KGB1_CAEEL
ID KGB1_CAEEL Reviewed; 390 AA.
AC O44408;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=GLH-binding kinase 1 {ECO:0000303|PubMed:12435362};
DE EC=2.7.11.24 {ECO:0000269|PubMed:15116070};
GN Name=kgb-1 {ECO:0000312|WormBase:T07A9.3};
GN ORFNames=T07A9.3 {ECO:0000312|WormBase:T07A9.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP GLH-1; GLH-2; GLH-3 AND GLH-4.
RX PubMed=12435362; DOI=10.1006/dbio.2002.0832;
RA Smith P., Leung-Chiu W.-M., Montgomery R., Orsborn A., Kuznicki K.,
RA Gressman-Coberly E., Mutapcic L., Bennett K.;
RT "The GLH proteins, Caenorhabditis elegans P granule components, associate
RT with CSN-5 and KGB-1, proteins necessary for fertility, and with ZYX-1, a
RT predicted cytoskeletal protein.";
RL Dev. Biol. 251:333-347(2002).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF LYS-67; SER-198 AND TYR-200.
RX PubMed=15116070; DOI=10.1038/sj.emboj.7600226;
RA Mizuno T., Hisamoto N., Terada T., Kondo T., Adachi M., Nishida E.,
RA Kim D.H., Ausubel F.M., Matsumoto K.;
RT "The Caenorhabditis elegans MAPK phosphatase VHP-1 mediates a novel JNK-
RT like signaling pathway in stress response.";
RL EMBO J. 23:2226-2234(2004).
RN [4] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY CRY5B.
RX PubMed=15256590; DOI=10.1073/pnas.0404073101;
RA Huffman D.L., Abrami L., Sasik R., Corbeil J., van der Goot F.G.,
RA Aroian R.V.;
RT "Mitogen-activated protein kinase pathways defend against bacterial pore-
RT forming toxins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10995-11000(2004).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP CSN-5 AND GLH-1.
RX PubMed=17699606; DOI=10.1242/dev.005181;
RA Orsborn A.M., Li W., McEwen T.J., Mizuno T., Kuzmin E., Matsumoto K.,
RA Bennett K.L.;
RT "GLH-1, the C. elegans P granule protein, is controlled by the JNK KGB-1
RT and by the COP9 subunit CSN-5.";
RL Development 134:3383-3392(2007).
RN [6] {ECO:0000305}
RP PHOSPHORYLATION AT SER-198 AND TYR-200.
RX PubMed=18809575; DOI=10.1128/mcb.00938-08;
RA Mizuno T., Fujiki K., Sasakawa A., Hisamoto N., Matsumoto K.;
RT "Role of the Caenorhabditis elegans Shc adaptor protein in the c-Jun N-
RT terminal kinase signaling pathway.";
RL Mol. Cell. Biol. 28:7041-7049(2008).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21408619; DOI=10.1371/journal.ppat.1001314;
RA Kao C.Y., Los F.C., Huffman D.L., Wachi S., Kloft N., Husmann M.,
RA Karabrahimi V., Schwartz J.L., Bellier A., Ha C., Sagong Y., Fan H.,
RA Ghosh P., Hsieh M., Hsu C.S., Chen L., Aroian R.V.;
RT "Global functional analyses of cellular responses to pore-forming toxins.";
RL PLoS Pathog. 7:E1001314-E1001314(2011).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21670305; DOI=10.1073/pnas.1104830108;
RA Nix P., Hisamoto N., Matsumoto K., Bastiani M.;
RT "Axon regeneration requires coordinate activation of p38 and JNK MAPK
RT pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10738-10743(2011).
RN [9] {ECO:0000305}
RP FUNCTION, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22554143; DOI=10.1111/j.1474-9726.2012.00829.x;
RA Twumasi-Boateng K., Wang T.W., Tsai L., Lee K.H., Salehpour A., Bhat S.,
RA Tan M.W., Shapira M.;
RT "An age-dependent reversal in the protective capacities of JNK signaling
RT shortens Caenorhabditis elegans lifespan.";
RL Aging Cell 11:659-667(2012).
