Ser1679
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Home > Phosphorylation Site Page: > Ser1679  -  MAP2 (human)

Site Information
NVKsKIGstDNIKYQ   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 456808

In vivo Characterization
Methods used to characterize site in vivo:
mass spectrometry ( 1 , 2 , 3 ) , mass spectrometry (in vitro) ( 4 ) , microscopy-colocalization with upstream kinase ( 4 ) , mutation of modification site ( 4 )
Disease tissue studied:
luminal A breast cancer ( 1 ) , luminal B breast cancer ( 1 ) , breast cancer, triple negative ( 1 ) , melanoma skin cancer ( 2 )
Relevant cell line - cell type - tissue:
breast ( 1 ) , HeLa (cervical) ( 4 ) , Jurkat (T lymphocyte) ( 3 ) , WM239A (melanocyte) ( 2 )

Upstream Regulation
Putative in vivo kinases:
PKACA (human) ( 4 )
Kinases, in vitro:
PKACA (human) ( 4 )

Downstream Regulation
Effects of modification on MAP2:
intracellular localization ( 4 ) , molecular association, regulation ( 4 )
Effects of modification on biological processes:
cytoskeletal reorganization ( 4 )
Induce interaction with:
ACTB (human) ( 4 ) , TUBA1A (human) ( 4 )

References 

1

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

2

Stuart SA, et al. (2015) A Phosphoproteomic Comparison of B-RAFV600E and MKK1/2 Inhibitors in Melanoma Cells. Mol Cell Proteomics 14, 1599-615
25850435   Curated Info

3

Possemato A (2007) CST Curation Set: 2928; Year: 2007; Biosample/Treatment: cell line, Jurkat/calyculin_A & pervanadate; Disease: T cell leukemia; SILAC: -; Specificities of Antibodies Used to Purify Peptides prior to LCMS: pY Antibodies Used to Purify Peptides prior to LCMS: Phospho-Tyrosine Mouse mAb (P-Tyr-100) Cat#: 9411, PTMScan(R) Phospho-Tyr Motif (Y*) Immunoaffinity Beads Cat#: 1991
Curated Info

4

Ozer RS, Halpain S (2000) Phosphorylation-dependent localization of microtubule-associated protein MAP2c to the actin cytoskeleton. Mol Biol Cell 11, 3573-87
11029056   Curated Info

5

Drewes G, et al. (1997) MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell 89, 297-308
9108484   Curated Info

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