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Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase (EC 2.7.11.1) (Myt1 kinase)

 PMYT1_HUMAN             Reviewed;         499 AA.
Q99640; B3KUN8; B4DXD4; D3DUA4; F8W164; I3L1V2; O14731; Q7LE24;
Q8TCM9;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
12-SEP-2018, entry version 171.
RecName: Full=Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase;
EC=2.7.11.1;
AltName: Full=Myt1 kinase;
Name=PKMYT1; Synonyms=MYT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ACTIVITY REGULATION.
PubMed=9268380; DOI=10.1074/jbc.272.35.22300;
Booher R.N., Holman P.S., Fattaey A.;
"Human Myt1 is a cell cycle-regulated kinase that inhibits Cdc2 but
not Cdk2 activity.";
J. Biol. Chem. 272:22300-22306(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=9001210; DOI=10.1128/MCB.17.2.571;
Liu F., Stanton J.J., Wu Z., Piwnica-Worms H.;
"The human Myt1 kinase preferentially phosphorylates Cdc2 on threonine
14 and localizes to the endoplasmic reticulum and Golgi complex.";
Mol. Cell. Biol. 17:571-583(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
TISSUE=Testis, and Thyroid;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-140; ARG-417 AND
ALA-445.
NIEHS SNPs program;
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 403-499 (ISOFORM 1).
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
INTERACTION WITH PIN1.
PubMed=9499405; DOI=10.1101/gad.12.5.706;
Shen M., Stukenberg P.T., Kirschner M.W., Lu K.P.;
"The essential mitotic peptidyl-prolyl isomerase Pin1 binds and
regulates mitosis-specific phosphoproteins.";
Genes Dev. 12:706-720(1998).
[9]
PHOSPHORYLATION, COMPONENT OF CDC2-CCNB1 COMPLEX, INTERACTION WITH
PIN1, AND MUTAGENESIS OF ASP-251.
PubMed=10504341;
Wells N.J., Watanabe N., Tokusumi T., Jiang W., Verdecia M.A.,
Hunter T.;
"The C-terminal domain of the Cdc2 inhibitory kinase Myt1 interacts
with Cdc2 complexes and is required for inhibition of G(2)/M
progression.";
J. Cell Sci. 112:3361-3371(1999).
[10]
FUNCTION, AND MUTAGENESIS OF ASN-238 AND 486-ARG--LEU-488.
PubMed=10373560; DOI=10.1128/MCB.19.7.5113;
Liu F., Rothblum-Oviatt C., Ryan C.E., Piwnica-Worms H.;
"Overproduction of human Myt1 kinase induces a G2 cell cycle delay by
interfering with the intracellular trafficking of Cdc2-cyclin B1
complexes.";
Mol. Cell. Biol. 19:5113-5123(1999).
[11]
PHOSPHORYLATION AT SER-426 AND THR-495.
PubMed=12738781; DOI=10.1074/jbc.C300126200;
Nakajima H., Toyoshima-Morimoto F., Taniguchi E., Nishida E.;
"Identification of a consensus motif for Plk (Polo-like kinase)
phosphorylation reveals Myt1 as a Plk1 substrate.";
J. Biol. Chem. 278:25277-25280(2003).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-17; SER-94; SER-469 AND
THR-495, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-469 AND
SER-473, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT THR-17 AND SER-160, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-94; SER-120;
SER-143; SER-469 AND SER-482, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
VARIANTS [LARGE SCALE ANALYSIS] GLN-103; CYS-140; HIS-246 AND LYS-351.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Acts as a negative regulator of entry into mitosis (G2
to M transition) by phosphorylation of the CDK1 kinase
specifically when CDK1 is complexed to cyclins. Mediates
phosphorylation of CDK1 predominantly on 'Thr-14'. Also involved
in Golgi fragmentation. May be involved in phosphorylation of CDK1
on 'Tyr-15' to a lesser degree, however tyrosine kinase activity
is unclear and may be indirect. May be a downstream target of
Notch signaling pathway during eye development.
{ECO:0000269|PubMed:10373560, ECO:0000269|PubMed:9001210}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ACTIVITY REGULATION: Negatively regulated by hyperphosphorylation
during mitosis. The hyperphosphorylated form does not associate
with CCNB1-CDC2 complexes. The PLK1 protein kinase may be required
for mitotic phosphorylation. {ECO:0000269|PubMed:9268380}.
-!- SUBUNIT: Interacts with CDC2-CCNB1 complex. Can also interact with
PIN1 when phosphorylated by CDC2-CCNB1.
{ECO:0000269|PubMed:10504341, ECO:0000269|PubMed:9499405}.
-!- INTERACTION:
P14635:CCNB1; NbExp=5; IntAct=EBI-495308, EBI-495332;
P06493:CDK1; NbExp=4; IntAct=EBI-495308, EBI-444308;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:9001210}; Peripheral membrane protein
{ECO:0000269|PubMed:9001210}. Golgi apparatus membrane
{ECO:0000269|PubMed:9001210}; Peripheral membrane protein
{ECO:0000269|PubMed:9001210}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q99640-1; Sequence=Displayed;
Name=2;
IsoId=Q99640-2; Sequence=VSP_045699;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q99640-3; Sequence=VSP_046846;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q99640-4; Sequence=VSP_046847;
Note=No experimental confirmation available.;
-!- DOMAIN: The membrane-association motif is essential for the
localization to membrane of Golgi stack. According to some
authors, it is a transmembrane domain; the existence of a
transmembrane region is however unproven.
-!- PTM: Autophosphorylated. Phosphorylated by CDC2-CCNB1 complexes on
undefined serine and threonine residues. The phosphorylation by
CDC2-CCNB1 complexes may inhibit the catalytic activity.
{ECO:0000269|PubMed:10504341, ECO:0000269|PubMed:12738781}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. WEE1 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=CAD28540.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/pkmyt1/";
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EMBL; AF014118; AAB71843.1; -; mRNA.
EMBL; U56816; AAC50949.1; -; mRNA.
EMBL; AK097642; BAG53500.1; -; mRNA.
EMBL; AK098452; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK301926; BAG63346.1; -; mRNA.
EMBL; AF549406; AAN40703.1; -; Genomic_DNA.
EMBL; AC004233; AAC04478.1; -; Genomic_DNA.
EMBL; AC004235; AAC04477.1; -; Genomic_DNA.
EMBL; CH471112; EAW85439.1; -; Genomic_DNA.
EMBL; CH471112; EAW85440.1; -; Genomic_DNA.
EMBL; AL713779; CAD28540.1; ALT_SEQ; mRNA.
CCDS; CCDS10486.1; -. [Q99640-1]
CCDS; CCDS45391.1; -. [Q99640-2]
CCDS; CCDS58414.1; -. [Q99640-3]
CCDS; CCDS58415.1; -. [Q99640-4]
RefSeq; NP_001245379.1; NM_001258450.1. [Q99640-4]
RefSeq; NP_001245380.1; NM_001258451.1. [Q99640-3]
RefSeq; NP_004194.3; NM_004203.4. [Q99640-1]
RefSeq; NP_872629.1; NM_182687.2. [Q99640-2]
RefSeq; XP_011521036.1; XM_011522734.2. [Q99640-1]
RefSeq; XP_011521037.1; XM_011522735.2. [Q99640-3]
RefSeq; XP_011521038.1; XM_011522736.2. [Q99640-3]
UniGene; Hs.732385; -.
PDB; 3P1A; X-ray; 1.70 A; A=75-362.
PDB; 5VCV; X-ray; 1.92 A; A=75-362.
PDB; 5VCW; X-ray; 2.25 A; A/B=75-362.
PDB; 5VCX; X-ray; 2.70 A; A=75-362.
PDB; 5VCY; X-ray; 1.56 A; A=75-362.
PDB; 5VCZ; X-ray; 1.50 A; A=75-362.
PDB; 5VD0; X-ray; 2.13 A; A=75-362.
PDB; 5VD1; X-ray; 1.70 A; A=75-362.
PDB; 5VD3; X-ray; 1.80 A; A=75-362.
PDBsum; 3P1A; -.
PDBsum; 5VCV; -.
PDBsum; 5VCW; -.
PDBsum; 5VCX; -.
PDBsum; 5VCY; -.
PDBsum; 5VCZ; -.
PDBsum; 5VD0; -.
PDBsum; 5VD1; -.
PDBsum; 5VD3; -.
ProteinModelPortal; Q99640; -.
SMR; Q99640; -.
BioGrid; 114544; 21.
ELM; Q99640; -.
IntAct; Q99640; 26.
MINT; Q99640; -.
STRING; 9606.ENSP00000262300; -.
BindingDB; Q99640; -.
ChEMBL; CHEMBL3984; -.
GuidetoPHARMACOLOGY; 2167; -.
iPTMnet; Q99640; -.
PhosphoSitePlus; Q99640; -.
BioMuta; PKMYT1; -.
