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Protein

Serine/threonine-protein phosphatase PP-Y

Gene

PpY-55A

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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 bindingi60 – 601Manganese 1By similarity
Metal bindingi62 – 621Manganese 1By similarity
Metal bindingi88 – 881Manganese 1By similarity
Metal bindingi88 – 881Manganese 2By similarity
Metal bindingi120 – 1201Manganese 2By similarity
Active sitei121 – 1211Proton donorBy similarity
Metal bindingi169 – 1691Manganese 2By similarity
Metal bindingi244 – 2441Manganese 2By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. protein dephosphorylation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

SignaLinkiP11612.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP-Y (EC:3.1.3.16)
Gene namesi
Name:PpY-55A
Synonyms:PpD19, PPY
ORF Names:CG10930
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0003140. PpY-55A.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. nucleus Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 314314Serine/threonine-protein phosphatase PP-YPRO_0000058889Add
BLAST

Proteomic databases

PaxDbiP11612.

Expressioni

Gene expression databases

BgeeiP11612.

Structurei

3D structure databases

ProteinModelPortaliP11612.
SMRiP11612. Positions 9-294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000062911.
InParanoidiP11612.
KOiK01090.
OMAiLWADLNH.
OrthoDBiEOG7CK377.
PhylomeDBiP11612.

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.

P11612-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVLTTHEID CIIKELTSLN GSECTLKEEL IERLIQQTRE VIKWQPMLLE
60 70 80 90 100
LQAPVNICGD IHGQFTDLLR IFKACGFPPK ANYLFLGDYV DRGKQSLETI
110 120 130 140 150
CLLFAYKVKY PLNFFLLRGN HESASINKIY GFYDEIKRRH TVRLWHSFTD
160 170 180 190 200
CFNWLPVAAL VGERIFCCHG GLSPSLRNLQ QINHIQRPTD IPDEGIMCDL
210 220 230 240 250
LWADLNHTTK GWGHNDRGVS FTFDKVIVRD FLKAFDLQLM VRAHEVVEDG
260 270 280 290 300
YEFFANRQLV TVFSAPNYCG MMNNAGGVMS VSTDLICSFV IILPCHKYKM
310
IATDANQMPT NEEE
Length:314
Mass (Da):35,980
Last modified:August 30, 2005 - v2
Checksum:i6078CB66571261F0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661T → K in AAB22467. (PubMed:1321058)Curated
Sequence conflicti123 – 1231S → C(PubMed:2541022)Curated
Sequence conflicti123 – 1231S → C(PubMed:2166691)Curated
Sequence conflicti147 – 1471S → N(PubMed:2541022)Curated
Sequence conflicti147 – 1471S → N(PubMed:2166691)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07510 mRNA. Translation: CAA68808.1.
AE013599 Genomic DNA. Translation: AAF57771.1.
AY075165 mRNA. Translation: AAL68035.1.
S40001 Genomic DNA. Translation: AAB22467.1.
PIRiS03963. PAFFY.
RefSeqiNP_001286554.1. NM_001299625.1.
NP_476689.1. NM_057341.4.
UniGeneiDm.3593.

Genome annotation databases

EnsemblMetazoaiFBtr0086817; FBpp0085996; FBgn0003140.
GeneIDi48532.
KEGGidme:Dmel_CG10930.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07510 mRNA. Translation: CAA68808.1.
AE013599 Genomic DNA. Translation: AAF57771.1.
AY075165 mRNA. Translation: AAL68035.1.
S40001 Genomic DNA. Translation: AAB22467.1.
PIRiS03963. PAFFY.
RefSeqiNP_001286554.1. NM_001299625.1.
NP_476689.1. NM_057341.4.
UniGeneiDm.3593.

3D structure databases

ProteinModelPortaliP11612.
SMRiP11612. Positions 9-294.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PaxDbiP11612.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086817; FBpp0085996; FBgn0003140.
GeneIDi48532.
KEGGidme:Dmel_CG10930.

Organism-specific databases

CTDi48532.
FlyBaseiFBgn0003140. PpY-55A.

Phylogenomic databases

eggNOGiCOG0639.
GeneTreeiENSGT00530000062911.
InParanoidiP11612.
KOiK01090.
OMAiLWADLNH.
OrthoDBiEOG7CK377.
PhylomeDBiP11612.

Enzyme and pathway databases

SignaLinkiP11612.

Miscellaneous databases

GenomeRNAii48532.
NextBioi839446.

Gene expression databases

BgeeiP11612.

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. "Molecular cloning and chromosomal localization of a novel Drosophila protein phosphatase."
    Dombradi V., Axton J.M., Glover D.M., Cohen P.T.W.
    FEBS Lett. 247:391-395(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Head.
  2. "Protein serine/threonine phosphatases; an expanding family."
    Cohen P.T.W., Brewis N.D., Hughes V., Mann D.J.
    FEBS Lett. 268:355-359(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: Testis.
  6. "Polymerase chain reactions using Saccharomyces, Drosophila and human DNA predict a large family of protein serine/threonine phosphatases."
    Chen M.X., Chen Y.H., Cohen P.T.W.
    FEBS Lett. 306:54-58(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-87.

Entry informationi

Entry nameiPPY_DROME
AccessioniPrimary (citable) accession number: P11612
Secondary accession number(s): Q26247, Q9V8A0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: August 30, 2005
Last modified: January 7, 2015
This is version 112 of the entry and version 2 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.