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TTK_HUMAN
ID   TTK_HUMAN               Reviewed;         857 AA.
AC   P33981; A8K8U5; B2RDW2; E1P543; Q15272; Q5TCS0; Q9BW51; Q9NTM0;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   03-AUG-2022, entry version 218.
DE   RecName: Full=Dual specificity protein kinase TTK;
DE            EC=2.7.12.1 {ECO:0000305|PubMed:29162720};
DE   AltName: Full=Phosphotyrosine picked threonine-protein kinase;
DE            Short=PYT;
GN   Name=TTK; Synonyms=MPS1, MPS1L1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1639825; DOI=10.1016/s0021-9258(19)49633-6;
RA   Mills G.B., Schmandt R., McGill M., Amendola A., Hill M., Jacobs K.,
RA   May C., Rodricks A.-M., Campbell S., Hogg D.;
RT   "Expression of TTK, a novel human protein kinase, is associated with cell
RT   proliferation.";
RL   J. Biol. Chem. 267:16000-16006(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye, and Testis;
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).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 504-802 (ISOFORM 1/2), AND CHARACTERIZATION.
RX   PubMed=7678926;
RA   Lindberg R.A., Fischer W.H., Hunter T.;
RT   "Characterization of a human protein threonine kinase isolated by screening
RT   an expression library with antibodies to phosphotyrosine.";
RL   Oncogene 8:351-359(1993).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 525-792 (ISOFORM 1/2).
RX   PubMed=1956325; DOI=10.1016/0076-6879(91)00126-h;
RA   Hanks S.K., Quinn A.M.;
RT   "Protein kinase catalytic domain sequence database: identification of
RT   conserved features of primary structure and classification of family
RT   members.";
RL   Methods Enzymol. 200:38-62(1991).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17924679; DOI=10.1021/pr070152u;
RA   Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT   "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT   and high confident phosphopeptide identification by cross-validation of
RT   MS/MS and MS/MS/MS spectra.";
RL   J. Proteome Res. 6:4150-4162(2007).
RN   [10]
RP   FUNCTION, AND MUTAGENESIS OF ASP-664.
RX   PubMed=18243099; DOI=10.1016/j.cell.2007.11.046;
RA   Jelluma N., Brenkman A.B., van den Broek N.J., Cruijsen C.W.A.,
RA   van Osch M.H.J., Lens S.M.A., Medema R.H., Kops G.J.P.L.;
RT   "Mps1 phosphorylates Borealin to control Aurora B activity and chromosome
RT   alignment.";
RL   Cell 132:233-246(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; THR-33; SER-37; SER-80;
RP   SER-281; SER-317; SER-393; SER-436 AND SER-821, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33; SER-321; SER-393 AND
RP   SER-821, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [14]
RP   INTERACTION WITH TPR.
RX   PubMed=19273613; DOI=10.1083/jcb.200811012;
RA   Lince-Faria M., Maffini S., Orr B., Ding Y., Florindo C., Sunkel C.E.,
RA   Tavares A., Johansen J., Johansen K.M., Maiato H.;
RT   "Spatiotemporal control of mitosis by the conserved spindle matrix protein
RT   Megator.";
RL   J. Cell Biol. 184:647-657(2009).
RN   [15]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT SER-7; THR-33; SER-281; SER-321; SER-436 AND SER-821, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33; SER-37; SER-281 AND
RP   SER-821, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [19]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; THR-33; SER-321; SER-436;
RP   SER-455 AND SER-821, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [21]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH MAD1L1 AND MAD2L1.
RX   PubMed=29162720; DOI=10.1074/jbc.ra117.000555;
RA   Ji W., Luo Y., Ahmad E., Liu S.T.;
RT   "Direct interactions of mitotic arrest deficient 1 (MAD1) domains with each
RT   other and MAD2 conformers are required for mitotic checkpoint signaling.";
RL   J. Biol. Chem. 293:484-496(2018).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) OF 510-857 OF APOPROTEIN AND IN
RP   COMPLEX WITH SP600125, AND MUTAGENESIS OF ASP-664 AND THR-686.
