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O61443 (MK14B_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. 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 14B

Short name=MAP kinase 14B
Short name=MAPK 14B
EC=2.7.11.24
Alternative name(s):
MAP kinase p38b
Short name=D-p38b
Gene names
Name:p38b
ORF Names:CG7393
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Kinase involved in dpp signal transduction pathway in the process of wing morphogenesis when the levels of dpp are enhanced or inhibited. 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. Ref.1

Subcellular location

Nucleus.

Tissue specificity

At mid-embryogenesis, highest expression is seen in developing anterior and posterior midguts. Almost ubiquitous expression throughout all development.

Developmental stage

Expressed both maternally and zygotically in the embryo, expression seen in all developmental stages.

Domain

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

Post-translational modification

Dually phosphorylated on Thr-183 and Tyr-185, which activates the enzyme By similarity.

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.1. 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

imaginal disc-derived wing morphogenesis

Inferred from direct assay Ref.2. Source: UniProtKB

immune response

Inferred from mutant phenotype Ref.1. Source: FlyBase

positive regulation of cell size

Inferred from mutant phenotype PubMed 19917724. Source: FlyBase

positive regulation of multicellular organism growth

Inferred from mutant phenotype PubMed 19917724. Source: FlyBase

positive regulation of protein phosphorylation

Inferred from genetic interaction PubMed 19917724. Source: FlyBase

protein phosphorylation

Non-traceable author statement PubMed 10908587. Source: FlyBase

regulation of BMP signaling pathway

Inferred from direct assay Ref.2. Source: UniProtKB

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

regulation of innate immune response

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of terminal button organization

Inferred from mutant phenotype PubMed 23904612. Source: FlyBase

response to bacterium

Inferred from direct assay PubMed 19748466. Source: FlyBase

response to heat

Inferred from mutant phenotype PubMed 19917724. Source: FlyBase

response to hydrogen peroxide

Inferred from mutant phenotype PubMed 19917724. Source: FlyBase

response to salt stress

Inferred from mutant phenotype PubMed 19917724PubMed 21829386. Source: FlyBase

response to starvation

Inferred from mutant phenotype PubMed 19917724. Source: FlyBase

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Inferred from sequence or structural similarity Ref.3. Source: FlyBase

SAP kinase activity

Non-traceable author statement PubMed 10878576. Source: FlyBase

protein serine/threonine kinase activity

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365Mitogen-activated protein kinase 14B
PRO_0000186301

Regions

Domain24 – 311288Protein kinase
Nucleotide binding30 – 389ATP By similarity
Motif183 – 1853TXY

Sites

Active site1531Proton acceptor By similarity
Binding site531ATP By similarity

Amino acid modifications

Modified residue1831Phosphothreonine Ref.7
Modified residue1851Phosphotyrosine Ref.7

Sequences

Sequence LengthMass (Da)Tools
O61443 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 3B3F217E467BAD53

FASTA36542,098
        10         20         30         40         50         60 
MSRKMAKFYK LDINRTEWEI PETYQNLQPV GQGAYGQVCK AVVRGTSTKV AIKKLARPFQ 

        70         80         90        100        110        120 
SAVHAKRTYR ELRLLKHMDH ENVIGLLDVF HPGQPADSLD QFQQVYMVTH LMDADLNNII 

       130        140        150        160        170        180 
RTQKLSDDHV QFLVYQILRG LKYIHSAGVI HRDLKPSNIA VNEDCELRIL DFGLARPAES 

       190        200        210        220        230        240 
EMTGYVATRW YRAPEIMLNW MHYNQTADIW SVGCIMAELL TGRTLFPGTD HIHQLNLIME 

       250        260        270        280        290        300 
VLGTPADEFM SRISSESARN YIRSLPVMPR RNFRDIFRGA NPLAIDLLEK MLELDADKRI 

       310        320        330        340        350        360 
TAEQALAHPY MEKYHDPTDE QTAALYDQSF EENELPVEKW REMVFSEVTA FKPTAAFAEL 


LPKEQ 

« Hide

References

« Hide 'large scale' references
[1]"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 [MRNA], FUNCTION, ENZYME REGULATION.
Tissue: Embryo.
[2]"p38 mitogen-activated protein kinase can be involved in transforming growth factor beta superfamily signal transduction in Drosophila wing morphogenesis."
Adachi-Yamada T., Nakamura M., Irie K., Tomoyasu Y., Sano Y., Mori E., Goto S., Ueno N., Nishida Y., Matsumoto K.
Mol. Cell. Biol. 19:2322-2329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Imaginal disk.
[3]"An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region."
Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R. expand/collapse author list , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.
Genetics 153:179-219(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"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.
[5]"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.
[6]"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: Embryo.
[7]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF035548 mRNA. Translation: AAC39032.1.
AB006364 mRNA. Translation: BAA35141.1.
AE014134 Genomic DNA. Translation: AAF53326.1.
AY058548 mRNA. Translation: AAL13777.1.
RefSeqNP_477361.1. NM_058013.4.
UniGeneDm.2953.

3D structure databases

ProteinModelPortalO61443.
SMRO61443. Positions 8-353.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid60814. 12 interactions.
DIPDIP-22779N.
IntActO61443. 6 interactions.
MINTMINT-760858.
STRING7227.FBpp0080111.

Proteomic databases

PaxDbO61443.
PRIDEO61443.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0080534; FBpp0080111; FBgn0024846.
GeneID34780.
KEGGdme:Dmel_CG7393.

Organism-specific databases

CTD34780.
FlyBaseFBgn0024846. p38b.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00550000074271.
InParanoidO61443.
KOK04441.
OMADIFRGAN.
OrthoDBEOG7PCJGV.
PhylomeDBO61443.

Enzyme and pathway databases

BRENDA2.7.11.24. 1994.
SignaLinkO61443.

Gene expression databases

BgeeO61443.

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

ChiTaRSp38b. drosophila.
GenomeRNAi34780.
NextBio790183.

Entry information

Entry nameMK14B_DROME
AccessionPrimary (citable) accession number: O61443
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 138 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