAST | 189 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 4149 – 4151 | Mediates motor neuron attachmentSequence analysis | 3 | |
Regioni | 4299 – 4301 | Mediates motor neuron attachmentSequence analysis | 3 |
Keywords - Domaini
EGF-like domain, Immunoglobulin domain, Laminin EGF-like domain, Repeat, SignalPhylogenomic databases
eggNOGi | KOG3509, Eukaryota |
GeneTreei | ENSGT00940000156670 |
HOGENOMi | CLU_000078_1_0_1 |
InParanoidi | P98160 |
OMAi | CDERGSM |
OrthoDBi | 414294at2759 |
PhylomeDBi | P98160 |
TreeFami | TF326548 |
Family and domain databases
CDDi | cd00112, LDLa, 4 hits |
Gene3Di | 2.60.40.10, 22 hits 4.10.400.10, 4 hits |
InterProi | View protein in InterPro IPR013320, ConA-like_dom_sf IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR007110, Ig-like_dom IPR036179, Ig-like_dom_sf IPR013783, Ig-like_fold IPR013098, Ig_I-set IPR003599, Ig_sub IPR003598, Ig_sub2 IPR013106, Ig_V-set IPR002049, Laminin_EGF IPR001791, Laminin_G IPR000034, Laminin_IV IPR036055, LDL_receptor-like_sf IPR023415, LDLR_class-A_CS IPR002172, LDrepeatLR_classA_rpt IPR000082, SEA_dom |
Pfami | View protein in Pfam PF00008, EGF, 2 hits PF07679, I-set, 9 hits PF13895, Ig_2, 1 hit PF00052, Laminin_B, 3 hits PF00053, Laminin_EGF, 9 hits PF00054, Laminin_G_1, 3 hits PF00057, Ldl_recept_a, 4 hits |
PRINTSi | PR00261, LDLRECEPTOR |
SMARTi | View protein in SMART SM00181, EGF, 11 hits SM00179, EGF_CA, 5 hits SM00180, EGF_Lam, 9 hits SM00409, IG, 22 hits SM00408, IGc2, 22 hits SM00406, IGv, 8 hits SM00281, LamB, 3 hits SM00282, LamG, 3 hits SM00192, LDLa, 4 hits SM00200, SEA, 1 hit |
SUPFAMi | SSF48726, SSF48726, 22 hits SSF49899, SSF49899, 3 hits SSF57424, SSF57424, 4 hits |
PROSITEi | View protein in PROSITE 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 |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 5 potential isoforms that are computationally mapped.Show allAlign All
P98160-1 [UniParc]FASTAAdd to basket
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
Computationally mapped potential isoform sequencesi
There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A3B3IT11 | A0A3B3IT11_HUMAN | Basement membrane-specific heparan ... | HSPG2 | 288 | Annotation score: | ||
A0A0U1RQT3 | A0A0U1RQT3_HUMAN | Basement membrane-specific heparan ... | HSPG2 | 307 | Annotation score: | ||
H0Y5A9 | H0Y5A9_HUMAN | Basement membrane-specific heparan ... | HSPG2 | 197 | Annotation score: | ||
A0A2R8YH07 | A0A2R8YH07_HUMAN | Basement membrane-specific heparan ... | HSPG2 | 236 | Annotation score: | ||
H7BYA5 | H7BYA5_HUMAN | Basement membrane-specific heparan ... | HSPG2 | 109 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 6 | A → P in CAA44373 (PubMed:1730768).Curated | 1 | |
Sequence conflicti | 6 | A → P in AAA52700 (PubMed:1569102).Curated | 1 | |
Sequence conflicti | 58 | D → Y in AAA52700 (PubMed:1569102).Curated | 1 | |
Sequence conflicti | 435 – 437 | TPI → APFL in CAA44373 (PubMed:1730768).Curated | 3 | |
Sequence conflicti | 450 | H → Q in CAA44373 (PubMed:1730768).Curated | 1 | |
Sequence conflicti | 502 | R → RA in CAA44373 (PubMed:1730768).Curated | 1 | |
Sequence conflicti | 793 | N → K in CAA44373 (PubMed:1730768).Curated | 1 | |
Sequence conflicti | 890 – 891 | EA → RT in AAB21121 (PubMed:1685141).Curated | 2 | |
Sequence conflicti | 909 | G → R in CAA44373 (PubMed:1730768).Curated | 1 | |
Sequence conflicti | 909 | G → R in AAB21121 (PubMed:1685141).Curated | 1 | |
Sequence conflicti | 1102 | V → L in AAB21121 (PubMed:1685141).Curated | 1 | |
Sequence conflicti | 1133 | R → L in AAB21121 (PubMed:1685141).Curated | 1 | |
Sequence conflicti | 1222 | H → L in AAB21121 (PubMed:1685141).Curated | 1 | |
Sequence conflicti | 1406 | D → G in AAA52699 (PubMed:1679749).Curated | 1 | |
Sequence conflicti | 1410 | A → G in AAA52699 (PubMed:1679749).Curated | 1 | |
Sequence conflicti | 1466 – 1470 | EFWRR → LNLRQ in AAA52699 (PubMed:1679749).Curated | 5 | |
Sequence conflicti | 1703 – 1704 | SP → RG in CAA44373 (PubMed:1730768).Curated | 2 | |
Sequence conflicti | 1753 | Q → R in CAA44373 (PubMed:1730768).Curated | 1 | |
Sequence conflicti | 2038 | I → M in AAA52700 (PubMed:1569102).Curated | 1 | |
Sequence conflicti | 2050 | P → Q in CAA44373 (PubMed:1730768).Curated | 1 | |
Sequence conflicti | 2052 | P → G in AAA52700 (PubMed:1569102).Curated | 1 | |
Sequence conflicti | 2093 | P → H in CAA44373 (PubMed:1730768).Curated | 1 | |
Sequence conflicti | 2627 | S → R in CAA44373 (PubMed:1730768).Curated | 1 | |
Sequence conflicti | 2770 | H → Y in CAA44373 (PubMed:1730768).Curated | 1 | |
Sequence conflicti | 3241 | P → R in CAA44373 (PubMed:1730768).Curated | 1 | |
Sequence conflicti | 3427 | R → Q in AAA52700 (PubMed:1569102).Curated | 1 | |
Sequence conflicti | 4004 | S → T in CAA44373 (PubMed:1730768).Curated | 1 | |
Sequence conflicti | 4135 | F → I in CAA44373 (PubMed:1730768).Curated | 1 | |
Sequence conflicti | 4332 | V → I in CAA44373 (PubMed:1730768).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_047979 | 68 | D → E. Corresponds to variant dbSNP:rs1869780EnsemblClinVar. | 1 | |
Natural variantiVAR_057051 | 303 | L → H. Corresponds to variant dbSNP:rs17460381Ensembl. | 1 | |
Natural variantiVAR_047980 | 638 | M → V3 PublicationsCorresponds to variant dbSNP:rs1874792EnsemblClinVar. | 1 | |
Natural variantiVAR_047981 | 765 | N → S3 PublicationsCorresponds to variant dbSNP:rs989994EnsemblClinVar. | 1 | |
Natural variantiVAR_047982 | 1186 | R → Q. Corresponds to variant dbSNP:rs2229481EnsemblClinVar. | 1 | |
Natural variantiVAR_057052 | 1323 | L → V. Corresponds to variant dbSNP:rs10917058EnsemblClinVar. | 1 | |
Natural variantiVAR_047983 | 1503 | A → V3 PublicationsCorresponds to variant dbSNP:rs897471EnsemblClinVar. | 1 | |
Natural variantiVAR_014122 | 1532 | C → Y in SJS1. 1 PublicationCorresponds to variant dbSNP:rs137853248EnsemblClinVar. | 1 | |
Natural variantiVAR_047984 | 1758 | R → Q. Corresponds to variant dbSNP:rs2229483Ensembl. | 1 | |
Natural variantiVAR_047985 | 1919 | R → C. Corresponds to variant dbSNP:rs2229474EnsemblClinVar. | 1 | |
Natural variantiVAR_047986 | 1967 | V → I. Corresponds to variant dbSNP:rs2229475EnsemblClinVar. | 1 | |
Natural variantiVAR_047987 | 2980 | L → H1 PublicationCorresponds to variant dbSNP:rs2229489EnsemblClinVar. | 1 | |
Natural variantiVAR_047988 | 2981 | V → I. Corresponds to variant dbSNP:rs2229490EnsemblClinVar. | 1 | |
Natural variantiVAR_047989 | 2995 | S → G1 PublicationCorresponds to variant dbSNP:rs2229491EnsemblClinVar. | 1 | |
Natural variantiVAR_047990 | 3168 | A → T1 PublicationCorresponds to variant dbSNP:rs2228349EnsemblClinVar. | 1 | |
Natural variantiVAR_047991 | 3256 | H → Y. Corresponds to variant dbSNP:rs2291827EnsemblClinVar. | 1 | |
Natural variantiVAR_047992 | 3530 | R → W. Corresponds to variant dbSNP:rs2270699EnsemblClinVar. | 1 | |
Natural variantiVAR_047993 | 3632 | R → Q1 PublicationCorresponds to variant dbSNP:rs2229493EnsemblClinVar. | 1 | |
Natural variantiVAR_047994 | 3640 | V → I. Corresponds to variant dbSNP:rs17459097EnsemblClinVar. | 1 | |
Natural variantiVAR_047995 | 4331 | S → N. Corresponds to variant dbSNP:rs3736360EnsemblClinVar. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M85289 mRNA Translation: AAA52700.1 X62515 mRNA Translation: CAA44373.1 AL590556 Genomic DNA No translation available. AL590103 Genomic DNA No translation available. 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 |
Genome annotation databases
Ensembli | ENST00000374695; ENSP00000363827; ENSG00000142798 |
GeneIDi | 3339 |
KEGGi | hsa:3339 |
UCSCi | uc001bfj.4, human |
Similar proteinsi
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 Genomic DNA No translation available. AL590103 Genomic DNA No translation available. 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 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3SH4 | X-ray | 1.50 | A | 4197-4391 | [»] | |
3SH5 | X-ray | 2.80 | A | 4197-4391 | [»] | |
SMRi | P98160 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 109571, 43 interactors |
IntActi | P98160, 35 interactors |
MINTi | P98160 |
STRINGi | 9606.ENSP00000363827 |
Chemistry databases
DrugBanki | DB00039, Palifermin |
PTM databases
CarbonylDBi | P98160 |
GlyConnecti | 653, 43 N-Linked glycans (5 sites), 2 O-Linked glycans (2 sites) |
GlyGeni | P98160, 54 sites, 1 N-linked glycan (1 site), 7 O-linked glycans (35 sites) |
iPTMneti | P98160 |
PhosphoSitePlusi | P98160 |
Genetic variation databases
BioMutai | HSPG2 |
DMDMi | 317373536 |
2D gel databases
DOSAC-COBS-2DPAGEi | P98160 |
Proteomic databases
EPDi | P98160 |
jPOSTi | P98160 |
MassIVEi | P98160 |
MaxQBi | P98160 |
PaxDbi | P98160 |
PeptideAtlasi | P98160 |
PRIDEi | P98160 |
ProteomicsDBi | 57796 |
Protocols and materials databases
Antibodypediai | 980, 467 antibodies |
Genome annotation databases
Ensembli | ENST00000374695; ENSP00000363827; ENSG00000142798 |
GeneIDi | 3339 |
KEGGi | hsa:3339 |
UCSCi | uc001bfj.4, human |
Organism-specific databases
CTDi | 3339 |
DisGeNETi | 3339 |
GeneCardsi | HSPG2 |
HGNCi | HGNC:5273, HSPG2 |
HPAi | ENSG00000142798, Tissue enhanced (smooth) |
MalaCardsi | HSPG2 |
MIMi | 142461, gene 224410, phenotype 255800, phenotype |
neXtProti | NX_P98160 |
OpenTargetsi | ENSG00000142798 |
