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O61443

- MK14B_DROME

UniProt

O61443 - MK14B_DROME

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Protein

Mitogen-activated protein kinase 14B

Gene

p38b

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

Functioni

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.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Enzyme regulationi

Activated by threonine and tyrosine phosphorylation by Mkk3.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531ATPPROSITE-ProRule annotation
Active sitei153 – 1531Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 389ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: FlyBase
  3. protein serine/threonine kinase activity Source: UniProtKB
  4. SAP kinase activity Source: FlyBase

GO - Biological processi

  1. cellular response to arsenic-containing substance Source: FlyBase
  2. cellular response to cadmium ion Source: FlyBase
  3. cellular response to reactive oxygen species Source: FlyBase
  4. defense response to bacterium Source: FlyBase
  5. defense response to fungus Source: FlyBase
  6. determination of adult lifespan Source: FlyBase
  7. heart morphogenesis Source: FlyBase
  8. imaginal disc-derived wing morphogenesis Source: UniProtKB
  9. immune response Source: FlyBase
  10. MAPK cascade Source: FlyBase
  11. paracrine signaling Source: FlyBase
  12. positive regulation of cell size Source: FlyBase
  13. positive regulation of multicellular organism growth Source: FlyBase
  14. positive regulation of protein phosphorylation Source: FlyBase
  15. protein phosphorylation Source: FlyBase
  16. reactive oxygen species metabolic process Source: FlyBase
  17. regulation of adult chitin-containing cuticle pigmentation Source: FlyBase
  18. regulation of BMP signaling pathway Source: UniProtKB
  19. regulation of cellular response to oxidative stress Source: FlyBase
  20. regulation of innate immune response Source: UniProtKB
  21. regulation of terminal button organization Source: FlyBase
  22. response to bacterium Source: FlyBase
  23. response to heat Source: FlyBase
  24. response to hydrogen peroxide Source: FlyBase
  25. response to salt stress Source: FlyBase
  26. 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_180302. KSRP destabilizes mRNA.
REACT_181712. Oxidative Stress Induced Senescence.
REACT_203135. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_221889. Platelet sensitization by LDL.
REACT_246045. CDO in myogenesis.
REACT_246078. p38MAPK events.
REACT_249521. NOD1/2 Signaling Pathway.
REACT_252605. VEGFA-VEGFR2 Pathway.
REACT_255277. ADP signalling through P2Y purinoceptor 1.
REACT_257192. activated TAK1 mediates p38 MAPK activation.
REACT_263734. ERK/MAPK targets.
REACT_34513. DSCAM interactions.
SignaLinkiO61443.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 14B (EC:2.7.11.24)
Short name:
MAP kinase 14B
Short name:
MAPK 14B
Alternative name(s):
MAP kinase p38b
Short name:
D-p38b
Gene namesi
Name:p38b
ORF Names:CG7393
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0024846. p38b.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 365365Mitogen-activated protein kinase 14BPRO_0000186301Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei183 – 1831Phosphothreonine1 Publication
Modified residuei185 – 1851Phosphotyrosine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO61443.
PRIDEiO61443.

Expressioni

Tissue specificityi

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

Developmental stagei

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

Gene expression databases

BgeeiO61443.

Interactioni

Protein-protein interaction databases

BioGridi60814. 12 interactions.
DIPiDIP-22779N.
IntActiO61443. 6 interactions.
MINTiMINT-760858.
STRINGi7227.FBpp0080111.

Structurei

3D structure databases

ProteinModelPortaliO61443.
SMRiO61443. Positions 8-353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 311288Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi183 – 1853TXY

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.
InParanoidiO61443.
KOiK04441.
OMAiDIFRGAN.
OrthoDBiEOG7PCJGV.
PhylomeDBiO61443.

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.

O61443-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRKMAKFYK LDINRTEWEI PETYQNLQPV GQGAYGQVCK AVVRGTSTKV
60 70 80 90 100
AIKKLARPFQ SAVHAKRTYR ELRLLKHMDH ENVIGLLDVF HPGQPADSLD
110 120 130 140 150
QFQQVYMVTH LMDADLNNII RTQKLSDDHV QFLVYQILRG LKYIHSAGVI
160 170 180 190 200
HRDLKPSNIA VNEDCELRIL DFGLARPAES EMTGYVATRW YRAPEIMLNW
210 220 230 240 250
MHYNQTADIW SVGCIMAELL TGRTLFPGTD HIHQLNLIME VLGTPADEFM
260 270 280 290 300
SRISSESARN YIRSLPVMPR RNFRDIFRGA NPLAIDLLEK MLELDADKRI
310 320 330 340 350
TAEQALAHPY MEKYHDPTDE QTAALYDQSF EENELPVEKW REMVFSEVTA
360
FKPTAAFAEL LPKEQ
Length:365
Mass (Da):42,098
Last modified:August 1, 1998 - v1
Checksum:i3B3F217E467BAD53
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035548 mRNA. Translation: AAC39032.1.
AB006364 mRNA. Translation: BAA35141.1.
AE014134 Genomic DNA. Translation: AAF53326.1.
AY058548 mRNA. Translation: AAL13777.1.
RefSeqiNP_477361.1. NM_058013.5.
UniGeneiDm.2953.

Genome annotation databases

EnsemblMetazoaiFBtr0080534; FBpp0080111; FBgn0024846.
GeneIDi34780.
KEGGidme:Dmel_CG7393.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035548 mRNA. Translation: AAC39032.1 .
AB006364 mRNA. Translation: BAA35141.1 .
AE014134 Genomic DNA. Translation: AAF53326.1 .
AY058548 mRNA. Translation: AAL13777.1 .
RefSeqi NP_477361.1. NM_058013.5.
UniGenei Dm.2953.

3D structure databases

ProteinModelPortali O61443.
SMRi O61443. Positions 8-353.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 60814. 12 interactions.
DIPi DIP-22779N.
IntActi O61443. 6 interactions.
MINTi MINT-760858.
STRINGi 7227.FBpp0080111.

Proteomic databases

PaxDbi O61443.
PRIDEi O61443.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0080534 ; FBpp0080111 ; FBgn0024846 .
GeneIDi 34780.
KEGGi dme:Dmel_CG7393.

Organism-specific databases

CTDi 34780.
FlyBasei FBgn0024846. p38b.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074271.
InParanoidi O61443.
KOi K04441.
OMAi DIFRGAN.
OrthoDBi EOG7PCJGV.
PhylomeDBi O61443.

Enzyme and pathway databases

BRENDAi 2.7.11.24. 1994.
Reactomei REACT_180302. KSRP destabilizes mRNA.
REACT_181712. Oxidative Stress Induced Senescence.
REACT_203135. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_221889. Platelet sensitization by LDL.
REACT_246045. CDO in myogenesis.
REACT_246078. p38MAPK events.
REACT_249521. NOD1/2 Signaling Pathway.
REACT_252605. VEGFA-VEGFR2 Pathway.
REACT_255277. ADP signalling through P2Y purinoceptor 1.
REACT_257192. activated TAK1 mediates p38 MAPK activation.
REACT_263734. ERK/MAPK targets.
REACT_34513. DSCAM interactions.
SignaLinki O61443.

Miscellaneous databases

ChiTaRSi p38b. fly.
GenomeRNAii 34780.
NextBioi 790183.

Gene expression databases

Bgeei O61443.

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. "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.
    , 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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. 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.

Entry informationi

Entry nameiMK14B_DROME
AccessioniPrimary (citable) accession number: O61443
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: August 1, 1998
Last modified: November 26, 2014
This is version 142 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