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Q66JT0

- WEE2_MOUSE

UniProt

Q66JT0 - WEE2_MOUSE

Protein

Wee1-like protein kinase 2

Gene

Wee2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 2 (05 Sep 2006)
      Previous versions | rss
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    Functioni

    Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1 and acts as a key regulator of meiosis during both prophase I and metaphase II. Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphorylating CDK1 at 'Tyr-15', leading to inhibit CDK1 activity and prevent meiotic reentry. Also required for metaphase II exit during egg activation by phosphorylating CDK1 at 'Tyr-15', to ensure exit from meiosis in oocytes and promote pronuclear formation.3 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei237 – 2371ATPCurated
    Active sitei334 – 3341Proton acceptorPROSITE-ProRule annotation
    Metal bindingi339 – 3391Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi375 – 3751Magnesium; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi214 – 2229ATPPROSITE-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 serine/threonine kinase activity Source: InterPro
    5. protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. female meiotic division Source: UniProtKB
    2. female pronucleus assembly Source: UniProtKB
    3. mitotic nuclear division Source: InterPro
    4. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
    5. negative regulation of oocyte maturation Source: UniProtKB
    6. peptidyl-tyrosine phosphorylation Source: GOC
    7. regulation of meiosis I Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Meiosis

    Keywords - Ligandi

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Wee1-like protein kinase 2 (EC:2.7.10.2)
    Alternative name(s):
    Wee1-like protein kinase 1B
    Wee1B kinase
    Short name:
    mWee1B
    Gene namesi
    Name:Wee2
    Synonyms:Wee1b
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:3027899. Wee2.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Localizes mainly in the nucleus. Exported from the nucleus to the cytoplasm before germinal vesicle breakdown (GVBD), allowing meiosis resumption.

    GO - Cellular componenti

    1. centrosome Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151S → A: Abolishes phosphorylation and impairs ability to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage and metaphase II exit during egg activation. 2 Publications
    Mutagenesisi15 – 151S → D: Mimicks phosphorylation state, lesading to enhance kinase activity and promote pronuclear formation. 2 Publications
    Mutagenesisi167 – 1693Missing: Abolishes nuclear localization.
    Mutagenesisi237 – 2371K → M: Loss of function. 2 Publications
    Mutagenesisi311 – 3111L → A: Abolishes the cytoplasmic localization; when associated with A-316; A-320 and A-322. 1 Publication
    Mutagenesisi316 – 3161L → A: Abolishes the cytoplasmic localization; when associated with A-311; A-320 and A-322. 1 Publication
    Mutagenesisi320 – 3201L → A: Abolishes the cytoplasmic localization; when associated with A-311; A-316 and A-322. 1 Publication
    Mutagenesisi322 – 3221L → A: Abolishes the cytoplasmic localization; when associated with A-311; A-316 and A-320. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 555555Wee1-like protein kinase 2PRO_0000248080Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei15 – 151Phosphoserine; by CaMK2 and PKA2 Publications
    Modified residuei71 – 711PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by PKA at Ser-15 in vitro, leading to activate kinase activity. Phosphorylation at Ser-15 by CaMK2, leading to increase its activity and promote metaphase II exit during egg activation.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ66JT0.

    Expressioni

    Tissue specificityi

    Ovary-specific.1 Publication

    Developmental stagei

    Detected only in the oocytes at all developmental stages of the follicle including primary, secondary, preantral, and antral follicles with an increase in signal during development. Readily detectable at the mature oocyte, but disappears at E2.5. Detected in germinal vesicle (GV) and metaphase II-stage oocyte (at protein level).2 Publications

    Gene expression databases

    BgeeiQ66JT0.
    CleanExiMM_WEE2.
    GenevestigatoriQ66JT0.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000038754.

    Structurei

    3D structure databases

    ProteinModelPortaliQ66JT0.
    SMRiQ66JT0. Positions 100-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini208 – 485278Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili488 – 51427Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi167 – 1693Nuclear localization signal
    Motifi310 – 32415Nuclear export signalAdd
    BLAST

    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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00530000063230.
    HOGENOMiHOG000004824.
    HOVERGENiHBG005050.
    InParanoidiQ66JT0.
    KOiK06632.
    OMAiIHELHIS.
    OrthoDBiEOG7N63M9.
    PhylomeDBiQ66JT0.
    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.

