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P23696

- PP2A_DROME

UniProt

P23696 - PP2A_DROME

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Protein

Serine/threonine-protein phosphatase PP2A

Gene

mts

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi57 – 571Manganese 1By similarity
Metal bindingi59 – 591Manganese 1By similarity
Metal bindingi85 – 851Manganese 1By similarity
Metal bindingi85 – 851Manganese 2By similarity
Metal bindingi117 – 1171Manganese 2By similarity
Active sitei118 – 1181Proton donorBy similarity
Metal bindingi167 – 1671Manganese 2By similarity
Metal bindingi241 – 2411Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphatase regulator activity Source: FlyBase
  3. protein serine/threonine phosphatase activity Source: FlyBase

GO - Biological processi

  1. actin filament organization Source: FlyBase
  2. asymmetric neuroblast division Source: FlyBase
  3. autophagy Source: FlyBase
  4. canonical Wnt signaling pathway Source: FlyBase
  5. cell adhesion Source: FlyBase
  6. centriole replication Source: FlyBase
  7. centrosome cycle Source: FlyBase
  8. centrosome duplication Source: FlyBase
  9. centrosome organization Source: FlyBase
  10. chromosome segregation Source: FlyBase
  11. establishment of epithelial cell polarity Source: FlyBase
  12. microtubule cytoskeleton organization Source: FlyBase
  13. mitotic cell cycle Source: FlyBase
  14. mitotic nuclear division Source: FlyBase
  15. negative regulation of neuroblast proliferation Source: FlyBase
  16. oogenesis Source: FlyBase
  17. phagocytosis Source: FlyBase
  18. positive regulation of smoothened signaling pathway Source: FlyBase
  19. protein dephosphorylation Source: FlyBase
  20. R7 cell fate commitment Source: FlyBase
  21. regulation of catalytic activity Source: GOC
  22. regulation of cell shape Source: FlyBase
  23. response to light stimulus Source: FlyBase
  24. spindle assembly Source: FlyBase
  25. spindle organization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_180232. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_180238. Spry regulation of FGF signaling.
REACT_180845. Cyclin D associated events in G1.
REACT_184313. Initiation of Nuclear Envelope Reformation.
REACT_184356. MASTL Facilitates Mitotic Progression.
REACT_205322. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_206319. Glycolysis.
REACT_220429. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_221837. Integration of energy metabolism.
SignaLinkiP23696.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP2A (EC:3.1.3.16)
Alternative name(s):
Protein microtubule star
Gene namesi
Name:mts
Synonyms:PP2A, Pp2A-28D
ORF Names:CG7109
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0004177. mts.

Subcellular locationi

GO - Cellular componenti

  1. centriole Source: FlyBase
  2. cytoplasm Source: FlyBase
  3. protein phosphatase type 2A complex Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Serine/threonine-protein phosphatase PP2APRO_0000058850Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei309 – 3091Leucine methyl esterBy similarity

Post-translational modificationi

Reversibly methyl esterified on Leu-309 by leucine carboxyl methyltransferase 1 (LCMT1) and protein phosphatase methylesterase 1 (PPME1). Carboxyl methylation influences the affinity of the catalytic subunit for the different regulatory subunits, thereby modulating the PP2A holoenzyme's substrate specificity, enzyme activity and cellular localization (By similarity).By similarity

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP23696.
PRIDEiP23696.

Expressioni

Gene expression databases

BgeeiP23696.

Interactioni

Protein-protein interaction databases

BioGridi70018. 59 interactions.
DIPiDIP-17814N.
IntActiP23696. 5 interactions.
MINTiMINT-333628.
STRINGi7227.FBpp0079148.

