PRKAR2A

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PRKAR2A
Protein PRKAR2A PDB 1l6e.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPRKAR2A, PKR2, PRKAR2, protein kinase cAMP-dependent type II regulatory subunit alpha
External IDsOMIM: 176910 MGI: 108025 HomoloGene: 3064 GeneCards: PRKAR2A
Orthologs
SpeciesHumanMouse
Entrez

5576

19087

Ensembl

ENSG00000114302

ENSMUSG00000032601

UniProt

P13861

P12367

RefSeq (mRNA)

NM_004157
NM_001321982
NM_001321983
NM_001321989

NM_008924

RefSeq (protein)

NP_001308911
NP_001308912
NP_001308918
NP_004148

n/a

Location (UCSC)Chr 3: 48.74 – 48.85 MbChr 9: 108.57 – 108.63 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

cAMP-dependent protein kinase type II-alpha regulatory subunit is an enzyme that in humans is encoded by the PRKAR2A gene.[5]

Function[]

cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent Protein Kinase, more commonly called Protein Kinase A (PKA), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of PKA is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits of PKA have been identified in humans. The protein encoded by this gene is one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic subunit. It may interact with various A-kinase anchoring proteins (AKAPs) and determine the subcellular localization of PKA. This subunit has been shown to regulate protein transport from endosomes to the Golgi apparatus and further to the endoplasmic reticulum (ER).[6]

Interactions[]

PRKAR2A has been shown to interact with:

See also[]

