TAOK3_RAT
ID TAOK3_RAT Reviewed; 898 AA.
AC Q53UA7;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Serine/threonine-protein kinase TAO3;
DE EC=2.7.11.1;
DE AltName: Full=Axotomy-related gene 357 protein;
DE AltName: Full=JNK/SAPK-inhibitory kinase;
DE AltName: Full=Jun kinase-inhibitory kinase;
DE AltName: Full=Thousand and one amino acid protein 3;
GN Name=Taok3; Synonyms=Arg357, Jik;
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], AND TISSUE SPECIFICITY.
RX PubMed=16092929; DOI=10.1111/j.1471-4159.2005.03389.x;
RA Wakabayashi T., Kosaka J., Oshika T.;
RT "JNK inhibitory kinase is up-regulated in retinal ganglion cells after
RT axotomy and enhances BimEL expression level in neuronal cells.";
RL J. Neurochem. 95:526-536(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-331; SER-343;
RP SER-349 AND SER-442, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Serine/threonine-protein kinase that acts as a regulator of
CC the p38/MAPK14 stress-activated MAPK cascade and of the MAPK8/JNK
CC cascade. Acts as an activator of the p38/MAPK14 stress-activated MAPK
CC cascade. In response to DNA damage, involved in the G2/M transition DNA
CC damage checkpoint by activating the p38/MAPK14 stress-activated MAPK
CC cascade, probably by mediating phosphorylation of upstream MAP2K3 and
CC MAP2K6 kinases. Inhibits basal activity of MAPK8/JNK cascade and
CC diminishes its activation in response epidermal growth factor (EGF) (By
CC similarity). {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=2.7.11.1;
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=2.7.11.1;
CC -!- SUBUNIT: Self-associates. Interacts with ERN1 and TRAF2. Interaction
CC with TRAF2 is facilitated under ER stress conditions, such as treatment
CC with tunicamycin, and may promote TRAF2 phosphorylation (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with a higher expression in
CC the retina. {ECO:0000269|PubMed:16092929}.
CC -!- PTM: Autophosphorylated. Phosphorylation at Ser-324 by ATM following
CC DNA damage is required for activation of the p38/MAPK14 stress-
CC activated MAPK cascade. Phosphorylated by LRRK2 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; AB195232; BAD97370.1; -; mRNA.
DR RefSeq; NP_001019425.1; NM_001024254.1.
DR AlphaFoldDB; Q53UA7; -.
DR SMR; Q53UA7; -.
DR IntAct; Q53UA7; 1.
DR STRING; 10116.ENSRNOP00000001503; -.
DR iPTMnet; Q53UA7; -.
DR PhosphoSitePlus; Q53UA7; -.
DR PaxDb; Q53UA7; -.
DR GeneID; 304530; -.
DR KEGG; rno:304530; -.
DR UCSC; RGD:1562861; rat.
DR CTD; 51347; -.
DR RGD; 1562861; Taok3.
DR eggNOG; KOG0577; Eukaryota.
DR InParanoid; Q53UA7; -.
DR OrthoDB; 617606at2759; -.
DR PhylomeDB; Q53UA7; -.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q53UA7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP 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; ISO:RGD.
DR GO; GO:0016740; F:transferase activity; ISO:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; ISO:RGD.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISO:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:RGD.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Coiled coil; Cytoplasm; DNA damage; DNA repair;
KW Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..898
FT /note="Serine/threonine-protein kinase TAO3"
FT /id="PRO_0000086740"
FT DOMAIN 24..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 316..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 452..502
FT /evidence="ECO:0000255"
FT COILED 548..649
FT /evidence="ECO:0000255"
FT COILED 753..871
FT /evidence="ECO:0000255"
FT COMPBIAS 337..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYC6"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 357
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYC6"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYC6"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 830
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BYC6"
SQ SEQUENCE 898 AA; 105474 MW; 64B140980D0F01AC CRC64;
MRKGVLKDPE IAELFFKEDP EELFIDLHEI GHGSFGAVYF ATNAHTNEVV AIKKMSYSGK
QTHEKWQDIL KEVRFLQQLK HPNTIEYKGC YLKEHTAWLV MEYCLGSASD LLEVHKKPLQ
EVEIAAITHG ALQGLAYLHF HSLIHRDIKA GNILLTEPGQ VKLADFGSAS MASPANSFVG
TPYWMAPEVI LAMDEGQYDG KVDIWSLGIT CIELAERKPP LFNMNAMSAL YHIAQNDSPT
LQSREWTDSF RRFVDYCLHK IPQERPAAAE LLRHDFIRRE RPPRVLIDLI QRTKDAVREL
DNLQYRKMKK ILFQETRNGP LNESQEEEED SEQGSNLNRE VDSLGSIHSI PSVSVSTGSR
SSSVNSMQEV MDEGSPELVM MQEDEGTVNS SSSMVHKKDH VFVRDEAGHG DPRPEPRPTQ
SVQSRALHYR NRERFATIKS ASLVTRQIHE HEQENELREQ MSGYKRMRRQ HQKQLIALEN
KLKAEMDEHR LKLQKEVETH ANNSSIELEK LAKKQVATIE KEAKVAAADE KKFQQQILAQ
QKKDLTTFLE SQKKQYKICK EKIKEEMNED HSTPKKEKQE RISKHKENLQ HTQAEEEAHL
LTQQRLYYDR NCRCFKRKIM TKRHEVEQQN IREELNKKRT QKEMEHAMLI RHDESTRELE
YRQLHTLQKL RMDLIRLQHQ TELENQLEYN KRRERELHRK HVMELRQQPK NLKAMEMQIK
KQFQDTCKVQ TKQYKALKNH QLEVTPKNEH KAILKTLKEE QTRKLAILAE QYEQSINEMM
ASQALRLDEA QEAECQALRL QLQQEMELLN AYQSKIKMQT EAQHERELQK LEQRVSLRRA
HLEQKIEEEL AALQKERSER IKTLLERQER ETETFDMESL RMGFGNLVTL DFPKEDYR
