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P33981 (TTK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity protein kinase TTK

EC=2.7.12.1
Alternative name(s):
Phosphotyrosine picked threonine-protein kinase
Short name=PYT
Gene names
Name:TTK
Synonyms:MPS1, MPS1L1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length857 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Inhibited by the ATP-competitive kinase inhibitor, SP600125.

Subunit structure

Interacts with TPR; the interactions occurs in a microtubule-independent manner. Ref.14

Tissue specificity

Present in rapidly proliferating cell lines.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAA61239.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB87580.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P33981-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P33981-2)

The sequence of this isoform differs from the canonical sequence as follows:
     420-420: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 857857Dual specificity protein kinase TTK
PRO_0000086774

Regions

Domain525 – 791267Protein kinase
Nucleotide binding531 – 5399ATP By similarity

Sites

Active site6471Proton acceptor By similarity
Binding site5531ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.15 Ref.19
Modified residue71Phosphoserine Ref.11 Ref.15
Modified residue331Phosphothreonine Ref.11 Ref.12 Ref.15 Ref.17
Modified residue371Phosphoserine Ref.11 Ref.17
Modified residue801Phosphoserine Ref.11
Modified residue2811Phosphoserine Ref.11 Ref.15 Ref.17
Modified residue3171Phosphoserine Ref.11
Modified residue3211Phosphoserine Ref.12 Ref.15
Modified residue3931Phosphoserine Ref.11 Ref.12
Modified residue4361Phosphoserine Ref.11 Ref.15
Modified residue8211Phosphoserine Ref.9 Ref.11 Ref.12 Ref.15 Ref.17

Natural variations

Alternative sequence4201Missing in isoform 2.
VSP_043072
Natural variant971A → V.
Corresponds to variant rs2230513 [ dbSNP | Ensembl ].
VAR_037141
Natural variant7581D → N.
Corresponds to variant rs2230512 [ dbSNP | Ensembl ].
VAR_037142

Experimental info

Mutagenesis6641D → A: Loss of kinase activity. Ref.10 Ref.20
Mutagenesis6861T → A: Loss of kinase activity. Ref.20
Sequence conflict3891S → A in AAA61239. Ref.1
Sequence conflict7681L → V in CAA49912. Ref.7
Sequence conflict7681L → V Ref.8

Secondary structure

...................................................................... 857
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 51F40A3CD1677AC5

FASTA85797,072
        10         20         30         40         50         60 
MESEDLSGRE LTIDSIMNKV RDIKNKFKNE DLTDELSLNK ISADTTDNSG TVNQIMMMAN 

        70         80         90        100        110        120 
NPEDWLSLLL KLEKNSVPLS DALLNKLIGR YSQAIEALPP DKYGQNESFA RIQVRFAELK 

       130        140        150        160        170        180 
AIQEPDDARD YFQMARANCK KFAFVHISFA QFELSQGNVK KSKQLLQKAV ERGAVPLEML 

       190        200        210        220        230        240 
EIALRNLNLQ KKQLLSEEEK KNLSASTVLT AQESFSGSLG HLQNRNNSCD SRGQTTKARF 

       250        260        270        280        290        300 
LYGENMPPQD AEIGYRNSLR QTNKTKQSCP FGRVPVNLLN SPDCDVKTDD SVVPCFMKRQ 

       310        320        330        340        350        360 
TSRSECRDLV VPGSKPSGND SCELRNLKSV QNSHFKEPLV SDEKSSELII TDSITLKNKT 

       370        380        390        400        410        420 
ESSLLAKLEE TKEYQEPEVP ESNQKQWQSK RKSECINQNP AASSNHWQIP ELARKVNTEQ 

       430        440        450        460        470        480 
KHTTFEQPVF SVSKQSPPIS TSKWFDPKSI CKTPSSNTLD DYMSCFRTPV VKNDFPPACQ 

       490        500        510        520        530        540 
LSTPYGQPAC FQQQQHQILA TPLQNLQVLA SSSANECISV KGRIYSILKQ IGSGGSSKVF 

