TTK (gene)

TTK

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2X9E, 2ZMC, 2ZMD, 3CEK, 3DBQ, 3GFW, 3H9F, 3HMN, 3HMO, 3HMP, 3VQU, 3W1F, 3WYX, 3WYY, 3WZJ, 3WZK, 4B94, 4BHZ, 4BI0, 4BI1, 4BI2, 4C4E, 4C4G, 4C4H, 4C4I, 4C4J, 4CV8, 4CV9, 4CVA, 4D2S, 4H7X, 4H7Y, 4JS8, 4JT3, 4O6L, 5AP0, 5AP1, 5AP2, 5AP3, 5AP4, 5AP5, 5AP6, 5AP7, 5EI2, 5EHY, 5EH0, 5EI6, 4ZEG, 5EI8

Identifiers

Aliases

TTK, CT96, ESK, MPH1, MPS1, MPS1L1, PYT, TTK protein kinase

External IDs

MGI: 1194921 HomoloGene: 2489 GeneCards: TTK

Gene ontology
Molecular function	• kinase activity • transferase activity • protein serine/threonine/tyrosine kinase activity • protein serine/threonine kinase activity • protein tyrosine kinase activity • nucleotide binding • protein kinase activity • protein binding • ATP binding
Cellular component	• spindle • membrane • cytoplasm
Biological process	• chromosome separation • mitotic spindle organization • positive regulation of pathway-restricted SMAD protein phosphorylation • spindle organization • mitotic spindle assembly checkpoint • positive regulation of cell proliferation • protein phosphorylation • phosphorylation • mitotic cell cycle checkpoint • peptidyl-tyrosine phosphorylation
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


7272


22137

Ensembl


ENSG00000112742


ENSMUSG00000038379

UniProt


P33981


P35761

RefSeq (mRNA)


NM_001166691 NM_003318


NM_001110265 NM_001284272 NM_009445

RefSeq (protein)


NP_001160163.1 NP_003309.2


n/a

Location (UCSC)

Chr 6: 80 – 80.04 Mb

Chr 9: 83.83 – 83.87 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Dual specificity protein kinase TTK also known as Mps1 is an enzyme that in humans is encoded by the TTK gene.^[3]^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Mills GB, Schmandt R, McGill M, Amendola A, Hill M, Jacobs K, May C, Rodricks AM, Campbell S, Hogg D (Aug 1992). "Expression of TTK, a novel human protein kinase, is associated with cell proliferation". J Biol Chem. 267 (22): 16000–6. PMID 1639825.
↑ "Entrez Gene: TTK TTK protein kinase".

Hanks SK, Quinn AM (1991). "Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members". Meth. Enzymol. Methods in Enzymology. 200: 38–62. doi:10.1016/0076-6879(91)00126-H. ISBN 978-0-12-182101-2. PMID 1956325.
Lindberg RA, Fischer WH, Hunter T (1993). "Characterization of a human protein threonine kinase isolated by screening an expression library with antibodies to phosphotyrosine". Oncogene. 8 (2): 351–9. PMID 7678926.
Lauzé E, Stoelcker B, Luca FC, et al. (1995). "Yeast spindle pole body duplication gene MPS1 encodes an essential dual specificity protein kinase". EMBO J. 14 (8): 1655–63. PMC 398258. PMID 7737118.
Cahill DP, da Costa LT, Carson-Walter EB, et al. (1999). "Characterization of MAD2B and other mitotic spindle checkpoint genes". Genomics. 58 (2): 181–7. doi:10.1006/geno.1999.5831. PMID 10366450.
Weinmann AS, Yan PS, Oberley MJ, et al. (2002). "Isolating human transcription factor targets by coupling chromatin immunoprecipitation and CpG island microarray analysis". Genes Dev. 16 (2): 235–44. doi:10.1101/gad.943102. PMC 155318. PMID 11799066.
Stucke VM, Silljé HH, Arnaud L, Nigg EA (2002). "Human Mps1 kinase is required for the spindle assembly checkpoint but not for centrosome duplication". EMBO J. 21 (7): 1723–32. doi:10.1093/emboj/21.7.1723. PMC 125937. PMID 11927556.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Liu ST, Chan GK, Hittle JC, et al. (2003). "Human MPS1 Kinase Is Required for Mitotic Arrest Induced by the Loss of CENP-E from Kinetochores". Mol. Biol. Cell. 14 (4): 1638–51. doi:10.1091/mbc.02-05-0074. PMC 153128. PMID 12686615.
Fisk HA, Mattison CP, Winey M (2004). "Human Mps1 protein kinase is required for centrosome duplication and normal mitotic progression". Proc. Natl. Acad. Sci. U.S.A. 100 (25): 14875–80. doi:10.1073/pnas.2434156100. PMC 299837. PMID 14657364.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Dou Z, Ding X, Zereshki A, et al. (2004). "TTK kinase is essential for the centrosomal localization of TACC2". FEBS Lett. 572 (1–3): 51–6. doi:10.1016/j.febslet.2004.06.092. PMID 15304323.
Wei JH, Chou YF, Ou YH, et al. (2005). "TTK/hMps1 participates in the regulation of DNA damage checkpoint response by phosphorylating CHK2 on threonine 68". J. Biol. Chem. 280 (9): 7748–57. doi:10.1074/jbc.M410152200. PMID 15618221.
Camacho E, Beà S, Salaverría I, et al. (2006). "Analysis of Aurora-A and hMPS1 mitotic kinases in mantle cell lymphoma". Int. J. Cancer. 118 (2): 357–63. doi:10.1002/ijc.21370. PMID 16080195.
Leng M, Chan DW, Luo H, et al. (2006). "MPS1-dependent mitotic BLM phosphorylation is important for chromosome stability". Proc. Natl. Acad. Sci. U.S.A. 103 (31): 11485–90. doi:10.1073/pnas.0601828103. PMC 1518802. PMID 16864798.
Bertheau P, Turpin E, Rickman DS, et al. (2007). "Exquisite Sensitivity of TP53 Mutant and Basal Breast Cancers to a Dose-Dense Epirubicin−Cyclophosphamide Regimen". PLoS Med. 4 (3): e90. doi:10.1371/journal.pmed.0040090. PMC 1831731. PMID 17388661.
Zhu S, Wang W, Clarke DC, Liu X (2007). "Activation of Mps1 promotes transforming growth factor-beta-independent Smad signaling". J. Biol. Chem. 282 (25): 18327–38. doi:10.1074/jbc.M700636200. PMID 17452325.
Kanai M, Ma Z, Izumi H, et al. (2007). "Physical and functional interaction between mortalin and Mps1 kinase". Genes Cells. 12 (6): 797–810. doi:10.1111/j.1365-2443.2007.01091.x. PMID 17573779.
Mattison CP, Old WM, Steiner E, et al. (2007). "Mps1 activation loop autophosphorylation enhances kinase activity". J. Biol. Chem. 282 (42): 30553–61. doi:10.1074/jbc.M707063200. PMID 17728254.

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated Mammalian target of rapamycin EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3

3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase

Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-

IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1

Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3

Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1

Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4

Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14

MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14

Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3

(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-

Tropomyosin kinase (EC 2.7.11.28)	-

Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-

Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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TTK (gene)

References

Further reading