NLK (original) (raw)

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Mammalian protein found in Homo sapiens

NLK
Identifiers
Aliases NLK, nemo like kinase
External IDs OMIM: 609476; MGI: 1201387; HomoloGene: 88836; GeneCards: NLK; OMA:NLK - orthologs
Gene location (Human)Chromosome 17 (human)Chr.Chromosome 17 (human)[1]Chromosome 17 (human)Genomic location for NLKGenomic location for NLKBand17q11.2Start28,041,737 bp[1]End28,196,381 bp[1]
Gene location (Mouse)Chromosome 11 (mouse)Chr.Chromosome 11 (mouse)[2]Chromosome 11 (mouse)Genomic location for NLKGenomic location for NLKBand11|11 B5Start78,457,994 bp[2]End78,588,199 bp[2]
RNA expression patternBgeeHuman Mouse (ortholog)Top expressed inmiddle temporal gyrusBrodmann area 23endothelial cellretinal pigment epitheliumprimary visual cortexParietal Lobesuperior frontal gyruspostcentral gyrusentorhinal cortexinternal globus pallidusTop expressed inRostral migratory streamretinal pigment epitheliumpineal glandprefrontal cortexmedial ganglionic eminencehabenulaolfactory tuberclesubstantia nigracumulus cellstria vascularisMore reference expression dataBioGPSn/a
Gene ontologyMolecular function transferase activity nucleotide binding transcription factor binding metal ion binding kinase activity protein binding ubiquitin protein ligase binding protein serine/threonine kinase activity SH2 domain binding ATP binding protein kinase activity magnesium ion binding MAP kinase activity Cellular component cytosol nucleoplasm nucleus cytoplasm Biological process phosphorylation protein stabilization Wnt signaling pathway transcription, DNA-templated MAPK cascade protein autophosphorylation transforming growth factor beta receptor signaling pathway Wnt signaling pathway, calcium modulating pathway regulation of transcription, DNA-templated negative regulation of Wnt signaling pathway protein phosphorylation peptidyl-threonine phosphorylation regulation of gene expression serine phosphorylation of STAT protein intracellular signal transduction Sources:Amigo / QuickGO
OrthologsSpeciesHuman MouseEntrez5170118099EnsemblENSG00000087095ENSMUSG00000017376UniProtQ9UBE8O54949RefSeq (mRNA)NM_016231NM_008702RefSeq (protein)NP_057315NP_032728Location (UCSC)Chr 17: 28.04 – 28.2 MbChr 11: 78.46 – 78.59 MbPubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Serine/threonine protein kinase NLK is an enzyme that in humans is encoded by the NLK gene.[5][6][7] Its name is an abbreviation for Nemo-Like Kinase, Nemo (nmo) being the Drosophila ortholog of the mammalian NLK gene.[8] This enzyme is a member of the Mitogen-activated protein kinase (MAPK) family, although not explicitly designated as such (it does not even have a numbered MAPK code). It is a highly divergent, atypical member of the MAPK group, lacking most features so characteristic of most mitogen-activated protein kinases (e.g. it does not have the dual phosphorylation motifs of typical MAPKs, and is not phosphorylated by any known MAP2 kinases). Its activation mechanism and downstream targets are still not well characterized.[9]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000087095Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000017376Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Brott BK, Pinsky BA, Erikson RL (Mar 1998). "Nlk is a murine protein kinase related to Erk/MAP kinases and localized in the nucleus". Proc Natl Acad Sci U S A. 95 (3): 963–8. Bibcode:1998PNAS...95..963B. doi:10.1073/pnas.95.3.963. PMC 18639. PMID 9448268.
  6. ^ Kehrer-Sawatzki H, Moschgath E, Maier C, Legius E, Elgar G, Krone W (Jul 2000). "Characterization of the Fugu rubripes NLK and FN5 genes flanking the NF1 (Neurofibromatosis type 1) gene in the 5' direction and mapping of the human counterparts". Gene. 251 (1): 63–71. doi:10.1016/S0378-1119(00)00188-8. PMID 10863097.
  7. ^ "Entrez Gene: NLK nemo-like kinase".
  8. ^ Ishitani T, Ishitani S (January 2013). "Nemo-like kinase, a multifaceted cell signaling regulator". Cell. Signal. 25 (1): 190–7. doi:10.1016/j.cellsig.2012.09.017. PMID 23000342.
  9. ^ Coulombe P, Meloche S (August 2007). "Atypical mitogen-activated protein kinases: structure, regulation and functions". Biochim. Biophys. Acta. 1773 (8): 1376–87. doi:10.1016/j.bbamcr.2006.11.001. PMID 17161475.