PPP2CA

Proteinska fosfataza 2, katalitička podjedinica, alfa izoforma
PDB rendering based on 2iae.
Dostupne strukture
2IAE​, 2IE3​, 2IE4​, 2NPP​, 2NYL​, 2NYM​, 3C5W​, 3DW8​, 3FGA​, 3K7V​, 3K7W​, 3P71​
Identifikatori
Simboli PPP2CA; PP2Ac; PP2CA; PP2Calpha; RP-C
Vanjski ID OMIM: 176915 MGI: 1321159 HomoloGene: 37660 GeneCards: PPP2CA Gene
EC broj 3.1.3.16
Ontologija gena
Molekularna funkcija • aktivnost fosfoproteinskte fosfataze
• proteinsko vezivanje
• vezivanje proteinskog C-terminusa
• vezivanje metalnog jona
• aktivnost proteinske dimerizacije
Celularna komponenta • proteinska fosfataza tip 2A kompleks
• hromozom, centromerni region
• pol vretena
• nukleus
• mitohondrija
Biološki proces • nuklearno-transkribovani iRNK katabolički proces
• inaktivacija MAPK aktivnosti
• regulacija DNK replikacija
• regulacija transkripcije, DNK-zavisna
Pregled RNK izražavanja
podaci
Ortolozi
Vrsta Čovek Miš
Entrez 5515 19052
Ensembl ENSG00000113575 ENSMUSG00000020349
UniProt P67775 P63330
RefSeq (mRNA) NM_002715.2 NM_019411.4
RefSeq (protein) NP_002706.1 NP_062284.1
Lokacija (UCSC) Chr 5:
133.53 - 133.56 Mb		 Chr 11:
52.1 - 52.13 Mb
PubMed pretraga [1] [2]

Serin/treonin proteinska fosfataza 2A katalitička podjedinica alfa izoforma je enzim koji je kod ljudi kodiran PPP2CA genom.[1]

Proteinska fosfataza 2A je jedna od četiri glavne Ser/Thr fosfataze. Ona učestvuje u negativnoj kontroli ćelijskog rasta i deobe. Ona se sastoji od heteromerne enzimske osnove, koji ima katalitičku i konstantnu regulatornu podjedinicu, za koji se vezuje niz regulatornih podjedinica. Ovaj gen kodira alfa izoformu katalitičke podjedinice.[2]

Interakcije

PPP2CA formira interakcije sa CCNG2,[3] CTTNBP2,[4] MOBKL3,[4] Bestrofin 1,[5] TLX1,[6] Bcl-2,[7] PPP2R3B,[4][8] Ciklin-zavisna kinaza 2,[9] STRN3,[4] Ciklin-zavisna kinaza 6,[9] IGBP1,[4][10][11][12] PPP2R5E,[4][13] STRN,[4] PPP2R5D,[4][13] PPP2R2A,[4][14] PPP2R1B,[4][15] PPP2R1A,[4][15] CTTNBP2NL,[4] FAM40A,[4] PPP2R5C,[4][13][16] PPP2R5B[4][13] and PPP2R5A.[4][13]