    Q66JT0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADTETDQGL NKKLSFSFCE EDTESEGQMT AQDIGGAQSQ KPGREESEEL    50
    EGPVPPTRDE LHTSLSRDKE SPGPDLWKSV SGPPKCPETP VLHSKSKLPV 100
    PTNFSTPKNS LGQPEISLLE KLSSRSSRHM RLTPASLMDE KTSLSLVNIN 150
    PFTPETYRKL LLQSKGKRKT RDYLEETGEE ESKSVQWLPA KRSILQETNM 200
    ASRYEKEFFE IEKIGVGEFG TVYKCIKRLD GCIYAIKRSA KSFSGLSNEL 250
    DLHEVYAHAV LGHHPHVVRY YSSWIEDDHV VIQNEYCNGG SLQAAISENT 300
    ASNNHFQEPK LKDILLQISL GLKYIHNSGM VHLDIKPSNI FICHKMQCDS 350
    PVGPEEAESE ADWFLNASVM YKIGDLGHAT SISKPKVEEG DTRFLANEIL 400
    QENYQHLPKA DIFALGLTIA VAAGAESLPI NGDMWHHIRK GNFPEISQEL 450
    SDDFYGLLKN MIHPAPKERP SAAALARSRI LWPFLEKTDE LQKQLNLEKS 500
    KTATLKRELK KARHIQTPQR EVHHCYYQIC KGSRHLLVGG RRKAPSSFTR 550
    GTSSV 555
    Length:555
    Mass (Da):62,343
    Last modified:September 5, 2006 - v2
    Checksum:i0D3FA3972C626693
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211E → K in AAH80784. (PubMed:15489334)Curated
    Sequence conflicti70 – 701E → G in AAH52883. (PubMed:15489334)Curated
    Sequence conflicti98 – 981L → P in AAH52883. (PubMed:15489334)Curated
    Sequence conflicti118 – 1181L → R in AAH80784. (PubMed:15489334)Curated
    Sequence conflicti138 – 1381M → V in AAH52883. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ011691 mRNA. Translation: AAY44075.1.
    AK163344 mRNA. Translation: BAE37310.1.
    AK143336 mRNA. Translation: BAE25345.1.
    AK139573 mRNA. Translation: BAE24069.1.
    BC052883 mRNA. Translation: AAH52883.1.
    BC080784 mRNA. Translation: AAH80784.1.
    CCDSiCCDS20029.1.
    RefSeqiNP_958758.2. NM_201370.2.
    XP_006506389.1. XM_006506326.1.
    UniGeneiMm.20593.

    Genome annotation databases

    EnsembliENSMUST00000038907; ENSMUSP00000038754; ENSMUSG00000037159.
    GeneIDi381759.
    KEGGimmu:381759.
    UCSCiuc009bmq.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ011691 mRNA. Translation: AAY44075.1 .
    AK163344 mRNA. Translation: BAE37310.1 .
    AK143336 mRNA. Translation: BAE25345.1 .
    AK139573 mRNA. Translation: BAE24069.1 .
    BC052883 mRNA. Translation: AAH52883.1 .
    BC080784 mRNA. Translation: AAH80784.1 .
    CCDSi CCDS20029.1.
    RefSeqi NP_958758.2. NM_201370.2.
    XP_006506389.1. XM_006506326.1.
    UniGenei Mm.20593.

    3D structure databases

    ProteinModelPortali Q66JT0.
    SMRi Q66JT0. Positions 100-510.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000038754.

    Proteomic databases

    PRIDEi Q66JT0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000038907 ; ENSMUSP00000038754 ; ENSMUSG00000037159 .
    GeneIDi 381759.
    KEGGi mmu:381759.
    UCSCi uc009bmq.2. mouse.

    Organism-specific databases

    CTDi 494551.
    MGIi MGI:3027899. Wee2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00530000063230.
    HOGENOMi HOG000004824.
    HOVERGENi HBG005050.
    InParanoidi Q66JT0.
    KOi K06632.
    OMAi IHELHIS.
    OrthoDBi EOG7N63M9.
    PhylomeDBi Q66JT0.
    TreeFami TF101088.

    Miscellaneous databases

    ChiTaRSi WEE2. mouse.
    NextBioi 402507.
    PROi Q66JT0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q66JT0.
    CleanExi MM_WEE2.
    Genevestigatori Q66JT0.

    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. "Wee1B is an oocyte-specific kinase involved in the control of meiotic arrest in the mouse."
      Han S.J., Chen R., Paronetto M.P., Conti M.
      Curr. Biol. 15:1670-1676(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-15, MUTAGENESIS OF SER-15.
      Strain: C57BL/6J.
    2. "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: Egg and Ovary.
    3. "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].
      Strain: C57BL/6J.
      Tissue: Egg.
    4. "Identification and characterization of human Wee1B, a new member of the Wee1 family of Cdk-inhibitory kinases."
      Nakanishi M., Ando H., Watanabe N., Kitamura K., Ito K., Okayama H., Miyamoto T., Agui T., Sasaki M.
      Genes Cells 5:839-847(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    5. "Wee1B, Myt1, and Cdc25 function in distinct compartments of the mouse oocyte to control meiotic resumption."
      Oh J.S., Han S.J., Conti M.
      J. Cell Biol. 188:199-207(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 167-LYS--LYS-169; LYS-237; LEU-311; LEU-316; LEU-320 AND LEU-322.
    6. "Protein tyrosine kinase Wee1B is essential for metaphase II exit in mouse oocytes."
      Oh J.S., Susor A., Conti M.
      Science 332:462-465(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-15, MUTAGENESIS OF SER-15 AND LYS-237.

    Entry informationi

    Entry nameiWEE2_MOUSE
    AccessioniPrimary (citable) accession number: Q66JT0
    Secondary accession number(s): Q4U4S4, Q7TPV9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 90 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