RGS14
From Wikipedia, the free encyclopedia
Regulator of G-protein signalling 14
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PDB rendering based on 1kjy. | ||||||||||||||
Available structures: 1kjy, 2jnu | ||||||||||||||
Identifiers | ||||||||||||||
Symbol(s) | RGS14; | |||||||||||||
External IDs | OMIM: 602513 MGI: 1859709 HomoloGene: 4735 | |||||||||||||
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RNA expression pattern | ||||||||||||||
Orthologs | ||||||||||||||
Human | Mouse | |||||||||||||
Entrez | 10636 | 51791 | ||||||||||||
Ensembl | ENSG00000169220 | ENSMUSG00000052087 | ||||||||||||
Uniprot | O43566 | Q8K2R4 | ||||||||||||
Refseq | NM_006480 (mRNA) NP_006471 (protein) |
XM_001004354 (mRNA) XP_001004354 (protein) |
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Location | Chr 5: 176.72 - 176.73 Mb | Chr 13: 55.38 - 55.39 Mb | ||||||||||||
Pubmed search | [1] | [2] |
Regulator of G-protein signalling 14, also known as RGS14, is a human gene.[1]
This gene encodes a member of the regulator of G-protein signaling family. This protein contains one RGS domain, two Raf-like Ras-binding domains (RBDs), and one GoLoco domain. The protein attenuates the signaling activity of G-proteins by binding, through its GoLoco domain, to specific types of activated, GTP-bound G alpha subunits. Acting as a GTPase activating protein (GAP), the protein increases the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.[1]
[edit] References
[edit] Further reading
- Snow BE, Antonio L, Suggs S, et al. (1997). "Molecular cloning and expression analysis of rat Rgs12 and Rgs14.". Biochem. Biophys. Res. Commun. 233 (3): 770–7. doi: . PMID 9168931.
- Traver S, Bidot C, Spassky N, et al. (2001). "RGS14 is a novel Rap effector that preferentially regulates the GTPase activity of galphao.". Biochem. J. 350 Pt 1: 19–29. PMID 10926822.
- Cho H, Kozasa T, Takekoshi K, et al. (2000). "RGS14, a GTPase-activating protein for Gialpha, attenuates Gialpha- and G13alpha-mediated signaling pathways.". Mol. Pharmacol. 58 (3): 569–76. PMID 10953050.
- Kimple RJ, De Vries L, Tronchère H, et al. (2001). "RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with guanine nucleotide dissociation inhibitor Activity.". J. Biol. Chem. 276 (31): 29275–81. doi: . PMID 11387333.
- Sierra DA, Gilbert DJ, Householder D, et al. (2002). "Evolution of the regulators of G-protein signaling multigene family in mouse and human.". Genomics 79 (2): 177–85. doi: . PMID 11829488.
- Kimple RJ, Kimple ME, Betts L, et al. (2002). "Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits.". Nature 416 (6883): 878–81. doi: . PMID 11976690.
- 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: . PMID 12477932.
- Hollinger S, Ramineni S, Hepler JR (2003). "Phosphorylation of RGS14 by protein kinase A potentiates its activity toward G alpha i.". Biochemistry 42 (3): 811–9. doi: . PMID 12534294.
- 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: . PMID 14702039.
- 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: . PMID 15489334.
- Martin-McCaffrey L, Willard FS, Oliveira-dos-Santos AJ, et al. (2004). "RGS14 is a mitotic spindle protein essential from the first division of the mammalian zygote.". Dev. Cell 7 (5): 763–9. doi: . PMID 15525537.
- Martin-McCaffrey L, Willard FS, Pajak A, et al. (2006). "RGS14 is a microtubule-associated protein.". Cell Cycle 4 (7): 953–60. PMID 15917656.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi: . PMID 16189514.