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Protein

Dual specificity testis-specific protein kinase 1

Gene

TESK1

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

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

Protein has several cofactor binding sites:

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 serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
  4. protein serine/threonine kinase activity Source: ProtInc
  5. protein tyrosine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. cell junction assembly Source: Reactome
  2. spermatogenesis Source: ProtInc
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ15569.
CleanExiHS_TESK1.
ExpressionAtlasiQ15569. baseline and differential.
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 25-328.
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.
GeneTreeiENSGT00530000063025.
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

        10         20         30         40         50
MAGERPPLRG PGPGPGEVPG EGPPGPGGTG GGPGRGRPSS YRALRSAVSS
60 70 80 90 100
LARVDDFHCA EKIGAGFFSE VYKVRHRQSG QVMVLKMNKL PSNRGNTLRE
110 120 130 140 150
VQLMNRLRHP NILRFMGVCV HQGQLHALTE YMNGGTLEQL LSSPEPLSWP
160 170 180 190 200
VRLHLALDIA RGLRYLHSKG VFHRDLTSKN CLVRREDRGF TAVVGDFGLA
210 220 230 240 250
EKIPVYREGA RKEPLAVVGS PYWMAPEVLR GELYDEKADV FAFGIVLCEL
260 270 280 290 300
IARVPADPDY LPRTEDFGLD VPAFRTLVGD DCPLPFLLLA IHCCNLEPST
310 320 330 340 350
RAPFTEITQH LEWILEQLPE PAPLTRTALT HNQGSVARGG PSATLPRPDP
360 370 380 390 400
RLSRSRSDLF LPPSPESPPN WGDNLTRVNP FSLREDLRGG KIKLLDTPSK
410 420 430 440 450
PVLPLVPPSP FPSTQLPLVT TPETLVQPGT PARRCRSLPS SPELPRRMET
460 470 480 490 500
ALPGPGPPAV GPSAEEKMEC EGSSPEPEPP GPAPQLPLAV ATDNFISTCS
510 520 530 540 550
SASQPWSPRS GPVLNNNPPA VVVNSPQGWA GEPWNRAQHS LPRAAALERT
560 570 580 590 600
EPSPPPSAPR EPDEGLPCPG CCLGPFSFGF LSMCPRPTPA VARYRNLNCE
610 620
AGSLLCHRGH HAKPPTPSLQ LPGARS
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:
EMBLi
GenBanki
DDBJi
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.
ENST00000620767; ENSP00000481045; ENSG00000107140.
GeneIDi7016.
KEGGihsa:7016.
UCSCiuc003zxa.3. human.

Polymorphism databases

DMDMi209572684.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ15569.
SMRiQ15569. Positions 25-328.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiQ15569.
ChEMBLiCHEMBL5604.
GuidetoPHARMACOLOGYi2239.

PTM databases

PhosphoSiteiQ15569.

Polymorphism databases

DMDMi209572684.

Proteomic databases

PaxDbiQ15569.
PRIDEiQ15569.

Protocols and materials databases

DNASUi7016.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336395; ENSP00000338127; ENSG00000107140.
ENST00000620767; ENSP00000481045; ENSG00000107140.
GeneIDi7016.
KEGGihsa:7016.
UCSCiuc003zxa.3. human.

Organism-specific databases

CTDi7016.
GeneCardsiGC09P035605.
HGNCiHGNC:11731. TESK1.
HPAiHPA017064.
MIMi601782. gene.
neXtProtiNX_Q15569.
PharmGKBiPA36448.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063025.
HOGENOMiHOG000231415.
HOVERGENiHBG058204.
InParanoidiQ15569.
KOiK08841.
OMAiKMECEGS.
OrthoDBiEOG7V7664.
PhylomeDBiQ15569.
TreeFamiTF318014.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiTESK1. human.
GeneWikiiTESK1.
GenomeRNAii7016.
NextBioi27411.
PROiQ15569.
SOURCEiSearch...

Gene expression databases

BgeeiQ15569.
CleanExiHS_TESK1.
ExpressionAtlasiQ15569. baseline and differential.
GenevestigatoriQ15569.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 147 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.