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KIN2/PAR-1/MARK kinase family

From Wikipedia, the free encyclopedia
Kinase associated domain 1
solution structure of kinase associated domain 1 of mouse map/microtubule affinity-regulating kinase 3
Identifiers
SymbolKA1
PfamPF02149
InterProIPR001772
SCOP21ul7 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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

Some proteins known to contain a KA1 domain are listed below:

References

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  1. ^ Tassan JP, Le Goff X (April 2004). "An overview of the KIN1/PAR-1/MARK kinase family". Biol. Cell. 96 (3): 193–9. doi:10.1016/j.biolcel.2003.10.009. PMID 15182702. S2CID 29770491.
  2. ^ Biernat J, Wu YZ, Timm T, Zheng-Fischhofer Q, Mandelkow E, Meijer L, Mandelkow EM (November 2002). "Protein kinase MARK/PAR-1 is required for neurite outgrowth and establishment of neuronal polarity". Mol. Biol. Cell. 13 (11): 4013–28. doi:10.1091/mbc.02-03-0046. PMC 133611. PMID 12429843.
  3. ^ Guo S, Kemphues KJ (May 1995). "par-1, a gene required for establishing polarity in C. elegans embryos, encodes a putative Ser/Thr kinase that is asymmetrically distributed". Cell. 81 (4): 611–20. doi:10.1016/0092-8674(95)90082-9. PMID 7758115. S2CID 15478890.
  4. ^ Elbert M, Rossi G, Brennwald P (February 2005). "The yeast par-1 homologs kin1 and kin2 show genetic and physical interactions with components of the exocytic machinery". Mol. Biol. Cell. 16 (2): 532–49. doi:10.1091/mbc.E04-07-0549. PMC 545889. PMID 15563607.
This article incorporates text from the public domain Pfam and InterPro: IPR001772