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Protein

Mitogen-activated protein kinase 14A

Gene

Mpk2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Kinase involved in a signal transduction pathway. May down-regulate insect immunity gene expression after prolonged infection.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by threonine and tyrosine phosphorylation by Mkk3 in response to environmental stress.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541ATPPROSITE-ProRule annotation
Active sitei154 – 1541Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 399ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • MAP kinase activity Source: FlyBase
  • protein serine/threonine kinase activity Source: FlyBase
  • SAP kinase activity Source: FlyBase

GO - Biological processi

  • cellular response to arsenic-containing substance Source: FlyBase
  • cellular response to cadmium ion Source: FlyBase
  • cellular response to reactive oxygen species Source: FlyBase
  • defense response to bacterium Source: FlyBase
  • defense response to fungus Source: FlyBase
  • determination of adult lifespan Source: FlyBase
  • heart morphogenesis Source: FlyBase
  • immune response Source: FlyBase
  • MAPK cascade Source: FlyBase
  • mucosal immune response Source: FlyBase
  • negative regulation of antimicrobial humoral response Source: FlyBase
  • paracrine signaling Source: FlyBase
  • positive regulation of cell size Source: FlyBase
  • protein phosphorylation Source: FlyBase
  • reactive oxygen species metabolic process Source: FlyBase
  • regulation of adult chitin-containing cuticle pigmentation Source: FlyBase
  • regulation of cellular response to oxidative stress Source: FlyBase
  • response to heat Source: FlyBase
  • response to hydrogen peroxide Source: FlyBase
  • response to osmotic stress Source: FlyBase
  • response to oxidative stress Source: FlyBase
  • response to starvation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.24. 1994.
ReactomeiREACT_285926. p38MAPK events.
REACT_288099. Oxidative Stress Induced Senescence.
REACT_293578. ADP signalling through P2Y purinoceptor 1.
REACT_294885. NOD1/2 Signaling Pathway.
REACT_301774. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_326561. KSRP destabilizes mRNA.
REACT_334576. activated TAK1 mediates p38 MAPK activation.
REACT_341998. CDO in myogenesis.
REACT_346571. VEGFA-VEGFR2 Pathway.
REACT_346877. Platelet sensitization by LDL.
SignaLinkiO62618.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 14A (EC:2.7.11.24)
Short name:
MAP kinase 14A
Short name:
MAPK 14A
Alternative name(s):
MAP kinase p38a
Short name:
D-p38a
p38 MAPK
Short name:
Dp38
Gene namesi
Name:Mpk2
Synonyms:p38a
ORF Names:CG5475
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0015765. Mpk2.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 366366Mitogen-activated protein kinase 14APRO_0000186300Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei184 – 1841PhosphothreonineBy similarity
Modified residuei186 – 1861Phosphotyrosine1 Publication

Post-translational modificationi

Dually phosphorylated on Thr-184 and Tyr-186, which activates the enzyme.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO62618.
PRIDEiO62618.

Expressioni

Developmental stagei

Expressed both maternally and zygotically. Levels are highest at the preblastoderm stage but low levels are present throughout development.1 Publication

Gene expression databases

BgeeiO62618.
GenevisibleiO62618. DM.

Interactioni

Protein-protein interaction databases

BioGridi67799. 4 interactions.
IntActiO62618. 2 interactions.
MINTiMINT-4080391.
STRINGi7227.FBpp0083966.

Structurei

3D structure databases

ProteinModelPortaliO62618.
SMRiO62618. Positions 9-356.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 312288Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi184 – 1863TXY

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.
InParanoidiO62618.
KOiK04441.
OMAiQALAHGY.
OrthoDBiEOG7PCJGV.
PhylomeDBiO62618.

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.

O62618-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVSITKKFY KLDINRTEWE IPDIYQDLQP VGSGAYGQVS KAVVRGTNMH
60 70 80 90 100
VAIKKLARPF QSAVHAKRTY RELRLLKHMD HENVIGLLDI FHPHPANGSL
110 120 130 140 150
ENFQQVYLVT HLMDADLNNI IRMQHLSDDH VQFLVYQILR GLKYIHSAGV
160 170 180 190 200
IHRDLKPSNI AVNEDCELRI LDFGLARPTE NEMTGYVATR WYRAPEIMLN
210 220 230 240 250
WMHYDQTVDI WSVGCIMAEL ITRRTLFPGT DHIHQLNLIM EMLGTPPAEF
260 270 280 290 300
LKKISSESAR SYIQSLPPMK GRSFKNVFKN ANPLAIDLLE KMLELDAEKR
310 320 330 340 350
ITAEEALSHP YLEKYAEPSV EQTSPPYDHS FEDMDLPVDK WKELIYKEVT
360
NFKPPPSYAQ VLKDVK
Length:366
Mass (Da):42,256
Last modified:August 1, 1998 - v1
Checksum:iB3592B869F97990E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271D → G in AAB97138 (PubMed:9584193).Curated
Sequence conflicti77 – 771K → R (PubMed:1378625).Curated
Sequence conflicti80 – 801D → A in AAB97138 (PubMed:9584193).Curated
Sequence conflicti108 – 1081L → LL (PubMed:1378625).Curated
Sequence conflicti124 – 1241Q → QQ (PubMed:1378625).Curated
Sequence conflicti149 – 1491Missing (PubMed:1378625).Curated
Sequence conflicti163 – 1631N → NN (PubMed:1378625).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U86867 mRNA. Translation: AAB97138.1.
AF035546 Genomic DNA. Translation: AAC39030.1.
AF035547 mRNA. Translation: AAC39031.1.
AE014297 Genomic DNA. Translation: AAF56244.1.
AE014297 Genomic DNA. Translation: AAN13984.1.
AY071670 mRNA. Translation: AAL49292.1.
RefSeqiNP_001163711.1. NM_001170240.2.
NP_477163.1. NM_057815.5.
NP_732959.1. NM_170126.5.
UniGeneiDm.2996.