RN [10]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=22388962; DOI=10.1038/nn.3052;
RA Li C., Hisamoto N., Nix P., Kanao S., Mizuno T., Bastiani M., Matsumoto K.;
RT "The growth factor SVH-1 regulates axon regeneration in C. elegans via the
RT JNK MAPK cascade.";
RL Nat. Neurosci. 15:551-557(2012).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=23352664; DOI=10.1016/j.celrep.2012.12.018;
RA Uno M., Honjoh S., Matsuda M., Hoshikawa H., Kishimoto S., Yamamoto T.,
RA Ebisuya M., Yamamoto T., Matsumoto K., Nishida E.;
RT "A fasting-responsive signaling pathway that extends life span in C.
RT elegans.";
RL Cell Rep. 3:79-91(2013).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH FOS-1.
RX PubMed=23437011; DOI=10.1371/journal.pgen.1003315;
RA Hattori A., Mizuno T., Akamatsu M., Hisamoto N., Matsumoto K.;
RT "The Caenorhabditis elegans JNK signaling pathway activates expression of
RT stress response genes by derepressing the Fos/HDAC repressor complex.";
RL PLoS Genet. 9:E1003315-E1003315(2013).
CC -!- FUNCTION: Mitogen-activated protein kinase which is an essential
CC component of the JNK pathway composed of mlk-1, mek-1 and kgb-1
CC (PubMed:15116070, PubMed:22554143, PubMed:23352664). Phosphorylates the
CC transcription factor fos-1 which prevents fos-1 dimerization and
CC promoter binding and results in activation of target genes including
CC F53A9.2/kreg-1 and lys-3/kreg-2 (PubMed:23437011). Phosphorylates jun-1
CC and activates the AP-1 transcription factor which is a heterodimer of
CC jun-1 and fos-1 (PubMed:23352664). Phosphorylates glh-1 in vitro which
CC may play a role in controlling glh-1 protein levels in the germline by
CC targeting it for degradation by the proteasome (PubMed:17699606).
CC Required for oogenesis and probably also for spermatogenesis
CC (PubMed:12435362). Involved in the response to environmental stress
CC such as heavy metals, infection and protein folding stress in an age-
CC dependent manner (PubMed:15116070, PubMed:22554143). In larvae, has a
CC protective role which becomes detrimental in adults (PubMed:22554143).
CC May control susceptibility to infection, heavy metal stress and
CC premature lethality by regulating daf-16 cellular localization
CC (PubMed:22554143). Involved in the transcriptional response to
CC bacterial pore-forming toxins and to fasting (PubMed:15256590,
CC PubMed:21408619, PubMed:23352664). Required for fasting-induced
CC longevity (PubMed:23352664). Involved in axon regeneration after injury
CC downstream of tyrosine receptor svh-2 (PubMed:21670305,
CC PubMed:22388962). {ECO:0000269|PubMed:12435362,
CC ECO:0000269|PubMed:15116070, ECO:0000269|PubMed:15256590,
CC ECO:0000269|PubMed:17699606, ECO:0000269|PubMed:21408619,
CC ECO:0000269|PubMed:21670305, ECO:0000269|PubMed:22388962,
CC ECO:0000269|PubMed:22554143, ECO:0000269|PubMed:23352664,
CC ECO:0000269|PubMed:23437011}.
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=2.7.11.24;
CC Evidence={ECO:0000269|PubMed:15116070};
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=2.7.11.24; Evidence={ECO:0000269|PubMed:15116070};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8WQG9};
CC -!- ACTIVITY REGULATION: Activated by mek-1 mediated phosphorylation. No
CC differences in basal activation between larvae and adults
CC (PubMed:22554143). Inhibited by phosphatase vhp-1 (PubMed:15116070).
CC {ECO:0000269|PubMed:15116070, ECO:0000269|PubMed:22554143}.