RX   PubMed=18480048; DOI=10.1074/jbc.m803026200;
RA   Chu M.L.H., Chavas L.M.G., Douglas K.T., Eyers P.A., Tabernero L.;
RT   "Crystal structure of the catalytic domain of the mitotic checkpoint kinase
RT   Mps1 in complex with SP600125.";
RL   J. Biol. Chem. 283:21495-21500(2008).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 515-857.
RX   PubMed=19120698; DOI=10.1111/j.1582-4934.2008.00605.x;
RA   Wang W., Yang Y., Gao Y., Xu Q., Wang F., Zhu S., Old W., Resing K.,
RA   Ahn N., Lei M., Liu X.;
RT   "Structural and mechanistic insights into Mps1 kinase activation.";
RL   J. Cell. Mol. Med. 13:1679-1694(2009).
CC   -!- FUNCTION: Phosphorylates proteins on serine, threonine, and tyrosine
CC       (PubMed:18243099, PubMed:29162720). Probably associated with cell
CC       proliferation (PubMed:18243099). Phosphorylates MAD1L1 to promote
CC       mitotic checkpoint signaling (PubMed:29162720). Essential for
CC       chromosome alignment by enhancing AURKB activity (via direct CDCA8
CC       phosphorylation) at the centromere, and for the mitotic checkpoint
CC       (PubMed:18243099). {ECO:0000269|PubMed:18243099,
CC       ECO:0000269|PubMed:29162720}.
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=2.7.12.1;
CC         Evidence={ECO:0000305|PubMed:29162720};
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=2.7.12.1; Evidence={ECO:0000305|PubMed:29162720};
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=2.7.12.1;
CC         Evidence={ECO:0000305|PubMed:29162720};
CC   -!- ACTIVITY REGULATION: Inhibited by the ATP-competitive kinase inhibitor,
CC       SP600125.
CC   -!- SUBUNIT: Interacts with TPR; the interactions occurs in a microtubule-
CC       independent manner (PubMed:19273613). Interacts with MAD1L1 and MAD2L1
CC       (PubMed:29162720). {ECO:0000269|PubMed:19273613,
CC       ECO:0000269|PubMed:29162720}.
CC   -!- INTERACTION:
CC       P33981-1; O14777: NDC80; NbExp=4; IntAct=EBI-15986834, EBI-715849;
CC       P33981-1; Q9BZD4: NUF2; NbExp=2; IntAct=EBI-15986834, EBI-724102;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P33981-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P33981-2; Sequence=VSP_043072;
CC   -!- TISSUE SPECIFICITY: Present in rapidly proliferating cell lines.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA61239.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M86699; AAA61239.1; ALT_INIT; mRNA.
DR   EMBL; AK292460; BAF85149.1; -; mRNA.
DR   EMBL; AK315696; BAG38059.1; -; mRNA.
DR   EMBL; AL133475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW48699.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48700.1; -; Genomic_DNA.
DR   EMBL; BC000633; AAH00633.1; -; mRNA.
DR   EMBL; BC032858; AAH32858.1; -; mRNA.
DR   EMBL; X70500; CAA49912.1; -; mRNA.
DR   CCDS; CCDS4993.1; -. [P33981-1]
DR   CCDS; CCDS55040.1; -. [P33981-2]
DR   PIR; A42861; A42861.
DR   RefSeq; NP_001160163.1; NM_001166691.1. [P33981-2]
DR   RefSeq; NP_003309.2; NM_003318.4. [P33981-1]
DR   RefSeq; XP_011534401.1; XM_011536099.2. [P33981-1]
DR   RefSeq; XP_011534402.1; XM_011536100.2. [P33981-2]
DR   PDB; 2X9E; X-ray; 3.10 A; A=514-828.
DR   PDB; 2ZMC; X-ray; 3.14 A; A=510-857.
DR   PDB; 2ZMD; X-ray; 2.88 A; A=510-857.
DR   PDB; 3CEK; X-ray; 2.30 A; A=519-808.
