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P47810 (WEE1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Wee1-like protein kinase

EC=2.7.10.2
Alternative name(s):
Wee1A kinase
Gene names
Name:Wee1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length646 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 2 magnesium ions per subunit By similarity.

Enzyme regulation

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.

Subunit structure

Binds to 14-3-3 protein zeta. Ref.5

Subcellular location

Nucleus By similarity.

Post-translational modification

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.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. WEE1 subfamily.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 646646Wee1-like protein kinase
PRO_0000086811

Regions

Domain298 – 568271Protein kinase
Nucleotide binding304 – 3129ATP By similarity
Compositional bias34 – 429Poly-Glu
Compositional bias74 – 774Poly-Arg
Compositional bias97 – 1015Poly-Gly

Sites

Active site4251Proton acceptor By similarity
Metal binding4301Magnesium; via carbonyl oxygen By similarity
Metal binding4621Magnesium; via carbonyl oxygen By similarity
Binding site3271ATP By similarity

Amino acid modifications

Modified residue521Phosphoserine; by PLK1 By similarity
Modified residue1231Phosphoserine; by CDK1 By similarity
Modified residue1271Phosphoserine By similarity
Modified residue1391Phosphoserine
Modified residue1501Phosphoserine By similarity
Modified residue1901Phosphothreonine By similarity
Modified residue2391Phosphothreonine By similarity
Modified residue3111Phosphoserine By similarity
Modified residue6421Phosphoserine; by BRSK1 and BRSK2 By similarity

Experimental info

Sequence conflict731E → Q in BAA06404. Ref.1
Sequence conflict4491D → Y in BAA06404. Ref.1
Sequence conflict4661V → D in BAA06404. Ref.1
Sequence conflict4741V → L in BAA06404. Ref.1
Sequence conflict5211Q → H in BAA06404. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P47810 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 80B7A156238E8AEA

FASTA64671,578
        10         20         30         40         50         60 
MSFLSRQQPP PTRRVGAAYS LRQKLIFSPG SDCEEEEEEE EEGSGHSTGE DSAFQEPDSP 

        70         80         90        100        110        120 
LPSARSPAEA EAERRRRSPG AEPSSPGELE DDLLLQGGGG GAQAAGGGAE GDSWEEEGFG 

       130        140        150        160        170        180 
SSSPVKSPST AYFLSSPFSP VRCGGPGDAS PQGCGAPRAM DDPCSPQPDY PSTPPHKTFR 

       190        200        210        220        230        240 
KLRLFDTPHT PKSLLSKARV IDSGSVKLRG SSLFMDTEKS GKREFDTRQT PQVNINPFTP 

       250        260        270        280        290        300 
DPVLLHSSGR CRGRKRAYFN DSSEDMEASD YEFEDETRPA KRITITESNM KSRYTTEFHE 

       310        320        330        340        350        360 
LEKIGSGEFG SVFKCVKRLD GCIYAIKRSK KPLAGSVDEQ NALREVYAHA VLGQHPHVVR 

       370        380        390        400        410        420 
YFSAWAEDDH MLIQNEYCNG GSLADAISEN YRVMSYLTEV ELKDLLLQVG RGLRYIHSMS 

       430        440        450        460        470        480 
LVHMDIKPSN IFISRTSIPN AVSEEGDEDD WISNKVMFKI GDLGHVTRIS SPQVEEGDSR 

       490        500        510        520        530        540 
FLANEVLQEN YSHLPKADIF ALALTVVCAA GAEPLPRNGE QWHEIRQGRL PRIPQVLSQE 

       550        560        570        580        590        600 
VTELLRVMIH PDPERRPSAM ELVKHSVLLS ASRKSAEQLR IELNAEKFKN SLLQKELKKA 

       610        620        630        640 
QMAAKVAAEE RALFTDRMAT RSTTQSNRTS RLIGKKMNRS VSLTIY 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D30743 mRNA. Translation: BAA06404.1.
AJ278435 Genomic DNA. Translation: CAC17145.1.
AK011212 mRNA. Translation: BAB27471.1.
BC006852 mRNA. Translation: AAH06852.1.
RefSeqNP_033542.2. NM_009516.3.
UniGeneMm.287173.

3D structure databases

ProteinModelPortalP47810.
SMRP47810. Positions 264-643.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204556. 2 interactions.
MINTMINT-1341936.
STRING10090.ENSMUSP00000033326.

PTM databases

PhosphoSiteP47810.

Proteomic databases

PRIDEP47810.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033326; ENSMUSP00000033326; ENSMUSG00000031016.
GeneID22390.
KEGGmmu:22390.
UCSCuc009jey.1. mouse.

Organism-specific databases

CTD7465.
MGIMGI:103075. Wee1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00530000063230.
HOGENOMHOG000004824.
HOVERGENHBG005050.
InParanoidP47810.
KOK06632.
OMARTYWNDS.
OrthoDBEOG7N63M9.
PhylomeDBP47810.
TreeFamTF101088.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.

Gene expression databases

BgeeP47810.
CleanExMM_WEE1.
GenevestigatorP47810.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR017164. Wee1-like_protein_kinase.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF037281. Wee1-like_protein_kinase. 1 hit.
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio302765.
PROP47810.
SOURCESearch...

Entry information

Entry nameWEE1_MOUSE
AccessionPrimary (citable) accession number: P47810
Secondary accession number(s): Q9EPL7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2002
Last modified: April 16, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot