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Q66JT0 (WEE2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. 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 2

EC=2.7.10.2
Alternative name(s):
Wee1-like protein kinase 1B
Wee1B kinase
Short name=mWee1B
Gene names
Name:Wee2
Synonyms:Wee1b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length555 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.6

Catalytic activity

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

Subcellular location

Cytoplasm. Nucleus. Note: Localizes mainly in the nucleus. Exported from the nucleus to the cytoplasm before germinal vesicle breakdown (GVBD), allowing meiosis resumption. Ref.4 Ref.5

Tissue specificity

Ovary-specific. Ref.1

Developmental stage

Detected only in the oocytes at all developmental stages of the follicle including primary, secondary, preantral, and antral follicles with an increase in signal during development. Readily detectable at the mature oocyte, but disappears at E2.5. Detected in germinal vesicle (GV) and metaphase II-stage oocyte (at protein level). Ref.1 Ref.6

Post-translational modification

Phosphorylated by PKA at Ser-15 in vitro, leading to activate kinase activity. Phosphorylation at Ser-15 by CaMK2, leading to increase its activity and promote metaphase II exit during egg activation. Ref.1 Ref.6

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processMeiosis
   Cellular componentCytoplasm
Nucleus
   DomainCoiled coil
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfemale meiotic division

Inferred from mutant phenotype Ref.1. Source: UniProtKB

female pronucleus assembly

Inferred from mutant phenotype Ref.6. Source: UniProtKB

mitotic nuclear division

Inferred from electronic annotation. Source: InterPro

negative regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from mutant phenotype Ref.6. Source: UniProtKB

negative regulation of oocyte maturation

Inferred from mutant phenotype Ref.1Ref.6. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Traceable author statement Ref.1Ref.6. Source: GOC

regulation of meiosis I

Inferred from mutant phenotype Ref.1. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.5. Source: UniProtKB

nucleus

Inferred from direct assay Ref.5. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: InterPro

protein tyrosine kinase activity

Traceable author statement Ref.1Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 555555Wee1-like protein kinase 2
PRO_0000248080

Regions

Domain208 – 485278Protein kinase
Nucleotide binding214 – 2229ATP By similarity
Coiled coil488 – 51427 Potential
Motif167 – 1693Nuclear localization signal
Motif310 – 32415Nuclear export signal

Sites

Active site3341Proton acceptor By similarity
Metal binding3391Magnesium; via carbonyl oxygen By similarity
Metal binding3751Magnesium; via carbonyl oxygen By similarity
Binding site2371ATP Probable

Amino acid modifications

Modified residue151Phosphoserine; by CaMK2 and PKA Ref.1 Ref.6
Modified residue711Phosphoserine By similarity

Experimental info

Mutagenesis151S → A: Abolishes phosphorylation and impairs ability to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage and metaphase II exit during egg activation. Ref.1 Ref.6
Mutagenesis151S → D: Mimicks phosphorylation state, lesading to enhance kinase activity and promote pronuclear formation. Ref.1 Ref.6
Mutagenesis167 – 1693Missing: Abolishes nuclear localization. Ref.5
Mutagenesis2371K → M: Loss of function. Ref.5 Ref.6
Mutagenesis3111L → A: Abolishes the cytoplasmic localization; when associated with A-316; A-320 and A-322. Ref.5
Mutagenesis3161L → A: Abolishes the cytoplasmic localization; when associated with A-311; A-320 and A-322. Ref.5
Mutagenesis3201L → A: Abolishes the cytoplasmic localization; when associated with A-311; A-316 and A-322. Ref.5
Mutagenesis3221L → A: Abolishes the cytoplasmic localization; when associated with A-311; A-316 and A-320. Ref.5
Sequence conflict211E → K in AAH80784. Ref.3
Sequence conflict701E → G in AAH52883. Ref.3
Sequence conflict981L → P in AAH52883. Ref.3
Sequence conflict1181L → R in AAH80784. Ref.3
Sequence conflict1381M → V in AAH52883. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q66JT0 [UniParc].

