Q15569 (TESK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity testis-specific protein kinase 1
EC=2.7.12.1

Alternative name(s):
Testicular protein kinase 1

Gene names

Name:

TESK1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	626 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell junction assembly Traceable author statement. Source: Reactome spermatogenesis Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Traceable author statement Ref.1. Source: ProtInc protein serine/threonine/tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SPRY4	Q9C004	4	EBI-354852,EBI-354861

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 626	626	Dual specificity testis-specific protein kinase 1		PRO_0000086746
Regions
	Domain	57 – 314	258	Protein kinase
	Nucleotide binding	63 – 71	9	ATP By similarity
Sites
	Active site	175	1	Proton acceptor By similarity
	Binding site	86	1	ATP By similarity
Amino acid modifications
	Modified residue	220	1	Phosphoserine; by autocatalysis By similarity
Natural variations
	Natural variant	539	1	H → Y in breast cancer samples; infiltrating ductal carcinoma; somatic mutation. Ref.6 Ref.7		VAR_035638
	Natural variant	574	1	G → S. Ref.7 Corresponds to variant rs55673450 [ dbSNP | Ensembl ].		VAR_041213
Experimental info
	Sequence conflict	43	1	A → V in BAA09459. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q15569 [UniParc]. Last modified October 14, 2008. Version 2. Checksum: 32F78E5E6AEDB0E5	FASTA	626	67,684
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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.
IPI	IPI00018182.
RefSeq	NP_006276.2. NM_006285.2.
UniGene	Hs.708096.
3D structure databases
ProteinModelPortal	Q15569.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15569. 6 interactions.
STRING	9606.ENSP00000338127.
PTM databases
PhosphoSite	Q15569.
Polymorphism databases
DMDM	209572684.
Proteomic databases
PaxDb	Q15569.
PRIDE	Q15569.
Protocols and materials databases
DNASU	7016.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000336395; ENSP00000338127; ENSG00000107140.
GeneID	7016.
KEGG	hsa:7016.
UCSC	uc003zxa.3. human.
Organism-specific databases
CTD	7016.
GeneCards	GC09P035605.
HGNC	HGNC:11731. TESK1.
HPA	HPA017064.
MIM	601782. gene.
neXtProt	NX_Q15569.
PharmGKB	PA36448.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000231415.
HOVERGEN	HBG058204.
InParanoid	Q15569.
KO	K08841.
OMA	GRPSSYR.
OrthoDB	EOG4THVT0.
PhylomeDB	Q15569.
Enzyme and pathway databases
BRENDA	2.7.10.2. 2681.
Reactome	REACT_111155. Cell-Cell communication.
Gene expression databases
ArrayExpress	Q15569.
Bgee	Q15569.
CleanEx	HS_TESK1.
Genevestigator	Q15569.
GermOnline	ENSG00000107140. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR015782. Testis-specific_kinase_1. IPR008266. Tyr_kinase_AS. [Graphical view]
PANTHER	PTHR23257:SF10. PTHR23257:SF10. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR00109. TYRKINASE.
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q15569.
ChEMBL	CHEMBL5604.
ChiTaRS	TESK1. human.
GenomeRNAi	7016.
NextBio	27411.
SOURCE	Search...

Entry information

Entry name

TESK1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.