Orphaneti | 1865, Dyssegmental dysplasia, Silverman-Handmaker type 800, Schwartz-Jampel syndrome |
PharmGKBi | PA29537 |
VEuPathDBi | HostDB:ENSG00000142798.17 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3509, Eukaryota |
GeneTreei | ENSGT00940000156670 |
HOGENOMi | CLU_000078_1_0_1 |
InParanoidi | P98160 |
OMAi | CDERGSM |
OrthoDBi | 414294at2759 |
PhylomeDBi | P98160 |
TreeFami | TF326548 |
Enzyme and pathway databases
PathwayCommonsi | P98160 |
Reactomei | R-HSA-1474228, Degradation of the extracellular matrix R-HSA-1971475, A tetrasaccharide linker sequence is required for GAG synthesis R-HSA-2022928, HS-GAG biosynthesis R-HSA-2024096, HS-GAG degradation R-HSA-216083, Integrin cell surface interactions R-HSA-3000157, Laminin interactions R-HSA-3000171, Non-integrin membrane-ECM interactions R-HSA-3000178, ECM proteoglycans R-HSA-3560783, Defective B4GALT7 causes EDS, progeroid type R-HSA-3560801, Defective B3GAT3 causes JDSSDHD R-HSA-3656237, Defective EXT2 causes exostoses 2 R-HSA-3656253, Defective EXT1 causes exostoses 1, TRPS2 and CHDS R-HSA-4420332, Defective B3GALT6 causes EDSP2 and SEMDJL1 R-HSA-975634, Retinoid metabolism and transport R-HSA-977225, Amyloid fiber formation |
SIGNORi | P98160 |
Miscellaneous databases
BioGRID-ORCSi | 3339, 2 hits in 868 CRISPR screens |
ChiTaRSi | HSPG2, human |
GeneWikii | Perlecan |
GenomeRNAii | 3339 |
Pharosi | P98160, Tbio |
PROi | PR:P98160 |
RNActi | P98160, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000142798, Expressed in fundus of stomach and 231 other tissues |
ExpressionAtlasi | P98160, baseline and differential |
Genevisiblei | P98160, HS |
Family and domain databases
CDDi | cd00112, LDLa, 4 hits |
Gene3Di | 2.60.40.10, 22 hits 4.10.400.10, 4 hits |
InterProi | View protein in InterPro IPR013320, ConA-like_dom_sf IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR007110, Ig-like_dom IPR036179, Ig-like_dom_sf IPR013783, Ig-like_fold IPR013098, Ig_I-set IPR003599, Ig_sub IPR003598, Ig_sub2 IPR013106, Ig_V-set IPR002049, Laminin_EGF IPR001791, Laminin_G IPR000034, Laminin_IV IPR036055, LDL_receptor-like_sf IPR023415, LDLR_class-A_CS IPR002172, LDrepeatLR_classA_rpt IPR000082, SEA_dom |
Pfami | View protein in Pfam PF00008, EGF, 2 hits PF07679, I-set, 9 hits PF13895, Ig_2, 1 hit PF00052, Laminin_B, 3 hits PF00053, Laminin_EGF, 9 hits PF00054, Laminin_G_1, 3 hits PF00057, Ldl_recept_a, 4 hits |
PRINTSi | PR00261, LDLRECEPTOR |
SMARTi | View protein in SMART SM00181, EGF, 11 hits SM00179, EGF_CA, 5 hits SM00180, EGF_Lam, 9 hits SM00409, IG, 22 hits SM00408, IGc2, 22 hits SM00406, IGv, 8 hits SM00281, LamB, 3 hits SM00282, LamG, 3 hits SM00192, LDLa, 4 hits SM00200, SEA, 1 hit |
SUPFAMi | SSF48726, SSF48726, 22 hits SSF49899, SSF49899, 3 hits SSF57424, SSF57424, 4 hits |
PROSITEi | View protein in PROSITE 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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PGBM_HUMAN | |
Accessioni | P98160Primary (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: | February 10, 2021 | |
This is version 232 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references