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Mitogen-activated protein kinase kinase kinase nsy-1 (EC 2.7.11.25) (Apoptosis signal-regulating kinase 1) (ASK-1) (Neuronal symmetry kinase 1)

 NSY1_CAEEL              Reviewed;        1498 AA.
Q21029;
16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 4.
23-MAY-2018, entry version 149.
RecName: Full=Mitogen-activated protein kinase kinase kinase nsy-1 {ECO:0000305};
EC=2.7.11.25 {ECO:0000269|PubMed:11336672, ECO:0000269|PubMed:11751572};
AltName: Full=Apoptosis signal-regulating kinase 1 {ECO:0000303|PubMed:11336672};
Short=ASK-1 {ECO:0000303|PubMed:11336672};
AltName: Full=Neuronal symmetry kinase 1 {ECO:0000312|WormBase:F59A6.1};
Name=nsy-1 {ECO:0000312|WormBase:F59A6.1};
ORFNames=F59A6.1 {ECO:0000312|WormBase:F59A6.1};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=12142542; DOI=10.1126/science.1073759;
Kim D.H., Feinbaum R., Alloing G., Emerson F.E., Garsin D.A.,
Inoue H., Tanaka-Hino M., Hisamoto N., Matsumoto K., Tan M.-W.,
Ausubel F.M.;
"A conserved p38 MAP kinase pathway in Caenorhabditis elegans innate
immunity.";
Science 297:623-626(2002).
[2] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UNC-43, TISSUE
SPECIFICITY, AND MUTAGENESIS OF LYS-693.
PubMed=11336672; DOI=10.1016/S0092-8674(01)00313-0;
Sagasti A., Hisamoto N., Hyodo J., Tanaka-Hino M., Matsumoto K.,
Bargmann C.I.;
"The CaMKII UNC-43 activates the MAPKKK NSY-1 to execute a lateral
signaling decision required for asymmetric olfactory neuron fates.";
Cell 105:221-232(2001).
[4] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH SEK-1, AND
MUTAGENESIS OF LYS-693.
PubMed=11751572; DOI=10.1093/embo-reports/kvf001;
Tanaka-Hino M., Sagasti A., Hisamoto N., Kawasaki M., Nakano S.,
Ninomiya-Tsuji J., Bargmann C.I., Matsumoto K.;
"SEK-1 MAPKK mediates Ca2+ signaling to determine neuronal asymmetric
development in Caenorhabditis elegans.";
EMBO Rep. 3:56-62(2002).
[5] {ECO:0000305}
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15625192; DOI=10.1101/gad.1276505;
Chuang C.-F., Bargmann C.I.;
"A Toll-interleukin 1 repeat protein at the synapse specifies
asymmetric odorant receptor expression via ASK1 MAPKKK signaling.";
Genes Dev. 19:270-281(2005).
[6] {ECO:0000305}
FUNCTION.
PubMed=15888317; DOI=10.1016/j.mad.2004.11.012;
Kondo M., Yanase S., Ishii T., Hartman P.S., Matsumoto K., Ishii N.;
"The p38 signal transduction pathway participates in the oxidative
stress-mediated translocation of DAF-16 to Caenorhabditis elegans
nuclei.";
Mech. Ageing Dev. 126:642-647(2005).
[7] {ECO:0000305}
FUNCTION.
PubMed=18394898; DOI=10.1016/j.cub.2008.02.079;
Pujol N., Cypowyj S., Ziegler K., Millet A., Astrain A., Goncharov A.,
Jin Y., Chisholm A.D., Ewbank J.J.;
"Distinct innate immune responses to infection and wounding in the C.
elegans epidermis.";
Curr. Biol. 18:481-489(2008).
[8] {ECO:0000305}
FUNCTION.
PubMed=19497412; DOI=10.1016/j.cbi.2009.03.012;
Wang S., Wu L., Wang Y., Luo X., Lu Y.;
"Copper-induced germline apoptosis in Caenorhabditis elegans: the
independent roles of DNA damage response signaling and the dependent
roles of MAPK cascades.";
Chem. Biol. Interact. 180:151-157(2009).
[9]
FUNCTION.
PubMed=20062796; DOI=10.1371/journal.ppat.1000717;
Butschi A., Titz A., Waelti M.A., Olieric V., Paschinger K.,
Noebauer K., Guo X., Seeberger P.H., Wilson I.B., Aebi M.,
Hengartner M.O., Kuenzler M.;
"Caenorhabditis elegans N-glycan core beta-galactoside confers
sensitivity towards nematotoxic fungal galectin CGL2.";
PLoS Pathog. 6:E1000717-E1000717(2010).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21212236; DOI=10.1534/genetics.110.124883;
Hayakawa T., Kato K., Hayakawa R., Hisamoto N., Matsumoto K.,
Takeda K., Ichijo H.;
"Regulation of anoxic death in Caenorhabditis elegans by mammalian
apoptosis signal-regulating kinase (ASK) family proteins.";
Genetics 187:785-792(2011).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22216003; DOI=10.1371/journal.ppat.1002453;
Hoeven R.V., McCallum K.C., Cruz M.R., Garsin D.A.;
"Ce-Duox1/BLI-3 generated reactive oxygen species trigger protective
SKN-1 activity via p38 MAPK signaling during infection in C.
elegans.";
PLoS Pathog. 7:E1002453-E1002453(2011).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22308034; DOI=10.1074/jbc.M111.314146;
Lee K., Shim J., Bae J., Kim Y.J., Lee J.;
"Stabilization of RNT-1 protein, runt-related transcription factor
(RUNX) protein homolog of Caenorhabditis elegans, by oxidative stress
through mitogen-activated protein kinase pathway.";
J. Biol. Chem. 287:10444-10452(2012).
[13]
FUNCTION, AND PHOSPHORYLATION.
PubMed=24448648; DOI=10.1126/scisignal.2004822;
Maruyama T., Araki T., Kawarazaki Y., Naguro I., Heynen S.,
Aza-Blanc P., Ronai Z., Matsuzawa A., Ichijo H.;
"Roquin-2 promotes ubiquitin-mediated degradation of ASK1 to regulate
stress responses.";
Sci. Signal. 7:RA8-RA8(2014).
-!- FUNCTION: Serine/threonine-protein kinase which, by
phosphorylating and activating sek-1, plays an important role in
the activation of the p38 pathway also composed of the downstream
effectors sek-1 and pmk-1 (PubMed:11751572, PubMed:12142542,
PubMed:21212236, PubMed:24448648). Downstream of CaMKII unc-43 and
adapter protein tir-1, plays a role in determining asymmetric cell
fates in olfactory AWC neurons during neuronal development.
Activation results in the repression of odorant receptor str-2
expression in one of the 2 AWC neurons (PubMed:11336672,
PubMed:11751572, PubMed:15625192). Involved in resistance to
pathogenic Gram-positive and Gram-negative bacterial and fungal
infection (PubMed:12142542, PubMed:18394898, PubMed:24448648).
Involved in resistance to the nematotoxic C.cinerea galectin Cgl2
(PubMed:20062796). Probably by activating the sek1/pmk-1/skn-1
pathway, involved in the up-regulation of gcs-1 and glutathione-S-
transferase gst-4 expression upon bacterial infection
(PubMed:22216003). Probably downstream of tir-1 and nipi-3,
required for the expression of antimicrobial peptide nlp-29 in the
epidermis in response to fungal infection or physical injury
(PubMed:18394898). Plays a role in resistance to several
environmental stresses including oxidative, protein misfolding
(ER) and osmotic stresses, and DNA-damaging reagents
(PubMed:21212236, PubMed:15888317). Plays a role in the
stabilization of transcription factor rnt-1 in the intestine
during oxidative stress (PubMed:22308034). Involved in germline
apoptosis induced by heavy metals, such as Cu(2+)
(PubMed:19497412). Plays a role downstream of tir-1 in regulating
susceptibility to anoxia (PubMed:21212236). Involved in egg laying
(PubMed:12142542). {ECO:0000269|PubMed:11336672,
ECO:0000269|PubMed:11751572, ECO:0000269|PubMed:12142542,
ECO:0000269|PubMed:15625192, ECO:0000269|PubMed:15888317,
ECO:0000269|PubMed:18394898, ECO:0000269|PubMed:19497412,
ECO:0000269|PubMed:20062796, ECO:0000269|PubMed:21212236,
ECO:0000269|PubMed:22216003, ECO:0000269|PubMed:22308034,
ECO:0000269|PubMed:24448648}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:11336672, ECO:0000269|PubMed:11751572}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11751572};
-!- SUBUNIT: Interacts with unc-43 (PubMed:11336672). Interacts with
sek-1 (PubMed:11751572). {ECO:0000269|PubMed:11336672,
ECO:0000269|PubMed:11751572}.
-!- SUBCELLULAR LOCATION: Cell projection, axon
{ECO:0000269|PubMed:15625192}. Perikaryon
{ECO:0000269|PubMed:15625192}. Note=Localizes to post-synaptic
regions and is enriched in punctate structures in AWC neuron axon
where co-localizes with tir-1. Localization is regulated by tir-1.
{ECO:0000269|PubMed:15625192}.
-!- TISSUE SPECIFICITY: Expressed in intestine, hypodermis, rectal
gland cell and neurons including sensory AWC neurons.
{ECO:0000269|PubMed:11336672}.
-!- PTM: May be phosphorylated upon pathogenic bacterial infection.
May be regulated by proteosomal degradation mediated by the E3-
ubiquitin ligase rle-1. {ECO:0000269|PubMed:24448648}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in an
increase in survival rate in anoxic conditions (PubMed:21212236).
Upon infection by P.aeruginosa and E.faecalis, RNAi-mediated
knockdown results in a moderate reduction in the up-regulation of
gst-4 and gcs-1 expression (PubMed:22216003). Causes a severe
reduction in rnt-1 accumulation in the intestine during oxidative
stress mediated by paraquat (PubMed:22308034).
{ECO:0000269|PubMed:21212236, ECO:0000269|PubMed:22216003,
ECO:0000269|PubMed:22308034}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase kinase subfamily.
{ECO:0000305}.
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EMBL; BX284602; CCD70472.1; -; Genomic_DNA.
RefSeq; NP_001293513.1; NM_001306584.1.
ProteinModelPortal; Q21029; -.
SMR; Q21029; -.
IntAct; Q21029; 1.
STRING; 6239.F59A6.1; -.
EPD; Q21029; -.
PaxDb; Q21029; -.
PeptideAtlas; Q21029; -.
EnsemblMetazoa; F59A6.1a; F59A6.1a; WBGene00003822.
GeneID; 24104671; -.
KEGG; cel:CELE_F59A6.1; -.
UCSC; F59A6.1; c. elegans.
CTD; 24104671; -.
WormBase; F59A6.1; CE44901; WBGene00003822; nsy-1.
eggNOG; KOG4279; Eukaryota.
eggNOG; ENOG410XQGS; LUCA.
GeneTree; ENSGT00800000124036; -.
HOGENOM; HOG000293286; -.
InParanoid; Q21029; -.
KO; K04426; -.
OMA; LYHDTDA; -.
OrthoDB; EOG091G00SJ; -.
PhylomeDB; Q21029; -.
Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
SignaLink; Q21029; -.
PRO; PR:Q21029; -.
Proteomes; UP000001940; Chromosome II.
Bgee; WBGene00003822; -.
ExpressionAtlas; Q21029; baseline and differential.
GO; GO:1904115; C:axon cytoplasm; IDA:WormBase.
GO; GO:0005623; C:cell; IDA:WormBase.
GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0014069; C:postsynaptic density; IDA:WormBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:WormBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:WormBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:WormBase.
GO; GO:0000187; P:activation of MAPK activity; IMP:WormBase.
GO; GO:0000186; P:activation of MAPKK activity; IMP:WormBase.
GO; GO:0045165; P:cell fate commitment; IMP:WormBase.
GO; GO:0006935; P:chemotaxis; IMP:WormBase.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:WormBase.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:WormBase.
GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
GO; GO:0035545; P:determination of left/right asymmetry in nervous system; IMP:WormBase.
GO; GO:0045087; P:innate immune response; IMP:WormBase.
GO; GO:0000165; P:MAPK cascade; IGI:WormBase.
GO; GO:0018991; P:oviposition; IMP:UniProtKB.
GO; GO:0038066; P:p38MAPK cascade; IMP:WormBase.
GO; GO:0002225; P:positive regulation of antimicrobial peptide production; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:1901046; P:positive regulation of oviposition; IMP:WormBase.
GO; GO:1901244; P:positive regulation of transcription from RNA polymerase II promoter involved in defense response to fungus; IMP:UniProtKB.
GO; GO:1902097; P:positive regulation of transcription from RNA polymerase II promoter involved in defense response to Gram-negative bacterium; IMP:WormBase.
GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
GO; GO:0093002; P:response to nematicide; TAS:UniProtKB.
GO; GO:0042594; P:response to starvation; IMP:UniProtKB.
InterPro; IPR025136; DUF4071.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF13281; DUF4071; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Cell projection; Coiled coil; Complete proteome; Kinase;
Magnesium; Metal-binding; Neurogenesis; Nucleotide-binding;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Stress response; Transferase.
CHAIN 1 1498 Mitogen-activated protein kinase kinase
kinase nsy-1. {ECO:0000305}.
/FTId=PRO_0000433800.
DOMAIN 664 925 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 670 678 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COILED 1276 1314 {ECO:0000255}.
ACT_SITE 790 790 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 693 693 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MUTAGEN 693 693 K->M: Loss of kinase activity.
{ECO:0000269|PubMed:11336672,
ECO:0000269|PubMed:11751572}.
SEQUENCE 1498 AA; 169654 MW; 751756B7483CDA2C CRC64;
MSQNNKRQVQ HNHEMSNDVC PLPLPPRGAP PPTAYHASRM AATSSSTNGS FEKSAIPGNA
RKLHVVIVID QKVQKNLRVR EMALKDVQKV ADTLNVNLTR IDFDKLDFGE TETLDLFYNA
DVALVDVTVT HQQPSLCYHI GVRESMGQSY NMILTYWSPD PEYHIMDALK KTHAHLPMIV
YIHHQDSNQL QSYDKNNNDD DSKPPFARTN VPAKTITFQH RMKQVLKSVQ VEASAHSREK
FMSDLRKARE ITDGDQKNDY LDKMRTRLDN PDVLHPDTVS LMMLSYRDNQ NYGGMIRLVD
DLKRIPDCLK VVDTPVIRYQ YAFALNRRNK DGDRDLALNT VLSLVEGTTE NEEKNGPLSP
DVVCLAGRIY KDKFIASNYE DRESLNSAIE WYRRAFEMSP LEYSGINLTT LLRASGEHFE
NNLEMQQIAV VLNSLLGRKG ALQNLMEYWD VATYFEVSVL AENYQKACEA ALMMVKLKPP
VWYLKSTMEN IKLINRCAAT ISPIEKEKQQ FLFWSEFFME ATEADTDISC PRYPVLILEL
NKEFTPSYLT LNNEEGTVIL SHVLENSQQK KIHQSELRGI HRWHFARNNI KAVTESKRDD
RQLFLYVHEN SDDFNLLFPT KAHCKKAYDD MKSMADVADG NYQGRVLSNP DNEKIRFEYE
LSNSNERVVL GKGTYGTVYA ARDMDTQRQI VVKEIEVKYD EEVQPLMEEI SLHSTLCHAN
IVQYLGCDLV GKDGSNDHFL IFMEHVPGGS LSSLLRSKWG PMNENAMNYY GKQILEGLKY
LHELKIVHRD IKGDNVLVNT YSGVCKISDF GTCKRLAGLN PVTETFTGTL QYMAPEVIDH
GQRGYGAPAD IWSFGCTMVE MATGRPPFVE MQNPQAAMFR VGMFKTHPPI PTEITEKCRN
FIKSCFLPEA CDRPSAKDLL QDPFIYHNHH SISRTRSGSI NKKPATKIEL NHDKEKKEKS
KNQREMLRST SHIGGMGVVE RSPPTPEPMS ATLTAGFSHV HSQTVSNALS TAREEKKLHL
KIDHARNRTF SSSSPVPDGQ SSAGTNMSHP GFQLSQPSSP IVDDTNHPHL IVSPISLNTM
GSPLSSAALL NRTISDESSN SSSRFFMLQK DSERRRSLGQ FMQDYKDLII DSWSTLLIKQ
SDTELVVTVY MLEMLLDGMR DFLLKKDNTK MQKMIDDIRG LLDYDTAKIG QINLALYHFS
DSIQPVLRRL DIKPHWMFAL SNLITSAVQC AISILSPDLS LLLHAQDNLP STSSIVAIRN
SSLSEGEALI ESRPPSREER VREDRKELRT LQEENEILIE RLLQVERELN AQLKSGITRA
NRFRDFAMYR NTYPPFRTPP VAHAPPTPPF SASCGAQPSG TFTNQPPSFA SIKPIAQKII
MPPGTENNYQ VTRVQEELVS WLRGLEIDER SIALIASEAY TKSDMMDFVT RDELLSIGVG
GGSSCRIMRA IGEVRERQRR QPVFLSPMRS RDDSLDDYHS SSADDMYTGA AAETSSGN


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10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.001 mg


 

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