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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Serine/threonine-protein kinase greatwall

UniprotKB/SwissProt ID: Q96GX5 (Q96GX5)

Gene Name: MASTL

Organism: Homo sapiens (Human)

Function: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance (PubMed:19680222). Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-62' and 'Ser-67', respectively (PubMed:38123684). ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high (PubMed:20818157). Following DNA damage, it is also involved in checkpoint recovery by being inhibited. Phosphorylates histone protein in vitro; however such activity is unsure in vivo. May be involved in megakaryocyte differentiation

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cleavage furrow

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR000961 AGC-kinase_C
IPR011009 Kinase-like_dom_sf
IPR037638 MASTL_STKc
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS
IPR050236 Ser_Thr_kinase_AGC

The S-nitrosylation sites of Q96GX5

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 614 IEDPLIVTPD C QEKTSPKGVE