CC -!- SUBUNIT: Interacts with glh-1, glh-2 (via C-terminus), glh-3 (via C-
CC terminus) and glh-4 (via C-terminus) (PubMed:12435362,
CC PubMed:17699606). Interacts with csn-5; the interaction may prevent
CC glh-1 degradation induced by kgb-1 (PubMed:17699606). Interacts with
CC fos-1 (PubMed:23437011). {ECO:0000269|PubMed:12435362,
CC ECO:0000269|PubMed:17699606, ECO:0000269|PubMed:23437011}.
CC -!- INTERACTION:
CC O44408; Q966L9: glh-2; NbExp=2; IntAct=EBI-319489, EBI-1571876;
CC O44408; O01836: glh-3; NbExp=2; IntAct=EBI-319489, EBI-1571750;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17699606}.
CC Note=Uniformly cytoplasmic in distal germline but resolves into
CC discrete particles in developing oocytes.
CC {ECO:0000269|PubMed:17699606}.
CC -!- TISSUE SPECIFICITY: Expressed in somatic and germline tissues.
CC {ECO:0000269|PubMed:12435362}.
CC -!- INDUCTION: By B.thuringiensis pore-forming toxin Cry5B.
CC {ECO:0000269|PubMed:15256590}.
CC -!- PTM: May be phosphorylated by mek-1 on Ser-198 and/or Tyr-200
CC (PubMed:15116070). Phosphorylation is induced upon Cu(2+) and arsenite-
CC mediated cell stimulation and by fasting (PubMed:15116070,
CC PubMed:23352664). {ECO:0000269|PubMed:23352664,
CC ECO:0000305|PubMed:15116070}.
CC -!- DISRUPTION PHENOTYPE: Temperature-sensitive sterility in both
CC hermaphrodites and males which, in hermaphrodites, is associated with
CC disorganized gonads and with impaired production of endomitotic
CC oocytes, likely due to a defect in oocyte maturation which often
CC results in vulva protrusion (PubMed:12435362). Both hermaphrodites and
CC males produce sperm but it is defective (PubMed:12435362). In addition,
CC the formation of P granules is disrupted in later stage of oogenesis
CC and the protein levels of glh-1, a component of the P granules, are
CC increased (PubMed:12435362, PubMed:17699606). Old adults are bloated
CC and move more slowly (PubMed:17699606). Hypersensitivity and impaired
CC up-regulation of several genes in response to heavy metals (Cu(2+) and
CC Cd(2+)) and to bacterial pore-forming toxins exposure (PubMed:15256590,
CC PubMed:15116070, PubMed:21408619, PubMed:23437011). RNAi knockdown at
CC different developmental stages shows age-dependent defects: larvae are
CC hypersensitive to cadmium and protein folding stress and have a reduced
CC survival capacity but these effects are not observed in adults
CC (PubMed:22554143). Impaired fasting-induced longevity
CC (PubMed:23352664). RNAi knockdown in adults results in increased daf-16
CC nuclear localization in intestinal cells but not in response to fasting
CC (PubMed:22554143, PubMed:23352664). Mutants have impaired axon
CC regeneration (PubMed:21670305). {ECO:0000269|PubMed:12435362,
CC ECO:0000269|PubMed:15116070, ECO:0000269|PubMed:15256590,
CC ECO:0000269|PubMed:17699606, ECO:0000269|PubMed:21408619,
CC ECO:0000269|PubMed:21670305, ECO:0000269|PubMed:22554143,
CC ECO:0000269|PubMed:23352664, ECO:0000269|PubMed:23437011}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
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DR EMBL; FO081716; CCD73974.1; -; Genomic_DNA.
DR RefSeq; NP_499922.1; NM_067521.4.
DR AlphaFoldDB; O44408; -.
DR SMR; O44408; -.
DR DIP; DIP-24645N; -.
DR IntAct; O44408; 6.
DR STRING; 6239.T07A9.3; -.
DR iPTMnet; O44408; -.
DR EPD; O44408; -.
DR PaxDb; O44408; -.
