Heparanase (Protein name
), HPSE_HUMAN from NCBI database.
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General Annotation
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Antigen Annotation
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3D
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Predicted Eptitope
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Vaild Sequence
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Related Databases
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Citations (2)
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Gene name:
HPSE(HEP;HPA;HPA1;HPR1;HPSE1;HSE1);
Protein name:
Heparanase;
Alternative:
Heparanase-1(Hpa1);Endo-glucoronidase;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Heterodimer; heterodimer formation between the 8 kDa and the 50 kDa subunits is required for enzyme activity. Interacts with TF; the interaction, inhibited by heparin, enhances the generation of activated factor X and activates coagulation. Interacts with HRG; the interaction is enhanced at acidic pH, partially inhibits binding of HPSE to cell surface receptors and modulates its enzymatic activity. Interacts with SDC1; the interaction enhances the shedding of SDC1.
Function:
Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix (ECM) degradation and remodeling. Highly selective enzyme cleaving HSPGs at specific intrachain sites. It is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans, and increases endothelial invasion and angiogenesis in myelomas. Acts as procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extacellular matrix (ECM), independent of its enzymatic activity. Induces AKT1/PKB phosphorylation via lipid rafts increasing cell mobility and invasion. Heparin increases this AKT1/PKB activation. Regulates osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis.
Subcellular Location:
Lysosome membrane
Peripheral membrane protein
Secreted
Nucleus
Proheparanase is secreted via vesicles of the Golgi. Interacts with cell membrane heparan sulfate proteoglycans (HSPGs). Endocytosed and accumulates in endosomes. Transferred to lysosomes where it is proteolytically cleaved to produce the active enzyme. Under certain stimuli, transferred to the cell surface. Associates with lipid rafts. Colocalizes with SDC1 in endosomal/lysosomal vesicles. Accumulates in perinuclear lysosomal vesicles. Heparin retains proheparanase in the extracellular medium.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);VARIANT ARG-307;TISSUE SPECIFICITY
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);BIOPHYSICOCHEMICAL PROPERTIES;PROTEIN SEQUENCE OF 158-168; 326-337 AND 447-491;VARIANT ARG-307
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);GLYCOSYLATION;PROTEOLYTIC PROCESSING;VARIANT ARG-307
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);TISSUE SPECIFICITY;PROTEIN SEQUENCE OF 158-174; 263-272; 326-337; 433-436; 438-443; 466-468 AND 478-483;VARIANT ARG-307
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);BIOPHYSICOCHEMICAL PROPERTIES;TISSUE SPECIFICITY;VARIANT ARG-307
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);SUBCELLULAR LOCATION
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);PROTEIN SEQUENCE OF 36-41 AND 158-163;SUBUNIT;GLYCOSYLATION;BIOPHYSICOCHEMICAL PROPERTIES
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2);ALTERNATIVE SPLICING;VARIANT ARG-307
"Cloned heparanase from MCF-7 cells." Pinhal M.A.
,
Semedo P.
Submitted (2005-02) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);VARIANT ARG-307
10.
"Two new transcript variants of Homo sapiens heparanase (HPSE)." Jin S.
,
Yu L.
,
Gong F.
Submitted (2009-06) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4);VARIANT ARG-307
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1);VARIANT ARG-307
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1);VARIANT ARG-307
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Cited for: SUBCELLULAR LOCATION;PROTEOLYTIC PROCESSING;INTERACTION WITH SDC1
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Cited for: PROTEOLYTIC PROCESSING;ENZYME ACTIVITY;SUBCELLULAR LOCATION
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Cited for: GLYCOSYLATION AT ASN-162; ASN-178; ASN-200; ASN-217; ASN-238 AND ASN-459;MUTAGENESIS OF ASN-162; ASN-178; ASN-200; ASN-217; ASN-238 AND ASN-459
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Cited for: BIOPHYSICOCHEMICAL PROPERTIES;PROTEOLYTIC PROCESSING;SUBCELLULAR LOCATION
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Cited for: SUBCELLULAR LOCATION;PROTEOLYTIC PROCESSING;MUTAGENESIS OF TYR-156
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Cited for: HEPARIN/HS-BINDING DOMAINS;MUTAGENESIS OF LYS-158 AND LYS-161
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Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-217
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Cited for: FUNCTION OF THE C-TERMINAL DOMAIN;SUBCELLULAR LOCATION;MUTAGENESIS OF VAL-414; LYS-417; PRO-525; PHE-527; SER-528; TYR-529; PHE-531; VAL-533; ILE-534; ARG-535; ASN-536; ALA-537; LYS-538; VAL-539; ALA-540; ALA-541 AND CYS-542
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Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-217 AND ASN-238
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Cited for: FUNCTION;TISSUE SPECIFICITY;SUBCELLULAR LOCATION
Vaild Sequence:
