| A kinase (PRKA) anchor protein (yotiao) 9 | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | AKAP9; AKAP-9; AKAP350; AKAP450; CG-NAP; HYPERION; MU-RMS-40.16A; PPP1R45; PRKA9; YOTIAO | ||||||||||||
| External IDs | OMIM: 604001 MGI: 2178217 HomoloGene: 17517 GeneCards: AKAP9 Gene | ||||||||||||
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| RNA expression pattern | |||||||||||||
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| More reference expression data | |||||||||||||
| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 10142 | 100986 | |||||||||||
| Ensembl | ENSG00000127914 | ENSMUSG00000040407 | |||||||||||
| UniProt | Q99996 | Q70FJ1 | |||||||||||
| RefSeq (mRNA) | NM_005751.4 | NM_194462.2 | |||||||||||
| RefSeq (protein) | NP_005742.4 | NP_919444.2 | |||||||||||
| Location (UCSC) | Chr 7: 91.57 – 91.74 Mb |
Chr 5: 3.93 – 4.08 Mb |
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| PubMed search | [1] | [2] | |||||||||||
A-kinase anchor protein 9 is an enzyme that in humans is encoded by the AKAP9 gene.[1][2][3] 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. Alternate splicing of this gene results in many isoforms that localize to the centrosome and the Golgi apparatus, and interact with numerous signaling proteins from multiple signal transduction pathways. These signaling proteins include type II protein kinase A, serine/threonine kinase protein kinase N, protein phosphatase 1, protein phosphatase 2a, protein kinase C-epsilon and phosphodiesterase 4D3.[3]
Contents |
Model organisms [link]
| Characteristic | Phenotype |
|---|---|
| Homozygote viability | Abnormal |
| Recessive lethal study | Normal |
| Fertility | Normal |
| Body weight | Abnormal[4] |
| Anxiety | Normal |
| Neurological assessment | Normal |
| Grip strength | Normal |
| Hot plate | Normal |
| Dysmorphology | Normal |
| Indirect calorimetry | Abnormal[5] |
| Glucose tolerance test | Abnormal[6] |
| Auditory brainstem response | Normal |
| DEXA | Abnormal[7] |
| Radiography | Abnormal[8] |
| Body temperature | Normal |
| Eye morphology | Normal |
| Clinical chemistry | Abnormal[9] |
| Haematology | Normal |
| Peripheral blood lymphocytes | Abnormal |
| Micronucleus test | Normal |
| Heart weight | Normal |
| Skin Histopathology | Normal |
| Brain histopathology | Normal |
| Eye Histopathology | Normal |
| Salmonella infection | Normal[10] |
| Citrobacter infection | Normal[11][12] |
| All tests and analysis from[13] |
Model organisms have been used in the study of AKAP9 function. A conditional knockout mouse line, called Akap9tm1a(KOMP)Wtsi[14][15] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[16][17][18]
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[13][19] Twenty six tests were carried out on mutant mice and eight significant abnormalities were observed.[13] Fewer than expected homozygous mutant mice survived until weaning. The remaining tests were carried out on both homozygous and heterozygous mutant adult mice. Animals of both sex displayed decreased body fat and body weight, hematopoietic abnormalities and an atypical plasma chemistry panel. Female homozygotes also displayed abnormal tooth morphology while males heterozygous animals displayed an abnormal pelvic girdle bone morphology.[13]
Interactions [link]
AKAP9 has been shown to interact with Calmodulin 1,[20] FNBP1,[21] CALM2,[20] Protein kinase N1,[22] TRIP10,[21] KvLQT1[23] and PRKAR2A.[24][22]
References [link]
- ^ Lin JW, Wyszynski M, Madhavan R, Sealock R, Kim JU, Sheng M (Apr 1998). "Yotiao, a novel protein of neuromuscular junction and brain that interacts with specific splice variants of NMDA receptor subunit NR1". J Neurosci 18 (6): 2017–27. PMID 9482789.
- ^ Westphal RS, Tavalin SJ, Lin JW, Alto NM, Fraser ID, Langeberg LK, Sheng M, Scott JD (Jul 1999). "Regulation of NMDA receptors by an associated phosphatase-kinase signaling complex". Science 285 (5424): 93–6. DOI:10.1126/science.285.5424.93. PMID 10390370.
- ^ a b "Entrez Gene: AKAP9 A kinase (PRKA) anchor protein (yotiao) 9". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10142.
- ^ "Body weight data for Akap9". Wellcome Trust Sanger Institute. https://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/weight-curves/.
- ^ "Indirect calorimetry data for Akap9". Wellcome Trust Sanger Institute. https://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/indirect-calorimetry/.
- ^ "Glucose tolerance test data for Akap9". Wellcome Trust Sanger Institute. https://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/glucose-tolerance-ip/.
- ^ "DEXA data for Akap9". Wellcome Trust Sanger Institute. https://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/body-composition-dexa/.
- ^ "Radiography data for Akap9". Wellcome Trust Sanger Institute. https://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/x-ray-imaging/.
- ^ "Clinical chemistry data for Akap9". Wellcome Trust Sanger Institute. https://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/plasma-chemistry/.
- ^ "Salmonella infection data for Akap9". Wellcome Trust Sanger Institute. https://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/salmonella-challenge/.
- ^ "Citrobacter infection data for Akap9". Wellcome Trust Sanger Institute. https://www.sanger.ac.uk/mouseportal/phenotyping/MBFR/citrobacter-challenge/.
- ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
- ^ a b c d Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. DOI:10.1111/j.1755-3768.2010.4142.x.
- ^ "International Knockout Mouse Consortium". https://www.knockoutmouse.org/martsearch/search?query=Akap9.
- ^ "Mouse Genome Informatics". https://www.informatics.jax.org/searchtool/Search.do?query=MGI:4362642.
- ^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. DOI:10.1038/nature10163. PMID 21677750.
- ^ Dolgin E (2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. DOI:10.1038/474262a. PMID 21677718.
- ^ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell 128 (1): 9–13. DOI:10.1016/j.cell.2006.12.018. PMID 17218247.
- ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. DOI:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3218837.
- ^ a b Takahashi, Mikiko; Yamagiwa Akiko, Nishimura Tamako, Mukai Hideyuki, Ono Yoshitaka (Sep. 2002). "Centrosomal Proteins CG-NAP and Kendrin Provide Microtubule Nucleation Sites by Anchoring γ-Tubulin Ring Complex". Mol. Biol. Cell (United States) 13 (9): 3235–45. DOI:10.1091/mbc.E02-02-0112. ISSN 1059-1524. PMC 124155. PMID 12221128. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=124155.
- ^ a b Larocca, M Cecilia; Shanks Ryan A, Tian Lan, Nelson David L, Stewart Donn M, Goldenring James R (Jun. 2004). "AKAP350 Interaction with cdc42 Interacting Protein 4 at the Golgi Apparatus". Mol. Biol. Cell (United States) 15 (6): 2771–81. DOI:10.1091/mbc.E03-10-0757. ISSN 1059-1524. PMC 420101. PMID 15047863. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=420101.
- ^ a b Takahashi, M; Shibata H, Shimakawa M, Miyamoto M, Mukai H, Ono Y (Jun. 1999). "Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the golgi apparatus". J. Biol. Chem. (UNITED STATES) 274 (24): 17267–74. DOI:10.1074/jbc.274.24.17267. ISSN 0021-9258. PMID 10358086.
- ^ Marx, Steven O; Kurokawa Junko, Reiken Steven, Motoike Howard, D'Armiento Jeanine, Marks Andrew R, Kass Robert S (Jan. 2002). "Requirement of a macromolecular signaling complex for beta adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel". Science (United States) 295 (5554): 496–9. DOI:10.1126/science.1066843. PMID 11799244.
- ^ Alto, Neal M; Soderling Scott H, Hoshi Naoto, Langeberg Lorene K, Fayos Rosa, Jennings Patricia A, Scott John D (Apr. 2003). "Bioinformatic design of A-kinase anchoring protein-in silico: A potent and selective peptide antagonist of type II protein kinase A anchoring". Proc. Natl. Acad. Sci. U.S.A. (United States) 100 (8): 4445–50. DOI:10.1073/pnas.0330734100. ISSN 0027-8424. PMC 153575. PMID 12672969. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=153575.
Further reading [link]
- Nagase T, Ishikawa K, Suyama M, et al. (1999). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (5): 277–86. DOI:10.1093/dnares/5.5.277. PMID 9872452.
- Schmidt PH, Dransfield DT, Claudio JO, et al. (1999). "AKAP350, a multiply spliced protein kinase A-anchoring protein associated with centrosomes". J. Biol. Chem. 274 (5): 3055–66. DOI:10.1074/jbc.274.5.3055. PMID 9915845.
- Witczak O, Skålhegg BS, Keryer G, et al. (1999). "Cloning and characterization of a cDNA encoding an A-kinase anchoring protein located in the centrosome, AKAP450". EMBO J. 18 (7): 1858–68. DOI:10.1093/emboj/18.7.1858. PMC 1171271. PMID 10202149. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1171271.
