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FB:mts

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Contents

Species (Taxon ID) Drosophila melanogaster (fruit fly) (taxon:7227)
Gene Name(s) mts ( synonyms: 5559, CG7109, DmPp2A-28D, ER2-6, MTS/PP2A, Microtubule star, Mts, PP2, PP2A, PP2A 28D, PP2A C, PP2A catalytic subunit, PP2A-C, PP2A(C), PP2A((C)), PP2Ac, PP2a, PP2a 28D, Pp2A, Pp2A-28D, Protein phosphatase 2A at 28D, catalytic subunit C of type 2A protein phosphatase, dPP2A, l(2)02496, l(2)s5286, phosphatase 2A catalytic subunit, protein phosphatase 2A )
Protein Name(s) microtubule star,
External Links
FB FBgn0004177

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0000159

protein phosphatase type 2A complex

FB:FBrf0057179
PMID:1320961[1]

ISS: Inferred from Sequence or Structural Similarity

C

From FB

GO:0000226

microtubule cytoskeleton organization

FB:FBrf0193166
PMID:16957085[2]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0000278

mitotic cell cycle

FB:FBrf0192076
PMID:17306545[3]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0004722

protein serine/threonine phosphatase activity

FB:FBrf0057179
PMID:1320961[1]

ISS: Inferred from Sequence or Structural Similarity

F

From FB

GO:0004722

protein serine/threonine phosphatase activity

FB:FBrf0091177
PMID:9004035[4]

IMP: Inferred from Mutant Phenotype

F

From FB

GO:0004722

protein serine/threonine phosphatase activity

FB:FBrf0123819

NAS: Non-traceable Author Statement

F

From FB

GO:0004722

protein serine/threonine phosphatase activity

FB:FBrf0132098
PMID:10908587[5]

NAS: Non-traceable Author Statement

F

From FB

GO:0005737

cytoplasm

FB:FBrf0076752
PMID:7844174[6]

IDA: Inferred from Direct Assay

C

From FB

GO:0005737

cytoplasm

FB:FBrf0207940
PMID:19374896[7]

IDA: Inferred from Direct Assay

C

From FB

GO:0006470

protein dephosphorylation

FB:FBrf0091177
PMID:9004035[4]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0006470

protein dephosphorylation

FB:FBrf0123819

NAS: Non-traceable Author Statement

P

From FB

GO:0006470

protein dephosphorylation

FB:FBrf0132098
PMID:10908587[5]

NAS: Non-traceable Author Statement

P

From FB

GO:0006911

phagocytosis, engulfment

FB:FBrf0191376
PMID:16336044[8]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0007015

actin filament organization

FB:FBrf0167741
PMID:14527345[9]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0007051

spindle organization

FB:FBrf0091177
PMID:9004035[4]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0007059

chromosome segregation

FB:FBrf0192076
PMID:17306545[3]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0007067

mitosis

FB:FBrf0091177
PMID:9004035[4]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0007098

centrosome cycle

FB:FBrf0192076
PMID:17306545[3]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0007155

cell adhesion

FB:FBrf0167741
PMID:14527345[9]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0007406

negative regulation of neuroblast proliferation

FB:FBrf0208148
PMID:19502489[10]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0007465

R7 cell fate commitment

FB:FBrf0086675
PMID:8595878[11]

IGI: Inferred from Genetic Interaction

FB:FBgn0003205

P

From FB

GO:0008360

regulation of cell shape

FB:FBrf0167741
PMID:14527345[9]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0009416

response to light stimulus

FB:FBrf0202809
PMID:18256265[12]

IGI: Inferred from Genetic Interaction

FB:FBgn0004784

P

From FB

GO:0019208

phosphatase regulator activity

FB:FBrf0202809
PMID:18256265[12]

IDA: Inferred from Direct Assay

F

From FB

GO:0045880

positive regulation of smoothened signaling pathway

FB:FBrf0205418
PMID:18245841[13]

IGI: Inferred from Genetic Interaction

FB:FBgn0003444

P

From FB

GO:0045880

positive regulation of smoothened signaling pathway

FB:FBrf0205418
PMID:18245841[13]

IGI: Inferred from Genetic Interaction

FB:FBgn0004644

P

From FB

GO:0048477

oogenesis

FB:FBrf0086675
PMID:8595878[11]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0051225

spindle assembly

FB:FBrf0192076
PMID:17306545[3]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0051298

centrosome duplication

FB:FBrf0212030
PMID:20818332[14]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0055059

asymmetric neuroblast division

FB:FBrf0209035
PMID:19690050[15]

