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 27-MAR-2024, entry version 227. 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; 169. DR DIP; DIP-40642N; -. DR IntAct; P33981; 63. 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; 3 sites, 1 O-linked glycan (3 sites). 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; 9606-ENSP00000358813; -. DR PeptideAtlas; P33981; -. DR ProteomicsDB; 54932; -. [P33981-1] DR ProteomicsDB; 54933; -. [P33981-2] DR Pumba; P33981; -. DR Antibodypedia; 4121; 511 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 AGR; HGNC:12401; -. 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; TPKWIDP; -. DR OrthoDB; 8547at2759; -. 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; 688 hits in 1195 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 132 other cell types or tissues. DR ExpressionAtlas; P33981; baseline and differential. 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: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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc. 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 CDD; cd14131; PKc_Mps1; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR027084; Mps1_cat. 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; DUAL SPECIFICITY PROTEIN KINASE TTK; 1. DR PANTHER; PTHR22974; MIXED LINEAGE PROTEIN KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; P33981; HS. 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:7LQD" 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 //