TAOK1_MOUSE
ID TAOK1_MOUSE Reviewed; 1001 AA.
AC Q5F2E8; Q69ZL2; Q8JZX2; Q91VG7;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Serine/threonine-protein kinase TAO1;
DE EC=2.7.11.1;
DE AltName: Full=Thousand and one amino acid protein 1;
GN Name=Taok1; Synonyms=Kiaa1361;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 437-1001.
RC STRAIN=FVB/N; TISSUE=Mammary gland, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 657-1001.
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-421, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, 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 [8]
RP FUNCTION.
RX PubMed=33565190; DOI=10.1002/humu.24176;
RA van Woerden G.M., Bos M., de Konink C., Distel B., Avagliano Trezza R.,
RA Shur N.E., Baranano K., Mahida S., Chassevent A., Schreiber A., Erwin A.L.,
RA Gripp K.W., Rehman F., Brulleman S., McCormack R., de Geus G., Kalsner L.,
RA Sorlin A., Bruel A.L., Koolen D.A., Gabriel M.K., Rossi M.,
RA Fitzpatrick D.R., Wilkie A.O.M., Calpena E., Johnson D., Brooks A.,
RA van Slegtenhorst M., Fleischer J., Groepper D., Lindstrom K., Innes A.M.,
RA Goodwin A., Humberson J., Noyes A., Langley K.G., Telegrafi A., Blevins A.,
RA Hoffman J., Guillen Sacoto M.J., Juusola J., Monaghan K.G., Punj S.,
RA Simon M., Pfundt R., Elgersma Y., Kleefstra T.;
RT "TAOK1 is associated with neurodevelopmental disorder and essential for
RT neuronal maturation and cortical development.";
RL Hum. Mutat. 42:445-459(2021).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in various processes
CC such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response
CC and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6
CC and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK
CC cascade by mediating phosphorylation and subsequent activation of the
CC upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled
CC receptor signaling to p38/MAPK14. In response to DNA damage, involved
CC in the G2/M transition DNA damage checkpoint by activating the
CC p38/MAPK14 stress-activated MAPK cascade, probably by mediating
CC phosphorylation of MAP2K3 and MAP2K6. Acts as a regulator of
CC cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading
CC to activate MARK2 kinase activity and subsequent phosphorylation and
CC detachment of MAPT/TAU from microtubules. Also acts as a regulator of
CC apoptosis: regulates apoptotic morphological changes, including cell
CC contraction, membrane blebbing and apoptotic bodies formation via
CC activation of the MAPK8/JNK cascade (By similarity). During fetal
CC development, it plays an essential role in the regulation of neuronal
CC differentiation and migration to the cortical plate (PubMed:33565190).
CC {ECO:0000250, ECO:0000269|PubMed:33565190}.
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 -!- ACTIVITY REGULATION: Serine/threonine-protein kinase activity is
CC inhibited by SPRED1. {ECO:0000250}.
CC -!- SUBUNIT: Self-associates. Interacts with MAP2K3. Interacts with SPRED1
CC (By similarity). Interacts with TESK1; the interaction inhibits TAOK1
CC kinase activity (By similarity). Interacts with MAP3K7 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:O88664}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Proteolytically processed by caspase-3 (CASP3).
CC -!- PTM: Autophosphorylated (By similarity). Phosphorylated by ATM in
CC response to DNA damage. Phosphorylated by LRRK2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16522.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD32434.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL591136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016522; AAH16522.1; ALT_INIT; mRNA.
DR EMBL; BC034906; AAH34906.1; -; mRNA.
DR EMBL; AK173156; BAD32434.1; ALT_INIT; mRNA.
DR CCDS; CCDS36235.1; -.
DR RefSeq; NP_659074.2; NM_144825.2.
DR RefSeq; XP_006533021.1; XM_006532958.3.
DR RefSeq; XP_006533022.1; XM_006532959.3.
DR RefSeq; XP_011247231.1; XM_011248929.2.
DR RefSeq; XP_011247232.1; XM_011248930.2.
DR RefSeq; XP_011247233.1; XM_011248931.2.
DR AlphaFoldDB; Q5F2E8; -.
DR SMR; Q5F2E8; -.
DR BioGRID; 229824; 7.
DR IntAct; Q5F2E8; 1.
DR STRING; 10090.ENSMUSP00000055470; -.
DR iPTMnet; Q5F2E8; -.
DR PhosphoSitePlus; Q5F2E8; -.
DR EPD; Q5F2E8; -.
DR jPOST; Q5F2E8; -.
DR MaxQB; Q5F2E8; -.
DR PaxDb; Q5F2E8; -.
DR PRIDE; Q5F2E8; -.
DR ProteomicsDB; 262931; -.
