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P33981

- TTK_HUMAN

UniProt

P33981 - TTK_HUMAN

Protein

Dual specificity protein kinase TTK

Gene

TTK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Inhibited by the ATP-competitive kinase inhibitor, SP600125.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei553 – 5531ATPPROSITE-ProRule annotation
    Active sitei647 – 6471Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi531 – 5399ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
    4. protein serine/threonine kinase activity Source: ProtInc
    5. protein tyrosine kinase activity Source: ProtInc

    GO - Biological processi

    1. chromosome separation Source: InterPro
    2. mitotic spindle assembly checkpoint Source: ProtInc
    3. mitotic spindle organization Source: ProtInc
    4. peptidyl-tyrosine phosphorylation Source: GOC
    5. positive regulation of cell proliferation Source: ProtInc
    6. positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
    7. spindle organization Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.12.1. 2681.
    SignaLinkiP33981.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein kinase TTK (EC:2.7.12.1)
    Alternative name(s):
    Phosphotyrosine picked threonine-protein kinase
    Short name:
    PYT
    Gene namesi
    Name:TTK
    Synonyms:MPS1, MPS1L1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:12401. TTK.

    Subcellular locationi

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. spindle Source: ProtInc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi664 – 6641D → A: Loss of kinase activity. 2 Publications
    Mutagenesisi686 – 6861T → A: Loss of kinase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA37066.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 857857Dual specificity protein kinase TTKPRO_0000086774Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei7 – 71Phosphoserine2 Publications
    Modified residuei33 – 331Phosphothreonine4 Publications
    Modified residuei37 – 371Phosphoserine2 Publications
    Modified residuei80 – 801Phosphoserine1 Publication
    Modified residuei281 – 2811Phosphoserine3 Publications
    Modified residuei317 – 3171Phosphoserine1 Publication
    Modified residuei321 – 3211Phosphoserine2 Publications
    Modified residuei393 – 3931Phosphoserine2 Publications
    Modified residuei436 – 4361Phosphoserine2 Publications
    Modified residuei821 – 8211Phosphoserine5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP33981.
    PaxDbiP33981.
    PRIDEiP33981.

    PTM databases

    PhosphoSiteiP33981.

    Expressioni

    Tissue specificityi

    Present in rapidly proliferating cell lines.

    Gene expression databases

    ArrayExpressiP33981.
    BgeeiP33981.
    CleanExiHS_TTK.
    GenevestigatoriP33981.

    Organism-specific databases

    HPAiCAB010166.
    CAB013229.
    HPA016834.

    Interactioni

    Subunit structurei

    Interacts with TPR; the interactions occurs in a microtubule-independent manner.2 Publications

    Protein-protein interaction databases

    BioGridi113123. 22 interactions.
    IntActiP33981. 6 interactions.
    MINTiMINT-1203816.
    STRINGi9606.ENSP00000230510.

    Structurei

    Secondary structure

    1
    857
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi62 – 7514
    Helixi81 – 9717
    Helixi100 – 1034
    Helixi107 – 12317
    Helixi125 – 1273
    Helixi129 – 13810
    Helixi143 – 15513
    Helixi159 – 17113
    Helixi177 – 18812
    Beta strandi517 – 5204
    Beta strandi523 – 53311
    Beta strandi535 – 5439
    Beta strandi549 – 5568
    Helixi562 – 57716
    Turni578 – 5814
    Beta strandi583 – 5853
    Beta strandi588 – 5936
    Beta strandi595 – 6028
    Beta strandi606 – 6083
    Helixi609 – 6146
    Beta strandi616 – 6183
    Helixi621 – 64020
    Helixi650 – 6523
    Beta strandi653 – 6564
    Beta strandi659 – 6624
    Beta strandi666 – 6683
    Turni686 – 6894
    Helixi692 – 6965
    Helixi713 – 72917
    Turni733 – 7364
    Helixi740 – 7489
    Beta strandi750 – 7523
    Helixi762 – 77110
    Turni776 – 7783
    Helixi782 – 7854
    Helixi789 – 7924

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP33981.
    SMRiP33981. Positions 59-199, 485-822.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP33981.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini525 – 791267Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000013174.
    HOVERGENiHBG001029.
    InParanoidiP33981.
    KOiK08866.
    OMAiMSCFRTP.
    OrthoDBiEOG7DJSMF.
    PhylomeDBiP33981.
    TreeFamiTF105420.

    Family and domain databases

    InterProiIPR027084. 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]
    PANTHERiPTHR22974:SF21. PTHR22974:SF21. 1 hit.
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P33981-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MESEDLSGRE LTIDSIMNKV RDIKNKFKNE DLTDELSLNK ISADTTDNSG    50
    TVNQIMMMAN NPEDWLSLLL KLEKNSVPLS DALLNKLIGR YSQAIEALPP 100
    DKYGQNESFA RIQVRFAELK AIQEPDDARD YFQMARANCK KFAFVHISFA 150
    QFELSQGNVK KSKQLLQKAV ERGAVPLEML EIALRNLNLQ KKQLLSEEEK 200
    KNLSASTVLT AQESFSGSLG HLQNRNNSCD SRGQTTKARF LYGENMPPQD 250
    AEIGYRNSLR QTNKTKQSCP FGRVPVNLLN SPDCDVKTDD SVVPCFMKRQ 300
    TSRSECRDLV VPGSKPSGND SCELRNLKSV QNSHFKEPLV SDEKSSELII 350
    TDSITLKNKT ESSLLAKLEE TKEYQEPEVP ESNQKQWQSK RKSECINQNP 400
    AASSNHWQIP ELARKVNTEQ KHTTFEQPVF SVSKQSPPIS TSKWFDPKSI 450
    CKTPSSNTLD DYMSCFRTPV VKNDFPPACQ LSTPYGQPAC FQQQQHQILA 500
    TPLQNLQVLA SSSANECISV KGRIYSILKQ IGSGGSSKVF QVLNEKKQIY 550
    AIKYVNLEEA DNQTLDSYRN EIAYLNKLQQ HSDKIIRLYD YEITDQYIYM 600
    VMECGNIDLN SWLKKKKSID PWERKSYWKN MLEAVHTIHQ HGIVHSDLKP 650
    ANFLIVDGML KLIDFGIANQ MQPDTTSVVK DSQVGTVNYM PPEAIKDMSS 700
    SRENGKSKSK ISPKSDVWSL GCILYYMTYG KTPFQQIINQ ISKLHAIIDP 750
    NHEIEFPDIP EKDLQDVLKC CLKRDPKQRI SIPELLAHPY VQIQTHPVNQ 800
    MAKGTTEEMK YVLGQLVGLN SPNSILKAAK TLYEHYSGGE SHNSSSSKTF 850
    EKKRGKK 857
    Length:857
    Mass (Da):97,072
    Last modified:November 13, 2007 - v2
    Checksum:i51F40A3CD1677AC5
    GO
    Isoform 2 (identifier: P33981-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         420-420: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:856
    Mass (Da):96,944
    Checksum:i13FDD345AE1B52DA
    GO

    Sequence cautioni

    The sequence AAA61239.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAB87580.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti389 – 3891S → A in AAA61239. (PubMed:1639825)Curated
    Sequence conflicti768 – 7681L → V in CAA49912. (PubMed:7678926)Curated
    Sequence conflicti768 – 7681L → V(PubMed:1956325)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti97 – 971A → V.
    Corresponds to variant rs2230513 [ dbSNP | Ensembl ].
    VAR_037141
    Natural varianti758 – 7581D → N.
    Corresponds to variant rs2230512 [ dbSNP | Ensembl ].
    VAR_037142

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei420 – 4201Missing in isoform 2. 1 PublicationVSP_043072

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS4993.1. [P33981-1]
    CCDS55040.1. [P33981-2]
    PIRiA42861.
    RefSeqiNP_001160163.1. NM_001166691.1. [P33981-2]
    NP_003309.2. NM_003318.4. [P33981-1]
    UniGeneiHs.169840.

    Genome annotation databases

    EnsembliENST00000230510; ENSP00000230510; ENSG00000112742. [P33981-2]
    ENST00000369798; ENSP00000358813; ENSG00000112742. [P33981-1]
    ENST00000509894; ENSP00000422936; ENSG00000112742. [P33981-2]
    GeneIDi7272.
    KEGGihsa:7272.
    UCSCiuc003pjb.4. human. [P33981-2]
    uc003pjc.3. human. [P33981-1]

