Curated Information
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Home > Curated Information Page > PubMed Id: 19775205
Addison WN, Masica DL, Gray JJ, McKee MD (2010) Phosphorylation-dependent inhibition of mineralization by osteopontin ASARM peptides is regulated by PHEX cleavage. J Bone Miner Res 25, 695-705 19775205
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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S117-p - osteopontin (human)
Modsite: DVDDTDDsHQsDEsH SwissProt Entrez-Gene
Orthologous residues
osteopontin (human): S117‑p, osteopontin iso2 (human): S103‑p, osteopontin iso5 (human): S103‑p, osteopontin (mouse): , osteopontin (rat):
Characterization
Methods used to characterize site in vivo immunoprecipitation, mass spectrometry
Relevant cell lines - cell types - tissues:  MC3T3-E1 (preosteoblast)
Cellular systems studied:  cell lines
Species studied:  mouse
Downstream Regulation
Effect of modification (function):  activity, inhibited, molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Induces
Comments:  peptide with phosphorylated S117, S120, S123, S126 and S129 has increased binding to hydroxyapatite, and inhibits bone mineralization in vivo and in vitro
Associated Diseases
Diseases Alterations Comments
X-linked hypophosphatemia increased ASARM peptide carrying phosphorylated residues S117, S120, S123, S126 and S129 contributes towards the hypomineralization occuring in XLH

S120-p - osteopontin (human)
Modsite: DTDDsHQsDEsHHsD SwissProt Entrez-Gene
Orthologous residues
osteopontin (human): S120‑p, osteopontin iso2 (human): S106‑p, osteopontin iso5 (human): S106‑p, osteopontin (mouse): , osteopontin (rat):
Characterization
Methods used to characterize site in vivo immunoprecipitation, mass spectrometry
Relevant cell lines - cell types - tissues:  MC3T3-E1 (preosteoblast)
Cellular systems studied:  cell lines
Species studied:  mouse
Downstream Regulation
Effect of modification (function):  activity, inhibited, molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Induces
Comments:  peptide with phosphorylated S117, S120, S123, S126 and S129 has increased binding to hydroxyapatite, and inhibits bone mineralization in vivo and in vitro
Associated Diseases
Diseases Alterations Comments
X-linked hypophosphatemia increased ASARM peptide carrying phosphorylated residues S117, S120, S123, S126 and S129 contributes towards the hypomineralization occuring in XLH

S123-p - osteopontin (human)
Modsite: DsHQsDEsHHsDEsD SwissProt Entrez-Gene
Orthologous residues
osteopontin (human): S123‑p, osteopontin iso2 (human): S109‑p, osteopontin iso5 (human): S109‑p, osteopontin (mouse): S112‑p, osteopontin (rat): S112‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, mass spectrometry
Relevant cell lines - cell types - tissues:  MC3T3-E1 (preosteoblast)
Cellular systems studied:  cell lines
Species studied:  mouse
Downstream Regulation
Effect of modification (function):  activity, inhibited, molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Induces
Comments:  peptide with phosphorylated S117, S120, S123, S126 and S129 has increased binding to hydroxyapatite, and inhibits bone mineralization in vivo and in vitro
Associated Diseases
Diseases Alterations Comments
X-linked hypophosphatemia increased ASARM peptide carrying phosphorylated residues S117, S120, S123, S126 and S129 contributes towards the hypomineralization occuring in XLH

S126-p - osteopontin (human)
Modsite: QsDEsHHsDEsDELV SwissProt Entrez-Gene
Orthologous residues
osteopontin (human): S126‑p, osteopontin iso2 (human): S112‑p, osteopontin iso5 (human): S112‑p, osteopontin (mouse): S115‑p, osteopontin (rat): S115‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, mass spectrometry
Relevant cell lines - cell types - tissues:  MC3T3-E1 (preosteoblast)
Cellular systems studied:  cell lines
Species studied:  mouse
Downstream Regulation
Effect of modification (function):  activity, inhibited, molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Induces
Comments:  peptide with phosphorylated S117, S120, S123, S126 and S129 has increased binding to hydroxyapatite, and inhibits bone mineralization in vivo and in vitro
Associated Diseases
Diseases Alterations Comments
X-linked hypophosphatemia increased ASARM peptide carrying phosphorylated residues S117, S120, S123, S126 and S129 contributes towards the hypomineralization occuring in XLH

S129-p - osteopontin (human)
Modsite: EsHHsDEsDELVtDF SwissProt Entrez-Gene
Orthologous residues
osteopontin (human): S129‑p, osteopontin iso2 (human): S115‑p, osteopontin iso5 (human): S115‑p, osteopontin (mouse): S118‑p, osteopontin (rat): S118‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, mass spectrometry
Relevant cell lines - cell types - tissues:  MC3T3-E1 (preosteoblast)
Cellular systems studied:  cell lines
Species studied:  mouse
Downstream Regulation
Effect of modification (function):  activity, inhibited, molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Induces
Comments:  peptide with phosphorylated S117, S120, S123, S126 and S129 has increased binding to hydroxyapatite, and inhibits bone mineralization in vivo and in vitro
Associated Diseases
Diseases Alterations Comments
X-linked hypophosphatemia increased ASARM peptide carrying phosphorylated residues S117, S120, S123, S126 and S129 contributes towards the hypomineralization occuring in XLH