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P54350 (WEE1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Wee1-like protein kinase

Short name=Dwee1
EC=2.7.10.2
Gene names
Name:wee
ORF Names:CG4488
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length609 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Could act as a negative regulator of entry into mitosis (G2 to M transition). This kinase specifically phosphorylates and inactivates cyclin B1-complexed CDC2. Ref.1

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Cofactor

Binds 2 magnesium ions per subunit By similarity.

Enzyme regulation

Negatively regulated by phosphorylation in the M-phase.

Subcellular location

Nucleus By similarity.

Tissue specificity

Expressed in embryos; expression remains high in the proliferating cells of the central nervous system well after cells in the rest of the embryo have ceased dividing. Ref.1

Developmental stage

Expressed both maternally and zygotically during postblastoderm divisions of embryogenesis. Ref.1

Post-translational modification

Phosphorylated during M and G1 phases By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentNucleus
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcentrosome localization

Inferred from mutant phenotype PubMed 16139207. Source: FlyBase

centrosome separation

Inferred from mutant phenotype PubMed 16139207. Source: FlyBase

embryonic development via the syncytial blastoderm

Traceable author statement PubMed 14616073. Source: FlyBase

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

mitotic cell cycle checkpoint

Inferred from direct assay Ref.1. Source: FlyBase

negative regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from direct assay Ref.1. Source: FlyBase

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 19800237Ref.1. Source: GOC

protein phosphorylation

Non-traceable author statement PubMed 10908587. Source: FlyBase

spindle assembly

Inferred from mutant phenotype PubMed 16139207. Source: FlyBase

   Cellular_componentmicrotubule associated complex

Inferred from direct assay PubMed 18433294. Source: FlyBase

nucleus

Inferred from direct assay Ref.1. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein kinase activity

Non-traceable author statement PubMed 10908587. Source: FlyBase

protein tyrosine kinase activity

Inferred from direct assay PubMed 19800237Ref.1. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 609609Wee1-like protein kinase
PRO_0000086814

Regions

Domain239 – 517279Protein kinase
Nucleotide binding245 – 2539ATP By similarity
Compositional bias122 – 1265Poly-Ala

Sites

Active site3611Proton acceptor By similarity
Metal binding3661Magnesium; via carbonyl oxygen By similarity
Metal binding4121Magnesium; via carbonyl oxygen By similarity
Binding site2681ATP By similarity

Amino acid modifications

Modified residue231Phosphoserine Ref.6
Modified residue251Phosphoserine Ref.6
Modified residue271Phosphoserine Ref.6
Modified residue471Phosphothreonine Ref.6
Modified residue521Phosphoserine Ref.6
Modified residue1651Phosphothreonine Ref.6
Modified residue1681Phosphoserine Ref.6

Experimental info

Sequence conflict35 – 362KL → NV in AAC46913. Ref.1
Sequence conflict721D → G in AAC46913. Ref.1
Sequence conflict2751A → R in AAC46913. Ref.1
Sequence conflict5671N → K in AAC46913. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P54350 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 7E371EFDA2A5CD96

FASTA60968,809
        10         20         30         40         50         60 
MAFRQSEHEM SVTSLDSSVE LRSRSPSPQV FNPRKLRFAD DDFDKDTPEG ASPQHPLQQR 

        70         80         90        100        110        120 
PKLSSGEEQQ LDSKIGKEGG DGDVSMSPPC QKVRALRLFS TPATPKTILQ KSTTQCSNHL 

       130        140        150        160        170        180 
SAAAAAVNAS RRSDDLFRLS ERPRSLPLHN RKLPTQDTAN VNPFTPDSLM AHNKKRCRTQ 

       190        200        210        220        230        240 
FGRENLNLNV NAMQKYLLSD ACDDDVTEEA GDSMREIHQQ APKRLALHDT NISRFKREFM 

       250        260        270        280        290        300 
QVNVIGVGEF GVVFQCVNRL DGCIYAIKKS KKPVAGSSFE KRALNEVWAH AVLGKHDNVV 

       310        320        330        340        350        360 
RYYSAWAEDD HMLIQNEFCD GGSLHARIQD HCLGEAELKI VLMHVIEGLR YIHSNDLVHM 

       370        380        390        400        410        420 
DLKPENIFST MNPNAHKLVE VQPQQTKDDD GMDSVYEELR HSENLVTYKI GDLGHVTSVK 

       430        440        450        460        470        480 
EPYVEEGDCR YLPKEILHED YSNLFKADIF SLGITLFEAA GGGPLPKNGP EWHNLRDGKV 

       490        500        510        520        530        540 
PILPSLSRDF NELIAQMMHP YPDKRPTSQS IFSHPILSAV DSKSKLQLGL ELTVEKRKNE 

       550        560        570        580        590        600 
ILMNKLREAK KQIKLLEQRV NLLAVTNNPD SLDGQRCLRS FTRRMRTPFS SHGKFDSISD 


RNKNVITNI 

« Hide

References

« Hide 'large scale' references
[1]"Drosophila Wee1 kinase rescues fission yeast from mitotic catastrophe and phosphorylates Drosophila Cdc2 in vitro."
Campbell S.D., Sprenger F., Edgar B.A., O'Farrell P.H.
Mol. Biol. Cell 6:1333-1347(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]Campbell S.D.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO C-TERMINUS.
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
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.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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-23; SER-25; SER-27; THR-47; SER-52; THR-165 AND SER-168, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U17223 mRNA. Translation: AAC46913.2.
AE014134 Genomic DNA. Translation: AAF52453.2.
AY118942 mRNA. Translation: AAM50802.1.
RefSeqNP_001260167.1. NM_001273238.1.
NP_477035.1. NM_057687.4.
UniGeneDm.3106.

3D structure databases

ProteinModelPortalP54350.
SMRP54350. Positions 233-587.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid60116. 15 interactions.
DIPDIP-23536N.
IntActP54350. 2 interactions.
MINTMINT-885153.
STRING7227.FBpp0078999.

Proteomic databases

PaxDbP54350.
PRIDEP54350.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0079371; FBpp0078999; FBgn0011737.
FBtr0332329; FBpp0304607; FBgn0011737.
GeneID33965.
KEGGdme:Dmel_CG4488.

Organism-specific databases

CTD33965.
FlyBaseFBgn0011737. wee.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00530000063230.
InParanoidP54350.
KOK06632.
OMACIYAIKK.
OrthoDBEOG7N63M9.
PhylomeDBP54350.

Enzyme and pathway databases

BRENDA2.7.10.2. 1994.
SignaLinkP54350.

Gene expression databases

BgeeP54350.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017164. Wee1-like_protein_kinase.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF037281. Wee1-like_protein_kinase. 1 hit.
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi33965.
NextBio786174.
PROP54350.

Entry information

Entry nameWEE1_DROME
AccessionPrimary (citable) accession number: P54350
Secondary accession number(s): Q9VM70
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase