TESK1

This gene product is a serine/threonine protein kinase that contains an N-terminal protein kinase domain and a C-terminal proline-rich domain. Its protein kinase domain is most closely related to those of the LIM motif-containing protein kinases (LIMKs). The encoded protein can phosphorylate myelin basic protein and histone in vitro. The testicular germ cell-specific expression and developmental pattern of expression of the mouse gene suggests that this gene plays an important role at and after the meiotic phase of spermatogenesis. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Dec 2015]

TESK1 Gene(Protein Coding) Testis-Specific Kinase 1

Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues (By similarity).
Regulates the cellular cytoskeleton by enhancing actin stress fiber formation via phosphorylation of cofilin and by preventing microtubule breakdown via inhibition of TAOK1/MARKK kinase activity (By similarity).
Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (By similarity).
Positively regulates integrin-mediated cell spreading, via phosphorylation of cofilin (PubMed:15584898).
Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, suppression of ciliary vesicle directional trafficking to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (PubMed:25849865).
Probably plays a central role at and after the meiotic phase of spermatogenesis (By similarity).

Biological Process actin cytoskeleton organizationSource:GO_Central1 Publication
Biological Process establishment of vesicle localizationSource:UniProtKB1 Publication
Biological Process negative regulation of cilium assemblySource:UniProtKB1 Publication
Biological Process negative regulation of phosphorylationSource:UniProtKB
Biological Process negative regulation of protein autophosphorylationSource:ARUK-UCLBy Similarity
Biological Process negative regulation of protein serine/threonine kinase activitySource:ARUK-UCLBy Similarity
Biological Process podocyte cell migrationSource:UniProtKB
Biological Process positive regulation of protein localization to nucleusSource:UniProtKB1 Publication
Biological Process positive regulation of protein phosphorylationSource:UniProtKB1 Publication
Biological Process positive regulation of stress fiber assemblySource:ARUK-UCLBy Similarity
Biological Process positive regulation of substrate adhesion-dependent cell spreadingSource:UniProtKB1 Publication
Biological Process regulation of actin cytoskeleton organizationSource:UniProtKB
Biological Process regulation of protein localizationSource:ARUK-UCLBy Similarity
Biological Process spermatogenesisSource:ProtInc1 Publication

Autophosphorylated on serine and tyrosine residues.