DR   PDB; 3DBQ; X-ray; 2.70 A; A=515-857.
DR   PDB; 3GFW; X-ray; 2.74 A; A=519-808.
DR   PDB; 3H9F; X-ray; 2.60 A; A=519-808.
DR   PDB; 3HMN; X-ray; 2.70 A; A=510-809.
DR   PDB; 3HMO; X-ray; 2.40 A; A=510-809.
DR   PDB; 3HMP; X-ray; 2.30 A; A=510-809.
DR   PDB; 3VQU; X-ray; 2.40 A; A=516-820.
DR   PDB; 3W1F; X-ray; 2.70 A; A=516-820.
DR   PDB; 3WYX; X-ray; 2.90 A; A=516-820.
DR   PDB; 3WYY; X-ray; 3.05 A; A=516-820.
DR   PDB; 3WZJ; X-ray; 2.75 A; A=516-820.
DR   PDB; 3WZK; X-ray; 2.30 A; A=516-820.
DR   PDB; 4B94; X-ray; 2.20 A; A/B/C/D=62-239.
DR   PDB; 4BHZ; X-ray; 2.85 A; A=519-808.
DR   PDB; 4BI0; X-ray; 2.84 A; A=519-808.
DR   PDB; 4BI1; X-ray; 2.70 A; A=519-808.
DR   PDB; 4BI2; X-ray; 3.11 A; A=519-808.
DR   PDB; 4C4E; X-ray; 2.60 A; A=519-808.
DR   PDB; 4C4F; X-ray; 2.36 A; A=519-808.
DR   PDB; 4C4G; X-ray; 2.65 A; A=519-808.
DR   PDB; 4C4H; X-ray; 2.80 A; A=519-808.
DR   PDB; 4C4I; X-ray; 2.65 A; A=519-808.
DR   PDB; 4C4J; X-ray; 2.50 A; A=519-808.
DR   PDB; 4CV8; X-ray; 3.00 A; A=519-808.
DR   PDB; 4CV9; X-ray; 2.50 A; A=519-808.
DR   PDB; 4CVA; X-ray; 2.50 A; A=519-808.
DR   PDB; 4D2S; X-ray; 2.50 A; A=514-795.
DR   PDB; 4H7X; X-ray; 2.60 A; A/B=55-210.
DR   PDB; 4H7Y; X-ray; 1.80 A; A/B/C/D=55-210.
DR   PDB; 4JS8; X-ray; 1.94 A; A=515-795.
DR   PDB; 4JT3; X-ray; 2.20 A; A=515-795.
DR   PDB; 4O6L; X-ray; 2.38 A; A/B=515-795.
DR   PDB; 4ZEG; X-ray; 2.33 A; A=515-795.
DR   PDB; 5AP0; X-ray; 2.15 A; A=519-808.
DR   PDB; 5AP1; X-ray; 2.05 A; A=519-808.
DR   PDB; 5AP2; X-ray; 2.80 A; A=519-808.
DR   PDB; 5AP3; X-ray; 2.70 A; A=519-808.
DR   PDB; 5AP4; X-ray; 2.85 A; A=519-808.
DR   PDB; 5AP5; X-ray; 2.80 A; A=519-808.
DR   PDB; 5AP6; X-ray; 2.10 A; A=519-808.
DR   PDB; 5AP7; X-ray; 2.45 A; A=519-808.
DR   PDB; 5EH0; X-ray; 2.18 A; A=519-794.
DR   PDB; 5EHL; X-ray; 2.66 A; A=519-808.
DR   PDB; 5EHO; X-ray; 2.18 A; A=519-808.
DR   PDB; 5EHY; X-ray; 2.26 A; A=519-808.
DR   PDB; 5EI2; X-ray; 2.67 A; A=519-808.
DR   PDB; 5EI6; X-ray; 2.01 A; A=519-808.
DR   PDB; 5EI8; X-ray; 2.17 A; A=519-753.
DR   PDB; 5LJJ; X-ray; 3.00 A; A=519-808.
