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P47810

- WEE1_MOUSE

UniProt

P47810 - WEE1_MOUSE

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Protein
Wee1-like protein kinase
Gene
Wee1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 By similarity.

Catalytic activityi

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

Cofactori

Binds 2 magnesium ions per subunit By similarity.

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 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei327 – 3271ATP By similarity
Active sitei425 – 4251Proton acceptor By similarity
Metal bindingi430 – 4301Magnesium; via carbonyl oxygen By similarity
Metal bindingi462 – 4621Magnesium; via carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi304 – 3129ATP By similarity

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: MGI
  5. protein kinase activity Source: MGI
  6. protein serine/threonine kinase activity Source: InterPro

GO - Biological processi

  1. establishment of cell polarity Source: MGI
  2. microtubule cytoskeleton organization Source: MGI
  3. mitotic nuclear division Source: UniProtKB-KW
  4. neuron projection morphogenesis Source: MGI
  5. peptidyl-tyrosine phosphorylation Source: MGI
  6. protein phosphorylation Source: MGI
Complete GO annotation...

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. 3474.
ReactomeiREACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_206803. Cyclin A/B1 associated events during G2/M transition.
REACT_223573. G2/M DNA replication checkpoint.
REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.

Names & Taxonomyi

Protein namesi
Recommended name:
Wee1-like protein kinase (EC:2.7.10.2)
Alternative name(s):
Wee1A kinase
Gene namesi
Name:Wee1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:103075. Wee1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 646646Wee1-like protein kinase
PRO_0000086811Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521Phosphoserine; by PLK1 By similarity
Modified residuei123 – 1231Phosphoserine; by CDK1 By similarity
Modified residuei127 – 1271Phosphoserine By similarity
Modified residuei139 – 1391Phosphoserine
Modified residuei150 – 1501Phosphoserine By similarity
Modified residuei190 – 1901Phosphothreonine By similarity
Modified residuei239 – 2391Phosphothreonine By similarity
Modified residuei311 – 3111Phosphoserine By similarity
Modified residuei642 – 6421Phosphoserine; by BRSK1 and BRSK2 By similarity

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-52 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 By similarity.
Dephosphorylated at Thr-239 by CTDP1 By similarity.
Ubiquitinated and degraded at the onset of G2/M phase By similarity.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP47810.

PTM databases

PhosphoSiteiP47810.

Expressioni

Gene expression databases

BgeeiP47810.
CleanExiMM_WEE1.
GenevestigatoriP47810.

Interactioni

Subunit structurei

Binds to 14-3-3 protein zeta.1 Publication

Protein-protein interaction databases

BioGridi204556. 2 interactions.
MINTiMINT-1341936.
STRINGi10090.ENSMUSP00000033326.

Structurei

3D structure databases

ProteinModelPortaliP47810.
SMRiP47810. Positions 264-643.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini298 – 568271Protein kinase
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi34 – 429Poly-Glu
Compositional biasi74 – 774Poly-Arg
Compositional biasi97 – 1015Poly-Gly

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063230.
HOGENOMiHOG000004824.
HOVERGENiHBG005050.
InParanoidiP47810.
KOiK06632.
OMAiRTYWNDS.
OrthoDBiEOG7N63M9.
PhylomeDBiP47810.
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.

