Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

GLH-binding kinase 1

Gene

kgb-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mitogen-activated protein kinase which is an essential component of the JNK pathway composed of mlk-1, mek-1 and kgb-1 (PubMed:15116070, PubMed:22554143, PubMed:23352664). Phosphorylates the transcription factor fos-1 which prevents fos-1 dimerization and promoter binding and results in activation of target genes including F53A9.2/kreg-1 and lys-3/kreg-2 (PubMed:23437011). Phosphorylates jun-1 and activates the AP-1 transcription factor which is a heterodimer of jun-1 and fos-1 (PubMed:23352664). Phosphorylates glh-1 in vitro which may play a role in controlling glh-1 protein levels in the germline by targeting it for degradation by the proteasome (PubMed:17699606). Required for oogenesis and probably also for spermatogenesis (PubMed:12435362). Involved in the response to environmental stress such as heavy metals, infection and protein folding stress in an age-dependent manner (PubMed:15116070, PubMed:22554143). In larvae, has a protective role which becomes detrimental in adults (PubMed:22554143). May control susceptibility to infection, heavy metal stress and premature lethality by regulating daf-16 cellular localization (PubMed:22554143). Involved in the transcriptional response to bacterial pore-forming toxins and to fasting (PubMed:15256590, PubMed:21408619, PubMed:23352664). Required for fasting-induced longevity (PubMed:23352664). Involved in axon regeneration after injury downstream of tyrosine receptor svh-2 (PubMed:21670305, PubMed:22388962).10 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by mek-1 mediated phosphorylation. No differences in basal activation between larvae and adults (PubMed:22554143). Inhibited by phosphatase vhp-1 (PubMed:15116070).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei67 – 671ATPPROSITE-ProRule annotation
Active sitei164 – 1641Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi44 – 529ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DEAD/H-box RNA helicase binding Source: WormBase
  • JUN kinase activity Source: WormBase
  • protein C-terminus binding Source: WormBase
  • protein kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: WormBase
  • RNA polymerase II repressing transcription factor binding Source: WormBase

GO - Biological processi

  • cellular response to arsenite ion Source: UniProtKB
  • cellular response to toxic substance Source: UniProtKB
  • determination of adult lifespan Source: UniProtKB
  • female meiotic division Source: WormBase
  • JUN phosphorylation Source: WormBase
  • male meiosis Source: WormBase
  • MAPK cascade involved in axon regeneration Source: UniProtKB
  • negative regulation of defense response to bacterium Source: UniProtKB
  • negative regulation of protein homooligomerization Source: WormBase
  • negative regulation of protein localization to nucleus Source: UniProtKB
  • negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding Source: WormBase
  • oocyte maturation Source: WormBase
  • peptidyl-threonine phosphorylation Source: WormBase
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of RNA splicing Source: UniProtKB
  • regulation of protein localization to nucleus Source: UniProtKB
  • reproduction Source: WormBase
  • response to cadmium ion Source: UniProtKB
  • response to copper ion Source: WormBase
  • response to endoplasmic reticulum stress Source: WormBase
  • response to nematicide Source: UniProtKB
  • response to starvation Source: UniProtKB
  • response to unfolded protein Source: UniProtKB
  • spermatogenesis Source: UniProtKB-KW
  • stress response to copper ion Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Differentiation, Oogenesis, Spermatogenesis, Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiO44408.

Names & Taxonomyi

Protein namesi
Recommended name:
GLH-binding kinase 11 Publication (EC:2.7.11.241 Publication)
Gene namesi
Name:kgb-1Imported
ORF Names:T07A9.3Imported
OrganismiCaenorhabditis elegansImported
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome IV

Organism-specific databases

WormBaseiT07A9.3; CE29466; WBGene00002187; kgb-1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Temperature-sensitive sterility in both hermaphrodites and males which, in hermaphrodites, is associated with disorganized gonads and with impaired production of endomitotic oocytes, likely due to a defect in oocyte maturation which often results in vulva protrusion (PubMed:12435362). Both hermaphrodites and males produce sperm but it is defective (PubMed:12435362). In addition, the formation of P granules is disrupted in later stage of oogenesis and the protein levels of glh-1, a component of the P granules, are increased (PubMed:12435362, PubMed:17699606). Old adults are bloated and move more slowly (PubMed:17699606). Hypersensitivity and impaired up-regulation of several genes in response to heavy metals (Cu2+ and Cd2+) and to bacterial pore-forming toxins exposure (PubMed:15256590, PubMed:15116070, PubMed:21408619, PubMed:23437011). RNAi knockdown at different developmental stages shows age-dependent defects: larvae are hypersensitive to cadmium and protein folding stress and have a reduced survival capacity but these effects are not observed in adults (PubMed:22554143). Impaired fasting-induced longevity (PubMed:23352664). RNAi knockdown in adults results in increased daf-16 nuclear localization in intestinal cells but not in response to fasting (PubMed:22554143, PubMed:23352664). Mutants have impaired axon regeneration (PubMed:21670305).9 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671K → N: Loss of activity. 1 Publication
Mutagenesisi198 – 1981S → A: Loss of activity. 1 Publication
Mutagenesisi200 – 2001Y → F: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390GLH-binding kinase 1PRO_0000433301Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981Phosphoserine2 Publications
Modified residuei200 – 2001Phosphotyrosine2 Publications

Post-translational modificationi

May be phosphorylated by mek-1 on Ser-198 and/or Tyr-200 (PubMed:15116070). Phosphorylation is induced upon Cu2+ and arsenite-mediated cell stimulation and by fasting (PubMed:15116070, PubMed:23352664).1 Publication1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO44408.
PaxDbiO44408.
PRIDEiO44408.

PTM databases

iPTMnetiO44408.

Expressioni

Tissue specificityi

Expressed in somatic and germline tissues.1 Publication

Inductioni

By B.thuringiensis pore-forming toxin Cry5B.1 Publication

Interactioni

Subunit structurei

Interacts with glh-1, glh-2 (via C-terminus), glh-3 (via C-terminus) and glh-4 (via C-terminus) (PubMed:12435362, PubMed:17699606). Interacts with csn-5; the interaction may prevent glh-1 degradation induced by kgb-1 (PubMed:17699606). Interacts with fos-1 (PubMed:23437011).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
glh-2Q966L92EBI-319489,EBI-1571876
glh-3O018362EBI-319489,EBI-1571750

GO - Molecular functioni

  • DEAD/H-box RNA helicase binding Source: WormBase
  • protein C-terminus binding Source: WormBase
  • RNA polymerase II repressing transcription factor binding Source: WormBase

Protein-protein interaction databases

DIPiDIP-24645N.
IntActiO44408. 6 interactions.
MINTiMINT-1043899.
STRINGi6239.T07A9.3.

Structurei

3D structure databases

ProteinModelPortaliO44408.
SMRiO44408. Positions 5-378.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 338301Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0665. Eukaryota.
ENOG410XSHI. LUCA.
GeneTreeiENSGT00550000074271.
HOGENOMiHOG000233024.
InParanoidiO44408.
OMAiTIRDPIA.
OrthoDBiEOG78WKWJ.
PhylomeDBiO44408.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01772. JNKMAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O44408-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVDLPVHNE YDASRFHQVT IRDPIAGADS TFTIPTRYVN LSFLNAGAQG
60 70 80 90 100
TVVMADDLVT TQRVAIKKMQ QPFVMTMSAK RAYREFILLT TIKHPNIIRL
110 120 130 140 150
LNAFTPDTSL STFREVYLVM ELMTHNLHEV IHRLRLDHKT LSFFVYQSLC
160 170 180 190 200
AIKHLHNSGV IHRDLKPSNI VVNDRCVLKV LDFGLARKKN VDTSMRMSDY
210 220 230 240 250
VVTRYYRAPE VILGLPYSEK VDIWSVGCIF AEMINHTVLF PGKDRIDQWT
260 270 280 290 300
KIYSVLGTPD DHFISQLGQS AAMYVRSLPR HQARAFSEIV PDTNFLPETE
310 320 330 340 350
NPRVHLTPHV ARDLLFNMLK INPEERYSVE DALNHPYVKL WFKDDEVNAP
360 370 380 390
ASENRYDQEI DFADKTLIEW KELIFNEVQR YQADHDIFTG
Length:390
Mass (Da):45,157
Last modified:December 1, 2001 - v2
Checksum:iB3F09B5229C31A53
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081716 Genomic DNA. Translation: CCD73974.1.
RefSeqiNP_499922.1. NM_067521.4.
UniGeneiCel.7426.

Genome annotation databases

EnsemblMetazoaiT07A9.3; T07A9.3; WBGene00002187.
GeneIDi176866.
KEGGicel:CELE_T07A9.3.
UCSCiT07A9.3. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO081716 Genomic DNA. Translation: CCD73974.1.
RefSeqiNP_499922.1. NM_067521.4.
UniGeneiCel.7426.

3D structure databases

ProteinModelPortaliO44408.
SMRiO44408. Positions 5-378.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-24645N.
IntActiO44408. 6 interactions.
MINTiMINT-1043899.
STRINGi6239.T07A9.3.

PTM databases

iPTMnetiO44408.

Proteomic databases

EPDiO44408.
PaxDbiO44408.
PRIDEiO44408.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiT07A9.3; T07A9.3; WBGene00002187.
GeneIDi176866.
KEGGicel:CELE_T07A9.3.
UCSCiT07A9.3. c. elegans.

Organism-specific databases

CTDi176866.
WormBaseiT07A9.3; CE29466; WBGene00002187; kgb-1.

Phylogenomic databases

eggNOGiKOG0665. Eukaryota.
ENOG410XSHI. LUCA.
GeneTreeiENSGT00550000074271.
HOGENOMiHOG000233024.
InParanoidiO44408.
OMAiTIRDPIA.
OrthoDBiEOG78WKWJ.
PhylomeDBiO44408.

Enzyme and pathway databases

SignaLinkiO44408.

Miscellaneous databases

PROiO44408.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008351. MAPK_JNK.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01772. JNKMAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2Imported.
  2. "The GLH proteins, Caenorhabditis elegans P granule components, associate with CSN-5 and KGB-1, proteins necessary for fertility, and with ZYX-1, a predicted cytoskeletal protein."
    Smith P., Leung-Chiu W.-M., Montgomery R., Orsborn A., Kuznicki K., Gressman-Coberly E., Mutapcic L., Bennett K.
    Dev. Biol. 251:333-347(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, INTERACTION WITH GLH-1; GLH-2; GLH-3 AND GLH-4.
  3. "The Caenorhabditis elegans MAPK phosphatase VHP-1 mediates a novel JNK-like signaling pathway in stress response."
    Mizuno T., Hisamoto N., Terada T., Kondo T., Adachi M., Nishida E., Kim D.H., Ausubel F.M., Matsumoto K.
    EMBO J. 23:2226-2234(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-67; SER-198 AND TYR-200.
  4. "Mitogen-activated protein kinase pathways defend against bacterial pore-forming toxins."
    Huffman D.L., Abrami L., Sasik R., Corbeil J., van der Goot F.G., Aroian R.V.
    Proc. Natl. Acad. Sci. U.S.A. 101:10995-11000(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY CRY5B.
  5. "GLH-1, the C. elegans P granule protein, is controlled by the JNK KGB-1 and by the COP9 subunit CSN-5."
    Orsborn A.M., Li W., McEwen T.J., Mizuno T., Kuzmin E., Matsumoto K., Bennett K.L.
    Development 134:3383-3392(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH CSN-5 AND GLH-1.
  6. "Role of the Caenorhabditis elegans Shc adaptor protein in the c-Jun N-terminal kinase signaling pathway."
    Mizuno T., Fujiki K., Sasakawa A., Hisamoto N., Matsumoto K.
    Mol. Cell. Biol. 28:7041-7049(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-198 AND TYR-200.
  7. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "Axon regeneration requires coordinate activation of p38 and JNK MAPK pathways."
    Nix P., Hisamoto N., Matsumoto K., Bastiani M.
    Proc. Natl. Acad. Sci. U.S.A. 108:10738-10743(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  9. "An age-dependent reversal in the protective capacities of JNK signaling shortens Caenorhabditis elegans lifespan."
    Twumasi-Boateng K., Wang T.W., Tsai L., Lee K.H., Salehpour A., Bhat S., Tan M.W., Shapira M.
    Aging Cell 11:659-667(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, DISRUPTION PHENOTYPE.
  10. "The growth factor SVH-1 regulates axon regeneration in C. elegans via the JNK MAPK cascade."
    Li C., Hisamoto N., Nix P., Kanao S., Mizuno T., Bastiani M., Matsumoto K.
    Nat. Neurosci. 15:551-557(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION.
  11. "A fasting-responsive signaling pathway that extends life span in C. elegans."
    Uno M., Honjoh S., Matsuda M., Hoshikawa H., Kishimoto S., Yamamoto T., Ebisuya M., Yamamoto T., Matsumoto K., Nishida E.
    Cell Rep. 3:79-91(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, DISRUPTION PHENOTYPE.
  12. "The Caenorhabditis elegans JNK signaling pathway activates expression of stress response genes by derepressing the Fos/HDAC repressor complex."
    Hattori A., Mizuno T., Akamatsu M., Hisamoto N., Matsumoto K.
    PLoS Genet. 9:E1003315-E1003315(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH FOS-1.

Entry informationi

Entry nameiKGB1_CAEEL
AccessioniPrimary (citable) accession number: O44408
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 24, 2015
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.