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Q8QGV2

- WEE1B_XENLA

UniProt

Q8QGV2 - WEE1B_XENLA

Protein

Wee1-like protein kinase 1-B

Gene

wee1-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Acts as a zygotic 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.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei277 – 2771ATPPROSITE-ProRule annotation
    Active sitei375 – 3751Proton acceptorPROSITE-ProRule annotation
    Metal bindingi380 – 3801Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi412 – 4121Magnesium; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi254 – 2629ATPPROSITE-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

    GO - Biological processi

    1. mitotic nuclear division Source: UniProtKB-KW

    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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Wee1-like protein kinase 1-B (EC:2.7.10.2)
    Alternative name(s):
    Zygotic wee1-like protein kinase 1B
    Short name:
    Xe-Wee1B
    Short name:
    XeWee1B
    Gene namesi
    Name:wee1-b
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-6254033. wee1.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi181 – 1833NIN → AAA: Impairs without abolishing ability to phosphorylate cdk1.
    Mutagenesisi186 – 1861T → A: Abolishes kinase activity inhibition during M-phase. Does not affect ability to phosphorylate cdk1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 595595Wee1-like protein kinase 1-BPRO_0000409523Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei186 – 1861Phosphothreonine; by cdk11 Publication

    Post-translational modificationi

    Phosphorylation at Thr-186 during M-phase by cdk1 inhibits the kinase activity and leads to interaction with pin1.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Expressioni

    Tissue specificityi

    Zygotically expressed. Present in oocytes and postgastrula embryos (at least until the tailbud stage). Expression begins at the midblastula stage and increases after the early gastrula stage.1 Publication

    Interactioni

    Subunit structurei

    Interacts (when phosphorylated at Thr-186) with pin1.1 Publication

    Protein-protein interaction databases

    BioGridi100680. 1 interaction.
    DIPiDIP-60878N.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8QGV2.
    SMRiQ8QGV2. Positions 240-518.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini248 – 518271Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili526 – 56338Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi69 – 757Poly-Glu

    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

    HOVERGENiHBG005050.
    KOiK06632.

    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.

    Q8QGV2-1 [UniParc]FASTAAdd to Basket

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    MNVQPRNMNV QPRNMNVQPV RHKLFFSDTD EEEEDGHSTG EDSAFQESDS    50
    PVSRQREKQE GKPPGGTWEE LEEEEGFGSS PIKSPGDFFM SDSPSYRQLA 100
    PASPTRSPQG PTSPIPECPG TPPHKTFRKL RLFDTPHTPK SLLSKARGIG 150
    SSALRFRGGT LFREAEKAPK PEFVYSTPQV NINPFTPDSL EIQSSAGLCR 200
    GRKRALLNDS CGEDMEGSDC ELEDEDIRPA KRIPITESNM KSRYATEFHE 250
    LEKIGSGEFG SVFKCVKRLD GCIYAIKRSK KPLAGSVDEQ NALREVYAHA 300
    VLGQHPHVVR YYSAWAEDDH MLIQNEYCNG GSLSDVISEN YRTMQYFTEP 350
    ELKDLLLQVA RGLKYIHSMS LVHMDIKPSN IFISRTTLPN TAVEEADDEE 400
    CGSGKVIYKI GDLGHVTRVS SPQVEEGDSR FLANEVLQEN YTHLAKADIF 450
    ALALTVWSAA GAEPFPTNGD QWHEIRQGKL PRVPQLLSQE FVDLIKLMIS 500
    PDPEKRPSSV ALVKHSVLLS ASRKSAEQLR IELDAEKFKN ALLQKELKKA 550
    QIAKAAAEER AHFPDRIATR STTQNNRTTR LIGKKMNRSV SLTIY 595
    Length:595
    Mass (Da):66,600
    Last modified:June 1, 2002 - v1
    Checksum:i4E90E7FDA341CB1B
    GO

    Sequence cautioni

    The sequence AAH82404.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti67 – 671T → S in AAH82404. 1 PublicationCurated
    Sequence conflicti367 – 3671H → Y in AAH82404. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB071983 mRNA. Translation: BAB86797.1.
    BC082404 mRNA. Translation: AAH82404.1. Different initiation.
    RefSeqiNP_001084186.1. NM_001090717.1.
    UniGeneiXl.9986.

    Genome annotation databases

    GeneIDi399355.
    KEGGixla:399355.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB071983 mRNA. Translation: BAB86797.1 .
    BC082404 mRNA. Translation: AAH82404.1 . Different initiation.
    RefSeqi NP_001084186.1. NM_001090717.1.
    UniGenei Xl.9986.

    3D structure databases

    ProteinModelPortali Q8QGV2.
    SMRi Q8QGV2. Positions 240-518.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 100680. 1 interaction.
    DIPi DIP-60878N.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 399355.
    KEGGi xla:399355.

    Organism-specific databases

    CTDi 399355.
    Xenbasei XB-GENE-6254033. wee1.

    Phylogenomic databases

    HOVERGENi HBG005050.
    KOi K06632.

    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. "The existence of two distinct Wee1 isoforms in Xenopus: implications for the developmental regulation of the cell cycle."
      Okamoto K., Nakajo N., Sagata N.
      EMBO J. 21:2472-2484(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    2. NIH - Xenopus Gene Collection (XGC) project
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.
    3. "Mechanism for inactivation of the mitotic inhibitory kinase Wee1 at M phase."
      Okamoto K., Sagata N.
      Proc. Natl. Acad. Sci. U.S.A. 104:3753-3758(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-186, INTERACTION WITH PIN1, MUTAGENESIS OF 181-ASN--ASN-183 AND THR-186.

    Entry informationi

    Entry nameiWEE1B_XENLA
    AccessioniPrimary (citable) accession number: Q8QGV2
    Secondary accession number(s): Q641D3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 31, 2011
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 81 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3