DR   PDB; 5MRB; X-ray; 2.20 A; A=519-808.
DR   PDB; 5N7V; X-ray; 2.52 A; A=519-808.
DR   PDB; 5N84; X-ray; 2.30 A; A=519-808.
DR   PDB; 5N87; X-ray; 2.29 A; A=519-808.
DR   PDB; 5N93; X-ray; 2.10 A; A=519-808.
DR   PDB; 5N9S; X-ray; 2.30 A; A=519-808.
DR   PDB; 5NA0; X-ray; 2.90 A; A=519-808.
DR   PDB; 5NAD; X-ray; 2.80 A; A=519-808.
DR   PDB; 5NTT; X-ray; 2.75 A; A=519-797.
DR   PDB; 5O91; X-ray; 3.20 A; A=519-808.
DR   PDB; 6B4W; X-ray; 2.90 A; A=515-795.
DR   PDB; 6GVJ; X-ray; 2.41 A; A=400-808.
DR   PDB; 6H3K; X-ray; 2.48 A; A=519-794.
DR   PDB; 6N6O; X-ray; 2.60 A; A=515-795.
DR   PDB; 6TN9; X-ray; 2.60 A; A=515-806.
DR   PDB; 6TNB; X-ray; 2.65 A; A=515-806.
DR   PDB; 6TNC; X-ray; 2.30 A; A=515-806.
DR   PDB; 6TND; X-ray; 2.58 A; A=515-806.
DR   PDB; 7CHM; X-ray; 2.65 A; A=515-795.
DR   PDB; 7CHN; X-ray; 2.40 A; A=515-795.
DR   PDB; 7CHT; X-ray; 2.40 A; A=515-795.
DR   PDB; 7CIL; X-ray; 2.30 A; A=515-795.
DR   PDB; 7CJA; X-ray; 2.49 A; A=515-795.
DR   PDB; 7CLH; X-ray; 2.90 A; A=515-795.
DR   PDB; 7LQD; X-ray; 1.95 A; A=519-808.
DR   PDBsum; 2X9E; -.
DR   PDBsum; 2ZMC; -.
DR   PDBsum; 2ZMD; -.
DR   PDBsum; 3CEK; -.
DR   PDBsum; 3DBQ; -.
DR   PDBsum; 3GFW; -.
DR   PDBsum; 3H9F; -.
DR   PDBsum; 3HMN; -.
DR   PDBsum; 3HMO; -.
DR   PDBsum; 3HMP; -.
DR   PDBsum; 3VQU; -.
DR   PDBsum; 3W1F; -.
DR   PDBsum; 3WYX; -.
DR   PDBsum; 3WYY; -.
DR   PDBsum; 3WZJ; -.
DR   PDBsum; 3WZK; -.
DR   PDBsum; 4B94; -.
DR   PDBsum; 4BHZ; -.
DR   PDBsum; 4BI0; -.
DR   PDBsum; 4BI1; -.
DR   PDBsum; 4BI2; -.
DR   PDBsum; 4C4E; -.
DR   PDBsum; 4C4F; -.
DR   PDBsum; 4C4G; -.
DR   PDBsum; 4C4H; -.
DR   PDBsum; 4C4I; -.
DR   PDBsum; 4C4J; -.
DR   PDBsum; 4CV8; -.
DR   PDBsum; 4CV9; -.
DR   PDBsum; 4CVA; -.
DR   PDBsum; 4D2S; -.
DR   PDBsum; 4H7X; -.
DR   PDBsum; 4H7Y; -.
DR   PDBsum; 4JS8; -.
DR   PDBsum; 4JT3; -.
DR   PDBsum; 4O6L; -.
DR   PDBsum; 4ZEG; -.
DR   PDBsum; 5AP0; -.
DR   PDBsum; 5AP1; -.
DR   PDBsum; 5AP2; -.
DR   PDBsum; 5AP3; -.
DR   PDBsum; 5AP4; -.
DR   PDBsum; 5AP5; -.
