Q96S53 (TESK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity testis-specific protein kinase 2
EC=2.7.12.1

Alternative name(s):
Testicular protein kinase 2

Gene names

Name:

TESK2

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	571 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. Phosphorylates cofilin at 'Ser-3'. May play an important role in spermatogenesis.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity. Manganese By similarity.
Enzyme regulation	Activated by autophosphorylation on Ser-219 By similarity.
Subcellular location	Nucleus Ref.2.
Tissue specificity	Predominantly expressed in testis and prostate. Found predominantly in non-germinal Sertoli cells. Ref.1 Ref.2
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing 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	actin cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB focal adhesion assembly Inferred from sequence or structural similarity. Source: UniProtKB spermatogenesis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara nucleus Inferred from sequence or structural similarity. Source: UniProtKB
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 Inferred from sequence or structural similarity. Source: UniProtKB 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
HSP90AB1	P08238	2	EBI-1384110,EBI-352572

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q96S53-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q96S53-2)

The sequence of this isoform differs from the canonical sequence as follows:
     116-131: Missing.

Isoform 3 (identifier: Q96S53-3)

The sequence of this isoform differs from the canonical sequence as follows:
     265-293: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 571	571	Dual specificity testis-specific protein kinase 2		PRO_0000086749
Regions
	Domain	58 – 313	256	Protein kinase
	Nucleotide binding	64 – 72	9	ATP By similarity
Sites
	Active site	176	1	Proton acceptor By similarity
	Binding site	87	1	ATP By similarity
Amino acid modifications
	Modified residue	219	1	Phosphoserine; by autocatalysis By similarity
Natural variations
	Alternative sequence	116 – 131	16	Missing in isoform 2.		VSP_004930
	Alternative sequence	265 – 293	29	Missing in isoform 3.		VSP_004931
	Natural variant	11	1	G → A in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.7		VAR_041214
Experimental info
	Sequence conflict	455	1	R → C in AAH33085. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: D83B0E58321A46FA	FASTA	571	63,639
	10 20 30 40 50 60 MDRSKRNSIA GFPPRVERLE EFEGGGGGEG NVSQVGRVWP SSYRALISAF SRLTRLDDFT 70 80 90 100 110 120 CEKIGSGFFS EVFKVRHRAS GQVMALKMNT LSSNRANMLK EVQLMNRLSH PNILRFMGVC 130 140 150 160 170 180 VHQGQLHALT EYINSGNLEQ LLDSNLHLPW TVRVKLAYDI AVGLSYLHFK GIFHRDLTSK 190 200 210 220 230 240 NCLIKRDENG YSAVVADFGL AEKIPDVSMG SEKLAVVGSP FWMAPEVLRD EPYNEKADVF 250 260 270 280 290 300 SYGIILCEII ARIQADPDYL PRTENFGLDY DAFQHMVGDC PPDFLQLTFN CCNMDPKLRP 310 320 330 340 350 360 SFVEIGKTLE EILSRLQEEE QERDRKLQPT ARGLLEKAPG VKRLSSLDDK IPHKSPCPRR 370 380 390 400 410 420 TIWLSRSQSD IFSRKPPRTV SVLDPYYRPR DGAARTPKVN PFSARQDLMG GKIKFFDLPS 430 440 450 460 470 480 KSVISLVFDL DAPGPGTMPL ADWQEPLAPP IRRWRSLPGS PEFLHQEACP FVGREESLSD 490 500 510 520 530 540 GPPPRLSSLK YRVKEIPPFR ASALPAAQAH EAMDCSILQE ENGFGSRPQG TSPCPAGASE 550 560 570 EMEVEERPAG STPATFSTSG IGLQTQGKQD G
	Isoform 2 [UniParc]. Checksum: EFA1A38A53B68FD9	FASTA	555	61,887
	10 20 30 40 50 60 MDRSKRNSIA GFPPRVERLE EFEGGGGGEG NVSQVGRVWP SSYRALISAF SRLTRLDDFT 70 80 90 100 110 120 CEKIGSGFFS EVFKVRHRAS GQVMALKMNT LSSNRANMLK EVQLMNRLSH PNILRYINSG 130 140 150 160 170 180 NLEQLLDSNL HLPWTVRVKL AYDIAVGLSY LHFKGIFHRD LTSKNCLIKR DENGYSAVVA 190 200 210 220 230 240 DFGLAEKIPD VSMGSEKLAV VGSPFWMAPE VLRDEPYNEK ADVFSYGIIL CEIIARIQAD 250 260 270 280 290 300 PDYLPRTENF GLDYDAFQHM VGDCPPDFLQ LTFNCCNMDP KLRPSFVEIG KTLEEILSRL 310 320 330 340 350 360 QEEEQERDRK LQPTARGLLE KAPGVKRLSS LDDKIPHKSP CPRRTIWLSR SQSDIFSRKP 370 380 390 400 410 420 PRTVSVLDPY YRPRDGAART PKVNPFSARQ DLMGGKIKFF DLPSKSVISL VFDLDAPGPG 430 440 450 460 470 480 TMPLADWQEP LAPPIRRWRS LPGSPEFLHQ EACPFVGREE SLSDGPPPRL SSLKYRVKEI 490 500 510 520 530 540 PPFRASALPA AQAHEAMDCS ILQEENGFGS RPQGTSPCPA GASEEMEVEE RPAGSTPATF 550 STSGIGLQTQ GKQDG
