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P23696 (PP2A_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PP2A

EC=3.1.3.16
Alternative name(s):
Protein microtubule star
Gene names
Name:mts
Synonyms:PP2A, Pp2A-28D
ORF Names:CG7109
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit By similarity.

Sequence similarities

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

Ontologies

Keywords
   LigandIron
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processR7 cell fate commitment

Inferred from genetic interaction PubMed 8595878. Source: FlyBase

actin filament organization

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

asymmetric neuroblast division

Inferred from genetic interaction PubMed 19690050. Source: FlyBase

autophagy

Inferred from mutant phenotype PubMed 22330894. Source: FlyBase

canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 19556239. Source: FlyBase

cell adhesion

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

centriole replication

Inferred from mutant phenotype PubMed 21987638. Source: FlyBase

centrosome cycle

Inferred from mutant phenotype PubMed 17306545. Source: FlyBase

centrosome duplication

Inferred from mutant phenotype PubMed 20818332. Source: FlyBase

centrosome organization

Inferred from mutant phenotype PubMed 18798690. Source: FlyBase

chromosome segregation

Inferred from mutant phenotype PubMed 17306545. Source: FlyBase

establishment of epithelial cell polarity

Inferred from expression pattern PubMed 19690050. Source: FlyBase

microtubule cytoskeleton organization

Inferred from mutant phenotype PubMed 16957085. Source: FlyBase

mitosis

Inferred from mutant phenotype PubMed 9004035. Source: FlyBase

mitotic cell cycle

Inferred from mutant phenotype PubMed 17306545. Source: FlyBase

negative regulation of neuroblast proliferation

Inferred from mutant phenotype PubMed 19502489. Source: FlyBase

oogenesis

Inferred from mutant phenotype PubMed 8595878. Source: FlyBase

phagocytosis

Inferred from mutant phenotype PubMed 16336044. Source: FlyBase

positive regulation of smoothened signaling pathway

Inferred from genetic interaction PubMed 18245841. Source: FlyBase

protein dephosphorylation

Inferred from mutant phenotype PubMed 9004035. Source: FlyBase

regulation of catalytic activity

Inferred from direct assay PubMed 18256265. Source: GOC

regulation of cell shape

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

response to light stimulus

Inferred from genetic interaction PubMed 18256265. Source: FlyBase

spindle assembly

Inferred from mutant phenotype PubMed 17306545. Source: FlyBase

spindle organization

Inferred from mutant phenotype PubMed 9004035. Source: FlyBase

   Cellular_componentcentriole

Inferred from direct assay PubMed 18798690PubMed 21987638. Source: FlyBase

cytoplasm

Inferred from direct assay PubMed 18798690PubMed 19374896PubMed 7844174. Source: FlyBase

protein phosphatase type 2A complex

Inferred from sequence or structural similarity PubMed 1320961. Source: FlyBase

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatase regulator activity

Inferred from direct assay PubMed 18256265. Source: FlyBase

protein serine/threonine phosphatase activity

Inferred from mutant phenotype PubMed 9004035. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Serine/threonine-protein phosphatase PP2A
PRO_0000058850

Sites

Active site1181Proton donor By similarity
Metal binding571Iron By similarity
Metal binding591Iron By similarity
Metal binding851Iron By similarity
Metal binding851Manganese By similarity
Metal binding1171Manganese By similarity
Metal binding1671Manganese By similarity
Metal binding2411Manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
P23696 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 6F1E2486A514FBAF

FASTA30935,469
        10         20         30         40         50         60 
MEDKATTKDL DQWIEQLNEC NQLTETQVRT LCDKAKEILS KESNVQEVKC PVTVCGDVHG 

        70         80         90        100        110        120 
QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYRER ITILRGNHES 

       130        140        150        160        170        180 
RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALVD GQIFCLHGGL SPSIDSLDHI 

       190        200        210        220        230        240 
RALDRLQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGYTF GQDISETFNN TNGLTLVSRA 

       250        260        270        280        290        300 
HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAALMELDD SLKFSFLQFD PAPRRGEPHV 


TRRTPDYFL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55199 mRNA. Translation: CAA38984.1.
X78577 mRNA. Translation: CAA55315.1.
AE014134 Genomic DNA. Translation: AAF52567.2.
AY058571 mRNA. Translation: AAL13800.1.
PIRS12961.
RefSeqNP_476805.1. NM_057457.3.
UniGeneDm.4245.

3D structure databases

ProteinModelPortalP23696.
SMRP23696. Positions 7-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid70018. 59 interactions.
DIPDIP-17814N.
IntActP23696. 5 interactions.
MINTMINT-333628.
STRING7227.FBpp0079148.

Proteomic databases

PaxDbP23696.
PRIDEP23696.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0079525; FBpp0079148; FBgn0004177.
GeneID45959.
KEGGdme:Dmel_CG7109.

Organism-specific databases

CTD45959.
FlyBaseFBgn0004177. mts.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00550000074618.
InParanoidP23696.
KOK04382.
OMALMACKQL.
OrthoDBEOG74N5H2.
PhylomeDBP23696.

Enzyme and pathway databases

SignaLinkP23696.

Gene expression databases

BgeeP23696.

Family and domain databases

InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSmts. drosophila.
GenomeRNAi45959.
NextBio838521.

Entry information

Entry namePP2A_DROME
AccessionPrimary (citable) accession number: P23696
Secondary accession number(s): Q9VLW4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 16, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase