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A4PES0

- WEE2_PIG

UniProt

A4PES0 - WEE2_PIG

Protein

Wee1-like protein kinase 2

Gene

WEE2

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 57 (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 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.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 sitei243 – 2431ATPPROSITE-ProRule annotation
    Active sitei341 – 3411Proton acceptorPROSITE-ProRule annotation
    Metal bindingi346 – 3461Magnesium; via carbonyl oxygenBy similarity
    Metal bindingi382 – 3821Magnesium; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi220 – 2289ATPPROSITE-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: Ensembl
    3. meiotic prophase I Source: UniProtKB
    4. mitotic nuclear division Source: InterPro
    5. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: Ensembl
    6. negative regulation of oocyte development Source: UniProtKB
    7. negative regulation of oocyte maturation Source: Ensembl
    8. peptidyl-tyrosine phosphorylation Source: GOC
    9. 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:
    pWee1B
    Short name:
    pigWee1B
    Gene namesi
    Name:WEE2
    Synonyms:WEE1B
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Chromosome 18

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi77 – 771S → A: Abolishes phosphorylation and ability to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage. 1 Publication
    Mutagenesisi118 – 1181S → A: Does not affect phosphorylation. 1 Publication
    Mutagenesisi133 – 1331S → A: Does not affect phosphorylation. 1 Publication
    Mutagenesisi149 – 1491S → A: Does not affect phosphorylation. 1 Publication
    Mutagenesisi174 – 1752RK → TT: Abolishes nuclear localization.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 565565Wee1-like protein kinase 2PRO_0000409526Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei77 – 771Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation leads to increase its activity.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Expressioni

    Tissue specificityi

    Ovary-specific.1 Publication

    Developmental stagei

    Detected only in the oocytes throughout oocyte maturation period.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000017471.

    Structurei

    3D structure databases

    ProteinModelPortaliA4PES0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini214 – 492279Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili495 – 52127Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi173 – 1753Nuclear localization signal
    Motifi317 – 33115Nuclear export signalBy similarityAdd
    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.
    KOiK06632.
    OMAiICHKMQS.
    OrthoDBiEOG7N63M9.
    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.

    A4PES0-1 [UniParc]FASTAAdd to Basket

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    MGDNGDNKEL KQKLNFSYSE EEQEDEGQKE AQESKKVQYH TPERCGHQDS    50
    EAKFTPPRTP LNHVCELSTP QVKDRASPDQ GLRTPVSRPH TRPETPAPPD 100
    KSKPPPHCES PFTPRGHSSQ SVISTGKLPS RGSKHLRLTP GPLTDEMTSL 150
    ALVNINPFTP ESYRRQFLKS NGKRKTRRDL EEAGPEEGKV EKGLPAKRCV 200
    LRETNMACRY EKEFLEVEKI GVGEFGTVYK CIKRLDGCVY AIKRSTKPVS 250
    GLSDENLAMH EVYAHSVLGH HPHVVRYYSS WAEDDHMMIQ NEYCNGGSLQ 300
    AAISENAKSG NHFQEPKLKD ILLQISLGLK YIHNYGMVHM DIKPSNIFIC 350
    HKIPSDSPVV PEEAENEADW FLSANVTYKI GDLGHVTSIS EPQVEEGDSR 400
    FLAKEILQEN YQHLPKADIF ALGLTIAVAA GAEALPTNGT SWHHIREGQL 450
    PNIPQDLSKE FYNLLKDMID PDPVARPSAA ALTRSRVLCP SLGRTEELQQ 500
    QLNLEKFKTA TLERELKEVQ RAQSSKEGQS SPGVTGTHTG SRSTRRLVGG 550
    KSAKSSSFTW GQSSP 565
    Length:565
    Mass (Da):62,928
    Last modified:May 31, 2011 - v2
    Checksum:i2855273D6B1548BC
    GO

    Sequence cautioni

    The sequence BAF56108.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB276373 mRNA. Translation: BAF56108.1. Different initiation.
    RefSeqiNP_001090976.2. NM_001097507.2.
    XP_005673170.1. XM_005673113.1.
    UniGeneiSsc.43347.

    Genome annotation databases

    EnsembliENSSSCT00000017953; ENSSSCP00000017471; ENSSSCG00000016489.
    GeneIDi100048934.
    KEGGissc:100048934.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB276373 mRNA. Translation: BAF56108.1 . Different initiation.
    RefSeqi NP_001090976.2. NM_001097507.2.
    XP_005673170.1. XM_005673113.1.
    UniGenei Ssc.43347.

    3D structure databases

    ProteinModelPortali A4PES0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000017471.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSSSCT00000017953 ; ENSSSCP00000017471 ; ENSSSCG00000016489 .
    GeneIDi 100048934.
    KEGGi ssc:100048934.

    Organism-specific databases

    CTDi 399355.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00530000063230.
    HOGENOMi HOG000004824.
    HOVERGENi HBG005050.
    KOi K06632.
    OMAi ICHKMQS.
    OrthoDBi EOG7N63M9.
    TreeFami TF101088.

    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. "Critical effect of pigWee1B on the regulation of meiotic resumption in porcine immature oocytes."
      Shimaoka T., Nishimura T., Kano K., Naito K.
      Cell Cycle 8:2375-2384(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    2. "Insufficient amount of Cdc2 and continuous activation of Wee1 B are the cause of meiotic failure in porcine growing oocytes."
      Nishimura T., Shimaoka T., Kano K., Naito K.
      J. Reprod. Dev. 55:553-557(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SMALL OOCYTES.
    3. "Analyses of the regulatory mechanism of porcine WEE1B: the phosphorylation sites of porcine WEE1B and mouse WEE1B are different."
      Shimaoka T., Nishimura T., Kano K., Naito K.
      J. Reprod. Dev. 57:223-228(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-77, MUTAGENESIS OF SER-77; SER-118; SER-133; SER-149 AND 174-ARG-LYS-175.

    Entry informationi

    Entry nameiWEE2_PIG
    AccessioniPrimary (citable) accession number: A4PES0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 31, 2011
    Last sequence update: May 31, 2011
    Last modified: October 1, 2014
    This is version 57 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Continuous activation of WEE2 is a cause of meiotic failure of small oocytes. In mammals, oocytes with a diameter less than 80% of that of full-grown oocytes cannot start meiotic maturation (PubMed:19550110).1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3