P47810-1 [UniParc]FASTAAdd to Basket

« Hide

MSFLSRQQPP PTRRVGAAYS LRQKLIFSPG SDCEEEEEEE EEGSGHSTGE    50
DSAFQEPDSP LPSARSPAEA EAERRRRSPG AEPSSPGELE DDLLLQGGGG 100
GAQAAGGGAE GDSWEEEGFG SSSPVKSPST AYFLSSPFSP VRCGGPGDAS 150
PQGCGAPRAM DDPCSPQPDY PSTPPHKTFR KLRLFDTPHT PKSLLSKARV 200
IDSGSVKLRG SSLFMDTEKS GKREFDTRQT PQVNINPFTP DPVLLHSSGR 250
CRGRKRAYFN DSSEDMEASD YEFEDETRPA KRITITESNM KSRYTTEFHE 300
LEKIGSGEFG SVFKCVKRLD GCIYAIKRSK KPLAGSVDEQ NALREVYAHA 350
VLGQHPHVVR YFSAWAEDDH MLIQNEYCNG GSLADAISEN YRVMSYLTEV 400
ELKDLLLQVG RGLRYIHSMS LVHMDIKPSN IFISRTSIPN AVSEEGDEDD 450
WISNKVMFKI GDLGHVTRIS SPQVEEGDSR FLANEVLQEN YSHLPKADIF 500
ALALTVVCAA GAEPLPRNGE QWHEIRQGRL PRIPQVLSQE VTELLRVMIH 550
PDPERRPSAM ELVKHSVLLS ASRKSAEQLR IELNAEKFKN SLLQKELKKA 600
QMAAKVAAEE RALFTDRMAT RSTTQSNRTS RLIGKKMNRS VSLTIY 646
Length:646
Mass (Da):71,578
Last modified:January 23, 2002 - v2
Checksum:i80B7A156238E8AEA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731E → Q in BAA06404. 1 Publication
Sequence conflicti449 – 4491D → Y in BAA06404. 1 Publication
Sequence conflicti466 – 4661V → D in BAA06404. 1 Publication
Sequence conflicti474 – 4741V → L in BAA06404. 1 Publication
Sequence conflicti521 – 5211Q → H in BAA06404. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D30743 mRNA. Translation: BAA06404.1.
AJ278435 Genomic DNA. Translation: CAC17145.1.
AK011212 mRNA. Translation: BAB27471.1.
BC006852 mRNA. Translation: AAH06852.1.
CCDSiCCDS21743.1.
RefSeqiNP_033542.2. NM_009516.3.
UniGeneiMm.287173.

Genome annotation databases

EnsembliENSMUST00000033326; ENSMUSP00000033326; ENSMUSG00000031016.
GeneIDi22390.
KEGGimmu:22390.
UCSCiuc009jey.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D30743 mRNA. Translation: BAA06404.1 .
AJ278435 Genomic DNA. Translation: CAC17145.1 .
AK011212 mRNA. Translation: BAB27471.1 .
BC006852 mRNA. Translation: AAH06852.1 .
CCDSi CCDS21743.1.
RefSeqi NP_033542.2. NM_009516.3.
UniGenei Mm.287173.

3D structure databases

ProteinModelPortali P47810.
SMRi P47810. Positions 264-643.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204556. 2 interactions.
MINTi MINT-1341936.
STRINGi 10090.ENSMUSP00000033326.

PTM databases

PhosphoSitei P47810.

Proteomic databases

PRIDEi P47810.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033326 ; ENSMUSP00000033326 ; ENSMUSG00000031016 .
GeneIDi 22390.
KEGGi mmu:22390.
UCSCi uc009jey.1. mouse.

Organism-specific databases

CTDi 7465.
MGIi MGI:103075. Wee1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00530000063230.
HOGENOMi HOG000004824.
HOVERGENi HBG005050.
InParanoidi P47810.
KOi K06632.
OMAi RTYWNDS.
OrthoDBi EOG7N63M9.
PhylomeDBi P47810.
TreeFami TF101088.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_206803. Cyclin A/B1 associated events during G2/M transition.
REACT_223573. G2/M DNA replication checkpoint.
REACT_223647. Cyclin A:Cdk2-associated events at S phase entry.

Miscellaneous databases

NextBioi 302765.
PROi P47810.
SOURCEi Search...

Gene expression databases

Bgeei P47810.
CleanExi MM_WEE1.
Genevestigatori P47810.

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

« Hide 'large scale' publications
  1. "Mouse p87wee1 kinase is regulated by M-phase specific phosphorylation."
    Honda R., Tanaka H., Ohba Y., Yasuda H.
    Chromosome Res. 3:300-308(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
    Tissue: Calvaria.
  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].
  3. "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: Embryo.
  4. "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].
  5. "14-3-3 zeta protein binds to the carboxyl half of mouse wee1 kinase."
    Honda R., Ohba Y., Yasuda H.
    Biochem. Biophys. Res. Commun. 230:262-265(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH 14-3-3 ZETA.

Entry informationi

Entry nameiWEE1_MOUSE
AccessioniPrimary (citable) accession number: P47810
Secondary accession number(s): Q9EPL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2002
Last modified: September 3, 2014
This is version 132 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

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