	Isoform 3 [UniParc]. Checksum: A4BE7D25116F20E1	FASTA	542	60,332
	10 20 30 40 50 60 MDRSKRNSIA GFPPRVERLE EFEGGGGGEG NVSQVGRVWP SSYRALISAF SRLTRLDDFT 70 80 90 100 110 120 CEKIGSGFFS EVFKVRHRAS GQVMALKMNT LSSNRANMLK EVQLMNRLSH PNILRFMGVC 130 140 150 160 170 180 VHQGQLHALT EYINSGNLEQ LLDSNLHLPW TVRVKLAYDI AVGLSYLHFK GIFHRDLTSK 190 200 210 220 230 240 NCLIKRDENG YSAVVADFGL AEKIPDVSMG SEKLAVVGSP FWMAPEVLRD EPYNEKADVF 250 260 270 280 290 300 SYGIILCEII ARIQADPDYL PRTEMDPKLR PSFVEIGKTL EEILSRLQEE EQERDRKLQP 310 320 330 340 350 360 TARGLLEKAP GVKRLSSLDD KIPHKSPCPR RTIWLSRSQS DIFSRKPPRT VSVLDPYYRP 370 380 390 400 410 420 RDGAARTPKV NPFSARQDLM GGKIKFFDLP SKSVISLVFD LDAPGPGTMP LADWQEPLAP 430 440 450 460 470 480 PIRRWRSLPG SPEFLHQEAC PFVGREESLS DGPPPRLSSL KYRVKEIPPF RASALPAAQA 490 500 510 520 530 540 HEAMDCSILQ EENGFGSRPQ GTSPCPAGAS EEMEVEERPA GSTPATFSTS GIGLQTQGKQ DG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of TESK2, a novel member of the LIMK/TESK family of protein kinases, predominantly expressed in testis." Rosok O., Pedeutour F., Ree A.H., Aasheim H.-C. Genomics 61:44-54(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY. Tissue: Testis.
[2]	"Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular Sertoli cells." Toshima J., Toshima J.Y., Takeuchi K., Mori R., Mizuno K. J. Biol. Chem. 276:31449-31458(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton 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].
[6]	"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] (ISOFORM 3). Tissue: Brain.
[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: VARIANT [LARGE SCALE ANALYSIS] ALA-11.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ132545 mRNA. Translation: CAB41970.1. AB057597 mRNA. Translation: BAB62909.1. AK027573 mRNA. Translation: BAG51348.1. AL451136, AL359540 Genomic DNA. Translation: CAI13092.1. AL451136, AL359540 Genomic DNA. Translation: CAI13093.1. AL359540, AL451136 Genomic DNA. Translation: CAI21723.1. AL359540, AL451136 Genomic DNA. Translation: CAI21724.1. CH471059 Genomic DNA. Translation: EAX06987.1. BC033085 mRNA. Translation: AAH33085.1.
IPI	IPI00102677. IPI00217726. IPI00217728.
RefSeq	NP_009101.2. NM_007170.2.
UniGene	Hs.591499.
3D structure databases
ProteinModelPortal	Q96S53.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q96S53. 1 interaction.
STRING	9606.ENSP00000361158.
PTM databases
PhosphoSite	Q96S53.
Polymorphism databases
DMDM	25009462.
Proteomic databases
PaxDb	Q96S53.
PRIDE	Q96S53.
Protocols and materials databases
DNASU	10420.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000341771; ENSP00000343940; ENSG00000070759. ENST00000372084; ENSP00000361156; ENSG00000070759. ENST00000372086; ENSP00000361158; ENSG00000070759.
GeneID	10420.
KEGG	hsa:10420.
UCSC	uc001cns.1. human. uc009vxr.1. human.
Organism-specific databases
CTD	10420.
GeneCards	GC01M045809.
HGNC	HGNC:11732. TESK2.
HPA	HPA027257.
MIM	604746. gene.
neXtProt	NX_Q96S53.
PharmGKB	PA36449.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000231415.
HOVERGEN	HBG058204.
InParanoid	Q96S53.
KO	K08842.
OMA	PQEENGF.
OrthoDB	EOG4NZTSW.
PhylomeDB	Q96S53.
Enzyme and pathway databases
BRENDA	2.7.10.2. 2681.
Gene expression databases
ArrayExpress	Q96S53.
Bgee	Q96S53.
CleanEx	HS_TESK2.
Genevestigator	Q96S53.
GermOnline	ENSG00000070759. 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. IPR008266. Tyr_kinase_AS. [Graphical view]
Pfam	PF07714. Pkinase_Tyr. 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
ChiTaRS	TESK2. human.
GenomeRNAi	10420.
NextBio	39492.
SOURCE	Search...

Entry information

Entry name

TESK2_HUMAN

Accession

Primary (citable) accession number: Q96S53
Secondary accession number(s): Q5T422 , Q5T423, Q8N520, Q9Y3Q6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 116 of the entry and version 1 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.