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M-phase inducer phosphatase (EC 3.1.3.48) (Cdc25-like protein) (Protein string)

 MPIP_DROME              Reviewed;         479 AA.
P20483; Q9VAL9;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
25-OCT-2017, entry version 164.
RecName: Full=M-phase inducer phosphatase;
EC=3.1.3.48;
AltName: Full=Cdc25-like protein;
AltName: Full=Protein string;
Name=stg; Synonyms=cdc25; ORFNames=CG1395;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2702688; DOI=10.1016/0092-8674(89)90183-9;
Edgar B.A., O'Farrell P.H.;
"Genetic control of cell division patterns in the Drosophila embryo.";
Cell 57:177-187(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2120044;
Jimenez J., Alphey L., Nurse P., Glover D.M.;
"Complementation of fission yeast cdc2ts and cdc25ts mutants
identifies two cell cycle genes from Drosophila: a cdc2 homologue and
string.";
EMBO J. 9:3565-3571(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: 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
Cdk1 and activate the Cdk1 activity.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate.
-!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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EMBL; M24909; AAA28916.1; -; mRNA.
EMBL; X57495; CAA40732.1; -; mRNA.
EMBL; AE014297; AAF56885.1; -; Genomic_DNA.
EMBL; AY069704; AAL39849.1; -; mRNA.
PIR; A32290; A32290.
RefSeq; NP_001263066.1; NM_001276137.1.
RefSeq; NP_524547.1; NM_079823.4.
UniGene; Dm.3208; -.
ProteinModelPortal; P20483; -.
SMR; P20483; -.
BioGrid; 68333; 31.
DIP; DIP-19931N; -.
IntAct; P20483; 2.
MINT; MINT-848308; -.
STRING; 7227.FBpp0084766; -.
iPTMnet; P20483; -.
PaxDb; P20483; -.
PRIDE; P20483; -.
EnsemblMetazoa; FBtr0085397; FBpp0084766; FBgn0003525.
EnsemblMetazoa; FBtr0334867; FBpp0306890; FBgn0003525.
GeneID; 43466; -.
KEGG; dme:Dmel_CG1395; -.
CTD; 43466; -.
FlyBase; FBgn0003525; stg.
eggNOG; KOG3772; Eukaryota.
eggNOG; COG5105; LUCA.
GeneTree; ENSGT00390000018747; -.
HOGENOM; HOG000263899; -.
InParanoid; P20483; -.
KO; K16723; -.
OMA; KRHRCAA; -.
OrthoDB; EOG091G0LFI; -.
PhylomeDB; P20483; -.
Reactome; R-DME-156711; Polo-like kinase mediated events.
Reactome; R-DME-176187; Activation of ATR in response to replication stress.
Reactome; R-DME-5625740; RHO GTPases activate PKNs.
Reactome; R-DME-5689880; Ub-specific processing proteases.
Reactome; R-DME-69202; Cyclin E associated events during G1/S transition.
Reactome; R-DME-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-DME-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-DME-69656; Cyclin A:Cdk2-associated events at S phase entry.
Reactome; R-DME-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
GenomeRNAi; 43466; -.
PRO; PR:P20483; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0003525; -.
ExpressionAtlas; P20483; differential.
Genevisible; P20483; DM.
GO; GO:0005694; C:chromosome; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:FlyBase.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; NAS:FlyBase.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; IMP:FlyBase.
GO; GO:0007099; P:centriole replication; IMP:FlyBase.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:FlyBase.
GO; GO:0007369; P:gastrulation; IMP:FlyBase.
GO; GO:0007030; P:Golgi organization; IMP:FlyBase.
GO; GO:0007488; P:histoblast morphogenesis; IMP:FlyBase.
GO; GO:0046331; P:lateral inhibition; IMP:FlyBase.
GO; GO:0007498; P:mesoderm development; TAS:FlyBase.
GO; GO:0045792; P:negative regulation of cell size; IMP:FlyBase.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IMP:FlyBase.
GO; GO:0007424; P:open tracheal system development; TAS:FlyBase.
GO; GO:0007422; P:peripheral nervous system development; TAS:FlyBase.
GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IEA:InterPro.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:FlyBase.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:FlyBase.
GO; GO:0045977; P:positive regulation of mitotic cell cycle, embryonic; IMP:FlyBase.
GO; GO:0006470; P:protein dephosphorylation; IDA:FlyBase.
GO; GO:0060305; P:regulation of cell diameter; IMP:FlyBase.
GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:FlyBase.
CDD; cd01530; Cdc25; 1.
Gene3D; 3.40.250.10; -; 1.
InterPro; IPR000751; MPI_Phosphatase.
InterPro; IPR001763; Rhodanese-like_dom.
InterPro; IPR036873; Rhodanese-like_dom_sf.
Pfam; PF00581; Rhodanese; 1.
PRINTS; PR00716; MPIPHPHTASE.
SMART; SM00450; RHOD; 1.
SUPFAM; SSF52821; SSF52821; 1.
PROSITE; PS50206; RHODANESE_3; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Complete proteome; Hydrolase; Mitosis;
Phosphoprotein; Protein phosphatase; Reference proteome.
CHAIN 1 479 M-phase inducer phosphatase.
/FTId=PRO_0000198658.
DOMAIN 316 432 Rhodanese. {ECO:0000255|PROSITE-
ProRule:PRU00173}.
ACT_SITE 379 379 {ECO:0000250}.
MOD_RES 455 455 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CONFLICT 228 228 A -> T (in Ref. 1; AAA28916).
{ECO:0000305}.
SEQUENCE 479 AA; 54095 MW; 68483F3A285962CC CRC64;
MLWETIVEEN NCSMDCNISN NTSSSSSINK MSGSRRARRS LELMSMDQEE LSFYDDDVVP
QDQQRSASPE LMGLLSPEGS PQRFQIVRQP KILPAMGVSS DHTPARSFRI FNSLSSTCSM
ESSMDDEYME LFEMESQSQQ TALGFPSGLN SLISGQIKEQ PAAKSPAGLS MRRPSVRRCL
SMTESNTNST TTPPPKTPET ARDCFKRPEP PASANCSPIQ SKRHRCAAVE KENCPAPSPL
SQVTISHPPP LRKCMSLNDA EIMSALARSE NRNEPELIGD FSKAYALPLM EGRHRDLKSI
SSETVARLLK GEFSDKVASY RIIDCRYPYE FEGGHIEGAK NLYTTEQILD EFLTVQQTEL
QQQQNAESGH KRNIIIFHCE FSSERGPKMS RFLRNLDRER NTNAYPALHY PEIYLLHNGY
KEFFESHVEL CEPHAYRTML DPAYNEAYRH FRAKSKSWNG DGLGGATGRL KKSRSRLML


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