PMYT1_DROME
ID PMYT1_DROME Reviewed; 533 AA.
AC Q9NI63; Q961T4; Q9VRP6;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase;
DE EC=2.7.11.1;
DE AltName: Full=Myt1 kinase;
DE AltName: Full=dMyt1;
GN Name=Myt1; ORFNames=CG32417;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11882391; DOI=10.1016/s0898-6568(01)00276-5;
RA Cornwell W.D., Kaminski P.J., Jackson J.R.;
RT "Identification of Drosophila Myt1 kinase and its role in Golgi during
RT mitosis.";
RL Cell. Signal. 14:467-476(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RX PubMed=12072468; DOI=10.1093/genetics/161.2.721;
RA Price D.M., Jin Z., Rabinovitch S., Campbell S.D.;
RT "Ectopic expression of the Drosophila Cdk1 inhibitory kinases, Wee1 and
RT Myt1, interferes with the second mitotic wave and disrupts pattern
RT formation during eye development.";
RL Genetics 161:721-731(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-533.
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION.
RX PubMed=15581871; DOI=10.1016/j.ydbio.2004.08.043;
RA Fichelson P., Gho M.;
RT "Mother-daughter precursor cell fate transformation after Cdc2 down-
RT regulation in the Drosophila bristle lineage.";
RL Dev. Biol. 276:367-377(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504 AND SER-519, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Acts as a negative regulator of entry into mitosis (G2 to M
CC transition) by phosphorylation of Cdk1 specifically when Cdk1 is
CC complexed to cyclins (PubMed:11882391, PubMed:12072468,
CC PubMed:15581871). Mediates phosphorylation of Cdk1 predominantly on
CC 'Thr-14' (PubMed:11882391). Also involved in Golgi fragmentation
CC (PubMed:11882391). May be involved in phosphorylation of Cdk1 on 'Tyr-
CC 15' to a lesser degree, however tyrosine kinase activity is unclear and
CC may be indirect (PubMed:11882391). May be a downstream target of Notch
CC signaling pathway during eye development (PubMed:12072468).
CC {ECO:0000269|PubMed:11882391, ECO:0000269|PubMed:12072468,
CC ECO:0000269|PubMed:15581871}.
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 -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:11882391}; Peripheral membrane protein
CC {ECO:0000305|PubMed:11882391}.
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=AAF32288.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAK77309.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF215861; AAF32288.1; ALT_FRAME; mRNA.
DR EMBL; AE014296; AAF50747.3; -; Genomic_DNA.
DR EMBL; AY047577; AAK77309.1; ALT_INIT; mRNA.
DR RefSeq; NP_647987.2; NM_139730.3.
DR AlphaFoldDB; Q9NI63; -.
DR SMR; Q9NI63; -.
DR BioGRID; 64110; 9.
DR STRING; 7227.FBpp0076824; -.
DR iPTMnet; Q9NI63; -.
DR PaxDb; Q9NI63; -.
DR PRIDE; Q9NI63; -.
DR EnsemblMetazoa; FBtr0077118; FBpp0076824; FBgn0040298.
DR GeneID; 38649; -.
DR KEGG; dme:Dmel_CG32417; -.
DR CTD; 4661; -.
DR FlyBase; FBgn0040298; Myt1.
DR VEuPathDB; VectorBase:FBgn0040298; -.
DR eggNOG; KOG0601; Eukaryota.
DR GeneTree; ENSGT00940000159427; -.
DR HOGENOM; CLU_028362_0_0_1; -.
DR InParanoid; Q9NI63; -.
DR OMA; SHFEQCF; -.
DR OrthoDB; 1063695at2759; -.
DR PhylomeDB; Q9NI63; -.
DR Reactome; R-DME-156711; Polo-like kinase mediated events.
DR Reactome; R-DME-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-DME-69478; G2/M DNA replication checkpoint.
DR BioGRID-ORCS; 38649; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38649; -.
DR PRO; PR:Q9NI63; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0040298; Expressed in oocyte and 20 other tissues.
DR Genevisible; Q9NI63; DM.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0048142; P:germarium-derived cystoblast division; IMP:FlyBase.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:FlyBase.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0045793; P:positive regulation of cell size; IGI:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0048137; P:spermatocyte division; IMP:FlyBase.
DR GO; GO:0007284; P:spermatogonial cell division; IMP:FlyBase.
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; Golgi apparatus; Kinase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..533
FT /note="Membrane-associated tyrosine- and threonine-specific
FT cdc2-inhibitory kinase"
FT /id="PRO_0000086577"
FT DOMAIN 102..351
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 108..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 131
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 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 533 AA; 61131 MW; 3DCD3458914D0645 CRC64;
MEKHHRLPLP ELHDDKHRHK QCNGENSNRF RPPKYKTRGY VAVDNNNLNR SQSLGSCSTN
SSQIAHAISF RDAGCSDSST LPSSPVQAEL STLSLSHFEQ CFERLAKLGE GSFGEVFQVR
DRSDGQLYAV KISKQLFRGE QYRAERLEEV RRYEEFSGHE NCIRFIRAWE QYDRLYMQME
LCRESLEQYL LRCQRIPEER IWHILLDLLR GLKSLHDRNL IHLDIKLDNV LIGEDDETCK
LADFGLVIDV DRANSHHATE GDSRYMAPEI LQGHFSKAAD IFSLGIAMLE LACYMDLPSN
GPLWHELRHG ILPEEFINKI SLELQSVIKS MMKPDPAQRP TAEQLLSHPK LQYLQKKRKS
LMNFSMLSRS FRRSRRAVWG RMCNWKTAAF RYLLYFLEVL HLCKPITASQ PNINIVPSSP
SSKGVPLVPQ VEFQLVGSTP IANRDCYASD FLSGEDPLDL SNQGSPNVIN STPLNTNQGK
SRLDLLKNNV DSMGRYVHVH DFESPCSALS SAKVLDTSSF RRKKLFVLEY DDE