DR Antibodypedia; 2089; 390 antibodies from 32 providers.
DR DNASU; 216965; -.
DR Ensembl; ENSMUST00000017435; ENSMUSP00000017435; ENSMUSG00000017291.
DR Ensembl; ENSMUST00000058496; ENSMUSP00000055470; ENSMUSG00000017291.
DR GeneID; 216965; -.
DR KEGG; mmu:216965; -.
DR UCSC; uc007khc.1; mouse.
DR CTD; 57551; -.
DR MGI; MGI:1914490; Taok1.
DR VEuPathDB; HostDB:ENSMUSG00000017291; -.
DR eggNOG; KOG0577; Eukaryota.
DR GeneTree; ENSGT00940000155796; -.
DR HOGENOM; CLU_000288_2_2_1; -.
DR InParanoid; Q5F2E8; -.
DR OMA; XAKVMAN; -.
DR OrthoDB; 617606at2759; -.
DR PhylomeDB; Q5F2E8; -.
DR TreeFam; TF351444; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 216965; 10 hits in 114 CRISPR screens.
DR ChiTaRS; Taok1; mouse.
DR PRO; PR:Q5F2E8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5F2E8; protein.
DR Bgee; ENSMUSG00000017291; Expressed in ventromedial nucleus of hypothalamus and 261 other tissues.
DR ExpressionAtlas; Q5F2E8; baseline and differential.
DR Genevisible; Q5F2E8; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
DR GO; GO:0016301; F:kinase activity; ISO:MGI.
DR GO; GO:0031489; F:myosin V binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0030295; F:protein kinase activator activity; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:MGI.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0021954; P:central nervous system neuron development; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0097194; P:execution phase of apoptosis; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:MGI.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISO:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; ISO:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
DR GO; GO:1901985; P:positive regulation of protein acetylation; 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:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:MGI.
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 Apoptosis; 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..1001
FT /note="Serine/threonine-protein kinase TAO1"
FT /id="PRO_0000086729"
FT DOMAIN 28..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 324..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 458..651
FT /evidence="ECO:0000255"
FT COILED 754..877
FT /evidence="ECO:0000255"
FT COMPBIAS 340..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 34..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L7X3"
FT MOD_RES 669
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7L7X3"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L7X3"
SQ SEQUENCE 1001 AA; 116050 MW; 59DF437EAB8127C2 CRC64;
MPSTNRAGSL KDPEIAELFF KEDPEKLFTD LREIGHGSFG AVYFARDVRT NEVVAIKKMS
YSGKQSTEKW QDIIKEVKFL QRIKHPNSIE YKGCYLREHT AWLVMEYCLG SASDLLEVHK
KPLQEVEIAA ITHGALQGLA YLHSHTMIHR DIKAGNILLT EPGQVKLADF GSASMASPAN
SFVGTPYWMA PEVILAMDEG QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN
ESPTLQSNEW SDYFRNFVDS CLQKIPQDRP TSEELLKHMF VLRERPETVL IDLIQRTKDA
VRELDNLQYR KMKKLLFQEA HNGPAVEAQE EEEEQDHGVG RTGTVNSVGS NQSIPSMSIS
ASSQSSSVNS LPDASDDKSE LDMMEGDHTV MSNSSVIHLK PEEENYQEEG DPRTRASDPQ
SPPQVSRHKS HYRNREHFAT IRTASLVTRQ MQEHEQDSEL REQMSGYKRM RRQHQKQLMT
LENKLKAEMD EHRLRLDKDL ETQRNNFAAE MEKLIKKHQA AMEKEAKVMA NEEKKFQQHI
QAQQKKELNS FLESQKREYK LRKEQLKEEL NENQSTPKKE KQEWLSKQKE NIQHFQAEEE
ANLLRRQRQY LELECRRFKR RMLLGRHNLE QDLVREELNK RQTQKDLEHA MLLRQHESMQ
ELEFRHLNTI QKMRCELIRL QHQTELTNQL EYNKRREREL RRKHVMEVRQ QPKSLKSKEL
QIKKQFQDTC KIQTRQYKAL RNHLLETTPK SEHKAVLKRL KEEQTRKLAI LAEQYDHSIN
EMLSTQALRL DEAQEAECQV LKMQLQQELE LLNAYQSKIK MQAEAQHDRE LRELEQRVSL
RRALLEQKIE EEMLALQNER TERIRSLLER QAREIEAFDS ESMRLGFSNM VLSNLSPEAF
SHSYPGASSW SHNPTGGPGP HWGHPMGGTP QAWGHPMQGG PQPWGHPSGP MQGVPRGSSM
GVRNSPQALR RTASGGRTEQ GMSRSTSVTS QISNGSHMSY T
