DYRK1B

Dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 1B
Identifiers
Symbols DYRK1B; MIRK
External IDs OMIM604556 MGI1330302 HomoloGene31253 GeneCards: DYRK1B Gene
EC number 2.7.12.1
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 9149 13549
Ensembl ENSG00000105204 ENSMUSG00000002409
UniProt Q9Y463 n/a
RefSeq (mRNA) NM_004714.1 XM_992180
RefSeq (protein) NP_004705.1 XP_997274
Location (UCSC) Chr 19:
40.32 – 40.32 Mb
Chr 7:
28.96 – 28.97 Mb
PubMed search [1] [2]

Dual specificity tyrosine-phosphorylation-regulated kinase 1B is an enzyme that in humans is encoded by the DYRK1B gene.[1][2]

Contents

Function

DYRK1B is a member of the DYRK family of protein kinases. DYRK1B contains a bipartite nuclear localization signal and is found mainly in muscle and testis. The protein is proposed to be involved in the regulation of nuclear functions. Three isoforms of DYRK1B have been identified differing in the presence of two alternatively spliced exons within the catalytic domain.[2]

Interactions

DYRK1B has been shown to interact with PCBD1[3] and RANBP9.[4]

References

  1. ^ Leder S, Weber Y, Altafaj X, Estivill X, Joost HG, Becker W (Feb 1999). "Cloning and characterization of DYRK1B, a novel member of the DYRK family of protein kinases". Biochem Biophys Res Commun 254 (2): 474–9. doi:10.1006/bbrc.1998.9967. PMID 9918863. 
  2. ^ a b "Entrez Gene: DYRK1B dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 1B". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9149. 
  3. ^ Lim, Seunghwan; Jin Kideok, Friedman Eileen (Jul. 2002). "Mirk protein kinase is activated by MKK3 and functions as a transcriptional activator of HNF1alpha". J. Biol. Chem. (United States) 277 (28): 25040–6. doi:10.1074/jbc.M203257200. ISSN 0021-9258. PMID 11980910. 
  4. ^ Zou, Yonglong; Lim Seunghwan, Lee Kangmoon, Deng Xiaobing, Friedman Eileen (Dec. 2003). "Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M". J. Biol. Chem. (United States) 278 (49): 49573–81. doi:10.1074/jbc.M307556200. ISSN 0021-9258. PMID 14500717. 

Further reading