Ser280
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Home > Phosphorylation Site Page: > Ser280  -  osteopontin (human)

Site Information
FHsHEFHsHEDMLVV   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 455724
Available spectra:  1 CST

In vivo Characterization
Methods used to characterize site in vivo:
mass spectrometry ( 2 , 3 , 4 , 5 , 6 , 7 )
Disease tissue studied:
HER2 positive breast cancer ( 2 ) , luminal A breast cancer ( 2 ) , luminal B breast cancer ( 2 ) , breast cancer, surrounding tissue ( 2 ) , breast cancer, triple negative ( 2 ) , lung cancer ( 4 ) , non-small cell lung cancer ( 4 , 5 ) , non-small cell lung adenocarcinoma ( 4 ) , ovarian cancer ( 3 )
Relevant cell line - cell type - tissue:
A549 (pulmonary) ( 4 , 5 ) , breast ( 2 ) , lung ( 4 ) , milk ( 6 , 7 ) , NCI-H1355 (pulmonary) ( 4 ) , NCI-H1792 (pulmonary) ( 4 ) , NCI-H23 (pulmonary) ( 4 ) , NCI-H441 (pulmonary) ( 4 ) , ovary ( 3 ) , urine ( 6 )

References 

1

Yalak G, et al. (2019) Phosphorylated fibronectin enhances cell attachment and upregulates mechanical cell functions. PLoS One 14, e0218893
31291285   Curated Info

2

Mertins P, et al. (2016) Proteogenomics connects somatic mutations to signalling in breast cancer. Nature 534, 55-62
27251275   Curated Info

3

Mertins P, et al. (2014) Ischemia in tumors induces early and sustained phosphorylation changes in stress kinase pathways but does not affect global protein levels. Mol Cell Proteomics 13, 1690-704
24719451   Curated Info

4

Rikova K, Hall B (2013) CST Curation Set: 20736, 21163, 30158, 30159, 30160; Year: 2013; Biosample/Treatment: cell line, A549, H1355, H23, H441, H1792; Disease: -; TMT: Y; Specificities of Antibodies Used to Purify Peptides prior to LCMS: pY, p[ST], RXXp[ST], pSQ, p[ST]QG, LXRXXp[ST], p[ST]P
Curated Info

5

Rikova K (2012) CST Curation Set: 16144; Year: 2012; Biosample/Treatment: cell line, A549/iressa, gleevec, crizotinib; Disease: -; TMT: Y; Specificities of Antibodies Used to Purify Peptides prior to LCMS: p[ST]
Curated Info

6

Christensen B, Petersen TE, Sørensen ES (2008) Post-translational modification and proteolytic processing of urinary osteopontin. Biochem J 411, 53-61
18072945   Curated Info

7

Christensen B, et al. (2005) Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications. Biochem J 390, 285-92
15869464   Curated Info