DR   PDBsum; 5AP6; -.
DR   PDBsum; 5AP7; -.
DR   PDBsum; 5EH0; -.
DR   PDBsum; 5EHL; -.
DR   PDBsum; 5EHO; -.
DR   PDBsum; 5EHY; -.
DR   PDBsum; 5EI2; -.
DR   PDBsum; 5EI6; -.
DR   PDBsum; 5EI8; -.
DR   PDBsum; 5LJJ; -.
DR   PDBsum; 5MRB; -.
DR   PDBsum; 5N7V; -.
DR   PDBsum; 5N84; -.
DR   PDBsum; 5N87; -.
DR   PDBsum; 5N93; -.
DR   PDBsum; 5N9S; -.
DR   PDBsum; 5NA0; -.
DR   PDBsum; 5NAD; -.
DR   PDBsum; 5NTT; -.
DR   PDBsum; 5O91; -.
DR   PDBsum; 6B4W; -.
DR   PDBsum; 6GVJ; -.
DR   PDBsum; 6H3K; -.
DR   PDBsum; 6N6O; -.
DR   PDBsum; 6TN9; -.
DR   PDBsum; 6TNB; -.
DR   PDBsum; 6TNC; -.
DR   PDBsum; 6TND; -.
DR   PDBsum; 7CHM; -.
DR   PDBsum; 7CHN; -.
DR   PDBsum; 7CHT; -.
DR   PDBsum; 7CIL; -.
DR   PDBsum; 7CJA; -.
DR   PDBsum; 7CLH; -.
DR   PDBsum; 7LQD; -.
DR   AlphaFoldDB; P33981; -.
DR   SMR; P33981; -.
DR   BioGRID; 113123; 144.
DR   DIP; DIP-40642N; -.
DR   IntAct; P33981; 59.
DR   MINT; P33981; -.
DR   STRING; 9606.ENSP00000358813; -.
DR   BindingDB; P33981; -.
DR   ChEMBL; CHEMBL3983; -.
DR   DrugBank; DB15498; BOS172722.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugBank; DB01782; Pyrazolanthrone.
DR   DrugCentral; P33981; -.
DR   GuidetoPHARMACOLOGY; 2264; -.
DR   GlyGen; P33981; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P33981; -.
DR   PhosphoSitePlus; P33981; -.
DR   SwissPalm; P33981; -.
DR   BioMuta; TTK; -.
DR   DMDM; 160112977; -.
DR   EPD; P33981; -.
DR   jPOST; P33981; -.
DR   MassIVE; P33981; -.
DR   MaxQB; P33981; -.
DR   PaxDb; P33981; -.
DR   PeptideAtlas; P33981; -.
DR   PRIDE; P33981; -.
DR   ProteomicsDB; 54932; -. [P33981-1]
DR   ProteomicsDB; 54933; -. [P33981-2]
DR   Antibodypedia; 4121; 485 antibodies from 34 providers.
DR   DNASU; 7272; -.
DR   Ensembl; ENST00000230510.7; ENSP00000230510.3; ENSG00000112742.10. [P33981-2]
DR   Ensembl; ENST00000369798.7; ENSP00000358813.2; ENSG00000112742.10. [P33981-1]
DR   Ensembl; ENST00000509894.5; ENSP00000422936.1; ENSG00000112742.10. [P33981-2]
DR   GeneID; 7272; -.
DR   KEGG; hsa:7272; -.
DR   MANE-Select; ENST00000369798.7; ENSP00000358813.2; NM_003318.5; NP_003309.2.
DR   UCSC; uc003pjb.5; human. [P33981-1]
DR   CTD; 7272; -.
DR   DisGeNET; 7272; -.
DR   GeneCards; TTK; -.
DR   HGNC; HGNC:12401; TTK.
DR   HPA; ENSG00000112742; Group enriched (bone marrow, lymphoid tissue, testis).
DR   MIM; 604092; gene.
DR   neXtProt; NX_P33981; -.
DR   OpenTargets; ENSG00000112742; -.
DR   PharmGKB; PA37066; -.
