Reviewed, UniProtKB/Swiss-Prot Q15569 (TESK1_HUMAN)

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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	626 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 By similarity.
Subunit structure	Interacts with SPRY4.
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
Gene Ontology (GO)
Biological process	protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro spermatogenesis Ref.1 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.5 Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Ref.1 Traceable author statement. Source: ProtInc protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SPRY4	Q9C004	1	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.		VAR_035638
	Natural variant	574	1	G → S: dbSNP rs55673450.		VAR_041213
Experimental info
	Sequence conflict	43	1	A → V in BAA09459. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q15569-1 [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: 8537404] [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: 15164053] [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: 15489334] [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: 12027893] [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: 16959974] [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: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] TYR-539 AND SER-574.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
RefSeq	NP_006276.2.
UniGene	Hs.699324
3D structure databases
HSSP	HSSP built from PDB template 1FVR based on UniProtKB Q02763.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15569.
PTM databases
PhosphoSite	Q15569.
Genome annotation databases
Ensembl	ENSG00000107140. Homo sapiens. [Contig view]
GeneID	7016.
KEGG	hsa:7016.
Organism-specific databases
HGNC	HGNC:11731. TESK1.
HPA	HPA017064.
MIM	601782. gene.
PharmGKB	PA36448.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	Q15569.
HOVERGEN	Q15569.
Gene expression databases
CleanEx	HS_TESK1.
GermOnline	ENSG00000107140. Homo sapiens.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_bd_CS. IPR017442. Se/Thr_pkinase-rel. IPR015782. TESK1. IPR001245. Tyr_pkinase. IPR008266. Tyr_pkinase_AS. [Graphical view]
PANTHER	PTHR23257:SF10. TESK1. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
PRINTS	PR00109. TYRKINASE.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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:	November 25, 2008
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)