TAOK2_MOUSE
ID TAOK2_MOUSE Reviewed; 1240 AA.
AC Q6ZQ29; Q7TSS8;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Serine/threonine-protein kinase TAO2;
DE EC=2.7.11.1;
DE AltName: Full=Thousand and one amino acid protein 2;
GN Name=Taok2; Synonyms=Kiaa0881;
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] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Lung;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-663, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
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 [4]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-999 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in different
CC processes such as membrane blebbing and apoptotic bodies formation DNA
CC damage response and MAPK14/p38 MAPK stress-activated MAPK cascade.
CC Phosphorylates itself, MBP, activated MAPK8, MAP2K3, MAP2K6 and
CC tubulins. Activates the MAPK14/p38 MAPK signaling pathway through the
CC specific activation and phosphorylation of the upstream MAP2K3 and
CC MAP2K6 kinases. In response to DNA damage, involved in the G2/M
CC transition DNA damage checkpoint by activating the p38/MAPK14 stress-
CC activated MAPK cascade, probably by mediating phosphorylation of
CC upstream MAP2K3 and MAP2K6 kinases. May affect microtubule organization
CC and stability. May play a role in the osmotic stress-MAPK8 pathway.
CC Prevents MAP3K7-mediated activation of CHUK, and thus NF-kappa-B
CC activation. Isoform 2, but not isoform 1, is required for PCDH8
CC endocytosis. Following homophilic interactions between PCDH8
CC extracellular domains, isoform 2 phosphorylates and activates
CC MAPK14/p38 MAPK which in turn phosphorylates isoform 2. This process
CC leads to PCDH8 endocytosis and CDH2 cointernalization. Both isoforms
CC are involved in MAPK14/p38 MAPK activation (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=2.7.11.1;
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with MAP2K3 and MAP2K6 (By similarity). Self-
CC associates. Interacts with tubulins. Interacts with MAP3K7 and
CC interfers with MAP3K7-binding to CHUK and thus prevents NF-kappa-B
CC activation (By similarity). Isoform 2 interacts with PCDH8; this
CC complex may also include CDH2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Note=Found to be perinuclear and localized to vesicular
CC compartment. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell projection, dendrite
CC {ECO:0000250}. Note=In dendrites, colocalizes with PCDH8.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZQ29-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZQ29-2; Sequence=VSP_040543, VSP_040544;
CC -!- PTM: Autophosphorylated. Phosphorylated by ATM (By similarity).
CC {ECO:0000250}.
CC -!- PTM: [Isoform 2]: Phosphorylated on Ser-1037 by MAPK14. This
CC phosphorylation is required PCDH8 for endocytosis (By similarity).
CC {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=AAH52933.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N- and C-terminal parts.; Evidence={ECO:0000305};
CC Sequence=BAC98045.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129235; BAC98045.1; ALT_INIT; mRNA.
DR EMBL; BC052933; AAH52933.1; ALT_SEQ; mRNA.
DR EMBL; BC085152; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS52403.1; -. [Q6ZQ29-1]
DR CCDS; CCDS52404.1; -. [Q6ZQ29-2]
DR RefSeq; NP_001157246.1; NM_001163774.1. [Q6ZQ29-2]
DR RefSeq; NP_001157247.1; NM_001163775.1. [Q6ZQ29-1]
DR AlphaFoldDB; Q6ZQ29; -.
DR SMR; Q6ZQ29; -.
DR BioGRID; 238152; 8.
DR IntAct; Q6ZQ29; 8.
DR STRING; 10090.ENSMUSP00000112963; -.
DR iPTMnet; Q6ZQ29; -.
DR PhosphoSitePlus; Q6ZQ29; -.
DR EPD; Q6ZQ29; -.
DR jPOST; Q6ZQ29; -.
DR MaxQB; Q6ZQ29; -.
DR PaxDb; Q6ZQ29; -.
DR PeptideAtlas; Q6ZQ29; -.
DR PRIDE; Q6ZQ29; -.
DR ProteomicsDB; 263066; -. [Q6ZQ29-1]
DR ProteomicsDB; 263067; -. [Q6ZQ29-2]
DR Antibodypedia; 2082; 229 antibodies from 36 providers.
DR Ensembl; ENSMUST00000071268; ENSMUSP00000071246; ENSMUSG00000059981. [Q6ZQ29-2]
DR Ensembl; ENSMUST00000117394; ENSMUSP00000112963; ENSMUSG00000059981. [Q6ZQ29-1]
DR GeneID; 381921; -.
DR KEGG; mmu:381921; -.
DR UCSC; uc009jtg.2; mouse. [Q6ZQ29-2]
DR UCSC; uc009jth.2; mouse. [Q6ZQ29-1]
DR CTD; 9344; -.
DR MGI; MGI:1915919; Taok2.
DR VEuPathDB; HostDB:ENSMUSG00000059981; -.
DR eggNOG; KOG0577; Eukaryota.
DR GeneTree; ENSGT00940000159991; -.
DR HOGENOM; CLU_000288_2_2_1; -.
DR InParanoid; Q6ZQ29; -.
DR OMA; EMAMMGE; -.
DR OrthoDB; 617606at2759; -.
DR PhylomeDB; Q6ZQ29; -.
DR TreeFam; TF351444; -.
DR BioGRID-ORCS; 381921; 8 hits in 63 CRISPR screens.
DR ChiTaRS; Taok2; mouse.
DR PRO; PR:Q6ZQ29; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q6ZQ29; protein.
DR Bgee; ENSMUSG00000059981; Expressed in embryonic brain and 190 other tissues.
DR ExpressionAtlas; Q6ZQ29; baseline and differential.
DR Genevisible; Q6ZQ29; MM.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0044295; C:axonal growth cone; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0044294; C:dendritic growth cone; IDA:ARUK-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:ARUK-UCL.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; ISO:MGI.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISO:MGI.
DR GO; GO:0038191; F:neuropilin binding; IPI:ARUK-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; IMP:ARUK-UCL.
DR GO; GO:0150020; P:basal dendrite arborization; IDA:ARUK-UCL.
DR GO; GO:0150019; P:basal dendrite morphogenesis; IMP:ARUK-UCL.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; ISO:MGI.
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:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IMP:ARUK-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:ARUK-UCL.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0099179; P:regulation of synaptic membrane adhesion; ISO:MGI.
DR GO; GO:0051403; P:stress-activated MAPK cascade; ISS:UniProtKB.
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 Alternative splicing; ATP-binding; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Kinase; Magnesium; Membrane;
KW Methylation; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1240
FT /note="Serine/threonine-protein kinase TAO2"
FT /id="PRO_0000086734"
FT TRANSMEM 972..992
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 994..1014
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1019..1039
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1045..1065
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1175..1195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 28..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 320..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 493..528
FT /evidence="ECO:0000255"
FT COILED 581..608
FT /evidence="ECO:0000255"
FT COILED 688..720
FT /evidence="ECO:0000255"
FT COILED 805..934
FT /evidence="ECO:0000255"
FT COMPBIAS 345..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..403
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..944
FT /note="Pro 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 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL54"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL54"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL54"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL54"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UL54"
FT VAR_SEQ 752..1055
FT /note="VRAGQLPMGLPATGALGPLSTGTPSEEQPCSSGQEAILDQRMLGEEEEAVPE
FT RRILGKEGTTLEPEEQRILGEEMGTFSSSPQKHRSLANEEDWDISEEMKEIRVPSLASQ
FT ERNIIGQEEAAAWSLWEKEGGNLVDVEFKLGWVQGPVLTPVPEEEEEEEEEGGAPIGTH
FT RDPGDGCPSPDIPPEPPPSHLRQYPTSQLPGLLSHGLLAGLSFAVGSSSGLLPLLLLLL
FT LPLLAAQGGGGLQAALLALEVGLVGLGASYLFLCTALHLPPGLFLLLAQGTALLAVLSL
FT SWRRGLMGVPLGLGAA -> SKELQIKKQFQETCKIQTRQYKALRAHLLETTPKAQHKS
FT LLKRLKEEQTRKLAILAEQYDQSISEMLSSQALRLDETQEAEFQALRQQLQQELELLNA
FT YQSKIKIRTESQHERELRELEQRVALRRALLEQRVEEELLALQTGRSERIRSLLERQAR
FT EIEAFDAESMRLGFSSMALGGIPAEAAAQGYPAPPPAPAWPSRPVPRSGAHWSHGPPPP
FT GMPPPAWRQPALLAPPGPPNWLGPPTQSGTPRGGALLLLRNSPQPLRRAASGGSSGENV
FT GPPAAVPGPLSRSTSVASHILNGSSHFYS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_040543"
FT VAR_SEQ 1056..1240
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_040544"
FT MOD_RES Q6ZQ29-2:999
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q6ZQ29-2:1037
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1240 AA; 139297 MW; E6A989CD16B1AE54 CRC64;
MPAGGRAGSL KDPDVAELFF KDDPEKLFSD LREIGHGSFG AVYFARDVRN SEVVAIKKMS
YSGKQSNEKW QDIIKEVRFL QKLRHPNTIQ YRGCYLREHT AWLVMEYCLG SASDLLEVHK
KPLQEVEIAA VTHGALQGLA YLHSHNMIHR DVKAGNILLS EPGLVKLGDF GSASIMAPAN
SFVGTPYWMA PEVILAMDEG QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN
ESPALQSGHW SEYFRNFVDS CLQKIPQDRP TSEVLLKHRF VLRERPPTVI MDLIQRTKDA
VRELDNLQYR KMKKILFQEA PNGPGAEAPE EEELTPCSQE AEPYTHRAGT LTSLESSHSV
PSMSISASSQ SSSVNSLADA SDNEEEEEEE EEEEEEEEEE GPESREMAMM QEGEHTVTSH
SSIIHRLPGS DNLYDDPYQP EMTPGPLQPP AAPPTSTSSS ARRRAYCRNR DHFATIRTAS
LVSRQIQEHE QDSALREQLS GYKRMRRQHQ KQLLALESRL RGEREEHSGR LQRELEAQRA
GFGTEAEKLA RRHQAIGEKE ARAAQAEERK FQQHILGQQK KELAALLEAQ KRTYKLRKEQ
LKEELQENPS TPKREKAEWL LRQKEQLQQC QAEEEAGLLR RQRQYFELQC RQYKRKMLLA
RHSLDQDLLR EDLNKKQTQK DLECALLLRQ HEATRELELR QLQAVQRTRA ELTRLQHQTE
LGNQLEYNKR REQELRQKHA AQVRQQPKSL KVRAGQLPMG LPATGALGPL STGTPSEEQP
CSSGQEAILD QRMLGEEEEA VPERRILGKE GTTLEPEEQR ILGEEMGTFS SSPQKHRSLA
NEEDWDISEE MKEIRVPSLA SQERNIIGQE EAAAWSLWEK EGGNLVDVEF KLGWVQGPVL
TPVPEEEEEE EEEGGAPIGT HRDPGDGCPS PDIPPEPPPS HLRQYPTSQL PGLLSHGLLA
GLSFAVGSSS GLLPLLLLLL LPLLAAQGGG GLQAALLALE VGLVGLGASY LFLCTALHLP
PGLFLLLAQG TALLAVLSLS WRRGLMGVPL GLGAAWLLAW PSLALPLAAM AAGGKWVRQQ
GPQMRRGISR LWLRILLRLS PMVFRALQGC GAVGDRGLFA LYPKTNKNGF RSRLPVPWPR
QGNPRTTQHP LAQLTRVWAV CKGWNWRLAR ASHRLASCLP PWAVHILASW GLLKGERPSR
IPRLLPRSQR RLGLSASRQL PPGTVAGRRS QTRRTLPPWR
