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Protein

Serine/threonine-protein phosphatase alpha-2 isoform

Gene

Pp1-87B

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

Functioni

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

Catalytic activityi

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

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi62 – 621Manganese 1By similarity
Metal bindingi64 – 641Manganese 1By similarity
Metal bindingi90 – 901Manganese 1By similarity
Metal bindingi90 – 901Manganese 2By similarity
Metal bindingi122 – 1221Manganese 2By similarity
Active sitei123 – 1231Proton donorBy similarity
Metal bindingi171 – 1711Manganese 2By similarity
Metal bindingi246 – 2461Manganese 2By similarity

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • myosin phosphatase activity Source: FlyBase
  • protein serine/threonine phosphatase activity Source: FlyBase

GO - Biological processi

  • adult locomotory behavior Source: FlyBase
  • axon guidance Source: FlyBase
  • chromosome condensation Source: FlyBase
  • chromosome segregation Source: FlyBase
  • learning or memory Source: FlyBase
  • locomotion Source: FlyBase
  • mitotic metaphase plate congression Source: FlyBase
  • mitotic nuclear division Source: FlyBase
  • mitotic spindle assembly Source: FlyBase
  • mitotic spindle elongation Source: FlyBase
  • nervous system development Source: FlyBase
  • olfactory learning Source: FlyBase
  • oogenesis Source: FlyBase
  • phagocytosis Source: FlyBase
  • positive regulation of ERK1 and ERK2 cascade Source: FlyBase
  • positive regulation of Ras protein signal transduction Source: FlyBase
  • protein dephosphorylation Source: FlyBase
  • spindle assembly Source: FlyBase
  • visual learning Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_292430. Circadian Clock.
SignaLinkiP12982.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase alpha-2 isoform (EC:3.1.3.16)
Gene namesi
Name:Pp1-87B
ORF Names:CG5650
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0004103. Pp1-87B.

Subcellular locationi

GO - Cellular componenti

  • polytene chromosome Source: FlyBase
  • protein phosphatase type 1 complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 302302Serine/threonine-protein phosphatase alpha-2 isoformPRO_0000058792Add
BLAST

Proteomic databases

PaxDbiP12982.
PRIDEiP12982.

Expressioni

Gene expression databases

BgeeiP12982.
GenevisibleiP12982. DM.

Interactioni

Subunit structurei

Interacts with Nop17l.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Nop17lQ0E9G33EBI-152633,EBI-150380

Protein-protein interaction databases

BioGridi72126. 36 interactions.
DIPiDIP-18465N.
IntActiP12982. 42 interactions.
MINTiMINT-741838.
STRINGi7227.FBpp0082067.

Structurei

3D structure databases

ProteinModelPortaliP12982.
SMRiP12982. Positions 5-297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000062911.
InParanoidiP12982.
KOiK06269.
OMAiWNENDRG.
OrthoDBiEOG7TJ3K3.
PhylomeDBiP12982.

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.

P12982-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDVMNIDSI ISRLLEVRGA RPGKNVQLSE GEIRGLCLKS REIFLSQPIL
60 70 80 90 100
LELEAPLKIC GDIHGQYYDL LRLFEYGGFP PESNYLFLGD YVDRGKQSLE
110 120 130 140 150
TICLLLAYKI KYSENFFLLR GNHECASINR IYGFYDECKR RYSIKLWKTF
160 170 180 190 200
TDCFNCLPVA AIVDEKIFCC HGGLSPDLTS MEQIRRIMRP TDVPDQGLLC
210 220 230 240 250
DLLWSDPDKD TMGWGENDRG VSFTFGAEVV AKFLQKHEFD LICRAHQVVE
260 270 280 290 300
DGYEFFAKRM LVTLFSAPNY CGEFDNAGAM MSVDDTLMCS FQILKPADKR

KK
Length:302
Mass (Da):34,542
Last modified:January 1, 1990 - v1
Checksum:i68FE054996C9A062
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15583 mRNA. Translation: CAA33609.1.
S47852 Genomic DNA. Translation: AAB23957.1.
AE014297 Genomic DNA. Translation: AAF54810.1.
AY061063 mRNA. Translation: AAL28611.1.
PIRiS12960. PAFF1A.
RefSeqiNP_524937.1. NM_080198.3.
UniGeneiDm.1623.

Genome annotation databases

EnsemblMetazoaiFBtr0082595; FBpp0082067; FBgn0004103.
GeneIDi49260.
KEGGidme:Dmel_CG5650.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15583 mRNA. Translation: CAA33609.1.
S47852 Genomic DNA. Translation: AAB23957.1.
AE014297 Genomic DNA. Translation: AAF54810.1.
AY061063 mRNA. Translation: AAL28611.1.
PIRiS12960. PAFF1A.
RefSeqiNP_524937.1. NM_080198.3.
UniGeneiDm.1623.

3D structure databases

ProteinModelPortaliP12982.
SMRiP12982. Positions 5-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi72126. 36 interactions.
DIPiDIP-18465N.
IntActiP12982. 42 interactions.
MINTiMINT-741838.
STRINGi7227.FBpp0082067.

Proteomic databases

PaxDbiP12982.
PRIDEiP12982.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082595; FBpp0082067; FBgn0004103.
GeneIDi49260.
KEGGidme:Dmel_CG5650.

Organism-specific databases

CTDi49260.
FlyBaseiFBgn0004103. Pp1-87B.

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000062911.
InParanoidiP12982.
KOiK06269.
OMAiWNENDRG.
OrthoDBiEOG7TJ3K3.
PhylomeDBiP12982.

Enzyme and pathway databases

ReactomeiREACT_292430. Circadian Clock.
SignaLinkiP12982.

Miscellaneous databases

ChiTaRSiPp1-87B. fly.
GenomeRNAii49260.
NextBioi839723.
PROiP12982.

Gene expression databases

BgeeiP12982.
GenevisibleiP12982. DM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. 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.

Entry informationi

Entry nameiPP12_DROME
AccessioniPrimary (citable) accession number: P12982
Secondary accession number(s): Q4PIY5, Q9VG75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: July 22, 2015
This is version 152 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.