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osteopontin; bone sialoprotein 1; urinary stone protein; secreted phosphoprotein 1; nephropontin; uropontin (SPP1, BNSP, OPN)

Function: 1) multifunctional protein: 2) principal phosphorylated glycoprotein of bone a) binds tightly to hydroxyapatite b) appears to form an integral part of the mineralized matrix c) probably important to cell-matrix interaction 3) acts as a cytokine involved in enhancing production of interferon-gamma & interleukin-12 & reducing production of interleukin-10 & is essential in the pathway that leads to cellular immunity (putative) 4) ligand of CD44 5) ligand of integrin alpha-V/beta-3 6) extensively phosphorylated on clustered serine residues - phosphorylation sites are present in the extracellular medium Structure: - N-glycosylated & O-glycosylated - belongs to the osteopontin family Compartment: - constituent of amorphous material within normal elastic fibers in human skin & aorta Alternative splicing: named isoforms=4 Expression: 1) expressed in brain by: a) microvascular endothelial cells b) microglia c) reactive astrocytes d) neurons 2) expression induced by hypoxia Pathology: 1) abundant in plaques of multiple sclerosis 2) urinary stone protein

Interactions

molecular events

Related

CD44; phagocytic glycoprotein I; PGP-1; HUTCH-I; extracellular matrix receptor-III; ECMR-III; GP90 lymphocyte homing/adhesion receptor; Hermes antigen; hyaluronate receptor; heparan sulfate proteoglycan; epican; CDw44 (LHR, MDU2, MDU3, MIC4)

General

glycoprotein phosphoprotein secreted protein

Properties

SIZE: entity length = 314 aa MW = 35 kD COMPARTMENT: extracellular compartment MOTIF: signal sequence {1-16} Ser phosphorylation site {S24} Ser phosphorylation site {S26} Ser phosphorylation site {S27} Ser phosphorylation site {S62} Ser phosphorylation site {S63} Thr phosphorylation site {T66} Ser phosphorylation site {S76} N-glycosylation site {N79} Ser phosphorylation site {S81} Ser phosphorylation site {S99} Ser phosphorylation site {S102} Ser phosphorylation site {S105} N-glycosylation site {N106} Ser phosphorylation site {S108} Ser phosphorylation site {S117} Ser phosphorylation site {S120} Ser phosphorylation site {S123} Ser phosphorylation site {S126} Ser phosphorylation site {S129} Thr glycosylation site {T134} Thr glycosylation site {T138} Thr glycosylation site {T143} Thr glycosylation site {T147} Thr glycosylation site {T152} Cell attachment site {159-161} Thr phosphorylation site {T185} Ser phosphorylation site {S191} Ser phosphorylation site {S195} Ser phosphorylation site {S215} Ser phosphorylation site {S219} Ser phosphorylation site {S224} Ser phosphorylation site {S228} Ser phosphorylation site {S234} Ser phosphorylation site {S254} Ser phosphorylation site {S263} Ser phosphorylation site {S267} Ser phosphorylation site {S275} Ser phosphorylation site {S280} Ser phosphorylation site {S303} Ser phosphorylation site {S308} Ser phosphorylation site {S310}

Database Correlations

OMIM 166490 UniProt P10451 Pfam PF00865 Entrez Gene 6696 Kegg hsa:6696

References

  1. UniProt :accession P10451
  2. Atlas of Genetics & Cytogenetics in Oncology & Haematology http://atlasgeneticsoncology.org/genes/SPP1ID42379ch4q22.html
  3. Wikipedia; Note: osteopontin entry http://en.wikipedia.org/wiki/osteopontin
  4. Journal Watch 22(2):16, 2002 Chabas D et al The influence of the proinflammatory cytokine, osteopontin, on autoimmune demyelinating disease. Science 294:1731, 2001 PMID: 11721059
  5. OMIM :accession 166490

Component-of

molecular complex