TESK2_MOUSE
ID TESK2_MOUSE Reviewed; 570 AA.
AC Q8VCT9;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Dual specificity testis-specific protein kinase 2;
DE EC=2.7.12.1;
DE AltName: Full=Testicular protein kinase 2;
GN Name=Tesk2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456 AND SER-460, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Dual specificity protein kinase activity catalyzing
CC autophosphorylation and phosphorylation of exogenous substrates on both
CC serine/threonine and tyrosine residues. Phosphorylates cofilin at 'Ser-
CC 3'. May play an important role in spermatogenesis (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.12.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by autophosphorylation on Ser-219.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; BC019149; AAH19149.1; -; mRNA.
DR EMBL; BC029766; AAH29766.1; -; mRNA.
DR CCDS; CCDS18516.1; -.
DR RefSeq; NP_666263.3; NM_146151.4.
DR AlphaFoldDB; Q8VCT9; -.
DR SMR; Q8VCT9; -.
DR STRING; 10090.ENSMUSP00000041009; -.
DR iPTMnet; Q8VCT9; -.
DR PhosphoSitePlus; Q8VCT9; -.
DR MaxQB; Q8VCT9; -.
DR PaxDb; Q8VCT9; -.
DR PRIDE; Q8VCT9; -.
DR ProteomicsDB; 263107; -.
DR Antibodypedia; 32628; 318 antibodies from 32 providers.
DR DNASU; 230661; -.
DR Ensembl; ENSMUST00000045542; ENSMUSP00000041009; ENSMUSG00000033985.
DR GeneID; 230661; -.
DR KEGG; mmu:230661; -.
DR UCSC; uc008uhj.2; mouse.
DR CTD; 10420; -.
DR MGI; MGI:2385204; Tesk2.
DR VEuPathDB; HostDB:ENSMUSG00000033985; -.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR GeneTree; ENSGT00940000158765; -.
DR HOGENOM; CLU_018577_1_0_1; -.
DR InParanoid; Q8VCT9; -.
DR OMA; PPYCRQR; -.
DR OrthoDB; 219904at2759; -.
DR PhylomeDB; Q8VCT9; -.
DR TreeFam; TF318014; -.
DR BioGRID-ORCS; 230661; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Tesk2; mouse.
DR PRO; PR:Q8VCT9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8VCT9; protein.
DR Bgee; ENSMUSG00000033985; Expressed in granulocyte and 215 other tissues.
DR ExpressionAtlas; Q8VCT9; baseline and differential.
DR Genevisible; Q8VCT9; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..570
FT /note="Dual specificity testis-specific protein kinase 2"
FT /id="PRO_0000086750"
FT DOMAIN 58..313
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 316..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 64..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 219
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96S53"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 570 AA; 63470 MW; 7B5A48E16655EAD1 CRC64;
MDRSKRNSIA GFPPRVERLE EFEGGGGGDG NTVQVGRVSS SSYRAIISAF SRLTSLDDFT
REKIGSGFFS EVFKVRHRAS GQVMALKMNT LSSNRANLLK EMQLMNRLSH PNILRFMGVC
VHQGQLHALT EYINSGNLEQ LLDSDLYLPW TVRVKLAYDI AVGLSYLHFK GIFHRDLTSK
NCLIKRDENG YSAVVADFGL AEKIPDASIG REKLAVVGSP FWMAPEVLRD EPYNEKADVF
SYGIILCEII ARIQADPDYL PRTENFGLDY DAFQNMVGDC PSDFLQLTFN CCNMDPKLRP
SFEEIGKTLK EIMSRLPEEE LERDRKLQPT AKGPLEKVPG GKRLSSLDDK IPHKSPRPRR
TIWLSRSQSD IFSHKPPRTV SVLDPYYQPR DGATHTPKVN PFSARQDLKG GKVKFFDLPS
KSVISLVFDL DAPGPGSTTL ADCQEPLAMS SRRWRSLPGS PEFLHQACPF MGCEESLSDG
PPPRLSSLKY GVREIPPFRT SALSAASGHE AMDCSNPQEE NGFGPRLKGT SLCTGAASEE
MEVEEERPRR ASVYFSISGI SLQTQAKQDG
