HSPG2

This gene encodes the perlecan protein, which consists of a core protein to which three long chains of glycosaminoglycans (heparan sulfate or chondroitin sulfate) are attached. The perlecan protein is a large multidomain proteoglycan that binds to and cross-links many extracellular matrix components and cell-surface molecules. It has been shown that this protein interacts with laminin, prolargin, collagen type IV, FGFBP1, FBLN2, FGF7 and transthyretin, etc., and it plays essential roles in multiple biological activities. Perlecan is a key component of the vascular extracellular matrix, where it helps to maintain the endothelial barrier function. It is a potent inhibitor of smooth muscle cell proliferation and is thus thought to help maintain vascular homeostasis. It can also promote growth factor (e.g., FGF2) activity and thus stimulate endothelial growth and re-generation. It is a major component of basement membranes, where it is involved in the stabilization of other molecules as well as being involved with glomerular permeability to macromolecules and cell adhesion. Mutations in this gene cause Schwartz-Jampel syndrome type 1, Silverman-Handmaker type of dyssegmental dysplasia, and tardive dyskinesia. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, May 2014]

Description

Heparan sulfate proteoglycan 2

Tissue specificity

Low tissue specificity

Subcell location

Nucleoplasm, Plasma membrane, Cytosol

Predicted location

Intracellular, Secreted to extracellular matrix

Protein family

Disease related genes
Human disease related genes
Mapped to neXtProt
Mapped to UniProt SWISS-PROT
Metabolic proteins
Plasma proteins
Predicted intracellular proteins
Predicted secreted proteins
Protein evidence (Ezkurdia et al 2014)
Protein evidence (Kim et al 2014)

Chromosome

1 (21822244 - 21937310)

Ensembl ID

ENSG00000142798  (ver. 103.38)

Orthologs

Mouse Hspg2: ENSMUSG00000028763

UniProt

P98160

neXtProt

NX_P98160

Human splice variants
Mouse splice variants

Protein structure