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

Mitogen-activated protein kinase pmk-1

Gene

pmk-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating downstream targets. Functions downstream of the MAPKK sek-1 and the MAPKKK nsy-1 as the MAP kinase required for pathogen resistance.2 Publications

Catalytic activityi

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

Cofactori

Mg2+1 Publication

Enzyme regulationi

Activated by phosphorylation on threonine and tyrosine. Inhibited by pyridinyl-imidazole related compounds.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei64 – 641ATPPROSITE-ProRule annotation
Active sitei179 – 1791Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi41 – 499ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: UniProtKB
  3. protein kinase activity Source: WormBase
  4. protein serine/threonine kinase activity Source: WormBase
  5. transcription factor binding Source: WormBase

GO - Biological processi

  1. defense response to Gram-negative bacterium Source: WormBase
  2. defense response to Gram-positive bacterium Source: WormBase
  3. hyperosmotic response Source: WormBase
  4. innate immune response Source: WormBase
  5. intracellular signal transduction Source: UniProtKB
  6. MAPK cascade Source: WormBase
  7. p38MAPK cascade Source: WormBase
  8. peptidyl-serine phosphorylation Source: WormBase
  9. positive regulation of protein localization to nucleus Source: WormBase
  10. positive regulation of transcription from RNA polymerase II promoter Source: WormBase
  11. positive regulation of transcription from RNA polymerase II promoter involved in defense response to Gram-negative bacterium Source: WormBase
  12. programmed cell death Source: WormBase
  13. protein phosphorylation Source: WormBase
  14. response to osmotic stress Source: UniProtKB
  15. response to reactive oxygen species Source: WormBase
  16. response to superoxide Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_183100. KSRP destabilizes mRNA.
REACT_184347. Oxidative Stress Induced Senescence.
REACT_239816. CDO in myogenesis.
REACT_242972. ERK/MAPK targets.
REACT_246696. VEGFA-VEGFR2 Pathway.
REACT_249288. NOD1/2 Signaling Pathway.
REACT_250015. activated TAK1 mediates p38 MAPK activation.
REACT_250046. ADP signalling through P2Y purinoceptor 1.
REACT_255121. p38MAPK events.
REACT_271173. Platelet sensitization by LDL.
SignaLinkiQ17446.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase pmk-1 (EC:2.7.11.24)
Alternative name(s):
Stress-activated protein kinase pmk-1
p38 MAP kinase 1
Gene namesi
Name:pmk-1
ORF Names:B0218.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940: Chromosome IV

Organism-specific databases

WormBaseiB0218.3; CE06686; WBGene00004055; pmk-1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: WormBase
  2. nucleus Source: WormBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Mitogen-activated protein kinase pmk-1PRO_0000186303Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911PhosphothreonineBy similarity
Modified residuei193 – 1931PhosphotyrosineBy similarity

Post-translational modificationi

Dually phosphorylated on Thr-191 and Tyr-193, which activates the enzyme.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ17446.
PRIDEiQ17446.

Interactioni

Protein-protein interaction databases

BioGridi56238. 22 interactions.
DIPiDIP-26892N.
IntActiQ17446. 17 interactions.
MINTiMINT-1037719.
STRINGi6239.B0218.3.

Structurei

3D structure databases

ProteinModelPortaliQ17446.
SMRiQ17446. Positions 16-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 319285Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi191 – 1933TXY

Domaini

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074271.
HOGENOMiHOG000233024.
InParanoidiQ17446.
KOiK04441.
OMAiFQKNVAF.
OrthoDBiEOG7PCJGV.
PhylomeDBiQ17446.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01773. P38MAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q17446-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFPQTTMDHI LHPTPREGYY VVELNRSVWV VPNYYINLTP IGTGAYGTVC
60 70 80 90 100
AAECTRSGTR VAIKKFNRPF QSIIHARRTY RELRLLRCMC HENIIDLLDV
110 120 130 140 150
FTPNENVNDI EDVYFVSMLM GADLSNILKI QRLNDDHIQF LVYQILRGLK
160 170 180 190 200
YIHSADIIHR DLKPSNIAVN EDCELKILDF GLARQTDSEM TGYVATRWYR
210 220 230 240 250
APEIMLNWMH YTQTVDVWSV GCILAELITG KTLFPGSDHI DQLTRIMSVT
260 270 280 290 300
GTPDEEFLKK ISSEEARNYI RNLPKMTRRD FKRLFAQATP QAIDLLEKML
310 320 330 340 350
HLDPDRRPTA KEAMEHEYLA AYHDETDEPI AEEMDLNDDV RADTIDEWKK
360 370
IIWEEISDFQ KNVAFADEEE DEEKMES
Length:377
Mass (Da):43,919
Last modified:November 1, 1996 - v1
Checksum:iF20BC395B38EFD03
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080124 Genomic DNA. Translation: CCD61386.1.
PIRiT29750.
RefSeqiNP_501365.1. NM_068964.3.
UniGeneiCel.12534.

Genome annotation databases

EnsemblMetazoaiB0218.3; B0218.3; WBGene00004055.
GeneIDi191743.
KEGGicel:CELE_B0218.3.
UCSCiB0218.3. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080124 Genomic DNA. Translation: CCD61386.1.
PIRiT29750.
RefSeqiNP_501365.1. NM_068964.3.
UniGeneiCel.12534.

3D structure databases

ProteinModelPortaliQ17446.
SMRiQ17446. Positions 16-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi56238. 22 interactions.
DIPiDIP-26892N.
IntActiQ17446. 17 interactions.
MINTiMINT-1037719.
STRINGi6239.B0218.3.

Proteomic databases

PaxDbiQ17446.
PRIDEiQ17446.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiB0218.3; B0218.3; WBGene00004055.
GeneIDi191743.
KEGGicel:CELE_B0218.3.
UCSCiB0218.3. c. elegans.

Organism-specific databases

CTDi191743.
WormBaseiB0218.3; CE06686; WBGene00004055; pmk-1.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074271.
HOGENOMiHOG000233024.
InParanoidiQ17446.
KOiK04441.
OMAiFQKNVAF.
OrthoDBiEOG7PCJGV.
PhylomeDBiQ17446.

Enzyme and pathway databases

ReactomeiREACT_183100. KSRP destabilizes mRNA.
REACT_184347. Oxidative Stress Induced Senescence.
REACT_239816. CDO in myogenesis.
REACT_242972. ERK/MAPK targets.
REACT_246696. VEGFA-VEGFR2 Pathway.
REACT_249288. NOD1/2 Signaling Pathway.
REACT_250015. activated TAK1 mediates p38 MAPK activation.
REACT_250046. ADP signalling through P2Y purinoceptor 1.
REACT_255121. p38MAPK events.
REACT_271173. Platelet sensitization by LDL.
SignaLinkiQ17446.

Miscellaneous databases

NextBioi950180.
PROiQ17446.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01773. P38MAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of pmk-(1-3): three p38 homologs in Caenorhabditis elegans."
    Berman K., McKay J., Avery L., Cobb M.
    Mol. Cell Biol. Res. Commun. 4:337-344(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME REGULATION.
    Strain: Bristol N2.
  2. "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 N2.
  3. Cited for: FUNCTION.
    Strain: Bristol N2.

Entry informationi

Entry nameiPMK1_CAEEL
AccessioniPrimary (citable) accession number: Q17446
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: November 1, 1996
Last modified: January 7, 2015
This is version 131 of the entry and version 1 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

External Data

Dasty 3

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 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.