SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P20483

- MPIP_DROME

UniProt

P20483 - MPIP_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
M-phase inducer phosphatase
Gene
stg, cdc25, CG1395
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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 – 3791 By similarity

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: FlyBase
  2. protein tyrosine/serine/threonine phosphatase activity Source: FlyBase

GO - Biological processi

  1. G2/M transition of mitotic cell cycle Source: FlyBase
  2. Golgi organization Source: FlyBase
  3. cell proliferation Source: FlyBase
  4. cellular process Source: FlyBase
  5. centriole replication Source: FlyBase
  6. gastrulation Source: FlyBase
  7. lateral inhibition Source: FlyBase
  8. mesoderm development Source: FlyBase
  9. mitotic cell cycle Source: FlyBase
  10. mitotic nuclear division Source: UniProtKB-KW
  11. negative regulation of cell size Source: FlyBase
  12. negative regulation of mitotic cell cycle Source: FlyBase
  13. open tracheal system development Source: FlyBase
  14. peptidyl-tyrosine dephosphorylation Source: GOC
  15. peripheral nervous system development Source: FlyBase
  16. positive regulation of cell proliferation Source: FlyBase
  17. positive regulation of mitotic cell cycle Source: FlyBase
  18. positive regulation of mitotic cell cycle, embryonic Source: FlyBase
  19. protein dephosphorylation Source: FlyBase
  20. regulation of cell diameter Source: FlyBase
  21. 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_180658. G0 and Early G1.
REACT_208929. Polo-like kinase mediated events.
REACT_218568. Activation of ATR in response to replication stress.
REACT_222733. E2F-enabled inhibition of pre-replication complex formation.
REACT_222970. p53-Independent DNA Damage Response.
REACT_225636. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_225883. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.

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: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003525. stg.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479M-phase inducer phosphatase
PRO_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.

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini316 – 432117Rhodanese
Add
BLAST

Sequence similaritiesi

Belongs to the MPI phosphatase family.
Contains 1 rhodanese domain.

Phylogenomic databases

eggNOGiCOG5105.
GeneTreeiENSGT00390000018747.
HOGENOMiHOG000263899.
InParanoidiP20483.
KOiK16723.
OMAiYMELFEM.
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

MLWETIVEEN NCSMDCNISN NTSSSSSINK MSGSRRARRS LELMSMDQEE    50
LSFYDDDVVP QDQQRSASPE LMGLLSPEGS PQRFQIVRQP KILPAMGVSS 100
DHTPARSFRI FNSLSSTCSM ESSMDDEYME LFEMESQSQQ TALGFPSGLN 150
SLISGQIKEQ PAAKSPAGLS MRRPSVRRCL SMTESNTNST TTPPPKTPET 200
ARDCFKRPEP PASANCSPIQ SKRHRCAAVE KENCPAPSPL SQVTISHPPP 250
LRKCMSLNDA EIMSALARSE NRNEPELIGD FSKAYALPLM EGRHRDLKSI 300
SSETVARLLK GEFSDKVASY RIIDCRYPYE FEGGHIEGAK NLYTTEQILD 350
EFLTVQQTEL QQQQNAESGH KRNIIIFHCE FSSERGPKMS RFLRNLDRER 400
NTNAYPALHY PEIYLLHNGY KEFFESHVEL CEPHAYRTML DPAYNEAYRH 450
FRAKSKSWNG DGLGGATGRL KKSRSRLML 479
Length:479
Mass (Da):54,095
Last modified:December 1, 2000 - v2
Checksum:i68483F3A285962CC
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2281A → T in AAA28916. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_079823.3.
UniGeneiDm.3208.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M24909 mRNA. Translation: AAA28916.1 .
X57495 mRNA. Translation: CAA40732.1 .
AE014297 Genomic DNA. Translation: AAF56885.1 .
AY069704 mRNA. Translation: AAL39849.1 .
PIRi A32290.
RefSeqi NP_001263066.1. NM_001276137.1.
NP_524547.1. NM_079823.3.
UniGenei Dm.3208.

3D structure databases

ProteinModelPortali P20483.
SMRi P20483. Positions 277-439.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 68333. 22 interactions.
DIPi DIP-19931N.
IntActi P20483. 2 interactions.
MINTi MINT-848308.
STRINGi 7227.FBpp0084766.

Proteomic databases

PRIDEi P20483.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0085397 ; FBpp0084766 ; FBgn0003525 .
GeneIDi 43466.
KEGGi dme:Dmel_CG1395.

Organism-specific databases

CTDi 43466.
FlyBasei FBgn0003525. stg.

Phylogenomic databases

eggNOGi COG5105.
GeneTreei ENSGT00390000018747.
HOGENOMi HOG000263899.
InParanoidi P20483.
KOi K16723.
OMAi YMELFEM.
OrthoDBi EOG757D02.
PhylomeDBi P20483.

Enzyme and pathway databases

Reactomei REACT_180658. G0 and Early G1.
REACT_208929. Polo-like kinase mediated events.
REACT_218568. Activation of ATR in response to replication stress.
REACT_222733. E2F-enabled inhibition of pre-replication complex formation.
REACT_222970. p53-Independent DNA Damage Response.
REACT_225636. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_225883. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.

Miscellaneous databases

ChiTaRSi C6orf15. drosophila.
GenomeRNAii 43466.
NextBioi 834076.

Gene expression databases

Bgeei P20483.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
InterProi IPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view ]
Pfami PF00581. Rhodanese. 1 hit.
[Graphical view ]
PRINTSi PR00716. MPIPHPHTASE.
SMARTi SM00450. RHOD. 1 hit.
[Graphical view ]
SUPFAMi SSF52821. SSF52821. 1 hit.
PROSITEi PS50206. RHODANESE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 132 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