TESK2_RAT
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 03-AUG-2022, entry version 143.
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}.
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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; Q924U5; -.
DR PRIDE; Q924U5; -.
DR Ensembl; ENSRNOT00000023416; ENSRNOP00000023416; ENSRNOG00000017282.
DR GeneID; 170908; -.
DR KEGG; rno:170908; -.
DR UCSC; RGD:619984; rat.
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; PPYCRQR; -.
DR OrthoDB; 219904at2759; -.
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 tissues.
DR Genevisible; Q924U5; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
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 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 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
