WEE2B_XENLA
ID WEE2B_XENLA Reviewed; 554 AA.
AC O57473; B7ZQL0;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Wee1-like protein kinase 2-B;
DE EC=2.7.10.2;
DE AltName: Full=Wee1-like protein kinase 1;
DE AltName: Full=Xe-wee1;
GN Name=wee2-b; Synonyms=wee1;
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, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF LYS-242.
RX PubMed=9486797; DOI=10.1242/dev.125.2.237;
RA Murakami M.S., Vande Woude G.F.;
RT "Analysis of the early embryonic cell cycles of Xenopus; regulation of cell
RT cycle length by Xe-wee1 and Mos.";
RL Development 125:237-248(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION AT SER-38, UBIQUITINATION, INTERACTION WITH CDCA3, AND
RP MUTAGENESIS OF SER-38.
RX PubMed=12679038; DOI=10.1016/s0092-8674(03)00232-0;
RA Ayad N.G., Rankin S., Murakami M., Jebanathirajah J., Gygi S.P.,
RA Kirschner M.W.;
RT "Tome-1, a trigger of mitotic entry, is degraded during G1 via the APC.";
RL Cell 113:101-113(2003).
CC -!- FUNCTION: Oocyte and early embryo-specific protein tyrosine kinase that
CC phosphorylates and inhibits cdk1 and acts as a regulator of meiosis in
CC oocytes. Required to ensure the meiotic cell cycle in oocytes by
CC phosphorylating cdk1 at 'Tyr-15', leading to inhibit cdk1 activity and
CC prevent meiosis. {ECO:0000269|PubMed:9486797}.
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 ECO:0000269|PubMed:9486797};
CC -!- SUBUNIT: Interacts with cdca3. {ECO:0000269|PubMed:12679038}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Absent in stage VI oocytes and is expressed from
CC meiosis II until gastrulation. {ECO:0000269|PubMed:9486797}.
CC -!- PTM: Ubiquitinated and degraded at the onset of G2/M phase.
CC {ECO:0000269|PubMed:12679038}.
CC -!- PTM: Phosphorylated during M and G1 phases. Interacts with cdca3 when
CC phosphorylated at Ser-38. {ECO:0000269|PubMed:12679038}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. WEE1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Was initially assigned as wee1 (PubMed:9486797). However, it
CC corresponds to the meiosis-specific protein WEE2 in mammals.
CC {ECO:0000305|PubMed:9486797}.
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DR EMBL; AF035443; AAB99952.1; -; mRNA.
DR EMBL; BC169846; AAI69846.1; -; mRNA.
DR EMBL; BC169848; AAI69848.1; -; mRNA.
DR RefSeq; NP_001081724.1; NM_001088255.1.
DR AlphaFoldDB; O57473; -.
DR SMR; O57473; -.
DR iPTMnet; O57473; -.
DR GeneID; 398017; -.
DR KEGG; xla:398017; -.
DR CTD; 398017; -.
DR Xenbase; XB-GENE-17333442; wee2.S.
DR OrthoDB; 1063695at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 398017; Expressed in egg cell and 8 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:InterPro.
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; Coiled coil; Kinase; Magnesium; Meiosis; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase; Tyrosine-protein kinase; Ubl conjugation.
FT CHAIN 1..554
FT /note="Wee1-like protein kinase 2-B"
FT /id="PRO_0000409529"
FT DOMAIN 213..487
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 490..516
FT /evidence="ECO:0000255"
FT COMPBIAS 31..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 340
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 219..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12679038"
FT MUTAGEN 38
FT /note="S->A: Strongly reduces the interaction with cdca3."
FT /evidence="ECO:0000269|PubMed:12679038"
FT MUTAGEN 242
FT /note="K->M: Dominant-negative mutant; reduces the level of
FT cdk1 tyrosine phosphorylation and shortened the length of
FT the cell cycle."
FT /evidence="ECO:0000269|PubMed:9486797"
FT CONFLICT 190
FT /note="P -> S (in Ref. 2; AAI69848/AAI69846)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="A -> S (in Ref. 2; AAI69848/AAI69846)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="A -> V (in Ref. 2; AAI69848/AAI69846)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="T -> A (in Ref. 2; AAI69848/AAI69846)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 554 AA; 61666 MW; 30021FB7A95C5F0D CRC64;
MRMAMSCGGR LVQRLDFSSS EEEDGLSNRI NEAPQKGSPV SSWRTNNCPF PITPQRNERG
LSPTQELSPS SDYSPDPSDK GVGGECPGTP LHYSTWKKLK LCDTPYTPKS LLYKTLPSPG
SRVHCRGQRL LRFVAGTGAE TEDPTLVNVN PFTPQSYRQT HFQPNGKRKE RPEDDCSSDS
QMKFTDKEHP AVFQSKRFVL RETNMESRYK TEFLEIEKIG AGEFGSVFKC VKRLDGCFYV
IKRSKKPLAG STDEQLALRE VYAHAVLGHH PHVVRYYSAW AEDDHMIIQN EYCNGGSLQD
LIMENNKKGQ FVPEQELKEI LLQVSMGLKY IHGSGLVHMD IKPSNIFICR KQTEVGEDES
DGEDDVASAS VLYKIGDLGH VTSILNPQVE EGDSRFLANE ILQEDYRQLP KADIFALGLT
IALAAGAAPL PCNEDGWHHI RKGNLPHIPQ PLTPAFLALL KLLVHPDPAT RPPATSLAKN
SVLRRCVGKA AELQKQLNVE KFKTAMLERE LQAAKLAQDE CLDLPPVSGF SCRGRKRLVG
AKNARSLSFT CGGY
