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P30291

- WEE1_HUMAN

UniProt

P30291 - WEE1_HUMAN

Protein

Wee1-like protein kinase

Gene

WEE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      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.

    Catalytic activityi

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

    Cofactori

    Binds 2 magnesium ions per subunit.

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei328 – 3281ATPPROSITE-ProRule annotation
    Active sitei426 – 4261Proton acceptorPROSITE-ProRule annotation
    Metal bindingi431 – 4311Magnesium; via carbonyl oxygen1 Publication
    Metal bindingi463 – 4631Magnesium; via carbonyl oxygen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi305 – 3139ATPPROSITE-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: IntAct
    5. protein serine/threonine kinase activity Source: InterPro
    6. protein tyrosine kinase activity Source: ProtInc

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. establishment of cell polarity Source: Ensembl
    3. G1/S transition of mitotic cell cycle Source: Reactome
    4. G2/M transition of mitotic cell cycle Source: Reactome
    5. microtubule cytoskeleton organization Source: Ensembl
    6. mitotic cell cycle Source: Reactome
    7. mitotic nuclear division Source: UniProtKB-KW
    8. neuron projection morphogenesis Source: Ensembl
    9. regulation of cell cycle Source: Reactome

    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. 2681.
    ReactomeiREACT_1006. Polo-like kinase mediated events.
    REACT_1846. G2/M DNA replication checkpoint.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_407. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
    REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
    SignaLinkiP30291.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Wee1-like protein kinase (EC:2.7.10.2)
    Short name:
    WEE1hu
    Alternative name(s):
    Wee1A kinase
    Gene namesi
    Name:WEE1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:12761. WEE1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. nucleoplasm Source: Reactome
    3. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi53 – 531S → A: Abolishes phosphorylation by PLK1 and CDK1 and binding of the SCF(BTRC) complex, leading to stabilization of the protein; when associated with A-123. 1 Publication
    Mutagenesisi116 – 1172EE → AA: Impairs binding of the SCF(BTRC) complex.
    Mutagenesisi123 – 1231S → A: Abolishes phosphorylation by PLK1 and CDK1 and binding of the SCF(BTRC) complex, leading to stabilization of the protein; when associated with A-53. 1 Publication
    Mutagenesisi328 – 3281K → R: Abolishes activity. 1 Publication
    Mutagenesisi642 – 6421S → A: Abolishes phosphorylation by BRSK1 and BRSK2. 1 Publication

    Organism-specific databases

    PharmGKBiPA366.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 646646Wee1-like protein kinasePRO_0000086810Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 531Phosphoserine; by PLK11 Publication
    Modified residuei123 – 1231Phosphoserine; by CDK11 Publication
    Modified residuei127 – 1271Phosphoserine1 Publication
    Modified residuei139 – 1391Phosphoserine2 Publications
    Modified residuei150 – 1501Phosphoserine1 Publication
    Modified residuei190 – 1901Phosphothreonine1 Publication
    Modified residuei239 – 2391Phosphothreonine1 Publication
    Modified residuei312 – 3121Phosphoserine1 Publication
    Modified residuei642 – 6421Phosphoserine; by BRSK1 and BRSK22 Publications

    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-53 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.7 Publications
    Dephosphorylated at Thr-239 by CTDP1.
    Ubiquitinated and degraded at the onset of G2/M phase.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP30291.
    PaxDbiP30291.
    PRIDEiP30291.

    PTM databases

    PhosphoSiteiP30291.

    Miscellaneous databases

    PMAP-CutDBP30291.

    Expressioni

    Gene expression databases

    ArrayExpressiP30291.
    BgeeiP30291.
    CleanExiHS_WEE1.
    GenevestigatoriP30291.

    Organism-specific databases

    HPAiCAB004619.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BTRCQ9Y2972EBI-914695,EBI-307461
    FBXW11Q9UKB13EBI-914695,EBI-355189
    YWHAZP631043EBI-914695,EBI-347088

    Protein-protein interaction databases

    BioGridi113303. 21 interactions.
    DIPiDIP-37969N.
    IntActiP30291. 8 interactions.
    MINTiMINT-129561.
    STRINGi9606.ENSP00000402084.

    Structurei

    Secondary structure

    1
    646
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi294 – 2985
    Beta strandi299 – 30810
    Beta strandi311 – 3188
    Turni319 – 3213
    Beta strandi324 – 3318
    Beta strandi335 – 3373
    Helixi338 – 35215
    Beta strandi362 – 3687
    Beta strandi371 – 3777
    Helixi384 – 39411
    Helixi400 – 41920
    Helixi429 – 4313
    Beta strandi432 – 4354
    Beta strandi458 – 4614
    Helixi464 – 4663
    Helixi480 – 4823
    Helixi485 – 4884
    Helixi495 – 51016
    Beta strandi518 – 5203
    Helixi521 – 5277
    Helixi540 – 54910
    Helixi554 – 5563
    Helixi560 – 5645
    Helixi567 – 5693

