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Serine/threonine-protein kinase TAO3 (EC 2.7.11.1) (Kinase from chicken) (Thousand and one amino acid protein 3)

 TAOK3_CHICK             Reviewed;         898 AA.
Q9I9E0; Q5F3C7;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
25-OCT-2005, sequence version 2.
05-JUL-2017, entry version 97.
RecName: Full=Serine/threonine-protein kinase TAO3;
EC=2.7.11.1;
AltName: Full=Kinase from chicken;
AltName: Full=Thousand and one amino acid protein 3;
Name=TAOK3; Synonyms=KFC; ORFNames=RCJMB04_21d18;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Fibroblast;
PubMed=10698516; DOI=10.1038/sj.onc.1203342;
Yustein J.T., Li D., Robinson D., Kung H.-J.;
"KFC, a Ste20-like kinase with mitogenic potential and capability to
activate the SAPK/JNK pathway.";
Oncogene 19:710-718(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=CB; TISSUE=Bursa of Fabricius;
PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J.,
Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M.,
Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.;
"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
function analysis.";
Genome Biol. 6:R6.1-R6.9(2005).
-!- FUNCTION: Serine/threonine-protein kinase that acts as a regulator
of the p38/MAPK14 stress-activated MAPK cascade and of the
MAPK8/JNK cascade. Acts as an activator of the p38/MAPK14 stress-
activated MAPK cascade. In response to DNA damage, involved in the
G2/M transition DNA damage checkpoint by activating the p38/MAPK14
stress-activated MAPK cascade, probably by mediating
phosphorylation of upstream MAP kinase kinases. Inhibits basal
activity of MAPK8/JNK cascade (By similarity). {ECO:0000250,
ECO:0000269|PubMed:10698516}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. STE20 subfamily. {ECO:0000305}.
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EMBL; AF263314; AAF73045.1; -; mRNA.
EMBL; AJ851723; CAH65357.1; -; mRNA.
RefSeq; NP_001012541.1; NM_001012523.1.
UniGene; Gga.4360; -.
ProteinModelPortal; Q9I9E0; -.
SMR; Q9I9E0; -.
STRING; 9031.ENSGALP00000011954; -.
PaxDb; Q9I9E0; -.
GeneID; 395499; -.
KEGG; gga:395499; -.
CTD; 51347; -.
eggNOG; KOG0577; Eukaryota.
eggNOG; ENOG410Y259; LUCA.
HOGENOM; HOG000236358; -.
HOVERGEN; HBG088996; -.
InParanoid; Q9I9E0; -.
KO; K04429; -.
PhylomeDB; Q9I9E0; -.
PRO; PR:Q9I9E0; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:AgBase.
GO; GO:0016740; F:transferase activity; ISS:AgBase.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
GO; GO:0000165; P:MAPK cascade; ISS:AgBase.
GO; GO:0007095; P:mitotic G2 DNA damage checkpoint; ISS:UniProtKB.
GO; GO:0046329; P:negative regulation of JNK cascade; ISS:AgBase.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
GO; GO:0046330; P:positive regulation of JNK cascade; ISS:AgBase.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:AgBase.
GO; GO:0006468; P:protein phosphorylation; ISS:AgBase.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
2: Evidence at transcript level;
ATP-binding; Coiled coil; Complete proteome; Cytoplasm; DNA damage;
DNA repair; Kinase; Nucleotide-binding; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 898 Serine/threonine-protein kinase TAO3.
/FTId=PRO_0000086741.
DOMAIN 24 277 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 30 38 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COILED 452 502 {ECO:0000255}.
COILED 548 649 {ECO:0000255}.
COILED 754 875 {ECO:0000255}.
COMPBIAS 326 329 Poly-Glu.
COMPBIAS 331 393 Ser-rich.
ACT_SITE 147 147 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 53 53 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CONFLICT 111 111 M -> L (in Ref. 1; AAF73045).
{ECO:0000305}.
CONFLICT 216 218 ERK -> QRP (in Ref. 1; AAF73045).
{ECO:0000305}.
CONFLICT 387 387 T -> A (in Ref. 1; AAF73045).
{ECO:0000305}.
CONFLICT 545 545 M -> L (in Ref. 1; AAF73045).
{ECO:0000305}.
CONFLICT 742 742 L -> V (in Ref. 1; AAF73045).
{ECO:0000305}.
CONFLICT 787 787 R -> L (in Ref. 1; AAF73045).
{ECO:0000305}.
CONFLICT 811 811 A -> G (in Ref. 1; AAF73045).
{ECO:0000305}.
SEQUENCE 898 AA; 105459 MW; 62DD657B83DACFFB CRC64;
MRKGVPKDPE IADLFYKDDP EEIFVGLHEI GHGSFGAVYF ATNSHTNEVV AVKKMSYSGK
QTNEKWQDII KEVKFLQQLK HPNTIEYKGC YLKEHTAWLV MEYCLGSASD MLEVHKKPLQ
EVEIAAITHG ALQGLAYLHS HCKIHRDIKA GNILLTEPGQ VKLADFGSAS IVSPANSFVG
TPYWMAPEVI LAMDEGQYDG KVDVWSLGIT CIELAERKPP LFNMNAMSAL YHIAQNDSPT
LQSNEWSDSF RGFVDYCLQK IPQERPSSAD LLRHDFVRRD RPPRVLIDLI QRTKDAVREL
DNLQYRKMKK ILFQETRNGP LTESQEEEED SEHGSNLSRK MDSLGSNHSI PSMSVSTGSQ
SSSVSSMQEV LDESSPELVM MHSDESTVNS TSSVVQKKDH VFIRDEVGHR DRRPEVRPTQ
SVQNQALHYR NRERFATIKS ASLVTRQIHE HEQENELREQ MSGYKRMRRQ HQKQLIALEN
KLKAEMDEHR LKLQKEVETH ANNSSIELEK LAKKQVAVME KEAKTAAADE KKFQQQILAQ
QKKDMATFLE SQKKQYKLCK EKIKEEMNED HSTPKKEKQE RISKHKENLQ HTQAEEEAHL
LSQQRLYYDK NCRFFKRKTM IKRHELEQQN IREELNKKRT QKEMEHAMLI RHDESTRELE
YRQLHTLQKL RMDLIRLQHQ TELENQLEYN KRRERELHRK HFMELRQQPK NLKAMEMQIK
KQFQDTCKVQ TKQYKALKNH QLEVTPKSEH KTILKSLKDE QTRKLAILAE QYEQSINEMM
ASQALRRDEA QEAECQALRL QLQQEMELLN AYQSKIKMQT EAQHERELQK LEQRVSLRRA
HLEQKIEEEL AALQKERSER IKFLLERQER EIETFDMESL RMGFGNLVTL DYPKEDYR


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