- Takahashi M, Shibata H, Shimakawa M, et al. (1999). "Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the golgi apparatus". J. Biol. Chem. 274 (24): 17267–74. DOI:10.1074/jbc.274.24.17267. PMID 10358086.
- Husi H, Ward MA, Choudhary JS, et al. (2000). "Proteomic analysis of NMDA receptor-adhesion protein signaling complexes". Nat. Neurosci. 3 (7): 661–9. DOI:10.1038/76615. PMID 10862698.
- Takahashi M, Mukai H, Oishi K, et al. (2000). "Association of immature hypophosphorylated protein kinase cepsilon with an anchoring protein CG-NAP". J. Biol. Chem. 275 (44): 34592–6. DOI:10.1074/jbc.M005285200. PMID 10945988.
- Marx SO, Kurokawa J, Reiken S, et al. (2002). "Requirement of a macromolecular signaling complex for beta adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel". Science 295 (5554): 496–9. DOI:10.1126/science.1066843. PMID 11799244.
- Steadman BT, Schmidt PH, Shanks RA, et al. (2002). "Transforming acidic coiled-coil-containing protein 4 interacts with centrosomal AKAP350 and the mitotic spindle apparatus". J. Biol. Chem. 277 (33): 30165–76. DOI:10.1074/jbc.M201914200. PMID 12015314.
- Bray JD, Chennathukuzhi VM, Hecht NB (2002). "Identification and characterization of cDNAs encoding four novel proteins that interact with translin associated factor-X". Genomics 79 (6): 799–808. DOI:10.1006/geno.2002.6779. PMID 12036294.
- Shanks RA, Larocca MC, Berryman M, et al. (2002). "AKAP350 at the Golgi apparatus. II. Association of AKAP350 with a novel chloride intracellular channel (CLIC) family member". J. Biol. Chem. 277 (43): 40973–80. DOI:10.1074/jbc.M112277200. PMID 12163479.
- Takahashi M, Yamagiwa A, Nishimura T, et al. (2003). "Centrosomal Proteins CG-NAP and Kendrin Provide Microtubule Nucleation Sites by Anchoring γ-Tubulin Ring Complex". Mol. Biol. Cell 13 (9): 3235–45. DOI:10.1091/mbc.E02-02-0112. PMC 124155. PMID 12221128. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=124155.
- Sillibourne JE, Milne DM, Takahashi M, et al. (2002). "Centrosomal anchoring of the protein kinase CK1delta mediated by attachment to the large, coiled-coil scaffolding protein CG-NAP/AKAP450". J. Mol. Biol. 322 (4): 785–97. DOI:10.1016/S0022-2836(02)00857-4. PMID 12270714.
- 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. DOI:10.1073/pnas.242603899. PMC 139241. PMID 12477932. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human Chromosome 7: DNA Sequence and Biology". Science 300 (5620): 767–72. DOI:10.1126/science.1083423. PMC 2882961. PMID 12690205. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2882961.
- Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7". Nature 424 (6945): 157–64. DOI:10.1038/nature01782. PMID 12853948.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. DOI:10.1038/ng1285. PMID 14702039.
- Tu H, Tang TS, Wang Z, Bezprozvanny I (2004). "Association of type 1 inositol 1,4,5-trisphosphate receptor with AKAP9 (Yotiao) and protein kinase A". J. Biol. Chem. 279 (18): 19375–82. DOI:10.1074/jbc.M313476200. PMID 14982933.
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Human Genome Organisation
The Human Genome Organisation (HUGO) is an organization involved in the Human Genome Project, a project about mapping the human genome. HUGO was established in 1989 as an international organization, primarily to foster collaboration between genome scientists around the world. The HUGO Gene Nomenclature Committee (HGNC), sometimes referred to as "HUGO", is one of HUGO's most active committees and aims to assign a unique gene name and symbol to each human gene.
History
HUGO was established in late April 1988 at the first meeting dedicated to genome mapping at Cold Spring Harbor. The idea of starting the organization stemmed from a South African biologist by the name of Sydney Brenner, who is known for his significant contributions to work on the genetic code and other areas of molecular biology, as well as winning the Nobel prize in Physiology of Medicine in 2002. A Founding Council was elected at the meeting that total 42 scientists from 17 different countries. HUGO is grounded in Geneva Switzerland, and later went on to elect an additional 178 members, bringing the total up to 220.