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X8BX-ray1.81A291-575[»]
    2IN6X-ray1.90A291-575[»]
    2IO6X-ray2.20A291-575[»]
    2Z2WX-ray2.22A291-575[»]
    3BI6X-ray2.20A291-575[»]
    3BIZX-ray2.20A291-575[»]
    3CQEX-ray2.50A291-575[»]
    3CR0X-ray2.30A291-575[»]
    DisProtiDP00611.
    ProteinModelPortaliP30291.
    SMRiP30291. Positions 253-640.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30291.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini299 – 569271Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi9 – 124Poly-Pro
    Compositional biasi34 – 4310Poly-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

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000004824.
    HOVERGENiHBG005050.
    InParanoidiP30291.
    KOiK06632.
    OMAiRTYWNDS.
    OrthoDBiEOG7N63M9.
    PhylomeDBiP30291.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30291-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSFLSRQQPP PPRRAGAACT LRQKLIFSPC SDCEEEEEEE EEEGSGHSTG    50
    EDSAFQEPDS PLPPARSPTE PGPERRRSPG PAPGSPGELE EDLLLPGACP 100
    GADEAGGGAE GDSWEEEGFG SSSPVKSPAA PYFLGSSFSP VRCGGPGDAS 150
    PRGCGARRAG EGRRSPRPDH PGTPPHKTFR KLRLFDTPHT PKSLLSKARG 200
    IDSSSVKLRG SSLFMDTEKS GKREFDVRQT PQVNINPFTP DSLLLHSSGQ 250
    CRRRKRTYWN DSCGEDMEAS DYELEDETRP AKRITITESN MKSRYTTEFH 300
    ELEKIGSGEF GSVFKCVKRL DGCIYAIKRS KKPLAGSVDE QNALREVYAH 350
    AVLGQHSHVV RYFSAWAEDD HMLIQNEYCN GGSLADAISE NYRIMSYFKE 400
    AELKDLLLQV GRGLRYIHSM SLVHMDIKPS NIFISRTSIP NAASEEGDED 450
    DWASNKVMFK IGDLGHVTRI SSPQVEEGDS RFLANEVLQE NYTHLPKADI 500
    FALALTVVCA AGAEPLPRNG DQWHEIRQGR LPRIPQVLSQ EFTELLKVMI 550
    HPDPERRPSA MALVKHSVLL SASRKSAEQL RIELNAEKFK NSLLQKELKK 600
    AQMAKAAAEE RALFTDRMAT RSTTQSNRTS RLIGKKMNRS VSLTIY 646
    Length:646
    Mass (Da):71,597
    Last modified:February 1, 1996 - v2
    Checksum:iDB00623D304562A0
    GO
    Isoform 2 (identifier: P30291-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-214: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:432
    Mass (Da):49,072
    Checksum:i48F8E9EC16E4184A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651A → E in CAA43979. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti210 – 2101G → C.1 Publication
    Corresponds to variant rs34412975 [ dbSNP | Ensembl ].
    VAR_041302
    Natural varianti472 – 4721S → I.1 Publication
    Corresponds to variant rs56411856 [ dbSNP | Ensembl ].
    VAR_041303

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 214214Missing in isoform 2. 1 PublicationVSP_044959Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10564 mRNA. Translation: AAB60401.1.
    AJ277546 Genomic DNA. Translation: CAC14173.1.
    AK122837 mRNA. Translation: BAG53753.1.
    AC011979 Genomic DNA. No translation available.
    AC122179 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68586.1.
    CH471064 Genomic DNA. Translation: EAW68587.1.
    CH471064 Genomic DNA. Translation: EAW68588.1.
    X62048 mRNA. Translation: CAA43979.1.
    CCDSiCCDS44536.1. [P30291-2]
    CCDS7800.1. [P30291-1]
    PIRiS55048.
    RefSeqiNP_001137448.1. NM_001143976.1. [P30291-2]
    NP_003381.1. NM_003390.3. [P30291-1]
    UniGeneiHs.249441.

    Genome annotation databases

    EnsembliENST00000299613; ENSP00000299613; ENSG00000166483. [P30291-2]
    ENST00000450114; ENSP00000402084; ENSG00000166483. [P30291-1]
    GeneIDi7465.
    KEGGihsa:7465.
    UCSCiuc001mhs.3. human. [P30291-1]

