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Q924U5 (TESK2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual specificity testis-specific protein kinase 2

EC=2.7.12.1
Alternative name(s):
Testicular protein kinase 2
Gene names
Name:Tesk2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

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 By similarity.

Tissue specificity

Predominantly expressed in testis and prostate. Found predominantly in non-germinal Sertoli cells.

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 570570Dual specificity testis-specific protein kinase 2
PRO_0000086751

Regions

Domain58 – 313256Protein kinase
Nucleotide binding64 – 729ATP By similarity

Sites

Active site1761Proton acceptor By similarity
Binding site871ATP By similarity

Amino acid modifications

Modified residue2191Phosphoserine; by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q924U5 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: D20073AD93EE9F9C

FASTA57063,559
        10         20         30         40         50         60 
MDRSKRNSIA GFPPRVERLE EFEGGGGGDG NTVQVGRVSS SSYRAIISAF SRLTSLDDFT 

        70         80         90        100        110        120 
REKIGSGFFS EVFKVRHRAS GQVMALKMNT LSSNRANLLK EMQLMNRLSH PNILRFMGVC 

       130        140        150        160        170        180 
VHQGQLHALT EYINSGNLEQ LLDSNLYLPW TVRVKLAYDI AVGLSYLHFK GIFHRDLTSK 

       190        200        210        220        230        240 
NCLIKRDENG YSAVVADFGL AEKIPDASIG SEKLAVVGSP FWMAPEVLRD EPYNEKADVF 

       250        260        270        280        290        300 
SYGIILCEII ARIQADPDYL PRTENFGLDY DAFQHMVGDC PSDFLQLTFN CCNMDPKLRP 

       310        320        330        340        350        360 
SFEEIGKTLE EIMSRLQEEE LERDRKLQPT AKGLLEKVPG GKRLSSLDDK IPHKSPRPRR 

       370        380        390        400        410        420 
TIWLSRSQSD IFSRKPPRTV NVLDPYYQPR DGATHTPKVN PFSARQDLKG GKVKFFDLPS 

       430        440        450        460        470        480 
KSVISLVFDL DAPGPGTVSL ADCQEPLAPS SRRWRSLPGS PEFLHQACPF VGCEESLSDG 

       490        500        510        520        530        540 
PPPRLSSLKY RVREIPPFRT SALSATSAHE AMDCSNPQEE NGFVPRPKGT SPCSGAASEE 

       550        560        570 
MEVEEERPRR APVHFSISGI SLQTQGEQDG 

« Hide

References

« Hide 'large scale' references
[1]"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].
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB049402 mRNA. Translation: BAB62908.1.
BC128727 mRNA. Translation: AAI28728.1.
RefSeqNP_596887.1. NM_133396.2.
XP_006238690.1. XM_006238628.1.
UniGeneRn.144652.

3D structure databases

ProteinModelPortalQ924U5.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ924U5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000023416; ENSRNOP00000023416; ENSRNOG00000017282.
GeneID170908.
KEGGrno:170908.
UCSCRGD:619984. rat.

Organism-specific databases

CTD10420.
RGD619984. Tesk2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00530000063025.
HOGENOMHOG000231415.
HOVERGENHBG058204.
InParanoidQ924U5.
KOK08842.
OMANVLDPYY.
OrthoDBEOG7V7664.
PhylomeDBQ924U5.
TreeFamTF318014.

Enzyme and pathway databases

BRENDA2.7.10.2. 5301.

Gene expression databases

GenevestigatorQ924U5.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio621355.
PROQ924U5.

Entry information

Entry nameTESK2_RAT
AccessionPrimary (citable) accession number: Q924U5
Secondary accession number(s): A1A5M5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families