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P12982 (PP12_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase alpha-2 isoform

EC=3.1.3.16
Gene names
Name:Pp1-87B
ORF Names:CG5650
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Is essential for the regulation of mitotic chromosomal segregation as well as regulation of chromatin condensation during interphase. Ref.2 Ref.6

Catalytic activity

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

Cofactor

Binds 2 manganese ions per subunit By similarity.

Subunit structure

Interacts with Nop17l. Ref.7

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult locomotory behavior

Inferred from mutant phenotype PubMed 8382739. Source: FlyBase

axon guidance

Inferred from mutant phenotype PubMed 16280124. Source: FlyBase

chromosome condensation

Inferred from mutant phenotype Ref.2. Source: FlyBase

chromosome segregation

Inferred from mutant phenotype PubMed 17306545. Source: FlyBase

learning or memory

Non-traceable author statement PubMed 11715043. Source: FlyBase

locomotion

Non-traceable author statement PubMed 11715043. Source: FlyBase

mitotic metaphase plate congression

Inferred from mutant phenotype PubMed 17306545. Source: FlyBase

mitotic nuclear division

Inferred from mutant phenotype Ref.2. Source: FlyBase

mitotic spindle elongation

Inferred from mutant phenotype PubMed 17412918. Source: FlyBase

nervous system development

Inferred from mutant phenotype PubMed 8224813. Source: FlyBase

olfactory learning

Inferred from mutant phenotype PubMed 8382739. Source: FlyBase

oogenesis

Inferred from mutant phenotype PubMed 8224813. Source: FlyBase

phagocytosis

Inferred from mutant phenotype PubMed 16336044. Source: FlyBase

protein dephosphorylation

Inferred from mutant phenotype PubMed 8224813. Source: FlyBase

spindle assembly

Inferred from mutant phenotype PubMed 17306545. Source: FlyBase

visual learning

Inferred from mutant phenotype PubMed 8382739. Source: FlyBase

   Cellular_componentpolytene chromosome

Inferred from direct assay PubMed 12524522. Source: FlyBase

protein phosphatase type 1 complex

Inferred from sequence or structural similarity Ref.1. Source: FlyBase

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

myosin phosphatase activity

Inferred from direct assay PubMed 15269282. Source: FlyBase

protein binding

Inferred from physical interaction PubMed 14605208Ref.7. Source: IntAct

protein serine/threonine phosphatase activity

Inferred from mutant phenotype PubMed 8224813. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Nop17lQ0E9G33EBI-152633,EBI-150380

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302Serine/threonine-protein phosphatase alpha-2 isoform
PRO_0000058792

Sites

Active site1231Proton donor By similarity
Metal binding621Manganese 1 By similarity
Metal binding641Manganese 1 By similarity
Metal binding901Manganese 1 By similarity
Metal binding901Manganese 2 By similarity
Metal binding1221Manganese 2 By similarity
Metal binding1711Manganese 2 By similarity
Metal binding2461Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P12982 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 68FE054996C9A062

FASTA30234,542
        10         20         30         40         50         60 
MGDVMNIDSI ISRLLEVRGA RPGKNVQLSE GEIRGLCLKS REIFLSQPIL LELEAPLKIC 

        70         80         90        100        110        120 
GDIHGQYYDL LRLFEYGGFP PESNYLFLGD YVDRGKQSLE TICLLLAYKI KYSENFFLLR 

       130        140        150        160        170        180 
GNHECASINR IYGFYDECKR RYSIKLWKTF TDCFNCLPVA AIVDEKIFCC HGGLSPDLTS 

       190        200        210        220        230        240 
MEQIRRIMRP TDVPDQGLLC DLLWSDPDKD TMGWGENDRG VSFTFGAEVV AKFLQKHEFD 

       250        260        270        280        290        300 
LICRAHQVVE DGYEFFAKRM LVTLFSAPNY CGEFDNAGAM MSVDDTLMCS FQILKPADKR 


KK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and chromosomal localization of Drosophila cDNA encoding the catalytic subunit of protein phosphatase 1 alpha. High conservation between mammalian and insect sequences."
Dombradi V., Axton J.M., Glover D.M., Cohen P.T.W.
Eur. J. Biochem. 183:603-610(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Head.
[2]"Protein phosphorylation is involved in the regulation of chromatin condensation during interphase."
Dombradi V., Cohen P.T.W.
FEBS Lett. 312:21-26(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: Canton-S.
[3]"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.
[4]"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.
[5]"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.
[6]"Protein phosphatase 1 activity in Drosophila mutants with abnormalities in mitosis and chromosome condensation."
Dombradi V., Axton J.M., Barker H.M., Cohen P.T.W.
FEBS Lett. 275:39-43(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Towards a comprehensive analysis of the protein phosphatase 1 interactome in Drosophila."
Bennett D., Lyulcheva E., Alphey L.
J. Mol. Biol. 364:196-212(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NOP17L.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15583 mRNA. Translation: CAA33609.1.
S47852 Genomic DNA. Translation: AAB23957.1.
AE014297 Genomic DNA. Translation: AAF54810.1.
AY061063 mRNA. Translation: AAL28611.1.
PIRPAFF1A. S12960.
RefSeqNP_524937.1. NM_080198.3.
UniGeneDm.1623.

3D structure databases

ProteinModelPortalP12982.
SMRP12982. Positions 5-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid72126. 35 interactions.
DIPDIP-18465N.
IntActP12982. 41 interactions.
MINTMINT-741838.

Proteomic databases

PaxDbP12982.
PRIDEP12982.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0082595; FBpp0082067; FBgn0004103.
GeneID49260.
KEGGdme:Dmel_CG5650.

Organism-specific databases

CTD49260.
FlyBaseFBgn0004103. Pp1-87B.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00530000062911.
InParanoidP12982.
KOK06269.
OMAMGDVMNI.
OrthoDBEOG7TJ3K3.
PhylomeDBP12982.

Enzyme and pathway databases

SignaLinkP12982.

Gene expression databases

BgeeP12982.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPp1-87B. drosophila.
GenomeRNAi49260.
NextBio839723.

Entry information

Entry namePP12_DROME
AccessionPrimary (citable) accession number: P12982
Secondary accession number(s): Q4PIY5, Q9VG75
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: July 9, 2014
This is version 142 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