Last modified September 5, 2006. Version 2.
Checksum: 0D3FA3972C626693

FASTA55562,343
        10         20         30         40         50         60 
MADTETDQGL NKKLSFSFCE EDTESEGQMT AQDIGGAQSQ KPGREESEEL EGPVPPTRDE 

        70         80         90        100        110        120 
LHTSLSRDKE SPGPDLWKSV SGPPKCPETP VLHSKSKLPV PTNFSTPKNS LGQPEISLLE 

       130        140        150        160        170        180 
KLSSRSSRHM RLTPASLMDE KTSLSLVNIN PFTPETYRKL LLQSKGKRKT RDYLEETGEE 

       190        200        210        220        230        240 
ESKSVQWLPA KRSILQETNM ASRYEKEFFE IEKIGVGEFG TVYKCIKRLD GCIYAIKRSA 

       250        260        270        280        290        300 
KSFSGLSNEL DLHEVYAHAV LGHHPHVVRY YSSWIEDDHV VIQNEYCNGG SLQAAISENT 

       310        320        330        340        350        360 
ASNNHFQEPK LKDILLQISL GLKYIHNSGM VHLDIKPSNI FICHKMQCDS PVGPEEAESE 

       370        380        390        400        410        420 
ADWFLNASVM YKIGDLGHAT SISKPKVEEG DTRFLANEIL QENYQHLPKA DIFALGLTIA 

       430        440        450        460        470        480 
VAAGAESLPI NGDMWHHIRK GNFPEISQEL SDDFYGLLKN MIHPAPKERP SAAALARSRI 

       490        500        510        520        530        540 
LWPFLEKTDE LQKQLNLEKS KTATLKRELK KARHIQTPQR EVHHCYYQIC KGSRHLLVGG 

       550 
RRKAPSSFTR GTSSV 

« Hide

References

« Hide 'large scale' references
[1]"Wee1B is an oocyte-specific kinase involved in the control of meiotic arrest in the mouse."
Han S.J., Chen R., Paronetto M.P., Conti M.
Curr. Biol. 15:1670-1676(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-15, MUTAGENESIS OF SER-15.
Strain: C57BL/6J.
[2]"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: Egg and Ovary.
[3]"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].
Strain: C57BL/6J.
Tissue: Egg.
[4]"Identification and characterization of human Wee1B, a new member of the Wee1 family of Cdk-inhibitory kinases."
Nakanishi M., Ando H., Watanabe N., Kitamura K., Ito K., Okayama H., Miyamoto T., Agui T., Sasaki M.
Genes Cells 5:839-847(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[5]"Wee1B, Myt1, and Cdc25 function in distinct compartments of the mouse oocyte to control meiotic resumption."
Oh J.S., Han S.J., Conti M.
J. Cell Biol. 188:199-207(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 167-LYS--LYS-169; LYS-237; LEU-311; LEU-316; LEU-320 AND LEU-322.
[6]"Protein tyrosine kinase Wee1B is essential for metaphase II exit in mouse oocytes."
Oh J.S., Susor A., Conti M.
Science 332:462-465(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-15, MUTAGENESIS OF SER-15 AND LYS-237.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ011691 mRNA. Translation: AAY44075.1.
AK163344 mRNA. Translation: BAE37310.1.
AK143336 mRNA. Translation: BAE25345.1.
AK139573 mRNA. Translation: BAE24069.1.
BC052883 mRNA. Translation: AAH52883.1.
BC080784 mRNA. Translation: AAH80784.1.
CCDSCCDS20029.1.
RefSeqNP_958758.2. NM_201370.2.
XP_006506389.1. XM_006506326.1.
UniGeneMm.20593.

3D structure databases

ProteinModelPortalQ66JT0.
SMRQ66JT0. Positions 100-510.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000038754.

Proteomic databases

PRIDEQ66JT0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000038907; ENSMUSP00000038754; ENSMUSG00000037159.
GeneID381759.
KEGGmmu:381759.
UCSCuc009bmq.2. mouse.

Organism-specific databases

CTD494551.
MGIMGI:3027899. Wee2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00530000063230.
HOGENOMHOG000004824.
HOVERGENHBG005050.
InParanoidQ66JT0.
KOK06632.
OMAIHELHIS.
OrthoDBEOG7N63M9.
PhylomeDBQ66JT0.
TreeFamTF101088.

Gene expression databases

BgeeQ66JT0.
CleanExMM_WEE2.
GenevestigatorQ66JT0.

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

ChiTaRSWEE2. mouse.
NextBio402507.
PROQ66JT0.
SOURCESearch...

Entry information

Entry nameWEE2_MOUSE
AccessionPrimary (citable) accession number: Q66JT0
Secondary accession number(s): Q4U4S4, Q7TPV9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: July 9, 2014
This is version 88 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