Homologous Superfamily

KA1 domain/Ssp2, C-terminal (IPR028375)

Short name: KA1/Ssp2_C

Overlapping entries


This entry represents the kinase associated domain 1 (KA1) and the C-terminal domain of the SNF1-like protein kinase Ssp2.

Members of the KIN2/PAR-1/MARK kinase subfamily are conserved from yeast to human and share the same domain organisation: an N-terminal kinase domain (IPR000719) and a C-terminal kinase associated domain 1 (KA1). Some members of the KIN1/PAR-1/MARK family also contain an UBA domain (IPR015940) [PMID: 12672455]. Members of this kinase subfamily are involved in various biological processes such as cell polarity, cell cycle control, intracellular signalling, microtubule stability and protein stability [PMID: 15182702]. The function of the KA1 domain is not yet known.

Some proteins known to contain this domain are listed below:

  • Mammalian MAP/microtubule affinity-regulating kinases (MARK 1,2,3). They regulate polarity in neuronal cell models and appear to function redundantly in phosphorylating MT-associated proteins and in regulating MT stability [PMID: 12429843].
  • 5'-AMP-activated protein kinase catalytic subunit alpha 1/2 (AMPK subunit alpha-1/2).
  • SNF1-like protein kinase Ssp2 [PMID: 22140232] and protein kinase domain-containing protein ppk9 from Schizosaccharomyces pombe.
  • Mammalian maternal embryonic leucine zipper kinase (MELK). It phosphorylates ZNF622 and may contribute to its redirection to the nucleus. It may be involved in the inhibition of spliceosome assembly during mitosis.
  • Caenorhabditis elegans and drosophila PAR-1 protein. It is required for establishing polarity in embryos where it is asymmetrically distributed [PMID: 7758115].
  • Fungal Kin1 and Kin2 protein kinases involved in regulation of exocytosis. They localise to the cytoplasmic face of the plasma membrane [PMID: 15563607].
  • CBL-interacting protein kinases and CBL-interacting serine/threonine-protein kinases from plants.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.