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   27-MAR-2024, entry version 172.
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; 10090-ENSMUSP00000041009; -.
DR   ProteomicsDB; 263107; -.
DR   Antibodypedia; 32628; 349 antibodies from 32 providers.
DR   DNASU; 230661; -.
DR   Ensembl; ENSMUST00000045542.13; ENSMUSP00000041009.7; ENSMUSG00000033985.18.
DR   GeneID; 230661; -.
DR   KEGG; mmu:230661; -.
DR   UCSC; uc008uhj.2; mouse.
DR   AGR; MGI:2385204; -.
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; SNQHLPW; -.
DR   OrthoDB; 5474815at2759; -.
DR   PhylomeDB; Q8VCT9; -.
DR   TreeFam; TF318014; -.
DR   BioGRID-ORCS; 230661; 2 hits in 80 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 218 other cell types or tissues.
DR   ExpressionAtlas; Q8VCT9; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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   CDD; cd14155; PKc_TESK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR46485:SF6; DUAL SPECIFICITY TESTIS-SPECIFIC PROTEIN KINASE 2; 1.
DR   PANTHER; PTHR46485; LIM DOMAIN KINASE 1; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   Genevisible; Q8VCT9; MM.
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
//