       550        560        570        580        590        600 
QVLNEKKQIY AIKYVNLEEA DNQTLDSYRN EIAYLNKLQQ HSDKIIRLYD YEITDQYIYM 

       610        620        630        640        650        660 
VMECGNIDLN SWLKKKKSID PWERKSYWKN MLEAVHTIHQ HGIVHSDLKP ANFLIVDGML 

       670        680        690        700        710        720 
KLIDFGIANQ MQPDTTSVVK DSQVGTVNYM PPEAIKDMSS SRENGKSKSK ISPKSDVWSL 

       730        740        750        760        770        780 
GCILYYMTYG KTPFQQIINQ ISKLHAIIDP NHEIEFPDIP EKDLQDVLKC CLKRDPKQRI 

       790        800        810        820        830        840 
SIPELLAHPY VQIQTHPVNQ MAKGTTEEMK YVLGQLVGLN SPNSILKAAK TLYEHYSGGE 

       850 
SHNSSSSKTF EKKRGKK 

« Hide

Isoform 2 [UniParc].

Checksum: 13FDD345AE1B52DA
Show »

FASTA85696,944

References

« Hide 'large scale' references
[1]"Expression of TTK, a novel human protein kinase, is associated with cell proliferation."
Mills G.B., Schmandt R., McGill M., Amendola A., Hill M., Jacobs K., May C., Rodricks A.-M., Campbell S., Hogg D.
J. Biol. Chem. 267:16000-16006(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Testis.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Eye and Testis.
[7]"Characterization of a human protein threonine kinase isolated by screening an expression library with antibodies to phosphotyrosine."
Lindberg R.A., Fischer W.H., Hunter T.
Oncogene 8:351-359(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 504-802 (ISOFORM 1/2), CHARACTERIZATION.
[8]"Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members."
Hanks S.K., Quinn A.M.
Methods Enzymol. 200:38-62(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 525-792 (ISOFORM 1/2).
[9]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Mps1 phosphorylates Borealin to control Aurora B activity and chromosome alignment."
Jelluma N., Brenkman A.B., van den Broek N.J., Cruijsen C.W.A., van Osch M.H.J., Lens S.M.A., Medema R.H., Kops G.J.P.L.
Cell 132:233-246(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-664.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; THR-33; SER-37; SER-80; SER-281; SER-317; SER-393; SER-436 AND SER-821, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33; SER-321; SER-393 AND SER-821, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Spatiotemporal control of mitosis by the conserved spindle matrix protein Megator."
Lince-Faria M., Maffini S., Orr B., Ding Y., Florindo C., Sunkel C.E., Tavares A., Johansen J., Johansen K.M., Maiato H.
J. Cell Biol. 184:647-657(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TPR.
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; THR-33; SER-281; SER-321; SER-436 AND SER-821, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33; SER-37; SER-281 AND SER-821, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Crystal structure of the catalytic domain of the mitotic checkpoint kinase Mps1 in complex with SP600125."
Chu M.L.H., Chavas L.M.G., Douglas K.T., Eyers P.A., Tabernero L.
J. Biol. Chem. 283:21495-21500(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) OF 510-857 OF APOPROTEIN AND IN COMPLEX WITH SP600125, MUTAGENESIS OF ASP-664 AND THR-686.
[21]"Structural and mechanistic insights into Mps1 kinase activation."
Wang W., Yang Y., Gao Y., Xu Q., Wang F., Zhu S., Old W., Resing K., Ahn N., Lei M., Liu X.
J. Cell. Mol. Med. 13:1679-1694(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 515-857.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86699 mRNA. Translation: AAA61239.1. Different initiation.
AK292460 mRNA. Translation: BAF85149.1.
AK315696 mRNA. Translation: BAG38059.1.
AL133475 Genomic DNA. Translation: CAB87580.1. Different initiation.
CH471051 Genomic DNA. Translation: EAW48699.1.
CH471051 Genomic DNA. Translation: EAW48700.1.
BC000633 mRNA. Translation: AAH00633.1.
BC032858 mRNA. Translation: AAH32858.1.
X70500 mRNA. Translation: CAA49912.1.
CCDSCCDS4993.1. [P33981-1]
CCDS55040.1. [P33981-2]
PIRA42861.
RefSeqNP_001160163.1. NM_001166691.1. [P33981-2]
NP_003309.2. NM_003318.4. [P33981-1]
UniGeneHs.169840.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2X9EX-ray3.10A514-828[»]
2ZMCX-ray3.14A510-857[»]
2ZMDX-ray2.88A510-857[»]
3CEKX-ray2.30A519-808[»]
3DBQX-ray2.70A515-857[»]
3GFWX-ray2.74A519-808[»]
3H9FX-ray2.60A519-808[»]
3HMNX-ray2.70A510-809[»]
3HMOX-ray2.40A510-809[»]
3HMPX-ray2.30A510-809[»]
3VQUX-ray2.40A516-820[»]
3W1FX-ray2.70A516-820[»]
4B94X-ray2.20A/B/C/D62-239[»]
4BHZX-ray2.85A519-808[»]
4BI0X-ray2.84A519-808[»]
4BI1X-ray2.70A519-808[»]
4BI2X-ray3.11A519-808[»]
4C4EX-ray2.60A519-808[»]
4C4FX-ray2.36A519-808[»]
4C4GX-ray2.65A519-808[»]
4C4HX-ray2.80A519-808[»]
4C4IX-ray2.65A519-808[»]
4C4JX-ray2.50A519-808[»]
4H7XX-ray2.60A/B55-210[»]
4H7YX-ray1.80A/B/C/D55-210[»]
4JS8X-ray1.94A515-795[»]
4JT3X-ray2.20A515-795[»]
ProteinModelPortalP33981.
SMRP33981. Positions 59-199, 485-822.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113123. 22 interactions.
IntActP33981. 5 interactions.
MINTMINT-1203816.
STRING9606.ENSP00000230510.