Genome annotation databases

EnsemblMetazoaiFBtr0084580; FBpp0083965; FBgn0015765.
FBtr0084581; FBpp0083966; FBgn0015765.
FBtr0300572; FBpp0289799; FBgn0015765.
GeneIDi42866.
KEGGidme:Dmel_CG5475.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U86867 mRNA. Translation: AAB97138.1.
AF035546 Genomic DNA. Translation: AAC39030.1.
AF035547 mRNA. Translation: AAC39031.1.
AE014297 Genomic DNA. Translation: AAF56244.1.
AE014297 Genomic DNA. Translation: AAN13984.1.
AY071670 mRNA. Translation: AAL49292.1.
RefSeqiNP_001163711.1. NM_001170240.2.
NP_477163.1. NM_057815.5.
NP_732959.1. NM_170126.5.
UniGeneiDm.2996.

3D structure databases

ProteinModelPortaliO62618.
SMRiO62618. Positions 9-356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67799. 4 interactions.
IntActiO62618. 2 interactions.
MINTiMINT-4080391.
STRINGi7227.FBpp0083966.

Proteomic databases

PaxDbiO62618.
PRIDEiO62618.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0084580; FBpp0083965; FBgn0015765.
FBtr0084581; FBpp0083966; FBgn0015765.
FBtr0300572; FBpp0289799; FBgn0015765.
GeneIDi42866.
KEGGidme:Dmel_CG5475.

Organism-specific databases

CTDi42866.
FlyBaseiFBgn0015765. Mpk2.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00550000074271.
InParanoidiO62618.
KOiK04441.
OMAiQALAHGY.
OrthoDBiEOG7PCJGV.
PhylomeDBiO62618.

Enzyme and pathway databases

BRENDAi2.7.11.24. 1994.
ReactomeiREACT_285926. p38MAPK events.
REACT_288099. Oxidative Stress Induced Senescence.
REACT_293578. ADP signalling through P2Y purinoceptor 1.
REACT_294885. NOD1/2 Signaling Pathway.
REACT_301774. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_326561. KSRP destabilizes mRNA.
REACT_334576. activated TAK1 mediates p38 MAPK activation.
REACT_341998. CDO in myogenesis.
REACT_346571. VEGFA-VEGFR2 Pathway.
REACT_346877. Platelet sensitization by LDL.
SignaLinkiO62618.

Miscellaneous databases

GenomeRNAii42866.
NextBioi830992.
PROiO62618.

Gene expression databases

BgeeiO62618.
GenevisibleiO62618. DM.

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. "Molecular cloning and characterization of a Drosophila p38 mitogen-activated protein kinase."
    Han S.-J., Choi K.-Y., Brey P.T., Lee W.-J.
    J. Biol. Chem. 273:369-374(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT TYR-186, FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
    Tissue: Hemocyte.
  2. "A conserved p38 mitogen-activated protein kinase pathway regulates Drosophila immunity gene expression."
    Han Z.S., Enslen H., Hu X., Meng X., Wu I.-H., Barrett T., Davis R.J., Ip Y.T.
    Mol. Cell. Biol. 18:3527-3539(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DEVELOPMENTAL STAGE, ENZYME REGULATION.
    Tissue: Embryo.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  6. "Primary structure, expression, and signal-dependent tyrosine phosphorylation of a Drosophila homolog of extracellular signal-regulated kinase."
    Biggs W.H. III, Zipursky S.L.
    Proc. Natl. Acad. Sci. U.S.A. 89:6295-6299(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 38-188.
    Tissue: Imaginal disk.

Entry informationi

Entry nameiMK14A_DROME
AccessioniPrimary (citable) accession number: O62618
Secondary accession number(s): A4V3C0, O46216, Q9TXB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: August 1, 1998
Last modified: July 22, 2015
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.