IGI: Inferred from Genetic Interaction

FB:FBgn0002121

P

From FB

GO:0055059

asymmetric neuroblast division

FB:FBrf0209035
PMID:19690050[15]

IGI: Inferred from Genetic Interaction

FB:FBgn0026192

P

From FB

GO:0060070

canonical Wnt receptor signaling pathway

FB:FBrf0208588
PMID:19556239[16]

IMP: Inferred from Mutant Phenotype

P

From FB

GO:0090162

establishment of epithelial cell polarity

FB:FBrf0209035
PMID:19690050[15]

IEP: Inferred from Expression Pattern

P

From FB


Notes

References

See Help:References for how to manage references in GONUTS.
  1. 1.0 1.1 Mayer-Jaekel RE et al. (1992) Molecular cloning and developmental expression of the catalytic and 65-kDa regulatory subunits of protein phosphatase 2A in Drosophila. Mol Biol Cell 3: 287-98 PubMed GONUTS page
  2. Viquez NM et al. (2006) The B' protein phosphatase 2A regulatory subunit well-rounded regulates synaptic growth and cytoskeletal stability at the Drosophila neuromuscular junction. J Neurosci 26: 9293-303 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 Chen F et al. (2007) Multiple protein phosphatases are required for mitosis in Drosophila. Curr Biol 17: 293-303 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 Snaith HA et al. (1996) Deficiency of protein phosphatase 2A uncouples the nuclear and centrosome cycles and prevents attachment of microtubules to the kinetochore in Drosophila microtubule star (mts) embryos. J Cell Sci 109 ( Pt 13): 3001-12 PubMed GONUTS page
  5. 5.0 5.1 Morrison DK et al. (2000) Protein kinases and phosphatases in the Drosophila genome. J Cell Biol 150: F57-62 PubMed GONUTS page
  6. Mayer-Jaekel RE et al. (1994) Drosophila mutants in the 55 kDa regulatory subunit of protein phosphatase 2A show strongly reduced ability to dephosphorylate substrates of p34cdc2. J Cell Sci 107 ( Pt 9): 2609-16 PubMed GONUTS page
  7. Chabu C & Doe CQ (2009) Twins/PP2A regulates aPKC to control neuroblast cell polarity and self-renewal. Dev Biol 330: 399-405 PubMed GONUTS page
  8. Stroschein-Stevenson SL et al. (2006) Identification of Drosophila gene products required for phagocytosis of Candida albicans. PLoS Biol 4: e4 PubMed GONUTS page
  9. 9.0 9.1 9.2 Kiger AA et al. (2003) A functional genomic analysis of cell morphology using RNA interference. J Biol 2: 27 PubMed GONUTS page
  10. Wang C et al. (2009) Protein phosphatase 2A regulates self-renewal of Drosophila neural stem cells. Development 136: 2287-96 PubMed GONUTS page
  11. 11.0 11.1 Wassarman DA et al. (1996) Protein phosphatase 2A positively and negatively regulates Ras1-mediated photoreceptor development in Drosophila. Genes Dev 10: 272-8 PubMed GONUTS page
  12. 12.0 12.1 Wang N et al. (2008) Role of protein phosphatase 2A in regulating the visual signaling in Drosophila. J Neurosci 28: 1444-51 PubMed GONUTS page
  13. 13.0 13.1 Casso DJ et al. (2008) A screen for modifiers of hedgehog signaling in Drosophila melanogaster identifies swm and mts. Genetics 178: 1399-413 PubMed GONUTS page
  14. Müller H et al. (2010) Proteomic and functional analysis of the mitotic Drosophila centrosome. EMBO J 29: 3344-57 PubMed GONUTS page
  15. 15.0 15.1 15.2 Ogawa H et al. (2009) Protein phosphatase 2A negatively regulates aPKC signaling by modulating phosphorylation of Par-6 in Drosophila neuroblast asymmetric divisions. J Cell Sci 122: 3242-9 PubMed GONUTS page
  16. Zhang W et al. (2009) PR55 alpha, a regulatory subunit of PP2A, specifically regulates PP2A-mediated beta-catenin dephosphorylation. J Biol Chem 284: 22649-56 PubMed GONUTS page
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