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Protein

M-phase inducer phosphatase

Gene

stg

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

Functioni

This protein functions as a dosage-dependent inducer in mitotic control. It is a tyrosine protein phosphatase required for progression of the cell cycle. It may directly dephosphorylate p34(cdc2) and activate the p34(cdc2) kinase activity.

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei379 – 3791By similarity

GO - Molecular functioni

  • protein tyrosine/serine/threonine phosphatase activity Source: FlyBase
  • protein tyrosine phosphatase activity Source: FlyBase

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • cell proliferation Source: FlyBase
  • centriole replication Source: FlyBase
  • G2/M transition of mitotic cell cycle Source: FlyBase
  • gastrulation Source: FlyBase
  • Golgi organization Source: FlyBase
  • lateral inhibition Source: FlyBase
  • mesoderm development Source: FlyBase
  • mitotic cell cycle Source: FlyBase
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of cell size Source: FlyBase
  • negative regulation of mitotic cell cycle Source: FlyBase
  • open tracheal system development Source: FlyBase
  • peptidyl-tyrosine dephosphorylation Source: GOC
  • peripheral nervous system development Source: FlyBase
  • positive regulation of cell proliferation Source: FlyBase
  • positive regulation of mitotic cell cycle Source: FlyBase
  • positive regulation of mitotic cell cycle, embryonic Source: FlyBase
  • protein dephosphorylation Source: FlyBase
  • regulation of cell diameter Source: FlyBase
  • regulation of mitotic cell cycle Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_276179. Cyclin A/B1 associated events during G2/M transition.
REACT_279787. Polo-like kinase mediated events.
REACT_299997. Cyclin A:Cdk2-associated events at S phase entry.
REACT_317616. E2F-enabled inhibition of pre-replication complex formation.
REACT_318147. G0 and Early G1.
REACT_319950. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_323570. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_331765. Activation of ATR in response to replication stress.
REACT_338123. Cyclin E associated events during G1/S transition.
REACT_340065. Cyclin B2 mediated events.
REACT_343247. p53-Independent DNA Damage Response.
REACT_357143. RHO GTPases activate PKNs.

Names & Taxonomyi

Protein namesi
Recommended name:
M-phase inducer phosphatase (EC:3.1.3.48)
Alternative name(s):
Cdc25-like protein
Protein string
Gene namesi
Name:stg
Synonyms:cdc25
ORF Names:CG1395
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003525. stg.

Subcellular locationi

GO - Cellular componenti

  • chromosome Source: FlyBase
  • nucleus Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479M-phase inducer phosphatasePRO_0000198658Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei455 – 4551Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP20483.

Expressioni

Gene expression databases

BgeeiP20483.
GenevisibleiP20483. DM.

Interactioni

Protein-protein interaction databases

BioGridi68333. 22 interactions.
DIPiDIP-19931N.
IntActiP20483. 2 interactions.
MINTiMINT-848308.
STRINGi7227.FBpp0084766.

Structurei

3D structure databases

ProteinModelPortaliP20483.
SMRiP20483. Positions 277-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini316 – 432117RhodanesePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the MPI phosphatase family.Curated
Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5105.
GeneTreeiENSGT00390000018747.
HOGENOMiHOG000263899.
InParanoidiP20483.
KOiK16723.
OMAiRHRDLKS.
OrthoDBiEOG757D02.
PhylomeDBiP20483.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSiPR00716. MPIPHPHTASE.
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20483-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLWETIVEEN NCSMDCNISN NTSSSSSINK MSGSRRARRS LELMSMDQEE
60 70 80 90 100
LSFYDDDVVP QDQQRSASPE LMGLLSPEGS PQRFQIVRQP KILPAMGVSS
110 120 130 140 150
DHTPARSFRI FNSLSSTCSM ESSMDDEYME LFEMESQSQQ TALGFPSGLN
160 170 180 190 200
SLISGQIKEQ PAAKSPAGLS MRRPSVRRCL SMTESNTNST TTPPPKTPET
210 220 230 240 250
ARDCFKRPEP PASANCSPIQ SKRHRCAAVE KENCPAPSPL SQVTISHPPP
260 270 280 290 300
LRKCMSLNDA EIMSALARSE NRNEPELIGD FSKAYALPLM EGRHRDLKSI
310 320 330 340 350
SSETVARLLK GEFSDKVASY RIIDCRYPYE FEGGHIEGAK NLYTTEQILD
360 370 380 390 400
EFLTVQQTEL QQQQNAESGH KRNIIIFHCE FSSERGPKMS RFLRNLDRER
410 420 430 440 450
NTNAYPALHY PEIYLLHNGY KEFFESHVEL CEPHAYRTML DPAYNEAYRH
460 470
FRAKSKSWNG DGLGGATGRL KKSRSRLML
Length:479
Mass (Da):54,095
Last modified:December 1, 2000 - v2
Checksum:i68483F3A285962CC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2281A → T in AAA28916 (PubMed:2702688).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24909 mRNA. Translation: AAA28916.1.
X57495 mRNA. Translation: CAA40732.1.
AE014297 Genomic DNA. Translation: AAF56885.1.
AY069704 mRNA. Translation: AAL39849.1.
PIRiA32290.
RefSeqiNP_001263066.1. NM_001276137.1.
NP_524547.1. NM_079823.4.
UniGeneiDm.3208.

Genome annotation databases

EnsemblMetazoaiFBtr0085397; FBpp0084766; FBgn0003525.
FBtr0334867; FBpp0306890; FBgn0003525.
GeneIDi43466.
KEGGidme:Dmel_CG1395.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M24909 mRNA. Translation: AAA28916.1.
X57495 mRNA. Translation: CAA40732.1.
AE014297 Genomic DNA. Translation: AAF56885.1.
AY069704 mRNA. Translation: AAL39849.1.
PIRiA32290.
RefSeqiNP_001263066.1. NM_001276137.1.
NP_524547.1. NM_079823.4.
UniGeneiDm.3208.

3D structure databases

ProteinModelPortaliP20483.
SMRiP20483. Positions 277-439.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68333. 22 interactions.
DIPiDIP-19931N.
IntActiP20483. 2 interactions.
MINTiMINT-848308.
STRINGi7227.FBpp0084766.

Proteomic databases

PRIDEiP20483.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085397; FBpp0084766; FBgn0003525.
FBtr0334867; FBpp0306890; FBgn0003525.
GeneIDi43466.
KEGGidme:Dmel_CG1395.

Organism-specific databases

CTDi43466.
FlyBaseiFBgn0003525. stg.

Phylogenomic databases

eggNOGiCOG5105.
GeneTreeiENSGT00390000018747.
HOGENOMiHOG000263899.
InParanoidiP20483.
KOiK16723.
OMAiRHRDLKS.
OrthoDBiEOG757D02.
PhylomeDBiP20483.

Enzyme and pathway databases

ReactomeiREACT_276179. Cyclin A/B1 associated events during G2/M transition.
REACT_279787. Polo-like kinase mediated events.
REACT_299997. Cyclin A:Cdk2-associated events at S phase entry.
REACT_317616. E2F-enabled inhibition of pre-replication complex formation.
REACT_318147. G0 and Early G1.
REACT_319950. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_323570. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_331765. Activation of ATR in response to replication stress.
REACT_338123. Cyclin E associated events during G1/S transition.
REACT_340065. Cyclin B2 mediated events.
REACT_343247. p53-Independent DNA Damage Response.
REACT_357143. RHO GTPases activate PKNs.

Miscellaneous databases

GenomeRNAii43466.
NextBioi834076.
PROiP20483.

Gene expression databases

BgeeiP20483.
GenevisibleiP20483. DM.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSiPR00716. MPIPHPHTASE.
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic control of cell division patterns in the Drosophila embryo."
    Edgar B.A., O'Farrell P.H.
    Cell 57:177-187(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complementation of fission yeast cdc2ts and cdc25ts mutants identifies two cell cycle genes from Drosophila: a cdc2 homologue and string."
    Jimenez J., Alphey L., Nurse P., Glover D.M.
    EMBO J. 9:3565-3571(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: Embryo.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiMPIP_DROME
AccessioniPrimary (citable) accession number: P20483
Secondary accession number(s): Q9VAL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: December 1, 2000
Last modified: June 24, 2015
This is version 142 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.