ID TESK2_RAT Reviewed; 570 AA. AC Q924U5; A1A5M5; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 151. 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 Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11418599; DOI=10.1074/jbc.m102988200; RA Toshima J., Toshima J.Y., Takeuchi K., Mori R., Mizuno K.; RT "Cofilin phosphorylation and actin reorganization activities of testicular RT protein kinase 2 and its predominant expression in testicular Sertoli RT cells."; RL J. Biol. Chem. 276:31449-31458(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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). 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 -!- TISSUE SPECIFICITY: Predominantly expressed in testis and prostate. CC Found predominantly in non-germinal Sertoli cells. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr CC protein kinase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB049402; BAB62908.1; -; mRNA. DR EMBL; BC128727; AAI28728.1; -; mRNA. DR RefSeq; NP_596887.1; NM_133396.2. DR RefSeq; XP_006238690.1; XM_006238628.3. DR AlphaFoldDB; Q924U5; -. DR SMR; Q924U5; -. DR STRING; 10116.ENSRNOP00000023416; -. DR iPTMnet; Q924U5; -. DR PhosphoSitePlus; Q924U5; -. DR PaxDb; 10116-ENSRNOP00000023416; -. DR Ensembl; ENSRNOT00000023416.5; ENSRNOP00000023416.3; ENSRNOG00000017282.7. DR Ensembl; ENSRNOT00055021271; ENSRNOP00055017207; ENSRNOG00055012476. DR Ensembl; ENSRNOT00060050567; ENSRNOP00060042085; ENSRNOG00060029122. DR Ensembl; ENSRNOT00065027849; ENSRNOP00065021969; ENSRNOG00065016699. DR GeneID; 170908; -. DR KEGG; rno:170908; -. DR UCSC; RGD:619984; rat. DR AGR; RGD:619984; -. DR CTD; 10420; -. DR RGD; 619984; Tesk2. DR eggNOG; ENOG502QTCP; Eukaryota. DR GeneTree; ENSGT00940000158765; -. DR HOGENOM; CLU_018577_1_0_1; -. DR InParanoid; Q924U5; -. DR OMA; SNQHLPW; -. DR OrthoDB; 5474815at2759; -. DR PhylomeDB; Q924U5; -. DR TreeFam; TF318014; -. DR BRENDA; 2.7.10.2; 5301. DR PRO; PR:Q924U5; -. DR Proteomes; UP000002494; Chromosome 5. DR Bgee; ENSRNOG00000017282; Expressed in jejunum and 19 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016604; C:nuclear body; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IDA: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; IDA: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; IMP:UniProtKB. DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB. DR GO; GO:0048041; P:focal adhesion assembly; IMP:UniProtKB. DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IEP: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; Q924U5; RN. PE 2: Evidence at transcript 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_0000086751" FT DOMAIN 58..313 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 513..570 FT /note="Disordered" 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:0000250|UniProtKB:Q96S53" FT MOD_RES 460 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8VCT9" SQ SEQUENCE 570 AA; 63559 MW; D20073AD93EE9F9C CRC64; MDRSKRNSIA GFPPRVERLE EFEGGGGGDG NTVQVGRVSS SSYRAIISAF SRLTSLDDFT REKIGSGFFS EVFKVRHRAS GQVMALKMNT LSSNRANLLK EMQLMNRLSH PNILRFMGVC VHQGQLHALT EYINSGNLEQ LLDSNLYLPW TVRVKLAYDI AVGLSYLHFK GIFHRDLTSK NCLIKRDENG YSAVVADFGL AEKIPDASIG SEKLAVVGSP FWMAPEVLRD EPYNEKADVF SYGIILCEII ARIQADPDYL PRTENFGLDY DAFQHMVGDC PSDFLQLTFN CCNMDPKLRP SFEEIGKTLE EIMSRLQEEE LERDRKLQPT AKGLLEKVPG GKRLSSLDDK IPHKSPRPRR TIWLSRSQSD IFSRKPPRTV NVLDPYYQPR DGATHTPKVN PFSARQDLKG GKVKFFDLPS KSVISLVFDL DAPGPGTVSL ADCQEPLAPS SRRWRSLPGS PEFLHQACPF VGCEESLSDG PPPRLSSLKY RVREIPPFRT SALSATSAHE AMDCSNPQEE NGFVPRPKGT SPCSGAASEE MEVEEERPRR APVHFSISGI SLQTQGEQDG //