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Q15569

- TESK1_HUMAN

UniProt

Q15569 - TESK1_HUMAN

Protein

Dual specificity testis-specific protein kinase 1

Gene

TESK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (14 Oct 2008)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity
    Manganese.By similarity

    Enzyme regulationi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei86 – 861ATPPROSITE-ProRule annotation
    Active sitei175 – 1751Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi63 – 719ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell junction assembly Source: Reactome
    2. spermatogenesis Source: ProtInc

    Keywords - Molecular functioni

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

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 2681.
    ReactomeiREACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
    SignaLinkiQ15569.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity testis-specific protein kinase 1 (EC:2.7.12.1)
    Alternative name(s):
    Testicular protein kinase 1
    Gene namesi
    Name:TESK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:11731. TESK1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36448.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 626626Dual specificity testis-specific protein kinase 1PRO_0000086746Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei220 – 2201Phosphoserine; by autocatalysisBy similarity

    Post-translational modificationi

    Autophosphorylated on serine and tyrosine residues.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ15569.
    PRIDEiQ15569.

    PTM databases

    PhosphoSiteiQ15569.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15569.
    BgeeiQ15569.
    CleanExiHS_TESK1.
    GenevestigatoriQ15569.

    Organism-specific databases

    HPAiHPA017064.

    Interactioni

    Subunit structurei

    Interacts with TAOK2; leading to inhibit TAOK2 activity. Interacts with SPRED1; leading to inhibit activity By similarity. Interacts with SPRY4.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SPRY4Q9C0044EBI-354852,EBI-354861

    Protein-protein interaction databases

    BioGridi112875. 12 interactions.
    IntActiQ15569. 6 interactions.
    MINTiMINT-210342.
    STRINGi9606.ENSP00000338127.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15569.
    SMRiQ15569. Positions 53-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini57 – 314258Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000231415.
    HOVERGENiHBG058204.
    InParanoidiQ15569.
    KOiK08841.
    OMAiKMECEGS.
    OrthoDBiEOG7V7664.
    PhylomeDBiQ15569.
    TreeFamiTF318014.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR015782. TESK1.
    IPR008266. Tyr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR23257:SF372. PTHR23257:SF372. 1 hit.
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q15569-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGERPPLRG PGPGPGEVPG EGPPGPGGTG GGPGRGRPSS YRALRSAVSS    50
    LARVDDFHCA EKIGAGFFSE VYKVRHRQSG QVMVLKMNKL PSNRGNTLRE 100
    VQLMNRLRHP NILRFMGVCV HQGQLHALTE YMNGGTLEQL LSSPEPLSWP 150
    VRLHLALDIA RGLRYLHSKG VFHRDLTSKN CLVRREDRGF TAVVGDFGLA 200
    EKIPVYREGA RKEPLAVVGS PYWMAPEVLR GELYDEKADV FAFGIVLCEL 250
    IARVPADPDY LPRTEDFGLD VPAFRTLVGD DCPLPFLLLA IHCCNLEPST 300
    RAPFTEITQH LEWILEQLPE PAPLTRTALT HNQGSVARGG PSATLPRPDP 350
    RLSRSRSDLF LPPSPESPPN WGDNLTRVNP FSLREDLRGG KIKLLDTPSK 400
    PVLPLVPPSP FPSTQLPLVT TPETLVQPGT PARRCRSLPS SPELPRRMET 450
    ALPGPGPPAV GPSAEEKMEC EGSSPEPEPP GPAPQLPLAV ATDNFISTCS 500
    SASQPWSPRS GPVLNNNPPA VVVNSPQGWA GEPWNRAQHS LPRAAALERT 550
    EPSPPPSAPR EPDEGLPCPG CCLGPFSFGF LSMCPRPTPA VARYRNLNCE 600
    AGSLLCHRGH HAKPPTPSLQ LPGARS 626
    Length:626
    Mass (Da):67,684
    Last modified:October 14, 2008 - v2
    Checksum:i32F78E5E6AEDB0E5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 431A → V in BAA09459. (PubMed:8537404)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti539 – 5391H → Y in breast cancer samples; infiltrating ductal carcinoma; somatic mutation. 2 Publications
    VAR_035638
    Natural varianti574 – 5741G → S.1 Publication
    Corresponds to variant rs55673450 [ dbSNP | Ensembl ].
    VAR_041213

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS6580.1.
    RefSeqiNP_006276.2. NM_006285.2.
    UniGeneiHs.708096.

    Genome annotation databases

    EnsembliENST00000336395; ENSP00000338127; ENSG00000107140.
    GeneIDi7016.
    KEGGihsa:7016.
    UCSCiuc003zxa.3. human.

    Polymorphism databases

    DMDMi209572684.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS6580.1.
    RefSeqi NP_006276.2. NM_006285.2.
    UniGenei Hs.708096.

    3D structure databases

    ProteinModelPortali Q15569.
    SMRi Q15569. Positions 53-328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112875. 12 interactions.
    IntActi Q15569. 6 interactions.
    MINTi MINT-210342.
    STRINGi 9606.ENSP00000338127.

    Chemistry

    BindingDBi Q15569.
    ChEMBLi CHEMBL5604.
    GuidetoPHARMACOLOGYi 2239.

    PTM databases

    PhosphoSitei Q15569.

    Polymorphism databases

    DMDMi 209572684.

    Proteomic databases

    PaxDbi Q15569.
    PRIDEi Q15569.

    Protocols and materials databases

    DNASUi 7016.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336395 ; ENSP00000338127 ; ENSG00000107140 .
    GeneIDi 7016.
    KEGGi hsa:7016.
    UCSCi uc003zxa.3. human.

    Organism-specific databases

    CTDi 7016.
    GeneCardsi GC09P035605.
    HGNCi HGNC:11731. TESK1.
    HPAi HPA017064.
    MIMi 601782. gene.
    neXtProti NX_Q15569.
    PharmGKBi PA36448.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000231415.
    HOVERGENi HBG058204.
    InParanoidi Q15569.
    KOi K08841.
    OMAi KMECEGS.
    OrthoDBi EOG7V7664.
    PhylomeDBi Q15569.
    TreeFami TF318014.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 2681.
    Reactomei REACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
    SignaLinki Q15569.

    Miscellaneous databases

    ChiTaRSi TESK1. human.
    GeneWikii TESK1.
    GenomeRNAii 7016.
    NextBioi 27411.
    PROi Q15569.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15569.
    Bgeei Q15569.
    CleanExi HS_TESK1.
    Genevestigatori Q15569.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR015782. TESK1.
    IPR008266. Tyr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR23257:SF372. PTHR23257:SF372. 1 hit.
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. Cited for: INTERACTION WITH SPRY4.
    6. 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.
      , 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.

    Entry informationi

    Entry nameiTESK1_HUMAN
    AccessioniPrimary (citable) accession number: Q15569
    Secondary accession number(s): Q8IXZ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 14, 2008
    Last modified: October 1, 2014
    This is version 144 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3