AKAP12

VALUE_ERROR (nil)
Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a
Wikidata
View/Edit Human

A-kinase anchor protein 12, aka AKAP250, is an enzyme that in humans is encoded by the AKAP12 gene.

Function

The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins, which have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining the holoenzyme to discrete locations within the cell. This gene encodes a member of the AKAP family. The encoded protein is expressed in endothelial cells, cultured fibroblasts, and osteosarcoma cells. It associates with protein kinase A and C and phosphatase, and serves as a scaffold protein in signal transduction. This protein and RII PKA colocalize at the cell periphery. This protein is a cell growth-related protein. Antibodies to this protein can be produced by patients with myasthenia gravis. Alternative splicing of this gene results in two transcript variants encoding different isoforms.

Interactions

AKAP12 has been shown to interact with Beta-2 adrenergic receptor.

External links

• Human AKAP12 genome location and AKAP12 gene details page in the UCSC Genome Browser.

Further reading

• Lester LB, Scott JD (1997). "Anchoring and scaffold proteins for kinases and phosphatases". Recent Prog. Horm. Res. 52: 409–29, discussion 429-30. PMID 9238861.
• Michel JJ, Scott JD (2002). "AKAP mediated signal transduction". Annu. Rev. Pharmacol. Toxicol. 42: 235–57. doi:10.1146/annurev.pharmtox.42.083101.135801. PMID 11807172.
• Yildirim M, Paydas S, Tanriverdi K, Seydaoglu G, Disel U, Yavuz S (2007). "Gravin gene expression in acute leukaemias: clinical importance and review of the literature". Leuk. Lymphoma. 48 (6): 1167–72. doi:10.1080/10428190701377055. PMID 17577780.
• Gordon T, Grove B, Loftus JC, O'Toole T, McMillan R, Lindstrom J, Ginsberg MH (1992). "Molecular cloning and preliminary characterization of a novel cytoplasmic antigen recognized by myasthenia gravis sera". J. Clin. Invest. 90 (3): 992–9. doi:10.1172/JCI115976. PMC 329955. PMID 1522245.
• Sato N, Kokame K, Shimokado K, Kato H, Miyata T (1998). "Changes of gene expression by lysophosphatidylcholine in vascular endothelial cells: 12 up-regulated distinct genes including 5 cell growth-related, 3 thrombosis-related, and 4 others". J. Biochem. 123 (6): 1119–26. doi:10.1093/oxfordjournals.jbchem.a022051. PMID 9604001.
• Shih M, Lin F, Scott JD, Wang HY, Malbon CC (1999). "Dynamic complexes of beta2-adrenergic receptors with protein kinases and phosphatases and the role of gravin". J. Biol. Chem. 274 (3): 1588–95. doi:10.1074/jbc.274.3.1588. PMID 9880537.
• Lin F, Wang Hy, Malbon CC (2000). "Gravin-mediated formation of signaling complexes in beta 2-adrenergic receptor desensitization and resensitization". J. Biol. Chem. 275 (25): 19025–34. doi:10.1074/jbc.275.25.19025. PMID 10858453.
• Fan G, Shumay E, Wang H, Malbon CC (2001). "The scaffold protein gravin (cAMP-dependent protein kinase-anchoring protein 250) binds the beta 2-adrenergic receptor via the receptor cytoplasmic Arg-329 to Leu-413 domain and provides a mobile scaffold during desensitization". J. Biol. Chem. 276 (26): 24005–14. doi:10.1074/jbc.M011199200. PMID 11309381.
• Grove BD, Bruchey AK (2001). "Intracellular distribution of gravin, a PKA and PKC binding protein, in vascular endothelial cells". J. Vasc. Res. 38 (2): 163–75. doi:10.1159/000051043. PMID 11316952.
• Sasaki H, Kunimatsu M, Fujii Y, Yamakawa Y, Fukai I, Kiriyama M, Nonaka M, Sasaki M (2001). "Autoantibody to gravin is expressed more strongly in younger and nonthymomatous patients with myasthenia gravis". Surg. Today. 31 (11): 1036–7. doi:10.1007/s005950170020. PMID 11766078.
• Piontek J, Brandt R (2003). "Differential and regulated binding of cAMP-dependent protein kinase and protein kinase C isoenzymes to gravin in human model neurons: Evidence that gravin provides a dynamic platform for the localization for kinases during neuronal development". J. Biol. Chem. 278 (40): 38970–9. doi:10.1074/jbc.M306749200. PMID 12857743.
• Tao J, Wang HY, Malbon CC (2003). "Protein kinase A regulates AKAP250 (gravin) scaffold binding to the beta2-adrenergic receptor". EMBO J. 22 (24): 6419–29. doi:10.1093/emboj/cdg628. PMC 291823. PMID 14657015.
• Choi MC, Jong HS, Kim TY, Song SH, Lee DS, Lee JW, Kim TY, Kim NK, Bang YJ (2004). "AKAP12/Gravin is inactivated by epigenetic mechanism in human gastric carcinoma and shows growth suppressor activity". Oncogene. 23 (42): 7095–103. doi:10.1038/sj.onc.1207932. PMID 15258566.
• Ballif BA, Villén J, Beausoleil SA, Schwartz D, Gygi SP (2004). "Phosphoproteomic analysis of the developing mouse brain". Mol. Cell. Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
• Streb JW, Miano JM (2005). "AKAP12alpha, an atypical serum response factor-dependent target gene". J. Biol. Chem. 280 (6): 4125–34. doi:10.1074/jbc.M412466200. PMID 15590635.
• Streb JW, Miano JM (2005). "Cross-species sequence analysis reveals multiple charged residue-rich domains that regulate nuclear/cytoplasmic partitioning and membrane localization of a kinase anchoring protein 12 (SSeCKS/Gravin)". J. Biol. Chem. 280 (30): 28007–14. doi:10.1074/jbc.M414017200. PMID 15923193.