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Q17446

- PMK1_CAEEL

UniProt

Q17446 - PMK1_CAEEL

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Protein

Mitogen-activated protein kinase pmk-1

Gene

pmk-1

Organism
Caenorhabditis elegans
Status
Reviewed - 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

Magnesium.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. p38MAPK cascade Source: WormBase
  7. peptidyl-serine phosphorylation Source: WormBase
  8. positive regulation of protein localization to nucleus Source: WormBase
  9. positive regulation of transcription from RNA polymerase II promoter Source: WormBase
  10. positive regulation of transcription from RNA polymerase II promoter involved in defense response to Gram-negative bacterium Source: WormBase
  11. programmed cell death Source: WormBase
  12. protein phosphorylation Source: WormBase
  13. response to osmotic stress Source: UniProtKB
  14. response to reactive oxygen species Source: WormBase
  15. 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

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.
OMAiHEYLAAY.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
FO080124 Genomic DNA. Translation: CCD61386.1 .
PIRi T29750.
RefSeqi NP_501365.1. NM_068964.3.
UniGenei Cel.12534.

3D structure databases

ProteinModelPortali Q17446.
SMRi Q17446. Positions 16-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 56238. 22 interactions.
DIPi DIP-26892N.
IntActi Q17446. 17 interactions.
MINTi MINT-1037719.
STRINGi 6239.B0218.3.

Proteomic databases

PaxDbi Q17446.
PRIDEi Q17446.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai B0218.3 ; B0218.3 ; WBGene00004055 .
GeneIDi 191743.
KEGGi cel:CELE_B0218.3.
UCSCi B0218.3. c. elegans.

Organism-specific databases

CTDi 191743.
WormBasei B0218.3 ; CE06686 ; WBGene00004055 ; pmk-1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074271.
HOGENOMi HOG000233024.
InParanoidi Q17446.
KOi K04441.
OMAi HEYLAAY.
OrthoDBi EOG7PCJGV.
PhylomeDBi Q17446.

Enzyme and pathway databases

SignaLinki Q17446.

Miscellaneous databases

NextBioi 950180.
PROi Q17446.

Family and domain databases

InterProi IPR011009. 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 ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR01773. P38MAPKINASE.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 129 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