TAOK3_MOUSE
ID TAOK3_MOUSE Reviewed; 898 AA.
AC Q8BYC6; Q3V3B3;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Serine/threonine-protein kinase TAO3;
DE EC=2.7.11.1;
DE AltName: Full=Thousand and one amino acid protein 3;
GN Name=Taok3;
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] OF 1-561 AND 766-898.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 556-757.
RA Ida H., Boylan S., Weigel A., Smit-McBride Z., Chao A., Gao J., Buchoff P.,
RA Wistow G., Hjelmeland L.;
RT "Expressed sequence tag analysis of mouse RPE/choroid.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 766-898.
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-346; SER-349;
RP THR-357 AND SER-359, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-830, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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 -!- 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; AK040531; BAC30618.1; -; mRNA.
DR EMBL; AK042181; BAE20625.1; -; mRNA.
DR EMBL; CJ197745; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CK625948; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CO813561; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS39233.1; -.
DR RefSeq; NP_001074777.1; NM_001081308.2.
DR RefSeq; NP_001186614.1; NM_001199685.1.
DR RefSeq; NP_899129.2; NM_183306.2.
DR RefSeq; XP_006530448.1; XM_006530385.3.
DR RefSeq; XP_011246521.1; XM_011248219.2.
DR RefSeq; XP_011246522.1; XM_011248220.2.
DR AlphaFoldDB; Q8BYC6; -.
DR SMR; Q8BYC6; -.
DR BioGRID; 236916; 16.
DR STRING; 10090.ENSMUSP00000107609; -.
DR iPTMnet; Q8BYC6; -.
DR PhosphoSitePlus; Q8BYC6; -.
DR EPD; Q8BYC6; -.
DR jPOST; Q8BYC6; -.
DR MaxQB; Q8BYC6; -.
DR PaxDb; Q8BYC6; -.
DR PRIDE; Q8BYC6; -.
DR ProteomicsDB; 263124; -.
DR Antibodypedia; 2111; 390 antibodies from 37 providers.
DR Ensembl; ENSMUST00000092889; ENSMUSP00000090565; ENSMUSG00000061288.
DR Ensembl; ENSMUST00000111978; ENSMUSP00000107609; ENSMUSG00000061288.
DR Ensembl; ENSMUST00000179276; ENSMUSP00000136750; ENSMUSG00000061288.
DR GeneID; 330177; -.
DR KEGG; mmu:330177; -.
DR UCSC; uc008zfh.2; mouse.
DR CTD; 51347; -.
DR MGI; MGI:3041177; Taok3.
DR VEuPathDB; HostDB:ENSMUSG00000061288; -.
DR eggNOG; KOG0577; Eukaryota.
DR GeneTree; ENSGT00940000155735; -.
DR InParanoid; Q8BYC6; -.
DR OMA; KEKIKEX; -.
DR OrthoDB; 617606at2759; -.
DR PhylomeDB; Q8BYC6; -.
DR TreeFam; TF351444; -.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 330177; 0 hits in 111 CRISPR screens.
DR ChiTaRS; Taok3; mouse.
DR PRO; PR:Q8BYC6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BYC6; protein.
DR Bgee; ENSMUSG00000061288; Expressed in rostral migratory stream and 258 other tissues.
DR ExpressionAtlas; Q8BYC6; baseline and differential.
DR Genevisible; Q8BYC6; MM.
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:MGI.
DR GO; GO:0016740; F:transferase activity; ISO:MGI.
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:MGI.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISO:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISO:MGI.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
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_0000086738"
FT DOMAIN 24..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 316..375
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 754..871
FT /evidence="ECO:0000255"
FT COMPBIAS 337..375
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; by ATM"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53UA7"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 357
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2K8"
FT MOD_RES 830
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 898 AA; 105336 MW; 2A68F2D48906EC05 CRC64;
MRKGALKDPE IADLFFKDDP EELFIDLHEI GHGSFGAVYF ATNAHTNEVV AVKKMSYSGK
QTHEKWQDIL KEVKFLQQLK HPNTIEYKGC YLKEHTAWLV MEYCLGSASD LLEVHKKPLQ
EVEIAAITHG ALQGLAYLHF HSLIHRDIKA GNILLTEPGQ VKLADFGSAS MASPANSFVG
TPYWMAPEVI LAMDEGQYDG KVDIWSLGIT CIELAERKPP LFNMNAMSAL YHIAQNDSPT
LQSREWTDSF RRFVDYCLHK IPQERPAAVE LLRHDFIRRE RPPKVLIDLI QRTKDAVREL
DNLQYRKMKK ILFQETRNGP LNESQEEEED GEQGSNLNRE VDSLGSIHSI PSTSVSTGSR
SSSVNSMQEV MDESSSELVM MQEDEGTANS SASTVHKKDH VFVRDEAGHG DPRPEPRPTQ
SVQSRALHYR NRERFATIKS ASLVTRQIHE HEQENELREQ MSGYKRMRRQ HQKQLIALEN
KLKAEMDEHR LKLQKEVETH ANNSSIELEK LAKKQVATIE KEAKVAAADE KKFQQQILAQ
QKKDLTTFLE SQKKQYKICK EKIKEEMNED HSTPKKEKQE RISKHKENLQ HTQAEEEAHL
LTQQRLYYDR NCRFFKRKIM IKRHEVEQQN IREELNKKRT QKEMEHAMLI RHDESTRELE
YRQLHTLQKL RMDLIRLQHQ TELENQLEYN KRRERELHRK HVMELRQQPK NLKAMEMQIK
KQFQDTCKVQ TKQYKALKNH QLEVTPKNEH KAILKTLKDE QTRKLAILAE QYEQSINEMM
ASQALRLDEA QEAECQALRL QLQQEMELLN AYQSKIKMQT EAQHERELQK LEQRVSLRRA
HLEQKIEEEL AALQKERSER IKTLLERQER ETETFDMESL RMGFGNLVTL DFPKEDYR
