CAB39

Calcium-binding protein 39 is a protein that in humans is encoded by the CAB39 gene.

CAB39
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1UPK, 1UPL, 2WTK, 3GNI, 4FZA, 4FZD, 4FZF, 4NZW, 4O27
Identifiers
Aliases	CAB39, MO25, CGI-66, calcium binding protein 39
External IDs	OMIM: 612174; MGI: 107438; HomoloGene: 69212; GeneCards: CAB39; OMA:CAB39 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2q37.1 Start 230,712,842 bp End 230,821,075 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1|1 C5 Start 85,721,162 bp End 85,779,297 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in amniotic fluid tibia middle temporal gyrus Skeletal muscle tissue of rectus abdominis Skeletal muscle tissue of biceps brachii mucosa of sigmoid colon palpebral conjunctiva glutes cartilage tissue triceps brachii muscle Top expressed in facial motor nucleus muscle of thigh anterior horn of spinal cord plantaris muscle transitional epithelium of urinary bladder soleus muscle extensor digitorum longus muscle gastrocnemius muscle parotid gland tibialis anterior muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein serine/threonine kinase activator activity protein kinase activator activity protein serine/threonine kinase activity kinase binding protein binding Cellular component cytoplasm cytosol serine/threonine protein kinase complex extracellular exosome extracellular region secretory granule lumen ficolin-1-rich granule lumen protein-containing complex Biological process intracellular signal transduction protein heterooligomerization signal transduction cellular hypotonic response positive regulation of protein serine/threonine kinase activity negative regulation of potassium ion transmembrane transporter activity positive regulation of peptidyl-threonine phosphorylation peptidyl-serine phosphorylation negative regulation of potassium ion transmembrane transport activation of protein kinase activity neutrophil degranulation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 51719 12283 Ensembl ENSG00000135932 ENSMUSG00000036707 UniProt Q9Y376 Q06138 RefSeq (mRNA) NM_001130849 NM_001130850 NM_016289 NM_133781 NM_001355046 NM_001355047 RefSeq (protein) NP_001124321 NP_001124322 NP_057373 NP_598542 NP_001341975 NP_001341976 Location (UCSC) Chr 2: 230.71 – 230.82 Mb Chr 1: 85.72 – 85.78 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

The protein encoded by this gene associates with STK11 (Serine/Threonine Kinase 11) and STRAD (STE20-Related ADaptor protein). CAB39 enhances formation of STK11/STRAD complexes and stimulates STK11 catalytic activity. CAB39 may function as a scaffolding component of the STK11/STRAD complex and regulates STK11 activity and cellular localization.

External links

• Human CAB39 genome location and CAB39 gene details page in the UCSC Genome Browser.

Further reading

• Baas AF, Smit L, Clevers H (2004). "LKB1 tumor suppressor protein: PARtaker in cell polarity". Trends Cell Biol. 14 (6): 312–9. doi:10.1016/j.tcb.2004.04.001. PMID 15183188.
• Hawley SA, Davison M, Woods A, et al. (1996). "Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase". J. Biol. Chem. 271 (44): 27879–87. doi:10.1074/jbc.271.44.27879. PMID 8910387.
• Lai CH, Chou CY, Ch'ang LY, et al. (2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics". Genome Res. 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876. PMID 10810093.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Boudeau J, Baas AF, Deak M, et al. (2003). "MO25α/β interact with STRADα/β enhancing their ability to bind, activate and localize LKB1 in the cytoplasm". EMBO J. 22 (19): 5102–14. doi:10.1093/emboj/cdg490. PMC 204473. PMID 14517248.
• Brajenovic M, Joberty G, Küster B, et al. (2004). "Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network". J. Biol. Chem. 279 (13): 12804–11. doi:10.1074/jbc.M312171200. PMID 14676191.
• Milburn CC, Boudeau J, Deak M, et al. (2004). "Crystal structure of MO25α in complex with the C terminus of the pseudo kinase STE20-related adaptor". Nat. Struct. Mol. Biol. 11 (2): 193–200. doi:10.1038/nsmb716. PMID 14730349. S2CID 18401688.
• Lizcano JM, Göransson O, Toth R, et al. (2005). "LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1". EMBO J. 23 (4): 833–43. doi:10.1038/sj.emboj.7600110. PMC 381014. PMID 14976552.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Boudeau J, Scott JW, Resta N, et al. (2005). "Analysis of the LKB1-STRAD-MO25 complex". J. Cell Sci. 117 (Pt 26): 6365–75. doi:10.1242/jcs.01571. PMID 15561763.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.