DR PeptideAtlas; O44408; -.
DR EnsemblMetazoa; T07A9.3.1; T07A9.3.1; WBGene00002187.
DR EnsemblMetazoa; T07A9.3.2; T07A9.3.2; WBGene00002187.
DR EnsemblMetazoa; T07A9.3.3; T07A9.3.3; WBGene00002187.
DR GeneID; 176866; -.
DR KEGG; cel:CELE_T07A9.3; -.
DR UCSC; T07A9.3; c. elegans.
DR CTD; 176866; -.
DR WormBase; T07A9.3; CE29466; WBGene00002187; kgb-1.
DR eggNOG; KOG0665; Eukaryota.
DR GeneTree; ENSGT00970000196719; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; O44408; -.
DR OMA; TAMRMSD; -.
DR OrthoDB; 741207at2759; -.
DR PhylomeDB; O44408; -.
DR BRENDA; 2.7.11.24; 1045.
DR Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-CEL-2871796; FCERI mediated MAPK activation.
DR Reactome; R-CEL-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-CEL-450341; Activation of the AP-1 family of transcription factors.
DR SignaLink; O44408; -.
DR PRO; PR:O44408; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00002187; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:WormBase.
DR GO; GO:0004705; F:JUN kinase activity; IDA:WormBase.
DR GO; GO:0004707; F:MAP kinase activity; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:WormBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:1903843; P:cellular response to arsenite ion; IMP:UniProtKB.
DR GO; GO:0097237; P:cellular response to toxic substance; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0007254; P:JNK cascade; IMP:UniProtKB.
DR GO; GO:0007258; P:JUN phosphorylation; ISS:WormBase.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:WormBase.
DR GO; GO:1900425; P:negative regulation of defense response to bacterium; IGI:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:WormBase.
DR GO; GO:1903026; P:negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0048599; P:oocyte development; IMP:WormBase.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IMP:UniProtKB.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IGI:UniProtKB.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0046686; P:response to cadmium ion; IMP:UniProtKB.
DR GO; GO:0046688; P:response to copper ion; IMP:WormBase.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:WormBase.
DR GO; GO:0093002; P:response to nematicide; IMP:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IMP:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IGI:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:1990169; P:stress response to copper ion; IMP:WormBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR008351; MAPK_JNK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01772; JNKMAPKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Differentiation; Kinase; Nucleotide-binding;
KW Oogenesis; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Spermatogenesis; Stress response;
KW Transferase.
FT CHAIN 1..390
FT /note="GLH-binding kinase 1"
FT /id="PRO_0000433301"
FT DOMAIN 38..338
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 44..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18809575,
FT ECO:0000269|PubMed:22388962"
FT MOD_RES 200
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18809575,
FT ECO:0000269|PubMed:22388962"
FT MUTAGEN 67
FT /note="K->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15116070"
FT MUTAGEN 198
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15116070"
FT MUTAGEN 200
FT /note="Y->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15116070"
SQ SEQUENCE 390 AA; 45157 MW; B3F09B5229C31A53 CRC64;
MEVDLPVHNE YDASRFHQVT IRDPIAGADS TFTIPTRYVN LSFLNAGAQG TVVMADDLVT
TQRVAIKKMQ QPFVMTMSAK RAYREFILLT TIKHPNIIRL LNAFTPDTSL STFREVYLVM
ELMTHNLHEV IHRLRLDHKT LSFFVYQSLC AIKHLHNSGV IHRDLKPSNI VVNDRCVLKV
LDFGLARKKN VDTSMRMSDY VVTRYYRAPE VILGLPYSEK VDIWSVGCIF AEMINHTVLF
PGKDRIDQWT KIYSVLGTPD DHFISQLGQS AAMYVRSLPR HQARAFSEIV PDTNFLPETE
NPRVHLTPHV ARDLLFNMLK INPEERYSVE DALNHPYVKL WFKDDEVNAP ASENRYDQEI
DFADKTLIEW KELIFNEVQR YQADHDIFTG
