PPP1CA

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Protein phosphatase 1, catalytic subunit, alpha isozyme
Protein PPP1CA PDB 1fjm.png
PDB rendering based on 1fjm.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols PPP1CA ; PP-1A; PP1A; PP1alpha; PPP1A
External IDs OMIM176875 MGI103016 HomoloGene105262 ChEMBL: 2164 GeneCards: PPP1CA Gene
EC number 3.1.3.16
RNA expression pattern
PBB GE PPP1CA 200846 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 5499 19045
Ensembl ENSG00000172531 ENSMUSG00000040385
UniProt P62136 P62137
RefSeq (mRNA) NM_001008709 NM_031868
RefSeq (protein) NP_001008709 NP_114074
Location (UCSC) Chr 11:
67.17 – 67.19 Mb
Chr 19:
4.19 – 4.2 Mb
PubMed search [1] [2]

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit is an enzyme that in humans is encoded by the PPP1CA gene.

The protein encoded by this gene is one of the three catalytic subunits of protein phosphatase 1 (PP1). PP1 is a serine/threonine specific protein phosphatase known to be involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. Increased PP1 activity has been observed in the end stage of heart failure. Studies in both human and mice suggest that PP1 is an important regulator of cardiac function. Mouse studies also suggest that PP1 functions as a suppressor of learning and memory. Three alternatively spliced transcript variants encoding different isoforms have been found for this gene.[1]

Interactive pathway map[edit]

Click on genes, proteins and metabolites below to link to respective articles. [§ 1]

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NicotineDopaminergic_WP1602 go to article go to article go to article Go to article go to article Go to article Go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article go to article Go to article go to article go to article go to article go to article Go to article Go to article go to article Go to article Go to article Go to article go to article Go to article Go to article Go to article go to article go to article go to article go to article go to article go to article Go to article go to article Go to article Go to article go to article go to article Go to article go to article Go to article Go to article go to article
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Nicotine Activity on Dopaminergic Neurons edit
  1. ^ The interactive pathway map can be edited at WikiPathways: "NicotineDopaminergic_WP1602". 

Interactions[edit]

PPP1CA has been shown to interact with LMTK2,[2] PPP1R15A,[3][4][5] AKAP11,[6][7] Host cell factor C1,[8] PHACTR3,[9] Protein kinase R,[10] BCL2-like 1,[11] BCL2L2,[11] CDC5L,[12] PPP1R8,[8][13] SMARCB1,[4] KvLQT1,[14] BRCA1[15] and PPP1R9B.[16]

References[edit]

  1. ^ "Entrez Gene: PPP1CA protein phosphatase 1, catalytic subunit, alpha isoform". 
  2. ^ Wang, Hong; Brautigan David L (December 2002). "A novel transmembrane Ser/Thr kinase complexes with protein phosphatase-1 and inhibitor-2". J. Biol. Chem. (United States) 277 (51): 49605–12. doi:10.1074/jbc.M209335200. ISSN 0021-9258. PMID 12393858. 
  3. ^ Hung, Wesley J; Roberson Rachel S; Taft Jaime; Wu Daniel Y (May 2003). "Human BAG-1 proteins bind to the cellular stress response protein GADD34 and interfere with GADD34 functions". Mol. Cell. Biol. (United States) 23 (10): 3477–86. doi:10.1128/MCB.23.10.3477-3486.2003. ISSN 0270-7306. PMC 164759. PMID 12724406. 
  4. ^ a b Wu, Daniel Y; Tkachuck Douglas C; Roberson Rachel S; Schubach William H (August 2002). "The human SNF5/INI1 protein facilitates the function of the growth arrest and DNA damage-inducible protein (GADD34) and modulates GADD34-bound protein phosphatase-1 activity". J. Biol. Chem. (United States) 277 (31): 27706–15. doi:10.1074/jbc.M200955200. ISSN 0021-9258. PMID 12016208. 
  5. ^ Connor, J H; Weiser D C; Li S; Hallenbeck J M; Shenolikar S (October 2001). "Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1". Mol. Cell. Biol. (United States) 21 (20): 6841–50. doi:10.1128/MCB.21.20.6841-6850.2001. ISSN 0270-7306. PMC 99861. PMID 11564868. 
  6. ^ Tanji, Chie; Yamamoto Hideki; Yorioka Noriaki; Kohno Nobuoki; Kikuchi Kunimi; Kikuchi Akira (October 2002). "A-kinase anchoring protein AKAP220 binds to glycogen synthase kinase-3beta (GSK-3beta ) and mediates protein kinase A-dependent inhibition of GSK-3beta". J. Biol. Chem. (United States) 277 (40): 36955–61. doi:10.1074/jbc.M206210200. ISSN 0021-9258. PMID 12147701. 
  7. ^ Schillace, R V; Scott J D (March 1999). "Association of the type 1 protein phosphatase PP1 with the A-kinase anchoring protein AKAP220". Curr. Biol. (ENGLAND) 9 (6): 321–4. doi:10.1016/S0960-9822(99)80141-9. ISSN 0960-9822. PMID 10209101. 
  8. ^ a b Ajuh, P M; Browne G J; Hawkes N A; Cohen P T; Roberts S G; Lamond A I (February 2000). "Association of a protein phosphatase 1 activity with the human factor C1 (HCF) complex". Nucleic Acids Res. (ENGLAND) 28 (3): 678–86. doi:10.1093/nar/28.3.678. PMC 102561. PMID 10637318. 
  9. ^ Sagara, Junji; Higuchi Tsukasa; Hattori Yukiko; Moriya Mie; Sarvotham Haritha; Shima Hiroshi; Shirato Haruki; Kikuchi Kunimi; Taniguchi Shunichiro (November 2003). "Scapinin, a putative protein phosphatase-1 regulatory subunit associated with the nuclear nonchromatin structure". J. Biol. Chem. (United States) 278 (46): 45611–9. doi:10.1074/jbc.M305227200. ISSN 0021-9258. PMID 12925532. 
  10. ^ Tan, Seng-Lai; Tareen Semih U; Melville Mark W; Blakely Collin M; Katze Michael G (September 2002). "The direct binding of the catalytic subunit of protein phosphatase 1 to the PKR protein kinase is necessary but not sufficient for inactivation and disruption of enzyme dimer formation". J. Biol. Chem. (United States) 277 (39): 36109–17. doi:10.1074/jbc.M205109200. ISSN 0021-9258. PMID 12138106. 
  11. ^ a b Ayllón, Verónica; Cayla Xavier; García Alphonse; Fleischer Aarne; Rebollo Angelita (July 2002). "The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad". Eur. J. Immunol. (Germany) 32 (7): 1847–55. doi:10.1002/1521-4141(200207)32:7<1847::AID-IMMU1847>3.0.CO;2-7. ISSN 0014-2980. PMID 12115603. 
  12. ^ Ajuh, P; Kuster B; Panov K; Zomerdijk J C; Mann M; Lamond A I (December 2000). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". EMBO J. (ENGLAND) 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. ISSN 0261-4189. PMC 305846. PMID 11101529. 
  13. ^ Jin, Qiming; van Eynde Aleyde; Beullens Monique; Roy Nivedita; Thiel Gerald; Stalmans Willy; Bollen Mathieu (August 2003). "The protein phosphatase-1 (PP1) regulator, nuclear inhibitor of PP1 (NIPP1), interacts with the polycomb group protein, embryonic ectoderm development (EED), and functions as a transcriptional repressor". J. Biol. Chem. (United States) 278 (33): 30677–85. doi:10.1074/jbc.M302273200. ISSN 0021-9258. PMID 12788942. 
  14. ^ Marx, Steven O; Kurokawa Junko, Reiken Steven, Motoike Howard, D'Armiento Jeanine, Marks Andrew R, Kass Robert S (January 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. 
  15. ^ Liu, Ying; Virshup David M; White Raymond L; Hsu Lih-Ching (November 2002). "Regulation of BRCA1 phosphorylation by interaction with protein phosphatase 1alpha". Cancer Res. (United States) 62 (22): 6357–61. ISSN 0008-5472. PMID 12438214. 
  16. ^ Hsieh-Wilson, L C; Allen P B; Watanabe T; Nairn A C; Greengard P (April 1999). "Characterization of the neuronal targeting protein spinophilin and its interactions with protein phosphatase-1". Biochemistry (United States) 38 (14): 4365–73. doi:10.1021/bi982900m. ISSN 0006-2960. PMID 10194355. 

Further reading[edit]