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Protein

Cdc25-like protein phosphatase twine

Gene

twe

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

Functioni

Required during meiosis. Regulates the transition from the extended G2 phase to the onset of the first meiotic division.

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei318 – 3181By 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
  • embryonic pattern specification Source: FlyBase
  • male meiosis Source: FlyBase
  • meiotic G2/MI transition Source: FlyBase
  • meiotic nuclear envelope disassembly Source: FlyBase
  • peptidyl-tyrosine dephosphorylation Source: GOC
  • protein dephosphorylation Source: FlyBase
  • regulation of meiotic cell cycle Source: FlyBase
  • regulation of syncytial blastoderm mitotic cell cycle Source: FlyBase
  • spermatogenesis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Meiosis

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:
Cdc25-like protein phosphatase twine (EC:3.1.3.48)
Gene namesi
Name:twe
ORF Names:CG4965
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0002673. twe.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Cdc25-like protein phosphatase twinePRO_0000198659Add
BLAST

Proteomic databases

PaxDbiQ03019.

Expressioni

Tissue specificityi

Expressed in developing male and female germ cells.

Gene expression databases

BgeeiQ03019.
ExpressionAtlasiQ03019. differential.
GenevisibleiQ03019. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
cdc2P235724EBI-138996,EBI-108689

Protein-protein interaction databases

BioGridi60966. 6 interactions.
DIPiDIP-23538N.
IntActiQ03019. 3 interactions.
MINTiMINT-942016.
STRINGi7227.FBpp0080412.

Structurei

3D structure databases

ProteinModelPortaliQ03019.
SMRiQ03019. Positions 221-387.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini265 – 371107RhodanesePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5105.
GeneTreeiENSGT00390000018747.
InParanoidiQ03019.
OMAiRAKTKSW.
OrthoDBiEOG757D02.
PhylomeDBiQ03019.

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.

Q03019-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASKRLMLDV EEEDDESGAC GQENFDPHDA DMEYQAKRRK SAVQETPLQW
60 70 80 90 100
MLKRHIPAST TVLSPITELS QNMNGARLDG TPKSTQRIPA NRTLNNFNSL
110 120 130 140 150
SSRTLGSFSS SCSSYESGNS LDDEYMDMFE MESAENHNLE LPDDLEVLLS
160 170 180 190 200
GQLKSESNLE EMSNKKGSLR RCLSMYPSEQ PEEAVQEPDQ ETNMPMKKMQ
210 220 230 240 250
RKTLSMNDAE IMRALGDEPE LIGDLSKPCT LPCLATGIRH RDLKTISSDT
260 270 280 290 300
LARLIQGEFD EQLGSQGGYE IIDCRYPYEF LGGHIRGAKN LYTRGQIQEA
310 320 330 340 350
FPTLTSNQEN RRIYVFHCEF SSERGPKLLR YLRSNDRSQH THNYPALDYP
360 370 380 390 400
ELYILHNGYK EFFGLYSQLC QPSQYVPMLA PAHNDEFRYF RAKTKSWQCG
410 420
EGGDSGIGGG GSRGLRKSRS RLLYAE
Length:426
Mass (Da):48,320
Last modified:October 1, 1996 - v2
Checksum:i0F8626692B683D08
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481L → M in CAA48783 (PubMed:1286615).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94158 mRNA. Translation: AAA28413.1.
AE014134 Genomic DNA. Translation: AAF53508.1.
AY061266 mRNA. Translation: AAL28814.1.
X69018 mRNA. Translation: CAA48783.1.
PIRiA41910.
RefSeqiNP_001260491.1. NM_001273562.2.
NP_001260492.1. NM_001273563.1.
NP_001260493.1. NM_001273564.2.
NP_476633.1. NM_057285.4.
UniGeneiDm.3667.

Genome annotation databases

EnsemblMetazoaiFBtr0080855; FBpp0080412; FBgn0002673.
FBtr0331444; FBpp0303861; FBgn0002673.
FBtr0331445; FBpp0303862; FBgn0002673.
FBtr0331446; FBpp0303863; FBgn0002673.
GeneIDi34954.
KEGGidme:Dmel_CG4965.
UCSCiCG4965-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94158 mRNA. Translation: AAA28413.1.
AE014134 Genomic DNA. Translation: AAF53508.1.
AY061266 mRNA. Translation: AAL28814.1.
X69018 mRNA. Translation: CAA48783.1.
PIRiA41910.
RefSeqiNP_001260491.1. NM_001273562.2.
NP_001260492.1. NM_001273563.1.
NP_001260493.1. NM_001273564.2.
NP_476633.1. NM_057285.4.
UniGeneiDm.3667.

3D structure databases

ProteinModelPortaliQ03019.
SMRiQ03019. Positions 221-387.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60966. 6 interactions.
DIPiDIP-23538N.
IntActiQ03019. 3 interactions.
MINTiMINT-942016.
STRINGi7227.FBpp0080412.

Proteomic databases

PaxDbiQ03019.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080855; FBpp0080412; FBgn0002673.
FBtr0331444; FBpp0303861; FBgn0002673.
FBtr0331445; FBpp0303862; FBgn0002673.
FBtr0331446; FBpp0303863; FBgn0002673.
GeneIDi34954.
KEGGidme:Dmel_CG4965.
UCSCiCG4965-RA. d. melanogaster.

Organism-specific databases

CTDi34954.
FlyBaseiFBgn0002673. twe.

Phylogenomic databases

eggNOGiCOG5105.
GeneTreeiENSGT00390000018747.
InParanoidiQ03019.
OMAiRAKTKSW.
OrthoDBiEOG757D02.
PhylomeDBiQ03019.

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

ChiTaRSitwe. fly.
GenomeRNAii34954.
NextBioi791075.
PROiQ03019.

Gene expression databases

BgeeiQ03019.
ExpressionAtlasiQ03019. differential.
GenevisibleiQ03019. 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. "Twine, a cdc25 homolog that functions in the male and female germline of Drosophila."
    Alphey L.S., Jimenez J., White-Cooper H., Dawson I., Nurse P., Glover D.M.
    Cell 69:977-988(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region."
    Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.
    , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.
    Genetics 153:179-219(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  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. "The Drosophila cdc25 homolog twine is required for meiosis."
    Courtot C., Fankhauser C., Simanis V., Lehner C.F.
    Development 116:405-416(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-426.

Entry informationi

Entry nameiTWINE_DROME
AccessioniPrimary (citable) accession number: Q03019
Secondary accession number(s): Q9V454
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 137 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.