Q63572 (TESK1_RAT) 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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	628 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. Ref.3
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium. Manganese.
Enzyme regulation	Activated by autophosphorylation on Ser-215. Kinase activity is inhibited by SPRED1. Ref.3 Ref.4
Subunit structure	Interacts with SPRY4 By similarity. Interacts with TAOK2; leading to inhibit TAOK2 activity. Interacts with SPRED1; leading to inhibit activity. Ref.4
Tissue specificity	Highly expressed in testicular germ cells. Expressed at low levels in brain, lung, heart, liver and kidney. Ref.3
Domain	The extracatalytic C-terminal part is highly rich in proline residues.
Post-translational modification	Autophosphorylated on serine and tyrosine residues. Ref.3
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
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	spermatogenesis Inferred from expression pattern Ref.1. Source: RGD
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 mutant phenotype Ref.1. Source: RGD 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 628	628	Dual specificity testis-specific protein kinase 1		PRO_0000086748
Regions
	Domain	52 – 310	259	Protein kinase
	Nucleotide binding	58 – 66	9	ATP By similarity
Sites
	Active site	170	1	Proton acceptor
	Binding site	81	1	ATP By similarity
Amino acid modifications
	Modified residue	215	1	Phosphoserine; by autocatalysis
	Modified residue	439	1	Phosphoserine By similarity
	Modified residue	443	1	Phosphoserine By similarity
Experimental info
	Mutagenesis	170	1	D → A: Loss of kinase and autophosphorylating activity.
	Mutagenesis	201	1	Y → A: No effect on autophosphorylation. Ref.3
	Mutagenesis	215	1	S → A: Loss of autophosphorylation site, loss of kinase activity. Ref.3
	Mutagenesis	215	1	S → E: Loss of autophosphorylation site, no effect on kinase activity. Ref.3
	Mutagenesis	217	1	Y → A: No effect on autophosphorylation. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q63572 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: F05F67FBD934B9AD	FASTA	628	67,988
	10 20 30 40 50 60 MAGERPPLRG PGPGETPVEG PGGAGGGPGR GRPSSYRALR SAVSSLARVD DFDCAEKIGA 70 80 90 100 110 120 GFFSEVYKVR HRQSGQVMVL KMNKLPSNRS NTLREVQLMN RLRHPNILRF MGVCVHQGQL 130 140 150 160 170 180 HALTEYMNGG TLEQLLSSPE PLSWPVRLHL ALDIAQGLRY LHAKGVFHRD LTSKNCLVRR 190 200 210 220 230 240 EDGGFTAVVG DFGLAEKIPV YREGARKEPL AVVGSPYWMA PEVLRGELYD EKADVFAFGI 250 260 270 280 290 300 VLCELIARVP ADPDYLPRTE DFGLDVPAFR TLVGNDCPLP FLLLAIHCCS MEPSARAPFT 310 320 330 340 350 360 EITQHLEQIL EQLPEPTPLA KMPLAKAPLT YNQGSVPRGG PSATLPRSDP RLSRSRSDLF 370 380 390 400 410 420 LPPSPESPPS WGDNLTRVNP FSLREDLRGG KIKLLDTPCK PATPLPLVPP SPLTSTQLPL 430 440 450 460 470 480 VASPESLVQP ETPVRRCRSL PSSPELPRRM ETALPGPGPS PVGPSTEERM DCEGSSPEPE 490 500 510 520 530 540 PPGPAPQLPL AVATDNFIST CSSASQPWSA RPGPSLNNNP PAVVVNSPQG WAREPWNRAQ 550 560 570 580 590 600 HSLPRAAALE RTEPSPPPSA PREQEEGLPC PGCCLSPFSF GFLSMCPRPT PAVARYRNLN 610 620 CEAGSLLCHR GHHAKPPTPS LQLPGARS

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]. Strain: Wistar. Tissue: Testis.
[2]	"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: Testis.
[3]	"Dual specificity protein kinase activity of testis-specific protein kinase 1 and its regulation by autophosphorylation of serine-215 within the activation loop." Toshima J., Tanaka T., Mizuno K. J. Biol. Chem. 274:12171-12176(1999) [PubMed: 10207045] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION, ENZYME REGULATION, MUTAGENESIS OF TYR-201; SER-215 AND TYR-217.
[4]	"Spred1 and TESK1--two new interaction partners of the kinase MARKK/TAO1 that link the microtubule and actin cytoskeleton." Johne C., Matenia D., Li X.Y., Timm T., Balusamy K., Mandelkow E.M. Mol. Biol. Cell 19:1391-1403(2008) [PubMed: 18216281] [Abstract] Cited for: INTERACTION WITH TAOK2 AND SPRED1, ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D50864 mRNA. Translation: BAA09460.1. BC081773 mRNA. Translation: AAH81773.1.
IPI	IPI00210162.
RefSeq	NP_113766.1. NM_031578.1.
UniGene	Rn.7006.
3D structure databases
ProteinModelPortal	Q63572.
ModBase	Search...
Protein-protein interaction databases
STRING	Q63572.
PTM databases
PhosphoSite	Q63572.
Proteomic databases
PRIDE	Q63572.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000023695; ENSRNOP00000023694; ENSRNOG00000017532.
GeneID	29460.
KEGG	rno:29460.
UCSC	NM_031578. rat.
Organism-specific databases
CTD	7016.
RGD	62059. Tesk1.
Phylogenomic databases
eggNOG	roNOG13484.
GeneTree	ENSGT00530000063025.
HOVERGEN	HBG058204.
InParanoid	Q63572.
OMA	DNFISTC.
OrthoDB	EOG4THVT0.
PhylomeDB	Q63572.
Enzyme and pathway databases
BRENDA	2.7.10.2. 5301.
Gene expression databases
ArrayExpress	Q63572.
Genevestigator	Q63572.
GermOnline	ENSRNOG00000017532. Rattus norvegicus.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR001245. Ser-Thr/Tyr_kinase. IPR015782. Testis-specific_kinase_1. IPR008266. Tyr_kinase_AS. [Graphical view]
KO	K08841.
PANTHER	PTHR23257:SF10. TESK1. 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
NextBio	609252.

Entry information

Entry name

TESK1_RAT

Accession

Primary (citable) accession number: Q63572

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	November 16, 2011
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program