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Q15569 (TESK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity testis-specific protein kinase 1

EC=2.7.12.1
Alternative name(s):
Testicular protein kinase 1
Gene names
Name:TESK1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length626 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Probably plays a central role at and after the meiotic phase of spermatogenesis By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Manganese By similarity.

Enzyme regulation

Activated by autophosphorylation on Ser-220. Kinase activity is inhibited by SPRED1 By similarity.

Subunit structure

Interacts with TAOK2; leading to inhibit TAOK2 activity. Interacts with SPRED1; leading to inhibit activity By similarity. Interacts with SPRY4. Ref.5

Domain

The extracatalytic C-terminal part is highly rich in proline residues.

Post-translational modification

Autophosphorylated on serine and tyrosine residues By similarity.

Sequence similarities

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

Contains 1 protein kinase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SPRY4Q9C0044EBI-354852,EBI-354861

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 626626Dual specificity testis-specific protein kinase 1
PRO_0000086746

Regions

Domain57 – 314258Protein kinase
Nucleotide binding63 – 719ATP By similarity

Sites

Active site1751Proton acceptor By similarity
Binding site861ATP By similarity

Amino acid modifications

Modified residue2201Phosphoserine; by autocatalysis By similarity

Natural variations

Natural variant5391H → Y in breast cancer samples; infiltrating ductal carcinoma; somatic mutation. Ref.6 Ref.7
VAR_035638
Natural variant5741G → S. Ref.7
Corresponds to variant rs55673450 [ dbSNP | Ensembl ].
VAR_041213

Experimental info

Sequence conflict431A → V in BAA09459. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q15569 [UniParc].

Last modified October 14, 2008. Version 2.
Checksum: 32F78E5E6AEDB0E5

FASTA62667,684
        10         20         30         40         50         60 
MAGERPPLRG PGPGPGEVPG EGPPGPGGTG GGPGRGRPSS YRALRSAVSS LARVDDFHCA 

        70         80         90        100        110        120 
EKIGAGFFSE VYKVRHRQSG QVMVLKMNKL PSNRGNTLRE VQLMNRLRHP NILRFMGVCV 

       130        140        150        160        170        180 
HQGQLHALTE YMNGGTLEQL LSSPEPLSWP VRLHLALDIA RGLRYLHSKG VFHRDLTSKN 

       190        200        210        220        230        240 
CLVRREDRGF TAVVGDFGLA EKIPVYREGA RKEPLAVVGS PYWMAPEVLR GELYDEKADV 

       250        260        270        280        290        300 
FAFGIVLCEL IARVPADPDY LPRTEDFGLD VPAFRTLVGD DCPLPFLLLA IHCCNLEPST 

       310        320        330        340        350        360 
RAPFTEITQH LEWILEQLPE PAPLTRTALT HNQGSVARGG PSATLPRPDP RLSRSRSDLF 

       370        380        390        400        410        420 
LPPSPESPPN WGDNLTRVNP FSLREDLRGG KIKLLDTPSK PVLPLVPPSP FPSTQLPLVT 

       430        440        450        460        470        480 
TPETLVQPGT PARRCRSLPS SPELPRRMET ALPGPGPPAV GPSAEEKMEC EGSSPEPEPP 

       490        500        510        520        530        540 
GPAPQLPLAV ATDNFISTCS SASQPWSPRS GPVLNNNPPA VVVNSPQGWA GEPWNRAQHS 

       550        560        570        580        590        600 
LPRAAALERT EPSPPPSAPR EPDEGLPCPG CCLGPFSFGF LSMCPRPTPA VARYRNLNCE 

       610        620 
AGSLLCHRGH HAKPPTPSLQ LPGARS 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of a novel protein kinase, TESK1, specifically expressed in testicular germ cells."
Toshima J., Ohashi K., Okano I., Nunoue K., Kishioka M., Kuma K., Miyata T., Hirai M., Baba T., Mizuno K.
J. Biol. Chem. 270:31331-31337(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hepatoma.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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].
[4]"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].
Tissue: Brain and Eye.
[5]"Human sprouty 4, a new ras antagonist on 5q31, interacts with the dual specificity kinase TESK1."
Leeksma O.C., van Achterberg T.A.E., Tsumura Y., Toshima J., Eldering E., Kroes W.G.M., Mellink C., Spaargaren M., Mizuno K., Pannekoek H., de Vries C.J.M.
Eur. J. Biochem. 269:2546-2556(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPRY4.
[6]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-539.
[7]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] TYR-539 AND SER-574.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50863 mRNA. Translation: BAA09459.1.
AL357874 Genomic DNA. Translation: CAI13441.1.
CH471071 Genomic DNA. Translation: EAW58375.1.
BC038448 mRNA. Translation: AAH38448.1.
BC067130 mRNA. Translation: AAH67130.1.
RefSeqNP_006276.2. NM_006285.2.
UniGeneHs.708096.

3D structure databases

ProteinModelPortalQ15569.
SMRQ15569. Positions 25-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112875. 12 interactions.
IntActQ15569. 6 interactions.
MINTMINT-210342.
STRING9606.ENSP00000338127.

Chemistry

BindingDBQ15569.
ChEMBLCHEMBL5604.
GuidetoPHARMACOLOGY2239.

PTM databases

PhosphoSiteQ15569.

Polymorphism databases

DMDM209572684.

Proteomic databases

PaxDbQ15569.
PRIDEQ15569.

Protocols and materials databases

DNASU7016.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336395; ENSP00000338127; ENSG00000107140.
GeneID7016.
KEGGhsa:7016.
UCSCuc003zxa.3. human.

Organism-specific databases

CTD7016.
GeneCardsGC09P035605.
HGNCHGNC:11731. TESK1.
HPAHPA017064.
MIM601782. gene.
neXtProtNX_Q15569.
PharmGKBPA36448.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000231415.
HOVERGENHBG058204.
InParanoidQ15569.
KOK08841.
OMAKMECEGS.
OrthoDBEOG7V7664.
PhylomeDBQ15569.
TreeFamTF318014.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111155. Cell-Cell communication.
SignaLinkQ15569.

Gene expression databases

ArrayExpressQ15569.
BgeeQ15569.
CleanExHS_TESK1.
GenevestigatorQ15569.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR015782. Testis-specific_kinase_1.
IPR008266. Tyr_kinase_AS.
[Graphical view]
PANTHERPTHR23257:SF10. PTHR23257:SF10. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTESK1. human.
GeneWikiTESK1.
GenomeRNAi7016.
NextBio27411.
PROQ15569.
SOURCESearch...

Entry information

Entry nameTESK1_HUMAN
AccessionPrimary (citable) accession number: Q15569
Secondary accession number(s): Q8IXZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 14, 2008
Last modified: April 16, 2014
This is version 139 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

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 9

Human chromosome 9: entries, gene names and cross-references to MIM