Structurei

3D structure databases

ProteinModelPortaliP23696.
SMRiP23696. Positions 7-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-2A subfamily.Curated

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00550000074618.
InParanoidiP23696.
KOiK04382.
OMAiQVKTLCD.
OrthoDBiEOG74N5H2.
PhylomeDBiP23696.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23696-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEDKATTKDL DQWIEQLNEC NQLTETQVRT LCDKAKEILS KESNVQEVKC
60 70 80 90 100
PVTVCGDVHG QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL
110 120 130 140 150
VALKVRYRER ITILRGNHES RQITQVYGFY DECLRKYGNA NVWKYFTDLF
160 170 180 190 200
DYLPLTALVD GQIFCLHGGL SPSIDSLDHI RALDRLQEVP HEGPMCDLLW
210 220 230 240 250
SDPDDRGGWG ISPRGAGYTF GQDISETFNN TNGLTLVSRA HQLVMEGYNW
260 270 280 290 300
CHDRNVVTIF SAPNYCYRCG NQAALMELDD SLKFSFLQFD PAPRRGEPHV

TRRTPDYFL
Length:309
Mass (Da):35,469
Last modified:November 1, 1991 - v1
Checksum:i6F1E2486A514FBAF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55199 mRNA. Translation: CAA38984.1.
X78577 mRNA. Translation: CAA55315.1.
AE014134 Genomic DNA. Translation: AAF52567.2.
AY058571 mRNA. Translation: AAL13800.1.
PIRiS12961.
RefSeqiNP_476805.1. NM_057457.4.
UniGeneiDm.4245.

Genome annotation databases

EnsemblMetazoaiFBtr0079525; FBpp0079148; FBgn0004177.
GeneIDi45959.
KEGGidme:Dmel_CG7109.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55199 mRNA. Translation: CAA38984.1 .
X78577 mRNA. Translation: CAA55315.1 .
AE014134 Genomic DNA. Translation: AAF52567.2 .
AY058571 mRNA. Translation: AAL13800.1 .
PIRi S12961.
RefSeqi NP_476805.1. NM_057457.4.
UniGenei Dm.4245.

3D structure databases

ProteinModelPortali P23696.
SMRi P23696. Positions 7-293.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 70018. 59 interactions.
DIPi DIP-17814N.
IntActi P23696. 5 interactions.
MINTi MINT-333628.
STRINGi 7227.FBpp0079148.

Proteomic databases

PaxDbi P23696.
PRIDEi P23696.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0079525 ; FBpp0079148 ; FBgn0004177 .
GeneIDi 45959.
KEGGi dme:Dmel_CG7109.

Organism-specific databases

CTDi 45959.
FlyBasei FBgn0004177. mts.

Phylogenomic databases

eggNOGi COG0639.
GeneTreei ENSGT00550000074618.
InParanoidi P23696.
KOi K04382.
OMAi QVKTLCD.
OrthoDBi EOG74N5H2.
PhylomeDBi P23696.

Enzyme and pathway databases

Reactomei REACT_180232. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_180238. Spry regulation of FGF signaling.
REACT_180845. Cyclin D associated events in G1.
REACT_184313. Initiation of Nuclear Envelope Reformation.
REACT_184356. MASTL Facilitates Mitotic Progression.
REACT_205322. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_206319. Glycolysis.
REACT_220429. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_221837. Integration of energy metabolism.
SignaLinki P23696.

Miscellaneous databases

ChiTaRSi mts. drosophila.
GenomeRNAii 45959.
NextBioi 838521.

Gene expression databases

Bgeei P23696.

Family and domain databases

Gene3Di 3.60.21.10. 1 hit.
InterProi IPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view ]
Pfami PF00149. Metallophos. 1 hit.
[Graphical view ]
PRINTSi PR00114. STPHPHTASE.
SMARTi SM00156. PP2Ac. 1 hit.
[Graphical view ]
SUPFAMi SSF56300. SSF56300. 1 hit.
PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The structure of protein phosphatase 2A is as highly conserved as that of protein phosphatase 1."
    Orgad S., Brewis N.D., Alphey L., Axton J.M., Dudai Y., Cohen P.T.W.
    FEBS Lett. 275:44-48(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiPP2A_DROME
AccessioniPrimary (citable) accession number: P23696
Secondary accession number(s): Q9VLW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: October 29, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3