    Polymorphism databases

    DMDMi160112977.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS4993.1. [P33981-1 ]
    CCDS55040.1. [P33981-2 ]
    PIRi A42861.
    RefSeqi NP_001160163.1. NM_001166691.1. [P33981-2 ]
    NP_003309.2. NM_003318.4. [P33981-1 ]
    UniGenei Hs.169840.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2X9E X-ray 3.10 A 514-828 [» ]
    2ZMC X-ray 3.14 A 510-857 [» ]
    2ZMD X-ray 2.88 A 510-857 [» ]
    3CEK X-ray 2.30 A 519-808 [» ]
    3DBQ X-ray 2.70 A 515-857 [» ]
    3GFW X-ray 2.74 A 519-808 [» ]
    3H9F X-ray 2.60 A 519-808 [» ]
    3HMN X-ray 2.70 A 510-809 [» ]
    3HMO X-ray 2.40 A 510-809 [» ]
    3HMP X-ray 2.30 A 510-809 [» ]
    3VQU X-ray 2.40 A 516-820 [» ]
    3W1F X-ray 2.70 A 516-820 [» ]
    4B94 X-ray 2.20 A/B/C/D 62-239 [» ]
    4BHZ X-ray 2.85 A 519-808 [» ]
    4BI0 X-ray 2.84 A 519-808 [» ]
    4BI1 X-ray 2.70 A 519-808 [» ]
    4BI2 X-ray 3.11 A 519-808 [» ]
    4C4E X-ray 2.60 A 519-808 [» ]
    4C4F X-ray 2.36 A 519-808 [» ]
    4C4G X-ray 2.65 A 519-808 [» ]
    4C4H X-ray 2.80 A 519-808 [» ]
    4C4I X-ray 2.65 A 519-808 [» ]
    4C4J X-ray 2.50 A 519-808 [» ]
    4H7X X-ray 2.60 A/B 55-210 [» ]
    4H7Y X-ray 1.80 A/B/C/D 55-210 [» ]
    4JS8 X-ray 1.94 A 515-795 [» ]
    4JT3 X-ray 2.20 A 515-795 [» ]
    ProteinModelPortali P33981.
    SMRi P33981. Positions 59-199, 485-822.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113123. 22 interactions.
    IntActi P33981. 6 interactions.
    MINTi MINT-1203816.
    STRINGi 9606.ENSP00000230510.

    Chemistry

    BindingDBi P33981.
    ChEMBLi CHEMBL3983.
    GuidetoPHARMACOLOGYi 2264.

    PTM databases

    PhosphoSitei P33981.

    Polymorphism databases

    DMDMi 160112977.

    Proteomic databases

    MaxQBi P33981.
    PaxDbi P33981.
    PRIDEi P33981.

    Protocols and materials databases

    DNASUi 7272.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000230510 ; ENSP00000230510 ; ENSG00000112742 . [P33981-2 ]
    ENST00000369798 ; ENSP00000358813 ; ENSG00000112742 . [P33981-1 ]
    ENST00000509894 ; ENSP00000422936 ; ENSG00000112742 . [P33981-2 ]
    GeneIDi 7272.
    KEGGi hsa:7272.
    UCSCi uc003pjb.4. human. [P33981-2 ]
    uc003pjc.3. human. [P33981-1 ]

    Organism-specific databases

    CTDi 7272.
    GeneCardsi GC06P080771.
    HGNCi HGNC:12401. TTK.
    HPAi CAB010166.
    CAB013229.
    HPA016834.
    MIMi 604092. gene.
    neXtProti NX_P33981.
    PharmGKBi PA37066.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000013174.
    HOVERGENi HBG001029.
    InParanoidi P33981.
    KOi K08866.
    OMAi MSCFRTP.
    OrthoDBi EOG7DJSMF.
    PhylomeDBi P33981.
    TreeFami TF105420.

    Enzyme and pathway databases

    BRENDAi 2.7.12.1. 2681.
    SignaLinki P33981.

    Miscellaneous databases

    EvolutionaryTracei P33981.
    GeneWikii TTK_(gene).
    GenomeRNAii 7272.
    NextBioi 28427.
    PROi P33981.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P33981.
    Bgeei P33981.
    CleanExi HS_TTK.
    Genevestigatori P33981.

    Family and domain databases

    InterProi IPR027084. 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 ]
    PANTHERi PTHR22974:SF21. PTHR22974:SF21. 1 hit.
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. 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.

    Entry informationi

    Entry nameiTTK_HUMAN
    AccessioniPrimary (citable) accession number: P33981
    Secondary accession number(s): A8K8U5
    , B2RDW2, E1P543, Q15272, Q5TCS0, Q9BW51, Q9NTM0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3