DR   VEuPathDB; HostDB:ENSG00000112742; -.
DR   eggNOG; KOG0596; Eukaryota.
DR   GeneTree; ENSGT00950000182984; -.
DR   HOGENOM; CLU_010380_0_0_1; -.
DR   InParanoid; P33981; -.
DR   OMA; PISTPKW; -.
DR   OrthoDB; 220433at2759; -.
DR   PhylomeDB; P33981; -.
DR   TreeFam; TF105420; -.
DR   BRENDA; 2.7.12.1; 2681.
DR   PathwayCommons; P33981; -.
DR   SignaLink; P33981; -.
DR   SIGNOR; P33981; -.
DR   BioGRID-ORCS; 7272; 671 hits in 1116 CRISPR screens.
DR   EvolutionaryTrace; P33981; -.
DR   GeneWiki; TTK_(gene); -.
DR   GenomeRNAi; 7272; -.
DR   Pharos; P33981; Tchem.
DR   PRO; PR:P33981; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; P33981; protein.
DR   Bgee; ENSG00000112742; Expressed in secondary oocyte and 131 other tissues.
DR   ExpressionAtlas; P33981; baseline and differential.
DR   Genevisible; P33981; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005819; C:spindle; TAS:ProtInc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0043515; F:kinetochore binding; IEA:Ensembl.
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; IBA:GO_Central.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; TAS:ProtInc.
DR   GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR   GO; GO:0051304; P:chromosome separation; IEA:InterPro.
DR   GO; GO:0016321; P:female meiosis chromosome segregation; IEA:Ensembl.
DR   GO; GO:0033316; P:meiotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0007052; P:mitotic spindle organization; TAS:ProtInc.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; TAS:BHF-UCL.
DR   GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR   GO; GO:0034501; P:protein localization to kinetochore; IBA:GO_Central.
DR   GO; GO:1903096; P:protein localization to meiotic spindle midzone; IEA:Ensembl.
DR   GO; GO:0007051; P:spindle organization; TAS:ProtInc.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027084; Prot_kin_Mps1_fam.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR22974:SF21; PTHR22974:SF21; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48452; SSF48452; 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   3D-structure; Acetylation; Alternative splicing; ATP-binding; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT   CHAIN           1..857
FT                   /note="Dual specificity protein kinase TTK"
FT                   /id="PRO_0000086774"
FT   DOMAIN          525..791
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          371..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          836..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        647
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         531..539
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         553
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19369195,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT   MOD_RES         33
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:20068231"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976"
FT   MOD_RES         281
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231"
FT   MOD_RES         317
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976"
FT   MOD_RES         321
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT   MOD_RES         393
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976"
FT   MOD_RES         436
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT   MOD_RES         455
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         821
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17924679,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         420
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043072"
FT   VARIANT         97
FT                   /note="A -> V (in dbSNP:rs2230513)"
FT                   /id="VAR_037141"
FT   VARIANT         758
FT                   /note="D -> N (in dbSNP:rs2230512)"
FT                   /id="VAR_037142"
FT   MUTAGEN         664
FT                   /note="D->A: Loss of kinase activity."
FT                   /evidence="ECO:0000269|PubMed:18243099,
FT                   ECO:0000269|PubMed:18480048"
FT   MUTAGEN         686
FT                   /note="T->A: Loss of kinase activity."
