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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 26

UniprotKB/SwissProt ID: Q9P289 (Q9P289)

Gene Name: STK26

Organism: Homo sapiens (Human)

Function: Serine/threonine-protein kinase that acts as a mediator of cell growth (PubMed:11641781, PubMed:17360971). Modulates apoptosis (PubMed:11641781, PubMed:17360971). In association with STK24 negatively regulates Golgi reorientation in polarized cell migration upon RHO activation (PubMed:27807006). Phosphorylates ATG4B at 'Ser-383', thereby increasing autophagic flux (PubMed:29232556). Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (PubMed:18782753)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Golgi apparatus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR011009 Kinase-like_dom_sf
IPR046409 PDC10_dimerisation_sf
IPR048288 PDCD10_N
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR050629 STE20/SPS1-PAK
IPR035056 STK_MST4

The S-nitrosylation sites of Q9P289

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 254 TKSFKEFIDA C LNKDPSFRPT   
2 392 EKSIAVAEAA C PGITDKMVKK