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P47817 (WEE2A_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 98. 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-A

EC=2.7.10.2
Alternative name(s):
Maternally supplied wee1-like protein kinase 1A
Short name=Xe-wee1A
Gene names
Name:wee2-a
Synonyms:wee1a
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

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. Required to maintain meiotic arrest in oocytes by phosphorylating cdk1 at 'Tyr-15', which inhibits cdk1 activity and prevents meiotic reentry. Negative regulator of mitosis. Involved in the mitotic DNA replication checkpoint. Ref.1 Ref.3 Ref.4 Ref.5

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.1 Ref.5

Subunit structure

Interacts with prmt5; this promotes protesomal degradation of wee2-a in the nucleus. The interaction with prmt5 is disrupted upon activation of the DNA replication checkpoint. Ref.5

Subcellular location

Nucleus. Cytoplasmcytosol Ref.5.

Tissue specificity

Detected in egg (at protein level). Oocyte-specific maternally supplied protein. Present in immature and mature oocytes and in early (pregastrula) embryos, but not in post-gastrula embryos. Ref.3 Ref.4 Ref.5

Developmental stage

Expressed only after meiosis I. Not detected in full-grown stage VI immature oocytes (arrested at prophase I) and in oocytes undergoing germinal vesicle breakdown (GVBD) or meiosis I, while it is present in oocytes from 1-1.5 hour after GVBD, or from the onset of meiosis II. Ref.3 Ref.4

Post-translational modification

Subject to proteasomal degradation in the nucleus.

Sequence similarities

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

Contains 1 protein kinase domain.

Caution

Was initially assigned as wee1 (Ref.1). However, it corresponds to the meiosis-specific protein WEE2 in mammals.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 555555Wee1-like protein kinase 2-A
PRO_0000086813

Regions

Domain210 – 480271Protein kinase
Nucleotide binding216 – 2249ATP By similarity
Coiled coil487 – 51327 Potential

Sites

Active site3371Proton acceptor By similarity
Metal binding3421Magnesium; via carbonyl oxygen By similarity
Metal binding3741Magnesium; via carbonyl oxygen By similarity
Binding site2391ATP By similarity

Amino acid modifications

Modified residue5491Phosphoserine Ref.6

Experimental info

Sequence conflict2281I → V in AAC59664. Ref.1
Sequence conflict4521I → V in AAC59664. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P47817 [UniParc].

Last modified May 31, 2011. Version 2.
Checksum: F51CBA73B0CDA448

FASTA55561,716
        10         20         30         40         50         60 
MRTAMSCGGG LVQRLDFSSS DEEDGLSNGI NEGPQKGSPV SSWRTNNCPF PITPQRNERE 

        70         80         90        100        110        120 
LSPTQELSPS SDYSPDPSVG AECPGTPLHY STWKKLKLCD TPYTPKSLLY KTLPSPGSRV 

       130        140        150        160        170        180 
HCRGQRLLRF VAGTGAELDD PSLVNINPFT PESYRQTHFQ PNGKRKERPE DDCRTDRQMK 

       190        200        210        220        230        240 
YAEKEHPAVF QSKRFVLRET NMGSRYKTEF LEIEKIGAGE FGSVFKCIKR LDGCFYAIKR 

       250        260        270        280        290        300 
SKKPLAGSTD EQLALREVYA HAVLGHHPHV VRYYSAWAED DHMIIQNEYC NGGSLQDLIV 

       310        320        330        340        350        360 
DNNKEGQFVL EQELKEILLQ VSMGLKYIHG SGLVHMDIKP SNIFICRKQT ELGQEESDGE 

       370        380        390        400        410        420 
DDLSSGSVLY KIGDLGHVTS ILNPQVEEGD SRFLANEILQ EDYSQLPKAD IFALGLTIAL 

       430        440        450        460        470        480 
AAGAAPLPCN EDSWHHIRKG NLPHVPQLLT PIFLALLKLL VHPDPVMRPP AASLAKNSVL 

       490        500        510        520        530        540 
RRCVGKAAQL QKQLNVEKFK TAMLERELKA AKLAQTSGKD ECSDLPPMSG FSCRGRKRLV 

       550 
GAKNTRSLSF TCGGY 

« Hide

References

« Hide 'large scale' references
[1]"Cell cycle regulation of a Xenopus Wee1-like kinase."
Mueller P.R., Coleman T.R., Dunphy W.G.
Mol. Biol. Cell 6:119-134(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, PHOSPHORYLATION.
Tissue: Oocyte.
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
[3]"Absence of Wee1 ensures the meiotic cell cycle in Xenopus oocytes."
Nakajo N., Yoshitome S., Iwashita J., Iida M., Uto K., Ueno S., Okamoto K., Sagata N.
Genes Dev. 14:328-338(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[4]"The existence of two distinct Wee1 isoforms in Xenopus: implications for the developmental regulation of the cell cycle."
Okamoto K., Nakajo N., Sagata N.
EMBO J. 21:2472-2484(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[5]"DNA replication checkpoint control of Wee1 stability by vertebrate Hsl7."
Yamada A., Duffy B., Perry J.A., Kornbluth S.
J. Cell Biol. 167:841-849(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PRMT5, SUBCELLULAR LOCATION, PROTEASOMAL DEGRADATION, TISSUE SPECIFICITY.
[6]"Changes in regulatory phosphorylation of Cdc25C Ser287 and Wee1 Ser549 during normal cell cycle progression and checkpoint arrests."
Stanford J.S., Ruderman J.V.
Mol. Biol. Cell 16:5749-5760(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-549.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U13962 mRNA. Translation: AAC59664.1.
BC081031 mRNA. Translation: AAH81031.1.
PIRI51671.
RefSeqNP_001081784.1. NM_001088315.1.
UniGeneXl.1694.

3D structure databases

ProteinModelPortalP47817.
SMRP47817. Positions 202-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid99384. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID398049.
KEGGxla:398049.

Organism-specific databases

CTD398049.
XenbaseXB-GENE-6538740. wee2.

Phylogenomic databases

HOVERGENHBG005050.
KOK06632.

Enzyme and pathway databases

BRENDA2.7.10.2. 6726.

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 nameWEE2A_XENLA
AccessionPrimary (citable) accession number: P47817
Secondary accession number(s): Q66J76
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 31, 2011
Last modified: May 14, 2014
This is version 98 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