FT                   /evidence="ECO:0000269|PubMed:18480048"
FT   CONFLICT        389
FT                   /note="S -> A (in Ref. 1; AAA61239)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        768
FT                   /note="L -> V (in Ref. 7; CAA49912 and 8)"
FT                   /evidence="ECO:0000305"
FT   HELIX           62..75
FT                   /evidence="ECO:0007829|PDB:4H7Y"
FT   HELIX           81..97
FT                   /evidence="ECO:0007829|PDB:4H7Y"
FT   HELIX           100..103
FT                   /evidence="ECO:0007829|PDB:4H7Y"
FT   HELIX           107..123
FT                   /evidence="ECO:0007829|PDB:4H7Y"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:4H7Y"
FT   HELIX           129..138
FT                   /evidence="ECO:0007829|PDB:4H7Y"
FT   HELIX           143..155
FT                   /evidence="ECO:0007829|PDB:4H7Y"
FT   HELIX           159..171
FT                   /evidence="ECO:0007829|PDB:4H7Y"
FT   HELIX           177..188
FT                   /evidence="ECO:0007829|PDB:4H7Y"
FT   STRAND          517..520
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   STRAND          523..533
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   STRAND          535..543
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   STRAND          549..556
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   HELIX           557..559
FT                   /evidence="ECO:0007829|PDB:5EHO"
FT   HELIX           562..577
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   TURN            578..581
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   STRAND          583..585
FT                   /evidence="ECO:0007829|PDB:5EH0"
FT   STRAND          588..593
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   STRAND          595..602
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   STRAND          606..608
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   HELIX           609..614
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   STRAND          616..618
FT                   /evidence="ECO:0007829|PDB:3W1F"
FT   HELIX           621..640
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   HELIX           650..652
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   STRAND          653..656
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   STRAND          659..662
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   STRAND          666..668
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   HELIX           676..679
FT                   /evidence="ECO:0007829|PDB:6GVJ"
FT   TURN            686..689
FT                   /evidence="ECO:0007829|PDB:4JT3"
FT   HELIX           692..696
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   HELIX           713..729
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   TURN            733..736
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   HELIX           740..748
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   STRAND          750..752
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   HELIX           762..771
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   TURN            776..778
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   HELIX           782..785
FT                   /evidence="ECO:0007829|PDB:4JS8"
FT   HELIX           789..792
FT                   /evidence="ECO:0007829|PDB:4JS8"
SQ   SEQUENCE   857 AA;  97072 MW;  51F40A3CD1677AC5 CRC64;
     MESEDLSGRE LTIDSIMNKV RDIKNKFKNE DLTDELSLNK ISADTTDNSG TVNQIMMMAN
     NPEDWLSLLL KLEKNSVPLS DALLNKLIGR YSQAIEALPP DKYGQNESFA RIQVRFAELK
     AIQEPDDARD YFQMARANCK KFAFVHISFA QFELSQGNVK KSKQLLQKAV ERGAVPLEML
     EIALRNLNLQ KKQLLSEEEK KNLSASTVLT AQESFSGSLG HLQNRNNSCD SRGQTTKARF
     LYGENMPPQD AEIGYRNSLR QTNKTKQSCP FGRVPVNLLN SPDCDVKTDD SVVPCFMKRQ
     TSRSECRDLV VPGSKPSGND SCELRNLKSV QNSHFKEPLV SDEKSSELII TDSITLKNKT
     ESSLLAKLEE TKEYQEPEVP ESNQKQWQSK RKSECINQNP AASSNHWQIP ELARKVNTEQ
     KHTTFEQPVF SVSKQSPPIS TSKWFDPKSI CKTPSSNTLD DYMSCFRTPV VKNDFPPACQ
     LSTPYGQPAC FQQQQHQILA TPLQNLQVLA SSSANECISV KGRIYSILKQ IGSGGSSKVF
     QVLNEKKQIY AIKYVNLEEA DNQTLDSYRN EIAYLNKLQQ HSDKIIRLYD YEITDQYIYM
     VMECGNIDLN SWLKKKKSID PWERKSYWKN MLEAVHTIHQ HGIVHSDLKP ANFLIVDGML
     KLIDFGIANQ MQPDTTSVVK DSQVGTVNYM PPEAIKDMSS SRENGKSKSK ISPKSDVWSL
     GCILYYMTYG KTPFQQIINQ ISKLHAIIDP NHEIEFPDIP EKDLQDVLKC CLKRDPKQRI
     SIPELLAHPY VQIQTHPVNQ MAKGTTEEMK YVLGQLVGLN SPNSILKAAK TLYEHYSGGE
     SHNSSSSKTF EKKRGKK
 
 
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