PMYT1_XENLA
ID PMYT1_XENLA Reviewed; 548 AA.
AC Q91618;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase;
DE EC=2.7.11.1;
DE AltName: Full=Myt1 kinase;
GN Name=pkmyt1; Synonyms=myt1;
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].
RX PubMed=7569953; DOI=10.1126/science.270.5233.86;
RA Mueller P.R., Coleman T.R., Kumagai A., Dunphy W.G.;
RT "Myt1: a membrane-associated inhibitory kinase that phosphorylates Cdc2 on
RT both threonine-14 and tyrosine-15.";
RL Science 270:86-90(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION, AND ACTIVITY REGULATION.
RX PubMed=9724639; DOI=10.1093/emboj/17.17.5037;
RA Palmer A., Gavin A.-C., Nebreda A.R.;
RT "A link between MAP kinase and p34(cdc2)/cyclin B during oocyte maturation:
RT p90(rsk) phosphorylates and inactivates the p34(cdc2) inhibitory kinase
RT Myt1.";
RL EMBO J. 17:5037-5047(1998).
RN [4]
RP FUNCTION, AND INTERACTION WITH MOS.
RX PubMed=11959823; DOI=10.1242/dev.129.9.2129;
RA Peter M., Labbe J.-C., Doree M., Mandart E.;
RT "A new role for Mos in Xenopus oocyte maturation: targeting Myt1
RT independently of MAPK.";
RL Development 129:2129-2139(2002).
RN [5]
RP PHOSPHORYLATION AT THR-478 BY CDK1, AND PHOSPHORYLATION BY PLK1.
RX PubMed=15692562; DOI=10.1038/sj.emboj.7600567;
RA Inoue D., Sagata N.;
RT "The Polo-like kinase Plx1 interacts with and inhibits Myt1 after
RT fertilization of Xenopus eggs.";
RL EMBO J. 24:1057-1067(2005).
CC -!- FUNCTION: Acts as a negative regulator of entry into mitosis (G2 to M
CC transition) by phosphorylation of the CDK1 kinase specifically when
CC CDK1 is complexed to cyclins. Mediates phosphorylation of CDK1
CC predominantly on 'Thr-14'. Also involved in Golgi fragmentation. May be
CC involved in phosphorylation of CDK1 on 'Tyr-15' to a lesser degree,
CC however tyrosine kinase activity is unclear and may be indirect. May be
CC a downstream target of Notch signaling pathway during eye development.
CC {ECO:0000269|PubMed:11959823}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Negatively regulated by hyperphosphorylation
CC during mitosis. The plk1/plk1 protein kinase may be required for
CC mitotic phosphorylation. Inactivated during oocyte maturation by
CC phosphorylation by RSK2 and Mos kinase. {ECO:0000269|PubMed:9724639}.
CC -!- SUBUNIT: Interacts with CDC2-CCNB1 complex (By similarity). Interacts
CC with Mos during oocyte maturation. {ECO:0000250,
CC ECO:0000269|PubMed:11959823}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}. Golgi apparatus membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC -!- PTM: Autophosphorylated. Phosphorylated on undefined residues by RSK2
CC and Mos kinases. Phosphorylation at Thr-478 by cdk1 creates a docking
CC site for plk1/plx1, leading to subsequent phosphorylation by plk1/plk1
CC and inhibition of the protein kinase activity kinase activity.
CC {ECO:0000269|PubMed:15692562, ECO:0000269|PubMed:9724639}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. WEE1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U28931; AAC59716.1; -; mRNA.
DR EMBL; BC057703; AAH57703.1; -; mRNA.
DR PIR; A57247; A57247.
DR RefSeq; NP_001079935.1; NM_001086466.1.
DR RefSeq; XP_018092679.1; XM_018237190.1.
DR RefSeq; XP_018092680.1; XM_018237191.1.
DR RefSeq; XP_018092681.1; XM_018237192.1.
DR AlphaFoldDB; Q91618; -.
DR SMR; Q91618; -.
DR BioGRID; 97869; 1.
DR iPTMnet; Q91618; -.
DR GeneID; 379626; -.
DR KEGG; xla:379626; -.
DR CTD; 379626; -.
DR Xenbase; XB-GENE-969856; pkmyt1.S.
DR OMA; PCTPPKD; -.
DR OrthoDB; 1063695at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 379626; Expressed in camera-type eye and 19 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; 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; IPR016235; Tyr/Thr_kinase_Cdc2_inhib.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000567; TYPK_Myt1; 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; Endoplasmic reticulum; Golgi apparatus; Kinase;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..548
FT /note="Membrane-associated tyrosine- and threonine-specific
FT cdc2-inhibitory kinase"
FT /id="PRO_0000086575"
FT DOMAIN 103..353
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 61..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 226
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 109..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 478
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:15692562"
SQ SEQUENCE 548 AA; 61785 MW; 2E189A7A65575102 CRC64;
MPVPGDDMGE TPLTRTPIPM PAYFSQAEQS FSLKKRGRSL CYTLPPRPPV KSALPVSRIF
PNKQRSWSQP RPQSVSFRSP QNKTPASKLY DQSKGDTFFK QCFKSICKLG RGSFGEVYKV
QSLEDGCFYA VKRSVSPFRG ESDRQRKLQE VRKHERVGEH PNCLRFVRAW EEKRMLYLQT
ELCAGSLQQH SEEFAGSLPP RRVWNITCDL LHGLKHLHDR NLLHLDIKPA NVFISFSGVC
KLGDFGLMVE LDGTEGSGEA QEGDPRYMAP ELLDGIFSKA ADVFSLGMSL LEVACNMELP
KGGDGWQQLR QGHLPTEFTS DLPPDFLKVL SAMLEPDYRR RATVDWLLSL PAIRNAERWR
MVTLAQERTL GKIIAVYQFI VWLLSFVFQW LNRPVIGFLH YCGLRALPRS PPCSPFPNHL
GESSFSSDWD DESLGDDVFE VPPSPLATHR NLTYHGQELI GRHSPDLLSR PSLGSTSTPR
NLSPEFSMRK RSALPLTPNV SRISQDSTGK SRSPSTSHSS SGFVDAEVQR TLFLPRNLLG
MFDDATEQ
