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Protein

Dual specificity testis-specific protein kinase 1

Gene

Tesk1

Organism
Rattus norvegicus (Rat)
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.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Activated by autophosphorylation on Ser-215. Kinase activity is inhibited by SPRED1.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei81 – 811ATPPROSITE-ProRule annotation
Active sitei170 – 1701Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi58 – 669ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • spermatogenesis Source: RGD
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. 5301.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi62059. Tesk1.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi170 – 1701D → A: Loss of kinase and autophosphorylating activity.
Mutagenesisi201 – 2011Y → A: No effect on autophosphorylation. 1 Publication
Mutagenesisi215 – 2151S → A: Loss of autophosphorylation site, loss of kinase activity. 1 Publication
Mutagenesisi215 – 2151S → E: Loss of autophosphorylation site, no effect on kinase activity. 1 Publication
Mutagenesisi217 – 2171Y → A: No effect on autophosphorylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 628628Dual specificity testis-specific protein kinase 1PRO_0000086748Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei215 – 2151Phosphoserine; by autocatalysis1 Publication

Post-translational modificationi

Autophosphorylated on serine and tyrosine residues.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ63572.
PRIDEiQ63572.

PTM databases

iPTMnetiQ63572.
PhosphoSiteiQ63572.

Expressioni

Tissue specificityi

Highly expressed in testicular germ cells. Expressed at low levels in brain, lung, heart, liver and kidney.1 Publication

Gene expression databases

GenevisibleiQ63572. RN.

Interactioni

Subunit structurei

Interacts with SPRY4 (By similarity). Interacts with TAOK2; leading to inhibit TAOK2 activity. Interacts with SPRED1; leading to inhibit activity.By similarity1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023694.

Structurei

3D structure databases

ProteinModelPortaliQ63572.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 310259Protein 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

eggNOGiENOG410IF1S. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00530000063025.
HOGENOMiHOG000231415.
HOVERGENiHBG058204.
InParanoidiQ63572.
KOiK08841.
OMAiKMECEGS.
OrthoDBiEOG7V7664.
PhylomeDBiQ63572.
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:SF383. PTHR23257:SF383. 1 hit.
PfamiPF07714. Pkinase_Tyr. 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.

Q63572-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGERPPLRG PGPGETPVEG PGGAGGGPGR GRPSSYRALR SAVSSLARVD
60 70 80 90 100
DFDCAEKIGA GFFSEVYKVR HRQSGQVMVL KMNKLPSNRS NTLREVQLMN
110 120 130 140 150
RLRHPNILRF MGVCVHQGQL HALTEYMNGG TLEQLLSSPE PLSWPVRLHL
160 170 180 190 200
ALDIAQGLRY LHAKGVFHRD LTSKNCLVRR EDGGFTAVVG DFGLAEKIPV
210 220 230 240 250
YREGARKEPL AVVGSPYWMA PEVLRGELYD EKADVFAFGI VLCELIARVP
260 270 280 290 300
ADPDYLPRTE DFGLDVPAFR TLVGNDCPLP FLLLAIHCCS MEPSARAPFT
310 320 330 340 350
EITQHLEQIL EQLPEPTPLA KMPLAKAPLT YNQGSVPRGG PSATLPRSDP
360 370 380 390 400
RLSRSRSDLF LPPSPESPPS WGDNLTRVNP FSLREDLRGG KIKLLDTPCK
410 420 430 440 450
PATPLPLVPP SPLTSTQLPL VASPESLVQP ETPVRRCRSL PSSPELPRRM
460 470 480 490 500
ETALPGPGPS PVGPSTEERM DCEGSSPEPE PPGPAPQLPL AVATDNFIST
510 520 530 540 550
CSSASQPWSA RPGPSLNNNP PAVVVNSPQG WAREPWNRAQ HSLPRAAALE
560 570 580 590 600
RTEPSPPPSA PREQEEGLPC PGCCLSPFSF GFLSMCPRPT PAVARYRNLN
610 620
CEAGSLLCHR GHHAKPPTPS LQLPGARS
Length:628
Mass (Da):67,988
Last modified:November 1, 1996 - v1
Checksum:iF05F67FBD934B9AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50864 mRNA. Translation: BAA09460.1.
BC081773 mRNA. Translation: AAH81773.1.
RefSeqiNP_113766.1. NM_031578.1.
UniGeneiRn.7006.

Genome annotation databases

EnsembliENSRNOT00000080909; ENSRNOP00000071965; ENSRNOG00000053729.
GeneIDi29460.
KEGGirno:29460.
UCSCiRGD:62059. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50864 mRNA. Translation: BAA09460.1.
BC081773 mRNA. Translation: AAH81773.1.
RefSeqiNP_113766.1. NM_031578.1.
UniGeneiRn.7006.

3D structure databases

ProteinModelPortaliQ63572.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023694.

PTM databases

iPTMnetiQ63572.
PhosphoSiteiQ63572.

Proteomic databases

PaxDbiQ63572.
PRIDEiQ63572.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000080909; ENSRNOP00000071965; ENSRNOG00000053729.
GeneIDi29460.
KEGGirno:29460.
UCSCiRGD:62059. rat.

Organism-specific databases

CTDi7016.
RGDi62059. Tesk1.

Phylogenomic databases

eggNOGiENOG410IF1S. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00530000063025.
HOGENOMiHOG000231415.
HOVERGENiHBG058204.
InParanoidiQ63572.
KOiK08841.
OMAiKMECEGS.
OrthoDBiEOG7V7664.
PhylomeDBiQ63572.
TreeFamiTF318014.

Enzyme and pathway databases

BRENDAi2.7.10.2. 5301.

Miscellaneous databases

PROiQ63572.

Gene expression databases

GenevisibleiQ63572. RN.

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:SF383. PTHR23257:SF383. 1 hit.
PfamiPF07714. Pkinase_Tyr. 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].
    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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-215, 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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAOK2 AND SPRED1, ENZYME REGULATION.

Entry informationi

Entry nameiTESK1_RAT
AccessioniPrimary (citable) accession number: Q63572
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.