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P47817

- WEE2A_XENLA

UniProt

P47817 - WEE2A_XENLA

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Protein
Wee1-like protein kinase 2-A
Gene
wee2-a, wee1a
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei239 – 2391ATP By similarity
Active sitei337 – 3371Proton acceptor By similarity
Metal bindingi342 – 3421Magnesium; via carbonyl oxygen By similarity
Metal bindingi374 – 3741Magnesium; via carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi216 – 2249ATP 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 serine/threonine kinase activity Source: InterPro
  5. protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. meiotic nuclear division Source: UniProtKB-KW
  2. mitotic DNA replication checkpoint Source: UniProtKB
  3. mitotic nuclear division Source: UniProtKB-KW
  4. peptidyl-tyrosine phosphorylation Source: UniProtKB
  5. regulation of mitosis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Cell cycle, Cell division, Meiosis, Mitosis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 6726.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:wee2-a
Synonyms:wee1a
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6538740. wee2.

Subcellular locationi

Nucleus. Cytoplasmcytosol 1 Publication

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 555555Wee1-like protein kinase 2-A
PRO_0000086813Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei549 – 5491Phosphoserine1 Publication

Post-translational modificationi

Subject to proteasomal degradation in the nucleus.

Keywords - PTMi

Phosphoprotein

Expressioni

Tissue specificityi

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.3 Publications

Developmental stagei

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.2 Publications

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi99384. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP47817.
SMRiP47817. Positions 202-480.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini210 – 480271Protein kinase
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili487 – 51327 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOVERGENiHBG005050.
KOiK06632.

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.

P47817-1 [UniParc]FASTAAdd to Basket

« Hide

MRTAMSCGGG LVQRLDFSSS DEEDGLSNGI NEGPQKGSPV SSWRTNNCPF    50
PITPQRNERE LSPTQELSPS SDYSPDPSVG AECPGTPLHY STWKKLKLCD 100
TPYTPKSLLY KTLPSPGSRV HCRGQRLLRF VAGTGAELDD PSLVNINPFT 150
PESYRQTHFQ PNGKRKERPE DDCRTDRQMK YAEKEHPAVF QSKRFVLRET 200
NMGSRYKTEF LEIEKIGAGE FGSVFKCIKR LDGCFYAIKR SKKPLAGSTD 250
EQLALREVYA HAVLGHHPHV VRYYSAWAED DHMIIQNEYC NGGSLQDLIV 300
DNNKEGQFVL EQELKEILLQ VSMGLKYIHG SGLVHMDIKP SNIFICRKQT 350
ELGQEESDGE DDLSSGSVLY KIGDLGHVTS ILNPQVEEGD SRFLANEILQ 400
EDYSQLPKAD IFALGLTIAL AAGAAPLPCN EDSWHHIRKG NLPHVPQLLT 450
PIFLALLKLL VHPDPVMRPP AASLAKNSVL RRCVGKAAQL QKQLNVEKFK 500
TAMLERELKA AKLAQTSGKD ECSDLPPMSG FSCRGRKRLV GAKNTRSLSF 550
TCGGY 555
Length:555
Mass (Da):61,716
Last modified:May 31, 2011 - v2
Checksum:iF51CBA73B0CDA448
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2281I → V in AAC59664. 1 Publication
Sequence conflicti452 – 4521I → V in AAC59664. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U13962 mRNA. Translation: AAC59664.1.
BC081031 mRNA. Translation: AAH81031.1.
PIRiI51671.
RefSeqiNP_001081784.1. NM_001088315.1.
UniGeneiXl.1694.

Genome annotation databases

GeneIDi398049.
KEGGixla:398049.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U13962 mRNA. Translation: AAC59664.1 .
BC081031 mRNA. Translation: AAH81031.1 .
PIRi I51671.
RefSeqi NP_001081784.1. NM_001088315.1.
UniGenei Xl.1694.

3D structure databases

ProteinModelPortali P47817.
SMRi P47817. Positions 202-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 99384. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 398049.
KEGGi xla:398049.

Organism-specific databases

CTDi 398049.
Xenbasei XB-GENE-6538740. wee2.

Phylogenomic databases

HOVERGENi HBG005050.
KOi K06632.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 6726.

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. "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.

Entry informationi

Entry nameiWEE2A_XENLA
AccessioniPrimary (citable) accession number: P47817
Secondary accession number(s): Q66J76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 31, 2011
Last modified: September 3, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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