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P47817

- WEE2A_XENLA

UniProt

P47817 - WEE2A_XENLA

Protein

Wee1-like protein kinase 2-A

Gene

wee2-a

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 100 (01 Oct 2014)
      Sequence version 2 (31 May 2011)
      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. Required to maintain meiotic arrest in oocytes by phosphorylating cdk1 at 'Tyr-15', which inhibits cdk1 activity and prevents meiotic reentry. Negative regulator of mitosis. Involved in the mitotic DNA replication checkpoint.4 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.2 PublicationsPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei239 – 2391ATPPROSITE-ProRule annotation
    Active sitei337 – 3371Proton acceptorPROSITE-ProRule annotation
    Metal bindingi342 – 3421Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi374 – 3741Magnesium; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi216 – 2249ATPPROSITE-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. meiotic nuclear division Source: UniProtKB-KW
    2. mitotic DNA replication checkpoint Source: UniProtKB
    3. mitotic nuclear division Source: UniProtKB-KW
    4. peptidyl-tyrosine phosphorylation Source: UniProtKB
    5. regulation of mitosis Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Cell cycle, Cell division, Meiosis, Mitosis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 6726.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Wee1-like protein kinase 2-A (EC:2.7.10.2)
    Alternative name(s):
    Maternally supplied wee1-like protein kinase 1A
    Short name:
    Xe-wee1A
    Gene namesi
    Name:wee2-a
    Synonyms:wee1a
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-6538740. wee2.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasmcytosol 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 555555Wee1-like protein kinase 2-APRO_0000086813Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei549 – 5491Phosphoserine2 Publications

    Post-translational modificationi

    Subject to proteasomal degradation in the nucleus.

    Keywords - PTMi

    Phosphoprotein

    Expressioni

    Tissue specificityi

    Detected in egg (at protein level). Oocyte-specific maternally supplied protein. Present in immature and mature oocytes and in early (pregastrula) embryos, but not in post-gastrula embryos.3 Publications

    Developmental stagei

    Expressed only after meiosis I. Not detected in full-grown stage VI immature oocytes (arrested at prophase I) and in oocytes undergoing germinal vesicle breakdown (GVBD) or meiosis I, while it is present in oocytes from 1-1.5 hour after GVBD, or from the onset of meiosis II.2 Publications

    Interactioni

    Subunit structurei

    Interacts with prmt5; this promotes protesomal degradation of wee2-a in the nucleus. The interaction with prmt5 is disrupted upon activation of the DNA replication checkpoint.1 Publication

    Protein-protein interaction databases

    BioGridi99384. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP47817.
    SMRiP47817. Positions 202-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini210 – 480271Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili487 – 51327Sequence AnalysisAdd
    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

    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.

    P47817-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRTAMSCGGG LVQRLDFSSS DEEDGLSNGI NEGPQKGSPV SSWRTNNCPF    50
    PITPQRNERE LSPTQELSPS SDYSPDPSVG AECPGTPLHY STWKKLKLCD 100
    TPYTPKSLLY KTLPSPGSRV HCRGQRLLRF VAGTGAELDD PSLVNINPFT 150
    PESYRQTHFQ PNGKRKERPE DDCRTDRQMK YAEKEHPAVF QSKRFVLRET 200
    NMGSRYKTEF LEIEKIGAGE FGSVFKCIKR LDGCFYAIKR SKKPLAGSTD 250
    EQLALREVYA HAVLGHHPHV VRYYSAWAED DHMIIQNEYC NGGSLQDLIV 300
    DNNKEGQFVL EQELKEILLQ VSMGLKYIHG SGLVHMDIKP SNIFICRKQT 350
    ELGQEESDGE DDLSSGSVLY KIGDLGHVTS ILNPQVEEGD SRFLANEILQ 400
    EDYSQLPKAD IFALGLTIAL AAGAAPLPCN EDSWHHIRKG NLPHVPQLLT 450
    PIFLALLKLL VHPDPVMRPP AASLAKNSVL RRCVGKAAQL QKQLNVEKFK 500
    TAMLERELKA AKLAQTSGKD ECSDLPPMSG FSCRGRKRLV GAKNTRSLSF 550
    TCGGY 555
    Length:555
    Mass (Da):61,716
    Last modified:May 31, 2011 - v2
    Checksum:iF51CBA73B0CDA448
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti228 – 2281I → V in AAC59664. (PubMed:7749193)Curated
    Sequence conflicti452 – 4521I → V in AAC59664. (PubMed:7749193)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13962 mRNA. Translation: AAC59664.1.
    BC081031 mRNA. Translation: AAH81031.1.
    PIRiI51671.
    RefSeqiNP_001081784.1. NM_001088315.1.
    UniGeneiXl.1694.

    Genome annotation databases

    GeneIDi398049.
    KEGGixla:398049.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13962 mRNA. Translation: AAC59664.1 .
    BC081031 mRNA. Translation: AAH81031.1 .
    PIRi I51671.
    RefSeqi NP_001081784.1. NM_001088315.1.
    UniGenei Xl.1694.

    3D structure databases

    ProteinModelPortali P47817.
    SMRi P47817. Positions 202-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 99384. 1 interaction.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 398049.
    KEGGi xla:398049.

    Organism-specific databases

    CTDi 398049.
    Xenbasei XB-GENE-6538740. wee2.

    Phylogenomic databases

    HOVERGENi HBG005050.
    KOi K06632.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 6726.

    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. "Cell cycle regulation of a Xenopus Wee1-like kinase."
      Mueller P.R., Coleman T.R., Dunphy W.G.
      Mol. Biol. Cell 6:119-134(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, PHOSPHORYLATION.
      Tissue: Oocyte.
    2. NIH - Xenopus Gene Collection (XGC) project
      Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryo.
    3. "Absence of Wee1 ensures the meiotic cell cycle in Xenopus oocytes."
      Nakajo N., Yoshitome S., Iwashita J., Iida M., Uto K., Ueno S., Okamoto K., Sagata N.
      Genes Dev. 14:328-338(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    4. "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: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    5. "DNA replication checkpoint control of Wee1 stability by vertebrate Hsl7."
      Yamada A., Duffy B., Perry J.A., Kornbluth S.
      J. Cell Biol. 167:841-849(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PRMT5, SUBCELLULAR LOCATION, PROTEASOMAL DEGRADATION, TISSUE SPECIFICITY.
    6. "Changes in regulatory phosphorylation of Cdc25C Ser287 and Wee1 Ser549 during normal cell cycle progression and checkpoint arrests."
      Stanford J.S., Ruderman J.V.
      Mol. Biol. Cell 16:5749-5760(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-549.

    Entry informationi

    Entry nameiWEE2A_XENLA
    AccessioniPrimary (citable) accession number: P47817
    Secondary accession number(s): Q66J76
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: May 31, 2011
    Last modified: October 1, 2014
    This is version 100 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    Was initially assigned as wee1 (PubMed:7749193). However, it corresponds to the meiosis-specific protein WEE2 in mammals.1 Publication

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3