PMYT1_MOUSE
ID PMYT1_MOUSE Reviewed; 490 AA.
AC Q9ESG9; Q3TNN2; Q8R3L4;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 154.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1;
RA Van de Putte T., Francis A., Zwijsen A., Huylebroeck D.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 (By similarity). {ECO:0000250}.
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 hyperphosphorylated form does not associate with
CC CCNB1-CDC2 complexes. The PLK1 protein kinase may be required for
CC mitotic phosphorylation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CDC2-CCNB1 complex. Can also interact with PIN1
CC when phosphorylated by CDC2-CCNB1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- DOMAIN: The membrane-association motif is essential for the
CC localization to membrane of Golgi stack. According to some authors, it
CC is a transmembrane domain; the existence of a transmembrane region of
CC such is however unsure (By similarity). {ECO:0000250}.
CC -!- PTM: Autophosphorylated. Phosphorylated by CDC2-CCNB1 complexes on
CC undefined serine and threonine residues. The phosphorylation by CDC2-
CC CCNB1 complexes may inhibit the catalytic activity (By similarity).
CC {ECO:0000250}.
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; AF175892; AAG09210.1; -; mRNA.
DR EMBL; AK158550; BAE34554.1; -; mRNA.
DR EMBL; AK165164; BAE38056.1; -; mRNA.
DR EMBL; BC025061; AAH25061.1; -; mRNA.
DR CCDS; CCDS28460.1; -.
DR RefSeq; NP_075545.2; NM_023058.3.
DR AlphaFoldDB; Q9ESG9; -.
DR SMR; Q9ESG9; -.
DR STRING; 10090.ENSMUSP00000024701; -.
DR iPTMnet; Q9ESG9; -.
DR PhosphoSitePlus; Q9ESG9; -.
DR EPD; Q9ESG9; -.
DR MaxQB; Q9ESG9; -.
DR PaxDb; Q9ESG9; -.
DR PeptideAtlas; Q9ESG9; -.
DR PRIDE; Q9ESG9; -.
DR ProteomicsDB; 289774; -.
DR Antibodypedia; 23946; 528 antibodies from 34 providers.
DR DNASU; 268930; -.
DR Ensembl; ENSMUST00000024701; ENSMUSP00000024701; ENSMUSG00000023908.
DR GeneID; 268930; -.
DR KEGG; mmu:268930; -.
DR UCSC; uc008asz.1; mouse.
DR CTD; 9088; -.
DR MGI; MGI:2137630; Pkmyt1.
DR VEuPathDB; HostDB:ENSMUSG00000023908; -.
DR eggNOG; KOG0601; Eukaryota.
DR GeneTree; ENSGT00940000159427; -.
DR HOGENOM; CLU_000288_25_3_1; -.
DR InParanoid; Q9ESG9; -.
DR OMA; PCTPPKD; -.
DR OrthoDB; 1063695at2759; -.
DR PhylomeDB; Q9ESG9; -.
DR TreeFam; TF101087; -.
DR Reactome; R-MMU-156711; Polo-like kinase mediated events.
DR Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-MMU-69478; G2/M DNA replication checkpoint.
DR BioGRID-ORCS; 268930; 20 hits in 75 CRISPR screens.
DR ChiTaRS; Pkmyt1; mouse.
DR PRO; PR:Q9ESG9; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9ESG9; protein.
DR Bgee; ENSMUSG00000023908; Expressed in spermatocyte and 177 other tissues.
DR Genevisible; Q9ESG9; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
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 2: Evidence at transcript 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..490
FT /note="Membrane-associated tyrosine- and threonine-specific
FT cdc2-inhibitory kinase"
FT /id="PRO_0000086574"
FT DOMAIN 101..350
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..490
FT /note="Interaction with PIN1"
FT /evidence="ECO:0000250"
FT REGION 428..490
FT /note="Interaction with CDC2-CCNB1"
FT /evidence="ECO:0000250"
FT REGION 444..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 373..389
FT /note="Membrane-association motif"
FT /evidence="ECO:0000250"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 107..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99640"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99640"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99640"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99640"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99640"
FT MOD_RES 417
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000250"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99640"
FT MOD_RES 486
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250"
FT CONFLICT 252
FT /note="A -> T (in Ref. 1; AAG09210 and 3; AAH25061)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="P -> L (in Ref. 1; AAG09210)"
FT /evidence="ECO:0000305"
FT CONFLICT 414..415
FT /note="LD -> MN (in Ref. 1; AAG09210)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 54053 MW; 1308CD1F9D0293B2 CRC64;
MTMPTEGTPP PLSGTPIPVP AYFRHAEPGF SLKRPGGLSR SLPPRPPAKG CIPVSRLFPP
RTPGWHQPQP RRVSFLCETS EPLQSPGYDP SRPESFFQQN FQRLSRLGHG SYGEVFKVRS
KEDGRLYAVK RYMSPFRGPK DRTRKLAEVG GHEKVGQHPH CVRLERAWEE GGILYLQTEL
CGPSLQQHCE AWGASLPEAQ VWGYLRDILL ALDHLHSQGL VHLDVKPANI FLGPRGRCKL
GDFGLLVELG SAGAGEAQEG DPRYMAPELL QGSYGTAADV FSLGLTILEV ACNMELPHGG
EGWQQLRQGY LPPEFTAGLS SELRSVLAMM LEPDPQLRAT AEALLALPML RQPRPWNVLW
YMAAEALSRG WALWQALVTL LCWLWHGLVH PASWLQPPGP PATPPGSPPC SPLLDSTLSS
SWDNDSIGPS LSPETVLSRI TRRTSTPRGR YIPRDALDLT DVDSEPPRGP CPTFEPRNLL
SLFEDSLDPA
