CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006355
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dual specificity protein kinase TTK 
Protein Synonyms/Alias
 Phosphotyrosine picked threonine-protein kinase; PYT 
Gene Name
 TTK 
Gene Synonyms/Alias
 MPS1; MPS1L1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
19TIDSIMNKVRDIKNKubiquitination[1]
26KVRDIKNKFKNEDLTubiquitination[1]
28RDIKNKFKNEDLTDEubiquitination[1]
86LSDALLNKLIGRYSQubiquitination[1, 2, 3, 4, 5]
102IEALPPDKYGQNESFubiquitination[1, 3]
120QVRFAELKAIQEPDDubiquitination[1]
163QGNVKKSKQLLQKAVubiquitination[1]
168KSKQLLQKAVERGAVubiquitination[1]
191LRNLNLQKKQLLSEEubiquitination[1]
192RNLNLQKKQLLSEEEubiquitination[1]
200QLLSEEEKKNLSASTubiquitination[1]
201LLSEEEKKNLSASTVubiquitination[1]
287NSPDCDVKTDDSVVPubiquitination[1]
315DLVVPGSKPSGNDSCubiquitination[1]
328SCELRNLKSVQNSHFubiquitination[1]
336SVQNSHFKEPLVSDEubiquitination[1]
359DSITLKNKTESSLLAubiquitination[1]
372LAKLEETKEYQEPEVubiquitination[1, 3]
385EVPESNQKQWQSKRKubiquitination[1, 3]
415QIPELARKVNTEQKHubiquitination[1]
421RKVNTEQKHTTFEQPubiquitination[1]
434QPVFSVSKQSPPISTubiquitination[1]
443SPPISTSKWFDPKSIubiquitination[1]
448TSKWFDPKSICKTPSubiquitination[1]
452FDPKSICKTPSSNTLubiquitination[1, 6]
529GRIYSILKQIGSGGSubiquitination[1]
538IGSGGSSKVFQVLNEubiquitination[1, 2, 5]
546VFQVLNEKKQIYAIKubiquitination[1, 3, 6]
547FQVLNEKKQIYAIKYubiquitination[1, 7]
577NEIAYLNKLQQHSDKubiquitination[1]
584KLQQHSDKIIRLYDYubiquitination[1]
617NSWLKKKKSIDPWERubiquitination[1, 7]
649GIVHSDLKPANFLIVubiquitination[1]
680PDTTSVVKDSQVGTVubiquitination[1]
696YMPPEAIKDMSSSREubiquitination[1, 3]
762EFPDIPEKDLQDVLKubiquitination[1]
769KDLQDVLKCCLKRDPubiquitination[1]
803HPVNQMAKGTTEEMKubiquitination[1]
810KGTTEEMKYVLGQLVubiquitination[1, 3, 7]
827NSPNSILKAAKTLYEubiquitination[1, 2, 3, 4, 5, 7]
830NSILKAAKTLYEHYSubiquitination[1, 6]
848SHNSSSSKTFEKKRGubiquitination[1, 3]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Phosphorylates proteins on serine, threonine, and tyrosine. Probably associated with cell proliferation. Essential for chromosome alignment by enhancing AURKB activity (via direct CDCA8 phosphorylation) at the centromere, and for the mitotic checkpoint. 
Sequence Annotation
 DOMAIN 525 791 Protein kinase.
 NP_BIND 531 539 ATP (By similarity).
 ACT_SITE 647 647 Proton acceptor (By similarity).
 BINDING 553 553 ATP (By similarity).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 7 7 Phosphoserine.
 MOD_RES 33 33 Phosphothreonine.
 MOD_RES 37 37 Phosphoserine.
 MOD_RES 80 80 Phosphoserine.
 MOD_RES 281 281 Phosphoserine.
 MOD_RES 317 317 Phosphoserine.
 MOD_RES 321 321 Phosphoserine.
 MOD_RES 393 393 Phosphoserine.
 MOD_RES 436 436 Phosphoserine.
 MOD_RES 821 821 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 857 AA 
Protein Sequence
MESEDLSGRE LTIDSIMNKV RDIKNKFKNE DLTDELSLNK ISADTTDNSG TVNQIMMMAN 60
NPEDWLSLLL KLEKNSVPLS DALLNKLIGR YSQAIEALPP DKYGQNESFA RIQVRFAELK 120
AIQEPDDARD YFQMARANCK KFAFVHISFA QFELSQGNVK KSKQLLQKAV ERGAVPLEML 180
EIALRNLNLQ KKQLLSEEEK KNLSASTVLT AQESFSGSLG HLQNRNNSCD SRGQTTKARF 240
LYGENMPPQD AEIGYRNSLR QTNKTKQSCP FGRVPVNLLN SPDCDVKTDD SVVPCFMKRQ 300
TSRSECRDLV VPGSKPSGND SCELRNLKSV QNSHFKEPLV SDEKSSELII TDSITLKNKT 360
ESSLLAKLEE TKEYQEPEVP ESNQKQWQSK RKSECINQNP AASSNHWQIP ELARKVNTEQ 420
KHTTFEQPVF SVSKQSPPIS TSKWFDPKSI CKTPSSNTLD DYMSCFRTPV VKNDFPPACQ 480
LSTPYGQPAC FQQQQHQILA TPLQNLQVLA SSSANECISV KGRIYSILKQ IGSGGSSKVF 540
QVLNEKKQIY AIKYVNLEEA DNQTLDSYRN EIAYLNKLQQ HSDKIIRLYD YEITDQYIYM 600
VMECGNIDLN SWLKKKKSID PWERKSYWKN MLEAVHTIHQ HGIVHSDLKP ANFLIVDGML 660
KLIDFGIANQ MQPDTTSVVK DSQVGTVNYM PPEAIKDMSS SRENGKSKSK ISPKSDVWSL 720
GCILYYMTYG KTPFQQIINQ ISKLHAIIDP NHEIEFPDIP EKDLQDVLKC CLKRDPKQRI 780
SIPELLAHPY VQIQTHPVNQ MAKGTTEEMK YVLGQLVGLN SPNSILKAAK TLYEHYSGGE 840
SHNSSSSKTF EKKRGKK 857 
Gene Ontology
 GO:0005819; C:spindle; TAS:ProtInc.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; TAS:ProtInc.
 GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:EC.
 GO:0004713; F:protein tyrosine kinase activity; TAS:ProtInc.
 GO:0007094; P:mitotic spindle assembly checkpoint; TAS:ProtInc.
 GO:0007052; P:mitotic spindle organization; TAS:ProtInc.
 GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
 GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; TAS:BHF-UCL. 
Interpro
 IPR027084; Dual_sp_prot_kinse_Ttk.
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase 
SMART
 SM00220; S_TKc 
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS