PRKAR2A

PRKAR2A
PRKAR2A
Protein PRKAR2A PDB 1l6e.png
사용 가능한 구조
PDBOrtholog 검색: PDBe RCSB
식별자
에일리어스PRKAR2A, PKR2, PRKAR2, 단백질인산화효소 cAMP의존성 타입II 조절서브유닛α
외부 IDOMIM: 176910 MGI: 108025 HomoloGene: 3064 GeneCard: PRKAR2A
맞춤법
종.인간마우스
엔트레즈

5576

19087

앙상블

ENSG00000114302

ENSMUSG000032601

유니프로트

P13861

P12367

RefSeq(mRNA)

NM_004157
NM_001321982
NM_001321983
NM_001321989

NM_008924

RefSeq(단백질)

NP_001308911
NP_001308912
NP_001308918
NP_004148

없음

장소(UCSC)Chr 3: 48.74 ~48.85 MbChr 9: 108.57 ~108.63 Mb
PubMed 검색[3][4]
위키데이터
인간 보기/편집마우스 표시/편집

cAMP 의존성 단백질 키나제 타입 II-알파 조절 서브유닛은 PRKAR2A [5]유전자에 의해 인간에서 암호화되는 효소이다.

기능.

cAMP는 다양한 세포 기능에 중요한 신호 분자이다. cAMP는 다른 표적 단백질의 인산화 과정을 통해 신호를 변환하는 단백질 키나제 A(PKA)라고 더 흔히 불리는 cAMP 의존 단백질 키나제를 활성화함으로써 그 효과를 발휘한다.PKA의 불활성 홀로엔자임은 2개의 조절 서브유닛과 2개의 촉매 서브유닛으로 이루어진 사량체이다.cAMP는 불활성 홀로엔자임을 4개의 cAMP와 2개의 유리단량자 촉매 서브유닛에 결합된 조절 서브유닛의 이량체로 해리시킨다.4개의 다른 조절 서브유닛과 3개의 PKA 촉매 서브유닛이 사람에게서 확인되었다.이 유전자에 의해 암호화된 단백질은 조절 소단위 중 하나이다.이 서브유닛은 활성화된 촉매 서브유닛에 의해 인산화될 수 있다.다양한 A-키나아제 고정단백질(AKAPs)과 상호작용하여 PKA의 세포내 국재화를 결정할 수 있다.이 서브유닛은 엔도솜에서 골지 기기로, 나아가서는 소포체([6]ER)로의 단백질 이동을 조절하는 것으로 나타났다.

상호 작용

PRKAR2A는 다음과 상호작용하는 것으로 나타났습니다.

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레퍼런스

  1. ^ a b c GRCh38: 앙상블 릴리즈 89: ENSG00000114302 - 앙상블, 2017년 5월
  2. ^ a b c GRCm38: 앙상블 릴리즈 89: ENSMUSG000032601 - 앙상블, 2017년 5월
  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.

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