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O62618 (MK14A_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase 14A

Short name=MAP kinase 14A
Short name=MAPK 14A
EC=2.7.11.24
Alternative name(s):
MAP kinase p38a
Short name=D-p38a
p38 MAPK
Short name=Dp38
Gene names
Name:Mpk2
Synonyms:p38a
ORF Names:CG5475
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length366 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Kinase involved in a signal transduction pathway. May down-regulate insect immunity gene expression after prolonged infection. Ref.1 Ref.2

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium By similarity.

Enzyme regulation

Activated by threonine and tyrosine phosphorylation by Mkk3 in response to environmental stress. Ref.1 Ref.2

Subcellular location

Nucleus Ref.1.

Developmental stage

Expressed both maternally and zygotically. Levels are highest at the preblastoderm stage but low levels are present throughout development. Ref.2

Domain

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

Post-translational modification

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

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentNucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMAPK cascade

Inferred from direct assay Ref.2. Source: FlyBase

cellular response to arsenic-containing substance

Inferred from direct assay PubMed 16451733. Source: FlyBase

cellular response to cadmium ion

Inferred from direct assay PubMed 16451733. Source: FlyBase

cellular response to reactive oxygen species

Inferred from direct assay PubMed 16451733. Source: FlyBase

defense response to bacterium

Inferred from mutant phenotype PubMed 19748466PubMed 21076039. Source: FlyBase

defense response to fungus

Inferred from mutant phenotype PubMed 21076039. Source: FlyBase

determination of adult lifespan

Inferred from mutant phenotype PubMed 22014527. Source: FlyBase

immune response

Inferred from direct assay Ref.2. Source: FlyBase

mucosal immune response

Inferred from mutant phenotype PubMed 19668222. Source: FlyBase

negative regulation of antimicrobial humoral response

Inferred from mutant phenotype Ref.2. Source: FlyBase

positive regulation of cell size

Inferred from genetic interaction PubMed 19917724. Source: FlyBase

protein phosphorylation

Non-traceable author statement PubMed 10908587. Source: FlyBase

regulation of adult chitin-containing cuticle pigmentation

Inferred from genetic interaction PubMed 21878507. Source: FlyBase

regulation of cellular response to oxidative stress

Inferred from mutant phenotype PubMed 22014527. Source: FlyBase

response to heat

Inferred from mutant phenotype PubMed 19917724PubMed 21737674PubMed 22848763. Source: FlyBase

response to hydrogen peroxide

Inferred from mutant phenotype PubMed 19917724. Source: FlyBase

response to osmotic stress

Inferred from direct assay Ref.1. Source: FlyBase

response to oxidative stress

Inferred from mutant phenotype PubMed 21737674. Source: FlyBase

response to starvation

Inferred from mutant phenotype PubMed 19917724PubMed 21737674. Source: FlyBase

   Cellular_componentnucleus

Inferred from direct assay Ref.1. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Inferred from direct assay Ref.2. Source: FlyBase

SAP kinase activity

Traceable author statement PubMed 10878576. Source: FlyBase

protein serine/threonine kinase activity

Non-traceable author statement PubMed 10908587. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 366366Mitogen-activated protein kinase 14A
PRO_0000186300

Regions

Domain25 – 312288Protein kinase
Nucleotide binding31 – 399ATP By similarity
Motif184 – 1863TXY

Sites

Active site1541Proton acceptor By similarity
Binding site541ATP By similarity

Amino acid modifications

Modified residue1841Phosphothreonine By similarity
Modified residue1861Phosphotyrosine Ref.1

Experimental info

Sequence conflict271D → G in AAB97138. Ref.2
Sequence conflict771K → R Ref.6
Sequence conflict801D → A in AAB97138. Ref.2
Sequence conflict1081L → LL Ref.6
Sequence conflict1241Q → QQ Ref.6
Sequence conflict1491Missing Ref.6
Sequence conflict1631N → NN Ref.6

Sequences

Sequence LengthMass (Da)Tools
O62618 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: B3592B869F97990E

FASTA36642,256
        10         20         30         40         50         60 
MSVSITKKFY KLDINRTEWE IPDIYQDLQP VGSGAYGQVS KAVVRGTNMH VAIKKLARPF 

        70         80         90        100        110        120 
QSAVHAKRTY RELRLLKHMD HENVIGLLDI FHPHPANGSL ENFQQVYLVT HLMDADLNNI 

       130        140        150        160        170        180 
IRMQHLSDDH VQFLVYQILR GLKYIHSAGV IHRDLKPSNI AVNEDCELRI LDFGLARPTE 

       190        200        210        220        230        240 
NEMTGYVATR WYRAPEIMLN WMHYDQTVDI WSVGCIMAEL ITRRTLFPGT DHIHQLNLIM 

       250        260        270        280        290        300 
EMLGTPPAEF LKKISSESAR SYIQSLPPMK GRSFKNVFKN ANPLAIDLLE KMLELDAEKR 

       310        320        330        340        350        360 
ITAEEALSHP YLEKYAEPSV EQTSPPYDHS FEDMDLPVDK WKELIYKEVT NFKPPPSYAQ 


VLKDVK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001163711.1. NM_001170240.2.
NP_477163.1. NM_057815.5.
NP_732959.1. NM_170126.5.
UniGeneDm.2996.

3D structure databases

ProteinModelPortalO62618.
SMRO62618. Positions 9-356.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid67799. 4 interactions.
IntActO62618. 2 interactions.
MINTMINT-4080391.
STRING7227.FBpp0083966.

Proteomic databases

PaxDbO62618.
PRIDEO62618.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0084580; FBpp0083965; FBgn0015765.
FBtr0084581; FBpp0083966; FBgn0015765.
FBtr0300572; FBpp0289799; FBgn0015765.
GeneID42866.
KEGGdme:Dmel_CG5475.

Organism-specific databases

CTD42866.
FlyBaseFBgn0015765. Mpk2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074271.
InParanoidO62618.
KOK04441.
OMALNLIMEM.
OrthoDBEOG7PCJGV.
PhylomeDBO62618.

Enzyme and pathway databases

BRENDA2.7.11.24. 1994.
SignaLinkO62618.

Gene expression databases

BgeeO62618.

Family and domain databases

InterProIPR011009. 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_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR01773. P38MAPKINASE.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi42866.
NextBio830992.

Entry information

Entry nameMK14A_DROME
AccessionPrimary (citable) accession number: O62618
Secondary accession number(s): A4V3C0, O46216, Q9TXB4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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