WEE1B_XENLA
ID WEE1B_XENLA Reviewed; 595 AA.
AC Q8QGV2; Q641D3;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Wee1-like protein kinase 1-B;
DE EC=2.7.10.2;
DE AltName: Full=Zygotic wee1-like protein kinase 1B;
DE Short=Xe-Wee1B;
DE Short=XeWee1B;
GN Name=wee1-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12006499; DOI=10.1093/emboj/21.10.2472;
RA Okamoto K., Nakajo N., Sagata N.;
RT "The existence of two distinct Wee1 isoforms in Xenopus: implications for
RT the developmental regulation of the cell cycle.";
RL EMBO J. 21:2472-2484(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION AT THR-186, INTERACTION WITH PIN1, AND MUTAGENESIS OF
RP 181-ASN--ASN-183 AND THR-186.
RX PubMed=17360425; DOI=10.1073/pnas.0607357104;
RA Okamoto K., Sagata N.;
RT "Mechanism for inactivation of the mitotic inhibitory kinase Wee1 at M
RT phase.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3753-3758(2007).
CC -!- FUNCTION: Acts as a zygotic negative regulator of entry into mitosis
CC (G2 to M transition) by protecting the nucleus from cytoplasmically
CC activated cyclin B1-complexed cdk1 before the onset of mitosis by
CC mediating phosphorylation of cdk1 on 'Tyr-15'. Specifically
CC phosphorylates and inactivates cyclin B1-complexed cdk1 reaching a
CC maximum during G2 phase and a minimum as cells enter M phase.
CC Phosphorylation of cyclin B1-cdk1 occurs exclusively on 'Tyr-15' and
CC phosphorylation of monomeric cdk1 does not occur.
CC {ECO:0000269|PubMed:12006499}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
CC -!- SUBUNIT: Interacts (when phosphorylated at Thr-186) with pin1.
CC {ECO:0000269|PubMed:17360425}.
CC -!- INTERACTION:
CC Q8QGV2; Q9I9K6: pin1.L; NbExp=2; IntAct=EBI-15625605, EBI-959114;
CC Q8QGV2; Q8QGV2: wee1-b; NbExp=2; IntAct=EBI-15625605, EBI-15625605;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Zygotically expressed. Present in oocytes and
CC postgastrula embryos (at least until the tailbud stage). Expression
CC begins at the midblastula stage and increases after the early gastrula
CC stage. {ECO:0000269|PubMed:12006499}.
CC -!- PTM: Phosphorylation at Thr-186 during M-phase by cdk1 inhibits the
CC kinase activity and leads to interaction with pin1.
CC {ECO:0000269|PubMed:17360425}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. WEE1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH82404.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB071983; BAB86797.1; -; mRNA.
DR EMBL; BC082404; AAH82404.1; ALT_INIT; mRNA.
DR RefSeq; NP_001084186.1; NM_001090717.1.
DR AlphaFoldDB; Q8QGV2; -.
DR SMR; Q8QGV2; -.
DR BioGRID; 100680; 1.
DR DIP; DIP-60878N; -.
DR ELM; Q8QGV2; -.
DR IntAct; Q8QGV2; 3.
DR iPTMnet; Q8QGV2; -.
DR GeneID; 399355; -.
DR KEGG; xla:399355; -.
DR CTD; 399355; -.
DR Xenbase; XB-GENE-6254033; wee1.S.
DR OrthoDB; 1063695at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 399355; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:InterPro.
DR GO; GO:0045786; P:negative regulation of cell cycle; IDA:CACAO.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR017164; Wee1-like_protein_kinase.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF037281; Wee1-like_protein_kinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; Kinase; Magnesium;
KW Metal-binding; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..595
FT /note="Wee1-like protein kinase 1-B"
FT /id="PRO_0000409523"
FT DOMAIN 248..518
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 526..563
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 375
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 254..262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 277
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 380
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 186
FT /note="Phosphothreonine; by cdk1"
FT /evidence="ECO:0000269|PubMed:17360425"
FT MUTAGEN 181..183
FT /note="NIN->AAA: Impairs without abolishing ability to
FT phosphorylate cdk1."
FT /evidence="ECO:0000269|PubMed:17360425"
FT MUTAGEN 186
FT /note="T->A: Abolishes kinase activity inhibition during M-
FT phase. Does not affect ability to phosphorylate cdk1."
FT /evidence="ECO:0000269|PubMed:17360425"
FT CONFLICT 67
FT /note="T -> S (in Ref. 2; AAH82404)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="H -> Y (in Ref. 2; AAH82404)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 66600 MW; 4E90E7FDA341CB1B CRC64;
MNVQPRNMNV QPRNMNVQPV RHKLFFSDTD EEEEDGHSTG EDSAFQESDS PVSRQREKQE
GKPPGGTWEE LEEEEGFGSS PIKSPGDFFM SDSPSYRQLA PASPTRSPQG PTSPIPECPG
TPPHKTFRKL RLFDTPHTPK SLLSKARGIG SSALRFRGGT LFREAEKAPK PEFVYSTPQV
NINPFTPDSL EIQSSAGLCR GRKRALLNDS CGEDMEGSDC ELEDEDIRPA KRIPITESNM
KSRYATEFHE LEKIGSGEFG SVFKCVKRLD GCIYAIKRSK KPLAGSVDEQ NALREVYAHA
VLGQHPHVVR YYSAWAEDDH MLIQNEYCNG GSLSDVISEN YRTMQYFTEP ELKDLLLQVA
RGLKYIHSMS LVHMDIKPSN IFISRTTLPN TAVEEADDEE CGSGKVIYKI GDLGHVTRVS
SPQVEEGDSR FLANEVLQEN YTHLAKADIF ALALTVWSAA GAEPFPTNGD QWHEIRQGKL
PRVPQLLSQE FVDLIKLMIS PDPEKRPSSV ALVKHSVLLS ASRKSAEQLR IELDAEKFKN
ALLQKELKKA QIAKAAAEER AHFPDRIATR STTQNNRTTR LIGKKMNRSV SLTIY
