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P47810

- WEE1_MOUSE

UniProt

P47810 - WEE1_MOUSE

Protein

Wee1-like protein kinase

Gene

Wee1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (23 Jan 2002)
      Previous versions | rss
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    Functioni

    Acts as a negative regulator of entry into mitosis (G2 to M transition) by protecting the nucleus from cytoplasmically activated cyclin B1-complexed CDK1 before the onset of mitosis by mediating phosphorylation of CDK1 on 'Tyr-15'. Specifically phosphorylates and inactivates cyclin B1-complexed CDK1 reaching a maximum during G2 phase and a minimum as cells enter M phase. Phosphorylation of cyclin B1-CDK1 occurs exclusively on 'Tyr-15' and phosphorylation of monomeric CDK1 does not occur. Its activity increases during S and G2 phases and decreases at M phase when it is hyperphosphorylated. A correlated decrease in protein level occurs at M/G1 phase, probably due to its degradation By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 2 magnesium ions per subunit.By similarity

    Enzyme regulationi

    Synthesis is increased during S and G2 phases, presumably by an increase in transcription; activity is decreased by phosphorylation during m phase. Protein levels fall in M phase as a result of decreased synthesis combined with degradation. Activity seems to be negatively regulated by phosphorylation upon entry into mitosis, although N-terminal phosphorylation might also regulate the protein stability via protection from proteolysis or might regulate the subcellular location By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei327 – 3271ATPPROSITE-ProRule annotation
    Active sitei425 – 4251Proton acceptorPROSITE-ProRule annotation
    Metal bindingi430 – 4301Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi462 – 4621Magnesium; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi304 – 3129ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. magnesium ion binding Source: InterPro
    3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    4. protein binding Source: MGI
    5. protein kinase activity Source: MGI
    6. protein serine/threonine kinase activity Source: InterPro

    GO - Biological processi

    1. establishment of cell polarity Source: MGI
    2. microtubule cytoskeleton organization Source: MGI
    3. mitotic nuclear division Source: UniProtKB-KW
    4. neuron projection morphogenesis Source: MGI
    5. peptidyl-tyrosine phosphorylation Source: MGI
    6. protein phosphorylation Source: MGI

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 3474.
    ReactomeiREACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_206803. Cyclin A/B1 associated events during G2/M transition.
    REACT_223573. G2/M DNA replication checkpoint.
    REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Wee1-like protein kinase (EC:2.7.10.2)
    Alternative name(s):
    Wee1A kinase
    Gene namesi
    Name:Wee1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:103075. Wee1.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 646646Wee1-like protein kinasePRO_0000086811Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei52 – 521Phosphoserine; by PLK1By similarity
    Modified residuei123 – 1231Phosphoserine; by CDK1By similarity
    Modified residuei127 – 1271PhosphoserineBy similarity
    Modified residuei139 – 1391Phosphoserine
    Modified residuei150 – 1501PhosphoserineBy similarity
    Modified residuei190 – 1901PhosphothreonineBy similarity
    Modified residuei239 – 2391PhosphothreonineBy similarity
    Modified residuei311 – 3111PhosphoserineBy similarity
    Modified residuei642 – 6421Phosphoserine; by BRSK1 and BRSK2By similarity

    Post-translational modificationi

    Phosphorylated during M and G1 phases. Also autophosphorylated. Phosphorylation at Ser-642 by BRSK1 and BRSK2 in post-mitotic neurons, leads to down-regulate WEE1 activity in polarized neurons. Phosphorylated at Ser-52 and Ser-123 by PLK1 and CDK1, respectively, generating an signal for degradation that can be recognized by the SCF(BTRC) complex, leading to its ubiquitination and degradation at the onset of G2/M phase By similarity.By similarity
    Dephosphorylated at Thr-239 by CTDP1.By similarity
    Ubiquitinated and degraded at the onset of G2/M phase.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP47810.

    PTM databases

    PhosphoSiteiP47810.

    Expressioni

    Gene expression databases

    BgeeiP47810.
    CleanExiMM_WEE1.
    GenevestigatoriP47810.

    Interactioni

    Subunit structurei

    Binds to 14-3-3 protein zeta.

    Protein-protein interaction databases

    BioGridi204556. 2 interactions.
    MINTiMINT-1341936.
    STRINGi10090.ENSMUSP00000033326.

    Structurei

    3D structure databases

    ProteinModelPortaliP47810.
    SMRiP47810. Positions 264-643.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini298 – 568271Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi34 – 429Poly-Glu
    Compositional biasi74 – 774Poly-Arg
    Compositional biasi97 – 1015Poly-Gly

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00530000063230.
    HOGENOMiHOG000004824.
    HOVERGENiHBG005050.
    InParanoidiP47810.
    KOiK06632.
    OMAiRTYWNDS.
    OrthoDBiEOG7N63M9.
    PhylomeDBiP47810.
    TreeFamiTF101088.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    IPR017164. Wee1-like_protein_kinase.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037281. Wee1-like_protein_kinase. 1 hit.
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P47810-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFLSRQQPP PTRRVGAAYS LRQKLIFSPG SDCEEEEEEE EEGSGHSTGE    50
    DSAFQEPDSP LPSARSPAEA EAERRRRSPG AEPSSPGELE DDLLLQGGGG 100
    GAQAAGGGAE GDSWEEEGFG SSSPVKSPST AYFLSSPFSP VRCGGPGDAS 150
    PQGCGAPRAM DDPCSPQPDY PSTPPHKTFR KLRLFDTPHT PKSLLSKARV 200
    IDSGSVKLRG SSLFMDTEKS GKREFDTRQT PQVNINPFTP DPVLLHSSGR 250
    CRGRKRAYFN DSSEDMEASD YEFEDETRPA KRITITESNM KSRYTTEFHE 300
    LEKIGSGEFG SVFKCVKRLD GCIYAIKRSK KPLAGSVDEQ NALREVYAHA 350
    VLGQHPHVVR YFSAWAEDDH MLIQNEYCNG GSLADAISEN YRVMSYLTEV 400
    ELKDLLLQVG RGLRYIHSMS LVHMDIKPSN IFISRTSIPN AVSEEGDEDD 450
    WISNKVMFKI GDLGHVTRIS SPQVEEGDSR FLANEVLQEN YSHLPKADIF 500
    ALALTVVCAA GAEPLPRNGE QWHEIRQGRL PRIPQVLSQE VTELLRVMIH 550
    PDPERRPSAM ELVKHSVLLS ASRKSAEQLR IELNAEKFKN SLLQKELKKA 600
    QMAAKVAAEE RALFTDRMAT RSTTQSNRTS RLIGKKMNRS VSLTIY 646
    Length:646
    Mass (Da):71,578
    Last modified:January 23, 2002 - v2
    Checksum:i80B7A156238E8AEA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731E → Q in BAA06404. (PubMed:7551544)Curated
    Sequence conflicti449 – 4491D → Y in BAA06404. (PubMed:7551544)Curated
    Sequence conflicti466 – 4661V → D in BAA06404. (PubMed:7551544)Curated
    Sequence conflicti474 – 4741V → L in BAA06404. (PubMed:7551544)Curated
    Sequence conflicti521 – 5211Q → H in BAA06404. (PubMed:7551544)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D30743 mRNA. Translation: BAA06404.1.
    AJ278435 Genomic DNA. Translation: CAC17145.1.
    AK011212 mRNA. Translation: BAB27471.1.
    BC006852 mRNA. Translation: AAH06852.1.
    CCDSiCCDS21743.1.
    RefSeqiNP_033542.2. NM_009516.3.
    UniGeneiMm.287173.

    Genome annotation databases

    EnsembliENSMUST00000033326; ENSMUSP00000033326; ENSMUSG00000031016.
    GeneIDi22390.
    KEGGimmu:22390.
    UCSCiuc009jey.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D30743 mRNA. Translation: BAA06404.1 .
    AJ278435 Genomic DNA. Translation: CAC17145.1 .
    AK011212 mRNA. Translation: BAB27471.1 .
    BC006852 mRNA. Translation: AAH06852.1 .
    CCDSi CCDS21743.1.
    RefSeqi NP_033542.2. NM_009516.3.
    UniGenei Mm.287173.

    3D structure databases

    ProteinModelPortali P47810.
    SMRi P47810. Positions 264-643.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204556. 2 interactions.
    MINTi MINT-1341936.
    STRINGi 10090.ENSMUSP00000033326.

    PTM databases

    PhosphoSitei P47810.

    Proteomic databases

    PRIDEi P47810.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033326 ; ENSMUSP00000033326 ; ENSMUSG00000031016 .
    GeneIDi 22390.
    KEGGi mmu:22390.
    UCSCi uc009jey.1. mouse.

    Organism-specific databases

    CTDi 7465.
    MGIi MGI:103075. Wee1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00530000063230.
    HOGENOMi HOG000004824.
    HOVERGENi HBG005050.
    InParanoidi P47810.
    KOi K06632.
    OMAi RTYWNDS.
    OrthoDBi EOG7N63M9.
    PhylomeDBi P47810.
    TreeFami TF101088.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 3474.
    Reactomei REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_206803. Cyclin A/B1 associated events during G2/M transition.
    REACT_223573. G2/M DNA replication checkpoint.
    REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.

    Miscellaneous databases

    NextBioi 302765.
    PROi P47810.
    SOURCEi Search...

    Gene expression databases

    Bgeei P47810.
    CleanExi MM_WEE1.
    Genevestigatori P47810.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    IPR017164. Wee1-like_protein_kinase.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037281. Wee1-like_protein_kinase. 1 hit.
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mouse p87wee1 kinase is regulated by M-phase specific phosphorylation."
      Honda R., Tanaka H., Ohba Y., Yasuda H.
      Chromosome Res. 3:300-308(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Calvaria.
    2. "Comparative architectural aspects of regions of conserved synteny on human chromosome 11p15.3 and mouse chromosome 7 (including genes WEE1 and LMO1)."
      Cichutek A., Brueckmann T., Seipel B., Hauser H., Schlaubitz S., Prawitt D., Hankeln T., Schmidt E.R., Winterpacht A., Zabel B.U.
      Cytogenet. Cell Genet. 93:277-283(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "14-3-3 zeta protein binds to the carboxyl half of mouse wee1 kinase."
      Honda R., Ohba Y., Yasuda H.
      Biochem. Biophys. Res. Commun. 230:262-265(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH 14-3-3 ZETA.

    Entry informationi

    Entry nameiWEE1_MOUSE
    AccessioniPrimary (citable) accession number: P47810
    Secondary accession number(s): Q9EPL7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3