Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Putative mitogen-activated protein kinase 14C

Gene

p38c

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Kinase involved in a signal transduction pathway.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei49 – 491ATPPROSITE-ProRule annotation
Active sitei147 – 1471Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 349ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. regulation of adult chitin-containing cuticle pigmentation Source: FlyBase
  2. regulation of lipid storage Source: FlyBase
  3. regulation of response to oxidative stress Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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_305215. DSCAM interactions.
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.
SignaLinkiP83100.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative mitogen-activated protein kinase 14C (EC:2.7.11.24)
Short name:
MAP kinase 14C
Short name:
MAPK 14C
Alternative name(s):
MAP kinase p38c
Gene namesi
Name:p38c
ORF Names:CG33338
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0267339. p38c.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Putative mitogen-activated protein kinase 14CPRO_0000186302Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei177 – 1771PhosphothreonineBy similarity

Post-translational modificationi

The phosphorylation on Thr-177 activates the enzyme (By similarity). A conserved Tyr, which must also be phosphorylated to activate the enzyme in closely related sequences, is replaced by His-179 in this sequence.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP83100.
PRIDEiP83100.

Expressioni

Gene expression databases

BgeeiP83100.

Interactioni

Protein-protein interaction databases

IntActiP83100. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP83100.
SMRiP83100. Positions 2-353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 305286Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
InParanoidiP83100.
KOiK04441.
OMAiYDQNFEN.
OrthoDBiEOG75MVW7.
PhylomeDBiP83100.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
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.

P83100-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEFVRVAIN ESLWEFPDIY EFVRFLGGGS FGQVAKVRLR GTENYFAMKR
60 70 80 90 100
LMRPFEREED AKGTYREIRL LKHMNHRNVI SLLNVFHPPA HNMMEFQQVY
110 120 130 140 150
LVTHLMDADL HRYSRSKRMS DQEIRIILYQ ILRGLKYIHS AGVVHRDLKP
160 170 180 190 200
CNIAVNGNSE VRILDFGLSR MCADKMTDHV GTMWYLAPEI IFLRGQYTKA
210 220 230 240 250
IDVWSVGCIL AELITDRVLF RGENYVSQIR CLINIMGTPT REFITGISME
260 270 280 290 300
RSRNYLEGYP LRQRCDFHHL FMGYDVQAID LMEKMLEMVP EKRITAAEAM
310 320 330 340 350
LHPYLRDLIE PHHHAEDTAP VYDQNFENMV LPVKCWKELV SHEIRNFRPD

QLDLHF
Length:356
Mass (Da):41,969
Last modified:October 1, 2001 - v1
Checksum:iF90340860375BAF9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAS65203.1.
BT030917 mRNA. Translation: ABV82299.1.
BT030937 mRNA. Translation: ABV82319.1.
BT030954 mRNA. Translation: ABV82336.1.
BT032708 mRNA. Translation: ACD81722.1.
RefSeqiNP_996277.1. NM_206554.2.
UniGeneiDm.31337.

Genome annotation databases

EnsemblMetazoaiFBtr0084582; FBpp0083967; FBgn0267339.
GeneIDi2768679.
KEGGidme:Dmel_CG33338.
UCSCiCG33338-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAS65203.1.
BT030917 mRNA. Translation: ABV82299.1.
BT030937 mRNA. Translation: ABV82319.1.
BT030954 mRNA. Translation: ABV82336.1.
BT032708 mRNA. Translation: ACD81722.1.
RefSeqiNP_996277.1. NM_206554.2.
UniGeneiDm.31337.

3D structure databases

ProteinModelPortaliP83100.
SMRiP83100. Positions 2-353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP83100. 1 interaction.

Proteomic databases

PaxDbiP83100.
PRIDEiP83100.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0084582; FBpp0083967; FBgn0267339.
GeneIDi2768679.
KEGGidme:Dmel_CG33338.
UCSCiCG33338-RA. d. melanogaster.

Organism-specific databases

CTDi2768679.
FlyBaseiFBgn0267339. p38c.

Phylogenomic databases

eggNOGiCOG0515.
InParanoidiP83100.
KOiK04441.
OMAiYDQNFEN.
OrthoDBiEOG75MVW7.
PhylomeDBiP83100.

Enzyme and pathway databases

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_305215. DSCAM interactions.
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.
SignaLinkiP83100.

Miscellaneous databases

GenomeRNAii2768679.
NextBioi848055.
PROiP83100.

Gene expression databases

BgeeiP83100.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
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. "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.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Stapleton M., Carlson J.W., Booth B., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.

Entry informationi

Entry nameiMK14C_DROME
AccessioniPrimary (citable) accession number: P83100
Secondary accession number(s): A8E6X5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: October 1, 2001
Last modified: April 29, 2015
This is version 112 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.