HABP2

HABP2

Hyaluronan binding protein 2, also known as HABP2, is a human gene.cite web | title = Entrez Gene: HABP2 hyaluronan binding protein 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3026| accessdate = ]

PBB_Summary
section_title =
summary_text = The protein encoded by this gene is an extracellular serine protease which binds hyaluronic acid. It is involved in cell adhesion. The protein is synthesized as a single chain, but then undergoes an autoproteolytic event to form the functional heterodimer. Further autoproteolysis leads to smaller, inactive peptides. Two transcript variants utilizing alternative polyA sites exist for this gene.cite web | title = Entrez Gene: HABP2 hyaluronan binding protein 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3026| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Römisch J |title=Factor VII activating protease (FSAP): a novel protease in hemostasis. |journal=Biol. Chem. |volume=383 |issue= 7-8 |pages= 1119–24 |year= 2003 |pmid= 12437095 |doi=
*cite journal | author=Gupta S, Batchu RB, Datta K |title=Purification, partial characterization of rat kidney hyaluronic acid binding protein and its localization on the cell surface. |journal=Eur. J. Cell Biol. |volume=56 |issue= 1 |pages= 58–67 |year= 1992 |pmid= 1724753 |doi=
*cite journal | author=Choi-Miura NH, Tobe T, Sumiya J, "et al." |title=Purification and characterization of a novel hyaluronan-binding protein (PHBP) from human plasma: it has three EGF, a kringle and a serine protease domain, similar to hepatocyte growth factor activator. |journal=J. Biochem. |volume=119 |issue= 6 |pages= 1157–65 |year= 1996 |pmid= 8827452 |doi=
*cite journal | author=Sumiya J, Asakawa S, Tobe T, "et al." |title=Isolation and characterization of the plasma hyaluronan-binding protein (PHBP) gene (HABP2). |journal=J. Biochem. |volume=122 |issue= 5 |pages= 983–90 |year= 1998 |pmid= 9443814 |doi=
*cite journal | author=Choi-Miura NH, Yoda M, Saito K, "et al." |title=Identification of the substrates for plasma hyaluronan binding protein. |journal=Biol. Pharm. Bull. |volume=24 |issue= 2 |pages= 140–3 |year= 2001 |pmid= 11217080 |doi=
*cite journal | author=Choi-Miura NH, Takahashi K, Yoda M, "et al." |title=Proteolytic activation and inactivation of the serine protease activity of plasma hyaluronan binding protein. |journal=Biol. Pharm. Bull. |volume=24 |issue= 5 |pages= 448–52 |year= 2001 |pmid= 11379758 |doi=
*cite journal | author=Roemisch J, Feussner A, Nerlich C, "et al." |title=The frequent Marburg I polymorphism impairs the pro-urokinase activating potency of the factor VII activating protease (FSAP). |journal=Blood Coagul. Fibrinolysis |volume=13 |issue= 5 |pages= 433–41 |year= 2003 |pmid= 12138371 |doi=
*cite journal | author=Wang KK, Liu N, Radulovich N, "et al." |title=Novel candidate tumor marker genes for lung adenocarcinoma. |journal=Oncogene |volume=21 |issue= 49 |pages= 7598–604 |year= 2002 |pmid= 12386823 |doi= 10.1038/sj.onc.1205953
*cite journal | author=Etscheid M, Beer N, Fink E, "et al." |title=The hyaluronan-binding serine protease from human plasma cleaves HMW and LMW kininogen and releases bradykinin. |journal=Biol. Chem. |volume=383 |issue= 10 |pages= 1633–43 |year= 2003 |pmid= 12452440 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Willeit J, Kiechl S, Weimer T, "et al." |title=Marburg I polymorphism of factor VII--activating protease: a prominent risk predictor of carotid stenosis. |journal=Circulation |volume=107 |issue= 5 |pages= 667–70 |year= 2003 |pmid= 12578864 |doi=
*cite journal | author=Anderson NL, Polanski M, Pieper R, "et al." |title=The human plasma proteome: a nonredundant list developed by combination of four separate sources. |journal=Mol. Cell Proteomics |volume=3 |issue= 4 |pages= 311–26 |year= 2004 |pmid= 14718574 |doi= 10.1074/mcp.M300127-MCP200
*cite journal | author=Deloukas P, Earthrowl ME, Grafham DV, "et al." |title=The DNA sequence and comparative analysis of human chromosome 10. |journal=Nature |volume=429 |issue= 6990 |pages= 375–81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462
*cite journal | author=Hoppe B, Tolou F, Radtke H, "et al." |title=Marburg I polymorphism of factor VII-activating protease is associated with idiopathic venous thromboembolism. |journal=Blood |volume=105 |issue= 4 |pages= 1549–51 |year= 2005 |pmid= 15486068 |doi= 10.1182/blood-2004-08-3328
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Ireland H, Miller GJ, Webb KE, "et al." |title=The factor VII activating protease G511E (Marburg) variant and cardiovascular risk. |journal=Thromb. Haemost. |volume=92 |issue= 5 |pages= 986–92 |year= 2005 |pmid= 15543324 |doi= 10.1267/THRO04050986
*cite journal | author=Nakazawa F, Kannemeier C, Shibamiya A, "et al." |title=Extracellular RNA is a natural cofactor for the (auto-)activation of Factor VII-activating protease (FSAP). |journal=Biochem. J. |volume=385 |issue= Pt 3 |pages= 831–8 |year= 2005 |pmid= 15654766 |doi= 10.1042/BJ20041021
*cite journal | author=van Minkelen R, de Visser MC, Vos HL, "et al." |title=The Marburg I polymorphism of factor VII-activating protease is not associated with venous thrombosis. |journal=Blood |volume=105 |issue= 12 |pages= 4898; author reply 4899 |year= 2005 |pmid= 15933067 |doi= 10.1182/blood-2005-02-0576
*cite journal | author=Etscheid M, Beer N, Dodt J |title=The hyaluronan-binding protease upregulates ERK1/2 and PI3K/Akt signalling pathways in fibroblasts and stimulates cell proliferation and migration. |journal=Cell. Signal. |volume=17 |issue= 12 |pages= 1486–94 |year= 2006 |pmid= 16153533 |doi= 10.1016/j.cellsig.2005.03.007

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