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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