References[]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000114302 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032601 - Ensembl, 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. ^ Taskén K, Naylor SL, Solberg R, Jahnsen T (Jun 1998). "Mapping of the gene encoding the regulatory subunit RII alpha of cAMP-dependent protein kinase (locus PRKAR2A) to human chromosome region 3p21.3-p21.2". Genomics. 50 (3): 378–81. doi:10.1006/geno.1998.5326. PMID 9676433.
  6. ^ "Entrez Gene: PRKAR2A protein kinase, cAMP-dependent, regulatory, type II, alpha".
  7. ^ a b c d Alto NM, Soderling SH, Hoshi N, Langeberg LK, Fayos R, Jennings PA, Scott JD (Apr 2003). "Bioinformatic design of A-kinase anchoring protein-in silico: a potent and selective peptide antagonist of type II protein kinase A anchoring". Proceedings of the National Academy of Sciences of the United States of America. 100 (8): 4445–50. Bibcode:2003PNAS..100.4445A. doi:10.1073/pnas.0330734100. PMC 153575. PMID 12672969.
  8. ^ a b Tanji C, Yamamoto H, Yorioka N, Kohno N, Kikuchi K, Kikuchi A (Oct 2002). "A-kinase anchoring protein AKAP220 binds to glycogen synthase kinase-3beta (GSK-3beta ) and mediates protein kinase A-dependent inhibition of GSK-3beta". The Journal of Biological Chemistry. 277 (40): 36955–61. doi:10.1074/jbc.M206210200. PMID 12147701.
  9. ^ Lester LB, Coghlan VM, Nauert B, Scott JD (Apr 1996). "Cloning and characterization of a novel A-kinase anchoring protein. AKAP 220, association with testicular peroxisomes". The Journal of Biological Chemistry. 271 (16): 9460–5. doi:10.1074/jbc.271.16.9460. PMID 8621616.
  10. ^ Carr DW, Hausken ZE, Fraser ID, Stofko-Hahn RE, Scott JD (Jul 1992). "Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain". The Journal of Biological Chemistry. 267 (19): 13376–82. doi:10.1016/S0021-9258(18)42221-1. PMID 1618839.
  11. ^ Herberg FW, Maleszka A, Eide T, Vossebein L, Tasken K (Apr 2000). "Analysis of A-kinase anchoring protein (AKAP) interaction with protein kinase A (PKA) regulatory subunits: PKA isoform specificity in AKAP binding". Journal of Molecular Biology. 298 (2): 329–39. doi:10.1006/jmbi.2000.3662. PMID 10764601.
  12. ^ Kapiloff MS, Schillace RV, Westphal AM, Scott JD (Aug 1999). "mAKAP: an A-kinase anchoring protein targeted to the nuclear membrane of differentiated myocytes". Journal of Cell Science. 112 (16): 2725–36. doi:10.1242/jcs.112.16.2725. PMID 10413680.
  13. ^ Dong F, Feldmesser M, Casadevall A, Rubin CS (Mar 1998). "Molecular characterization of a cDNA that encodes six isoforms of a novel murine A kinase anchor protein". The Journal of Biological Chemistry. 273 (11): 6533–41. doi:10.1074/jbc.273.11.6533. PMID 9497389.
  14. ^ Vijayaraghavan S, Liberty GA, Mohan J, Winfrey VP, Olson GE, Carr DW (May 1999). "Isolation and molecular characterization of AKAP110, a novel, sperm-specific protein kinase A-anchoring protein". Molecular Endocrinology. 13 (5): 705–17. doi:10.1210/mend.13.5.0278. PMID 10319321.
  15. ^ Carr DW, Fujita A, Stentz CL, Liberty GA, Olson GE, Narumiya S (May 2001). "Identification of sperm-specific proteins that interact with A-kinase anchoring proteins in a manner similar to the type II regulatory subunit of PKA". The Journal of Biological Chemistry. 276 (20): 17332–8. doi:10.1074/jbc.M011252200. PMID 11278869.
  16. ^ Eide T, Coghlan V, Orstavik S, Holsve C, Solberg R, Skâlhegg BS, Lamb NJ, Langeberg L, Fernandez A, Scott JD, Jahnsen T, Taskén K (Feb 1998). "Molecular cloning, chromosomal localization, and cell cycle-dependent subcellular distribution of the A-kinase anchoring protein, AKAP95". Experimental Cell Research. 238 (2): 305–16. doi:10.1006/excr.1997.3855. PMID 9473338.
  17. ^ Collas P, Le Guellec K, Taskén K (Dec 1999). "The A-kinase-anchoring protein AKAP95 is a multivalent protein with a key role in chromatin condensation at mitosis". The Journal of Cell Biology. 147 (6): 1167–80. doi:10.1083/jcb.147.6.1167. PMC 2168084. PMID 10601332.
  18. ^ 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". The Journal of Biological Chemistry. 274 (24): 17267–74. doi:10.1074/jbc.274.24.17267. PMID 10358086.
  19. ^ Li H, Adamik R, Pacheco-Rodriguez G, Moss J, Vaughan M (Feb 2003). "Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2)". Proceedings of the National Academy of Sciences of the United States of America. 100 (4): 1627–32. Bibcode:2003PNAS..100.1627L. doi:10.1073/pnas.0337678100. PMC 149883. PMID 12571360.
  20. ^ Schillace RV, Andrews SF, Liberty GA, Davey MP, Carr DW (Feb 2002). "Identification and characterization of myeloid translocation gene 16b as a novel a kinase anchoring protein in T lymphocytes". Journal of Immunology. 168 (4): 1590–9. doi:10.4049/jimmunol.168.4.1590. PMID 11823486.
  21. ^ Dodge KL, Khouangsathiene S, Kapiloff MS, Mouton R, Hill EV, Houslay MD, Langeberg LK, Scott JD (Apr 2001). "mAKAP assembles a protein kinase A/PDE4 phosphodiesterase cAMP signaling module". The EMBO Journal. 20 (8): 1921–30. doi:10.1093/emboj/20.8.1921. PMC 125429. PMID 11296225.
  22. ^ Fukuyama T, Sueoka E, Sugio Y, Otsuka T, Niho Y, Akagi K, Kozu T (Sep 2001). "MTG8 proto-oncoprotein interacts with the regulatory subunit of type II cyclic AMP-dependent protein kinase in lymphocytes". Oncogene. 20 (43): 6225–32. doi:10.1038/sj.onc.1204794. PMID 11593431.

Further reading[]

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