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E2RSS3 (WEE2_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Gene names
Name:WEE2
Synonyms:WEE1B
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Catalytic activity

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

Subcellular location

Nucleus By similarity.

Post-translational modification

Phosphorylation leads to increase its activity By similarity.

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 componentNucleus
   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 meiosis

Inferred from sequence or structural similarity. Source: UniProtKB

female pronucleus assembly

Inferred from sequence or structural similarity. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: InterPro

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

Inferred from electronic annotation. Source: Ensembl

negative regulation of oocyte maturation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of meiosis I

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcentrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. 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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 567567Wee1-like protein kinase 2
PRO_0000409525

Regions

Domain215 – 494280Protein kinase
Nucleotide binding221 – 2299ATP By similarity
Coiled coil497 – 52327 Potential
Motif174 – 1763Nuclear localization signal By similarity
Motif318 – 33215Nuclear export signal By similarity

Sites

Active site3421Proton acceptor By similarity
Metal binding3471Magnesium; via carbonyl oxygen By similarity
Metal binding3841Magnesium; via carbonyl oxygen By similarity
Binding site2441ATP By similarity

Amino acid modifications

Modified residue771Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
E2RSS3 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: 97C445AF4E232354

FASTA56762,857
        10         20         30         40         50         60 
MDDSSINKEL KQKLNVSYCE EESESEGQKE APESRETQSQ TPDWAEGQES EAKFTPPRTP 

        70         80         90        100        110        120 
SSSIHGVGTF EEKDKMSPDQ ALRTPGPGFH KCPGTPAQPD SRSEVVHCES PYTPKSLLSQ 

       130        140        150        160        170        180 
SVISSTEKLP SRGSKHLRFT PVPFVDEMTS SALVNINPFT PESYRKQFLR SNGKRKTRGD 

       190        200        210        220        230        240 
LEEADPGEGK VEQGLPAKRC VLRETNMASR YEKEFLEVEK IGVGEFGTVY KCIKRLDGCV 

       250        260        270        280        290        300 
YAIKRSMKPV AGLSNENLAL HEVYAHAVLG HHPHVVRYYS AWAEDDHMII QNEYCNGGSL 

       310        320        330        340        350        360 
QTAISENTKS GNHFPELKLK DILLQISLGL KYIHNSGMVH LDIKPSNIFI CHKMQCDSPV 

       370        380        390        400        410        420 
VPEEIENEAD WFLSANVMYK IAGDLGHVTS ISKPKVEEGD SRFLANEILQ EDYQHLPKAD 

       430        440        450        460        470        480 
IFALGLTIAV AAGAESLPAN GAKWHHIREG NLPDIPQKLS EEFHNLLKNM IHPDPSERPS 

       490        500        510        520        530        540 
AAGLARSRVL RPSLRKAEEL QQQLNLEKSK TATLERELRE AQQAWSPQEE HSDPGVSGTP 

       550        560 
TGSRCTKRPV GGKSAKSSSF TCGKSSP 

« Hide

References

[1]"Genome sequence, comparative analysis and haplotype structure of the domestic dog."
Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., Smith D.R. expand/collapse author list , deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.
Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Boxer.

Cross-references

3D structure databases

ProteinModelPortalE2RSS3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Entry information

Entry nameWEE2_CANFA
AccessionPrimary (citable) accession number: E2RSS3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 24 of the entry and version 1 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