Chemistry

BindingDBP33981.
ChEMBLCHEMBL3983.
GuidetoPHARMACOLOGY2264.

PTM databases

PhosphoSiteP33981.

Polymorphism databases

DMDM160112977.

Proteomic databases

MaxQBP33981.
PaxDbP33981.
PRIDEP33981.

Protocols and materials databases

DNASU7272.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000230510; ENSP00000230510; ENSG00000112742. [P33981-2]
ENST00000369798; ENSP00000358813; ENSG00000112742. [P33981-1]
ENST00000509894; ENSP00000422936; ENSG00000112742. [P33981-2]
GeneID7272.
KEGGhsa:7272.
UCSCuc003pjb.4. human. [P33981-2]
uc003pjc.3. human. [P33981-1]

Organism-specific databases

CTD7272.
GeneCardsGC06P080771.
HGNCHGNC:12401. TTK.
HPACAB010166.
CAB013229.
HPA016834.
MIM604092. gene.
neXtProtNX_P33981.
PharmGKBPA37066.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000013174.
HOVERGENHBG001029.
InParanoidP33981.
KOK08866.
OMAMSCFRTP.
OrthoDBEOG7DJSMF.
PhylomeDBP33981.
TreeFamTF105420.

Enzyme and pathway databases

BRENDA2.7.12.1. 2681.
SignaLinkP33981.

Gene expression databases

ArrayExpressP33981.
BgeeP33981.
CleanExHS_TTK.
GenevestigatorP33981.

Family and domain databases

InterProIPR027084. Dual_sp_prot_kinse_Ttk.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR22974:SF21. PTHR22974:SF21. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP33981.
GeneWikiTTK_(gene).
GenomeRNAi7272.
NextBio28427.
PROP33981.
SOURCESearch...

Entry information

Entry nameTTK_HUMAN
AccessionPrimary (citable) accession number: P33981
Secondary accession number(s): A8K8U5 expand/collapse secondary AC list , B2RDW2, E1P543, Q15272, Q5TCS0, Q9BW51, Q9NTM0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 13, 2007
Last modified: July 9, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM