TAOK2_XENLA
ID TAOK2_XENLA Reviewed; 1025 AA.
AC Q6GPK9;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serine/threonine-protein kinase involved in different
CC processes such as apoptotic morphological changes, MAPK8/JNK and
CC MAPK14/p38 MAPK signaling pathway. {ECO:0000250}.
CC -!- FUNCTION: Activates the JNK MAP kinase pathway. {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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; BC073108; AAH73108.1; -; mRNA.
DR RefSeq; NP_001085661.1; NM_001092192.1.
DR AlphaFoldDB; Q6GPK9; -.
DR SMR; Q6GPK9; -.
DR BioGRID; 102250; 1.
DR IntAct; Q6GPK9; 2.
DR DNASU; 444087; -.
DR GeneID; 444087; -.
DR KEGG; xla:444087; -.
DR CTD; 444087; -.
DR Xenbase; XB-GENE-5714849; taok2.L.
DR OrthoDB; 617606at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 444087; Expressed in brain and 19 other tissues.
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; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Kinase; Magnesium; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1025
FT /note="Serine/threonine-protein kinase TAO2"
FT /id="PRO_0000086736"
FT DOMAIN 28..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 349..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 457..650
FT /evidence="ECO:0000255"
FT COILED 755..876
FT /evidence="ECO:0000255"
FT COMPBIAS 349..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1025
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"
SQ SEQUENCE 1025 AA; 118120 MW; E15640DC0E9E480D CRC64;
MPSNARAGNL KDPEVAELFF KDDPEKLFAD LREIGHGSFG AVYFARDIRN NEVVAIKKMS
YSGKQSNEKW QDIIKEVKFL QKLRHPNTIE YKGCYLREHT AWLVMEYCLG SASDLLEVHK
KPLQEMEIAA ITHGALQGLA YLHNHNMIHR DVKAGNILLT EPGLVKLGDF GSASIMAPAN
SFVGTPYWMA PEVILAMDEG QYDGKVDVWS LGITSIELAE RKPPLFNMNA MSALYHIAQN
ESPVLQSNHW SEYFRNFVDS CLQKIPQDRP TSDMLLKHRF LQRERPQTVI MELIQRTKDA
VRELDNLQYR KMKKILFQDT QNGPNTETTE EEEEAEQFLH CTGTITSMES SQSVPSMSIS
ASSQSSSVNS LADASDDSGE MAMMQEGEHT VTSNSSVIHR LPAHDNIYDD PYQPEMEAQQ
SSSAARRRAY CRNRDHFATI RTASLVTRQI QEHEQDSALR EQMSGYKRMR RQHQKQLMAL
ENKLKSELDE HQQRLDKELE AHRSNFSAEN EKISKKHQAI FEKEAKGGMT EEKKFQQHIL
GQQKKELTNL LESQKRQYKI RKEQLKEELQ ENQSTPKREK QEWLLRQKES MQHYQAEEEA
NLLRRQRQYF ELQCRQYKRK MLLARHNLDQ DLLREELNKK QTQRDLECAM LLRQHECTQE
LEFRHLQLLQ HTRSELIRMQ HQTELGNQLE YNKRREQELR QKHAAEVRQQ PKSLKSKELQ
IKRQFQDTCK IQTRQYKALR NHLLETTPKS EHKSILKRLK DEQTRKLAIL AEQYDHSINE
MLSTQALRLD ETQEAEYQEL RIQLQKELEL LNAYQSKIKI HTDAQHEREL KELEQRVSIR
RALLEQRIEE EMLALQTERS ERIRSLLERQ AREIEAFDSE SMRLGFSNMA LTGIPAEAFN
QGYQAPPPGW PSRPVPRSGS HWSHGVQNTG APQLWRQPTL LAPPSASWGL HPPGSSSSLS
ALPSSSSSSS SSPSSSSGGR PGLLLLRNSP QPLRRGGSGG PSEAGLSRST SVTSQLSNGS
HLSYS