DMDM; 55976573; -.
EPD; Q99640; -.
MaxQB; Q99640; -.
PaxDb; Q99640; -.
PeptideAtlas; Q99640; -.
PRIDE; Q99640; -.
ProteomicsDB; 78372; -.
DNASU; 9088; -.
Ensembl; ENST00000262300; ENSP00000262300; ENSG00000127564. [Q99640-1]
Ensembl; ENST00000440027; ENSP00000397739; ENSG00000127564. [Q99640-2]
Ensembl; ENST00000573944; ENSP00000459123; ENSG00000127564. [Q99640-3]
Ensembl; ENST00000574385; ENSP00000458943; ENSG00000127564. [Q99640-3]
Ensembl; ENST00000574730; ENSP00000460868; ENSG00000127564. [Q99640-4]
GeneID; 9088; -.
KEGG; hsa:9088; -.
UCSC; uc002csm.4; human. [Q99640-1]
CTD; 9088; -.
DisGeNET; 9088; -.
EuPathDB; HostDB:ENSG00000127564.16; -.
GeneCards; PKMYT1; -.
HGNC; HGNC:29650; PKMYT1.
HPA; HPA068860; -.
MIM; 602474; gene.
neXtProt; NX_Q99640; -.
OpenTargets; ENSG00000127564; -.
PharmGKB; PA385; -.
eggNOG; KOG0601; Eukaryota.
eggNOG; ENOG410XS1M; LUCA.
GeneTree; ENSGT00530000063230; -.
HOGENOM; HOG000293277; -.
HOVERGEN; HBG053623; -.
InParanoid; Q99640; -.
KO; K06633; -.
PhylomeDB; Q99640; -.
TreeFam; TF101087; -.
Reactome; R-HSA-156711; Polo-like kinase mediated events.
Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-HSA-69478; G2/M DNA replication checkpoint.
SignaLink; Q99640; -.
SIGNOR; Q99640; -.
ChiTaRS; PKMYT1; human.
EvolutionaryTrace; Q99640; -.
GeneWiki; PKMYT1; -.
GenomeRNAi; 9088; -.
PRO; PR:Q99640; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000127564; Expressed in 139 organ(s), highest expression level in right testis.
CleanEx; HS_MYT1; -.
CleanEx; HS_PKMYT1; -.
ExpressionAtlas; Q99640; baseline and differential.
Genevisible; Q99640; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IDA:HGNC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
GO; GO:0007088; P:regulation of mitotic nuclear division; TAS:ProtInc.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR016235; Tyr/Thr_kinase_Cdc2_inhib.
Pfam; PF00069; Pkinase; 1.
PIRSF; PIRSF000567; TYPK_Myt1; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Cell cycle; Complete proteome; Endoplasmic reticulum; Golgi apparatus;
Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 499 Membrane-associated tyrosine- and
threonine-specific cdc2-inhibitory
kinase.
/FTId=PRO_0000086573.
DOMAIN 110 359 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 116 124 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 398 499 Interaction with PIN1.
REGION 437 499 Interaction with CDC2-CCNB1.
MOTIF 382 398 Membrane-association motif.
COMPBIAS 5 72 Pro-rich.
ACT_SITE 233 233 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
METAL 238 238 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
METAL 251 251 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
BINDING 139 139 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 17 17 Phosphothreonine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231}.
MOD_RES 40 40 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 94 94 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 160 160 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 426 426 Phosphoserine; by PLK1.
{ECO:0000269|PubMed:12738781}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 473 473 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 482 482 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 495 495 Phosphothreonine; by PLK1.
{ECO:0000244|PubMed:18691976,
ECO:0000269|PubMed:12738781}.
VAR_SEQ 1 9 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046846.
VAR_SEQ 5 73 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046847.
VAR_SEQ 439 499 SLSPEAVLARTVGSTSTPRSRCTPRDALDLSDINSEPPRGS
FPSFEPRNLLSLFEDTLDPT -> GHPPCLACPPAGLHSPL
RLSWPGLWGAPPPPGAGAHPGMPWT (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045699.
VARIANT 103 103 E -> Q (in dbSNP:rs55834293).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041034.
VARIANT 140 140 R -> C (in dbSNP:rs4149796).
{ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.4}.
/FTId=VAR_019928.
VARIANT 246 246 R -> H (in dbSNP:rs35192104).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041035.
VARIANT 351 351 E -> K (in dbSNP:rs56382954).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041036.
VARIANT 417 417 P -> R (in dbSNP:rs4149800).
{ECO:0000269|Ref.4}.
/FTId=VAR_019929.
VARIANT 445 445 V -> A (in dbSNP:rs10546).
{ECO:0000269|Ref.4}.
/FTId=VAR_019930.
MUTAGEN 238 238 N->A: Loss of kinase activity.
{ECO:0000269|PubMed:10373560}.
MUTAGEN 251 251 D->A: Loss of kinase activity.
{ECO:0000269|PubMed:10504341}.
MUTAGEN 486 488 RNL->AAA: Loss of CDC2-CCNB1 interaction.
{ECO:0000269|PubMed:10373560}.
CONFLICT 131 131 E -> A (in Ref. 4; BAG53500).
{ECO:0000305}.
CONFLICT 415 415 G -> D (in Ref. 1; AAB71843).
{ECO:0000305}.
CONFLICT 427 427 L -> F (in Ref. 1; AAB71843).
{ECO:0000305}.
CONFLICT 491 491 L -> M (in Ref. 1; AAB71843).
{ECO:0000305}.
STRAND 84 87 {ECO:0000244|PDB:5VD1}.
STRAND 101 103 {ECO:0000244|PDB:5VCZ}.
HELIX 105 109 {ECO:0000244|PDB:5VCZ}.
STRAND 110 119 {ECO:0000244|PDB:5VCZ}.
STRAND 122 129 {ECO:0000244|PDB:5VCZ}.
TURN 130 132 {ECO:0000244|PDB:5VCZ}.
STRAND 135 144 {ECO:0000244|PDB:5VCZ}.
HELIX 148 164 {ECO:0000244|PDB:5VCZ}.
STRAND 173 179 {ECO:0000244|PDB:5VCZ}.
STRAND 182 188 {ECO:0000244|PDB:5VCZ}.
HELIX 194 201 {ECO:0000244|PDB:5VCZ}.
HELIX 207 226 {ECO:0000244|PDB:5VCZ}.
HELIX 236 238 {ECO:0000244|PDB:5VCZ}.
STRAND 239 241 {ECO:0000244|PDB:5VCZ}.
HELIX 243 245 {ECO:0000244|PDB:5VCZ}.
STRAND 247 249 {ECO:0000244|PDB:5VCZ}.
HELIX 252 254 {ECO:0000244|PDB:5VD0}.
STRAND 256 259 {ECO:0000244|PDB:5VCZ}.
STRAND 261 263 {ECO:0000244|PDB:5VCZ}.
TURN 271 273 {ECO:0000244|PDB:5VCZ}.
HELIX 276 280 {ECO:0000244|PDB:5VCZ}.
HELIX 286 301 {ECO:0000244|PDB:5VCZ}.
HELIX 309 315 {ECO:0000244|PDB:5VCZ}.
TURN 316 318 {ECO:0000244|PDB:5VCZ}.
HELIX 322 325 {ECO:0000244|PDB:5VCZ}.
HELIX 330 339 {ECO:0000244|PDB:5VCZ}.
TURN 344 346 {ECO:0000244|PDB:5VCZ}.
HELIX 350 354 {ECO:0000244|PDB:5VCZ}.
HELIX 357 359 {ECO:0000244|PDB:5VCZ}.
SEQUENCE 499 AA; 54521 MW; 4DF28A5965265567 CRC64;
MLERPPALAM PMPTEGTPPP LSGTPIPVPA YFRHAEPGFS LKRPRGLSRS LPPPPPAKGS
IPISRLFPPR TPGWHQLQPR RVSFRGEASE TLQSPGYDPS RPESFFQQSF QRLSRLGHGS
YGEVFKVRSK EDGRLYAVKR SMSPFRGPKD RARKLAEVGS HEKVGQHPCC VRLEQAWEEG
GILYLQTELC GPSLQQHCEA WGASLPEAQV WGYLRDTLLA LAHLHSQGLV HLDVKPANIF
LGPRGRCKLG DFGLLVELGT AGAGEVQEGD PRYMAPELLQ GSYGTAADVF SLGLTILEVA
CNMELPHGGE GWQQLRQGYL PPEFTAGLSS ELRSVLVMML EPDPKLRATA EALLALPVLR
QPRAWGVLWC MAAEALSRGW ALWQALLALL CWLWHGLAHP ASWLQPLGPP ATPPGSPPCS
LLLDSSLSSN WDDDSLGPSL SPEAVLARTV GSTSTPRSRC TPRDALDLSD INSEPPRGSF
PSFEPRNLLS LFEDTLDPT


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