Vidi još

  • PPP2CB

Reference

  1. ^ Jones TA, Barker HM, da Cruz e Silva EF, Mayer-Jaekel RE, Hemmings BA, Spurr NK, Sheer D, Cohen PT (1993). „Localization of the genes encoding the catalytic subunits of protein phosphatase 2A to human chromosome bands 5q23→q31 and 8p12→p11.2, respectively”. Cytogenet Cell Genet. 63 (1): 35—41. PMID 8383590. doi:10.1159/000133497. 
  2. ^ „Entrez Gene: PPP2CA protein phosphatase 2 (formerly 2A), catalytic subunit, alpha isoform”. 
  3. ^ Bennin, David A; Don Aruni S Arachchige; et al. (2002). „Cyclin G2 associates with protein phosphatase 2A catalytic and regulatory B' subunits in active complexes and induces nuclear aberrations and a G1/S phase cell cycle arrest”. J. Biol. Chem. United States. 277 (30): 27449—67. ISSN 0021-9258. PMID 11956189. doi:10.1074/jbc.M111693200. 
  4. ^ а б в г д ђ е ж з и ј к л љ м н Goudreault, Marilyn; D'Ambrosio Lisa M; et al. (2009). „A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein”. Mol. Cell Proteomics. United States. 8 (1): 157—71. PMC 2621004 Слободан приступ. PMID 18782753. doi:10.1074/mcp.M800266-MCP200. 
  5. ^ Marmorstein, Lihua Y; McLaughlin Precious J; et al. (2002). „Bestrophin interacts physically and functionally with protein phosphatase 2A”. J. Biol. Chem. United States. 277 (34): 30591—7. ISSN 0021-9258. PMID 12058047. doi:10.1074/jbc.M204269200. 
  6. ^ Kawabe, T; Muslin A J; et al. (1997). „HOX11 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint”. Nature. ENGLAND. 385 (6615): 454—8. ISSN 0028-0836. PMID 9009195. doi:10.1038/385454a0. 
  7. ^ Deng, X; Ito T; et al. (1998). „Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A”. J. Biol. Chem. UNITED STATES. 273 (51): 34157—63. ISSN 0021-9258. PMID 9852076. doi:10.1074/jbc.273.51.34157. 
  8. ^ Yan, Z; Fedorov S A; et al. (2000). „PR48, a novel regulatory subunit of protein phosphatase 2A, interacts with Cdc6 and modulates DNA replication in human cells”. Mol. Cell. Biol. UNITED STATES. 20 (3): 1021—9. ISSN 0270-7306. PMC 85219 Слободан приступ. PMID 10629059. doi:10.1128/MCB.20.3.1021-1029.2000. 
  9. ^ а б Cheng, A; Kaldis P; Solomon M J (2000). „Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C alpha and beta 2 isoforms”. J. Biol. Chem. UNITED STATES. 275 (44): 34744—9. ISSN 0021-9258. PMID 10934208. doi:10.1074/jbc.M006210200. 
  10. ^ Gingras, Anne-Claude; Caballero Michael; et al. (2005). „A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity”. Mol. Cell Proteomics. United States. 4 (11): 1725—40. ISSN 1535-9476. PMID 16085932. doi:10.1074/mcp.M500231-MCP200. 
  11. ^ Chen, J; Peterson R T; et al. (1998). „Alpha 4 associates with protein phosphatases 2A, 4, and 6”. Biochem. Biophys. Res. Commun. UNITED STATES. 247 (3): 827—32. ISSN 0006-291X. PMID 9647778. doi:10.1006/bbrc.1998.8792. 
  12. ^ Chung, H; Nairn A C; et al. (1999). „Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favors association with the alpha 4 subunit which promotes dephosphorylation of elongation factor-2”. Biochemistry. UNITED STATES. 38 (32): 10371—6. ISSN 0006-2960. PMID 10441131. doi:10.1021/bi990902g. 
  13. ^ а б в г д McCright, B; Rivers A M; et al. (1996). „The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm”. J. Biol. Chem. UNITED STATES. 271 (36): 22081—9. ISSN 0021-9258. PMID 8703017. doi:10.1074/jbc.271.36.22081. 
  14. ^ Kamibayashi, C; Lickteig R L; et al. (1992). „Expression of the A subunit of protein phosphatase 2A and characterization of its interactions with the catalytic and regulatory subunits”. J. Biol. Chem. UNITED STATES. 267 (30): 21864—72. ISSN 0021-9258. PMID 1328247. 
  15. ^ а б Zhou, Jin; Pham Huong T; et al. (2003). „Characterization of the Aalpha and Abeta subunit isoforms of protein phosphatase 2A: differences in expression, subunit interaction, and evolution”. Biochem. J. England. 369 (Pt 2): 387—98. ISSN 0264-6021. PMC 1223084 Слободан приступ. PMID 12370081. doi:10.1042/BJ20021244. 
  16. ^ Ito, A; Kataoka T R; et al. (2000). „A truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylation”. EMBO J. ENGLAND. 19 (4): 562—71. ISSN 0261-4189. PMC 305594 Слободан приступ. PMID 10675325. doi:10.1093/emboj/19.4.562. 

Literatura

  • Cohen P, Cohen PT (1990). „Protein phosphatases come of age.”. J. Biol. Chem. 264 (36): 21435—8. PMID 2557326. 
  • Zolnierowicz S (2000). „Type 2A protein phosphatase, the complex regulator of numerous signaling pathways.”. Biochem. Pharmacol. 60 (8): 1225—35. PMID 11007961. doi:10.1016/S0006-2952(00)00424-X. 
  • Kamibayashi C; Lickteig RL; Estes R; et al. (1992). „Expression of the A subunit of protein phosphatase 2A and characterization of its interactions with the catalytic and regulatory subunits.”. J. Biol. Chem. 267 (30): 21864—72. PMID 1328247. 
  • Goedert M, Cohen ES, Jakes R, Cohen P (1992). „p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. Implications for Alzheimer's disease [corrected]”. FEBS Lett. 312 (1): 95—9. PMID 1330687. doi:10.1016/0014-5793(92)81418-L. 
  • Khew-Goodall Y; Mayer RE; Maurer F; et al. (1991). „Structure and transcriptional regulation of protein phosphatase 2A catalytic subunit genes.”. Biochemistry. 30 (1): 89—97. PMID 1846293. doi:10.1021/bi00215a014. 
  • Scheidtmann KH, Virshup DM, Kelly TJ (1991). „Protein phosphatase 2A dephosphorylates simian virus 40 large T antigen specifically at residues involved in regulation of DNA-binding activity.”. J. Virol. 65 (4): 2098—101. PMC 240073 Слободан приступ. PMID 1848320. 
  • Scheidtmann KH, Mumby MC, Rundell K, Walter G (1991). „Dephosphorylation of simian virus 40 large-T antigen and p53 protein by protein phosphatase 2A: inhibition by small-t antigen.”. Mol. Cell. Biol. 11 (4): 1996—2003. PMC 359885 Слободан приступ. PMID 1848668. 
  • Virshup DM, Kauffman MG, Kelly TJ (1990). „Activation of SV40 DNA replication in vitro by cellular protein phosphatase 2A.”. EMBO J. 8 (12): 3891—8. PMC 402079 Слободан приступ. PMID 2555176. 
  • Arino J; Woon CW; Brautigan DL; et al. (1988). „Human liver phosphatase 2A: cDNA and amino acid sequence of two catalytic subunit isotypes.”. Proc. Natl. Acad. Sci. U.S.A. 85 (12): 4252—6. PMC 280405 Слободан приступ. PMID 2837763. doi:10.1073/pnas.85.12.4252. 
  • Stone SR; Mayer R; Wernet W; et al. (1989). „The nucleotide sequence of the cDNA encoding the human lung protein phosphatase 2A alpha catalytic subunit.”. Nucleic Acids Res. 16 (23): 11365. PMC 339016 Слободан приступ. PMID 2849764. doi:10.1093/nar/16.23.11365. 
  • Carrey EA, Campbell DG, Hardie DG (1986). „Phosphorylation and activation of hamster carbamyl phosphate synthetase II by cAMP-dependent protein kinase. A novel mechanism for regulation of pyrimidine nucleotide biosynthesis.”. EMBO J. 4 (13B): 3735—42. PMC 554725 Слободан приступ. PMID 4092695. 
  • McCright B, Virshup DM (1995). „Identification of a new family of protein phosphatase 2A regulatory subunits.”. J. Biol. Chem. 270 (44): 26123—8. PMID 7592815. doi:10.1074/jbc.270.44.26123. 
  • Favre B, Zolnierowicz S, Turowski P, Hemmings BA (1994). „The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo.”. J. Biol. Chem. 269 (23): 16311—7. PMID 8206937. 
  • Redpath NT, Price NT, Severinov KV, Proud CG (1993). „Regulation of elongation factor-2 by multisite phosphorylation.”. Eur. J. Biochem. 213 (2): 689—99. PMID 8386634. doi:10.1111/j.1432-1033.1993.tb17809.x. 
  • Muramatsu T, Kincaid RL (1993). „Molecular cloning of a full-length cDNA encoding the catalytic subunit of human calmodulin-dependent protein phosphatase (calcineurin A alpha).”. Biochim. Biophys. Acta. 1178 (1): 117—20. PMID 8392375. doi:10.1016/0167-4889(93)90117-8. 
  • Kissinger CR; Parge HE; Knighton DR; et al. (1996). „Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex.”. Nature. 378 (6557): 641—4. PMID 8524402. doi:10.1038/378641a0. 
  • Ohguro H; Rudnicka-Nawrot M; Buczyłko J; et al. (1996). „Structural and enzymatic aspects of rhodopsin phosphorylation.”. J. Biol. Chem. 271 (9): 5215—24. PMID 8617805. doi:10.1074/jbc.271.9.5215. 
  • McCright B, Rivers AM, Audlin S, Virshup DM (1996). „The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm.”. J. Biol. Chem. 271 (36): 22081—9. PMID 8703017. doi:10.1074/jbc.271.36.22081. 
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PDB Galerija
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    2iae​: Kristalna struktura proteinske fosfataze 2A (PP2A) holoenzima.
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  • 2ie4​: Struktura protein fosfataze 2A enzimska osnova vezana za okadainu kiselinu
    2ie4​: Struktura protein fosfataze 2A enzimska osnova vezana za okadainu kiselinu
  • 2npp​: Struktura protein fosfataze 2A holoenzima
    2npp​: Struktura protein fosfataze 2A holoenzima
  • 2nyl​: Struktura protein fosfataze 2A (PP2A) holoenzim sa katalitička podjedinica karboksilnog terminusa
    2nyl​: Struktura protein fosfataze 2A (PP2A) holoenzim sa katalitička podjedinica karboksilnog terminusa
  • 2nym​: Struktura protein fosfataze 2A (PP2A) sa skraćenim C-terminusom katalitičke podjedinice
    2nym​: Struktura protein fosfataze 2A (PP2A) sa skraćenim C-terminusom katalitičke podjedinice