Reviewed, UniProtKB/Swiss-Prot P33981 (TTK_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	857 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	mitotic cell cycle spindle assembly checkpoint Traceable author statement. Source: ProtInc mitotic spindle organization Traceable author statement. Source: ProtInc positive regulation of cell proliferation Ref.1 Traceable author statement. Source: ProtInc positive regulation of pathway-restricted SMAD protein phosphorylation Traceable author statement. Source: UniProtKB protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	spindle Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.10 Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Traceable author statement. Source: ProtInc protein tyrosine kinase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDCA8	Q53HL2	1	EBI-1645856,EBI-979174

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 857

857

Dual specificity protein kinase TTK

PRO_0000086774

Regions

Domain

525 – 791

267

Protein kinase

Nucleotide binding

531 – 539

9

ATP By similarity

Sites

Active site

647

1

Proton acceptor By similarity

Binding site

553

1

ATP By similarity

Amino acid modifications

Modified residue

3

1

Phosphoserine

Modified residue

7

1

Phosphoserine Ref.11

Modified residue

33

1

Phosphothreonine Ref.11 Ref.12

Modified residue

37

1

Phosphoserine Ref.11

Modified residue

49

1

Phosphoserine

Modified residue

80

1

Phosphoserine Ref.11

Modified residue

216

1

Phosphoserine Ref.16

Modified residue

218

1

Phosphoserine Ref.16

Modified residue

281

1

Phosphoserine Ref.11 Ref.12 Ref.14

Modified residue

317

1

Phosphoserine Ref.11

Modified residue

321

1

Phosphoserine Ref.12

Modified residue

393

1

Phosphoserine Ref.11 Ref.12

Modified residue

431

1

Phosphoserine

Modified residue

436

1

Phosphoserine Ref.11 Ref.9

Modified residue

453

1

Phosphothreonine

Modified residue

455

1

Phosphoserine

Modified residue

821

1

Phosphoserine Ref.11 Ref.12 Ref.14 Ref.8

Modified residue

824

1

Phosphoserine Ref.8

Natural variations

Natural variant

97

1

A → V: dbSNP rs2230513.

VAR_037141

Natural variant

758

1

D → N: dbSNP rs2230512.

VAR_037142

Experimental info

Mutagenesis

664

1

D → A: Loss of kinase activity. Ref.10 Ref.17

Mutagenesis

686

1

T → A: Loss of kinase activity. Ref.17

Sequence conflict

389

1

S → A in AAA61239. Ref.1

Sequence conflict

768

1

L → V in CAA49912. Ref.6

Sequence conflict

768

1

L → V Ref.7

Secondary structure

1

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857

Helix Strand Turn

Details...

Beta strand

524 – 530

7

Beta strand

537 – 543

7

Beta strand

549 – 556

8

Helix

562 – 578

17

Helix

579 – 581

3

Beta strand

588 – 593

6

Beta strand

595 – 602

8

Helix

609 – 615

7

Helix

621 – 640

20

Helix

650 – 652

3

Beta strand

653 – 655

3

Beta strand

660 – 662

3

Helix

687 – 689

3

Helix

692 – 695

4

Helix

713 – 719

7

Helix

723 – 728

6

Turn

733 – 736

4

Helix

740 – 748

9

Helix

762 – 771

10

Turn

776 – 778

3

Helix

782 – 786

5

Helix

789 – 792

4

Sequences

	Sequence		Length	Mass (Da)
	P33981-1 [UniParc]. Last modified November 13, 2007. Version 2. Checksum: 51F40A3CD1677AC5	FASTA	857	97,072
	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

References

	« Hide 'large scale' referencesShow '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: 1639825] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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: 14574404] [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. , 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].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye and Testis.
[6]	"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: 7678926] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 504-802, CHARACTERIZATION.
[7]	"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: 1956325] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 525-792.
[8]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821 AND SER-824, MASS SPECTROMETRY. Tissue: Epithelium.
[9]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436, MASS SPECTROMETRY.
[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: 18243099] [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: 18691976] [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, MASS SPECTROMETRY.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33; SER-281; SER-321; SER-393 AND SER-821, MASS SPECTROMETRY.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281 AND SER-821, MASS SPECTROMETRY.
[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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-7; THR-33; SER-49; SER-80; SER-281; SER-317; SER-321; SER-431; SER-436; THR-453; SER-455 AND SER-821, MASS SPECTROMETRY.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-218, MASS SPECTROMETRY. Tissue: T-cell.
[17]	"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: 18480048] [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.
[18]	"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. 0:0-0(2009) [PubMed: 19120698] [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.
AK315696 mRNA. Translation: BAG38059.1.
AL133475 Genomic DNA. Translation: CAB87580.1. Different initiation.
CH471051 Genomic DNA. Translation: EAW48699.1.
BC000633 mRNA. Translation: AAH00633.1.
BC032858 mRNA. Translation: AAH32858.1.
X70500 mRNA. Translation: CAA49912.1.

IPI

IPI00151170.

PIR

A42861.

RefSeq

NP_003309.2.

UniGene

Hs.169840

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P33981. 1 interaction.

STRING

P33981.

PTM databases

PhosphoSite

P33981.

Proteomic databases

PRIDE

P33981.

Genome annotation databases

Ensembl

ENST00000230510; ENSP00000230510; ENSG00000112742; Homo sapiens. [Genome view]

GeneID

7272.

UCSC

uc003pjc.1. human.

Organism-specific databases

CTD

7272.

GeneCards

GC06P080771.

HGNC

HGNC:12401. TTK.

HPA

CAB010166.
CAB013229.
HPA016834.

MIM

604092. gene.

PharmGKB

PA37066.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG10039.

HOGENOM

HBG715956.

HOVERGEN

P33981.

InParanoid

P33981.

OMA

QFELSQG.

PhylomeDB

P33981.

Enzyme and pathway databases

BRENDA

2.7.12.1. 247.

Gene expression databases

ArrayExpress

P33981.

Bgee

P33981.

CleanEx

HS_TTK.

Genevestigator

P33981.

GermOnline

ENSG00000112742. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

28427.

SOURCE

Search...

Entry information

Entry name

TTK_HUMAN

Accession

Primary (citable) accession number: P33981
Secondary accession number(s): B2RDW2 , Q15272, Q5TCS0, Q9BW51, Q9NTM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	November 13, 2007
Last modified:	February 9, 2010
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.