    Polymorphism databases

    DMDMi1351419.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10564 mRNA. Translation: AAB60401.1 .
    AJ277546 Genomic DNA. Translation: CAC14173.1 .
    AK122837 mRNA. Translation: BAG53753.1 .
    AC011979 Genomic DNA. No translation available.
    AC122179 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68586.1 .
    CH471064 Genomic DNA. Translation: EAW68587.1 .
    CH471064 Genomic DNA. Translation: EAW68588.1 .
    X62048 mRNA. Translation: CAA43979.1 .
    CCDSi CCDS44536.1. [P30291-2 ]
    CCDS7800.1. [P30291-1 ]
    PIRi S55048.
    RefSeqi NP_001137448.1. NM_001143976.1. [P30291-2 ]
    NP_003381.1. NM_003390.3. [P30291-1 ]
    UniGenei Hs.249441.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X8B X-ray 1.81 A 291-575 [» ]
    2IN6 X-ray 1.90 A 291-575 [» ]
    2IO6 X-ray 2.20 A 291-575 [» ]
    2Z2W X-ray 2.22 A 291-575 [» ]
    3BI6 X-ray 2.20 A 291-575 [» ]
    3BIZ X-ray 2.20 A 291-575 [» ]
    3CQE X-ray 2.50 A 291-575 [» ]
    3CR0 X-ray 2.30 A 291-575 [» ]
    DisProti DP00611.
    ProteinModelPortali P30291.
    SMRi P30291. Positions 253-640.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113303. 21 interactions.
    DIPi DIP-37969N.
    IntActi P30291. 8 interactions.
    MINTi MINT-129561.
    STRINGi 9606.ENSP00000402084.

    Chemistry

    BindingDBi P30291.
    ChEMBLi CHEMBL5491.
    GuidetoPHARMACOLOGYi 2278.

    PTM databases

    PhosphoSitei P30291.

    Polymorphism databases

    DMDMi 1351419.

    Proteomic databases

    MaxQBi P30291.
    PaxDbi P30291.
    PRIDEi P30291.

    Protocols and materials databases

    DNASUi 7465.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000299613 ; ENSP00000299613 ; ENSG00000166483 . [P30291-2 ]
    ENST00000450114 ; ENSP00000402084 ; ENSG00000166483 . [P30291-1 ]
    GeneIDi 7465.
    KEGGi hsa:7465.
    UCSCi uc001mhs.3. human. [P30291-1 ]

    Organism-specific databases

    CTDi 7465.
    GeneCardsi GC11P009595.
    HGNCi HGNC:12761. WEE1.
    HPAi CAB004619.
    MIMi 193525. gene.
    neXtProti NX_P30291.
    PharmGKBi PA366.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000004824.
    HOVERGENi HBG005050.
    InParanoidi P30291.
    KOi K06632.
    OMAi RTYWNDS.
    OrthoDBi EOG7N63M9.
    PhylomeDBi P30291.
    TreeFami TF101088.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_1006. Polo-like kinase mediated events.
    REACT_1846. G2/M DNA replication checkpoint.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_407. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
    REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
    SignaLinki P30291.

    Miscellaneous databases

    EvolutionaryTracei P30291.
    GeneWikii Wee1-like_protein_kinase.
    GenomeRNAii 7465.
    NextBioi 29236.
    PMAP-CutDB P30291.
    PROi P30291.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30291.
    Bgeei P30291.
    CleanExi HS_WEE1.
    Genevestigatori P30291.

    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. "Regulation of the human WEE1Hu CDK tyrosine 15-kinase during the cell cycle."
      Watanabe N., Broome M., Hunter T.
      EMBO J. 14:1878-1891(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    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].
      Tissue: Blood.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Amygdala.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Igarashi M.
      Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-214 (ISOFORM 1).
    7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 215-646 (ISOFORM 1).
    8. "Human Wee1 kinase inhibits cell division by phosphorylating p34cdc2 exclusively on Tyr15."
      McGowan C.H., Russell P.
      EMBO J. 12:75-85(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS OF LYS-328.
    9. "Human SAD1 kinase is involved in UV-induced DNA damage checkpoint function."
      Lu R., Niida H., Nakanishi M.
      J. Biol. Chem. 279:31164-31170(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-642.
      Tissue: Testis.
    10. "M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCFbeta-TrCP."
      Watanabe N., Arai H., Nishihara Y., Taniguchi M., Watanabe N., Hunter T., Osada H.
      Proc. Natl. Acad. Sci. U.S.A. 101:4419-4424(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-53 AND SER-123, UBIQUITINATION, MUTAGENESIS OF SER-53; 116-GLU-GLU-117 AND SER-123.
    11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150; THR-190 AND SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Persistence of the cell-cycle checkpoint kinase Wee1 in SadA- and SadB-deficient neurons disrupts neuronal polarity."
      Muller M., Lutter D., Puschel A.W.
      J. Cell Sci. 123:286-294(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-642, MUTAGENESIS OF SER-642.
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Fcp1-dependent dephosphorylation is required for M-phase-promoting factor inactivation at mitosis exit."
      Visconti R., Palazzo L., Della Monica R., Grieco D.
      Nat. Commun. 3:894-894(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-239, DEPHOSPHORYLATION.
    17. "Structure and inhibition of the human cell cycle checkpoint kinase, Wee1A kinase: an atypical tyrosine kinase with a key role in CDK1 regulation."
      Squire C.J., Dickson J.M., Ivanovic I., Baker E.N.
      Structure 13:541-550(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 291-575 IN COMPLEX WITH MAGNESIUM AND AN INHIBITOR.
    18. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-210 AND ILE-472.

    Entry informationi

    Entry nameiWEE1_HUMAN
    AccessioniPrimary (citable) accession number: P30291
    Secondary accession number(s): B3KVE1, D3DQV0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 159 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3