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P33981

- TTK_HUMAN

UniProt

P33981 - TTK_HUMAN

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Protein

Dual specificity protein kinase TTK

Gene
TTK, MPS1, MPS1L1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 5531ATP By similarity
Active sitei647 – 6471Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi531 – 5399ATP By similarity

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
Complete GO annotation...

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. spindle Source: ProtInc
Complete GO annotation...

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.1 Publication

Protein-protein interaction databases

BioGridi113123. 22 interactions.
IntActiP33981. 5 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.

Miscellaneous databases

EvolutionaryTraceiP33981.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini525 – 791267Protein kinaseAdd
BLAST

Sequence similaritiesi

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.

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. VSP_043072

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti389 – 3891S → A in AAA61239. 1 Publication
Sequence conflicti768 – 7681L → V in CAA49912. 1 Publication
Sequence conflicti768 – 7681L → V1 Publication

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. 5 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 151 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

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