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Protein

Dual specificity mitogen-activated protein kinase kinase dSOR1

Gene

Dsor1

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

Functioni

Required downstream of Raf in the sevenless (sev), torso (tor), and Drosophila EGF receptor homolog (DER) signal transduction pathways. Involved in both positive regulation (at the posterior terminus) and negative regulation (at the anterior domain) of tll, as in other terminal class gene products, maybe via the ERK-A kinase.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161ATPPROSITE-ProRule annotation
Active sitei209 – 2091Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi93 – 1019ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  • activation of MAPK activity Source: GOC
  • anterior/posterior axis specification, embryo Source: FlyBase
  • border follicle cell migration Source: FlyBase
  • cellular response to X-ray Source: FlyBase
  • hemocyte differentiation Source: FlyBase
  • MAPK cascade Source: FlyBase
  • mitotic DNA replication checkpoint Source: FlyBase
  • mitotic G2 DNA damage checkpoint Source: FlyBase
  • positive regulation of ERK1 and ERK2 cascade Source: FlyBase
  • positive regulation of multicellular organism growth Source: FlyBase
  • positive regulation of Ras protein signal transduction Source: FlyBase
  • protein phosphorylation Source: FlyBase
  • signal transduction Source: FlyBase
  • terminal region determination Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.4.1.222. 1994.
2.7.12.2. 1994.
ReactomeiR-DME-110056. MAPK3 (ERK1) activation.
R-DME-112411. MAPK1 (ERK2) activation.
R-DME-445144. Signal transduction by L1.
R-DME-5673000. RAF activation.
R-DME-5674135. MAP2K and MAPK activation.
R-DME-5674499. Negative feedback regulation of MAPK pathway.
SignaLinkiQ24324.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity mitogen-activated protein kinase kinase dSOR1 (EC:2.7.12.2)
Short name:
Downstream of RAF
Short name:
MAPKK
Gene namesi
Name:Dsor1
ORF Names:CG15793
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0010269. Dsor1.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 396396Dual specificity mitogen-activated protein kinase kinase dSOR1PRO_0000085928Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei237 – 2371Phosphoserine; by RAFBy similarity
Modified residuei241 – 2411Phosphoserine; by RAFBy similarity

Post-translational modificationi

Phosphorylation on Ser/Thr by MAP kinase kinase kinases regulates positively the kinase activity.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ24324.
PRIDEiQ24324.

Expressioni

Developmental stagei

Expressed both maternally and zygotically.1 Publication

Gene expression databases

BgeeiQ24324.
ExpressionAtlasiQ24324. differential.
GenevisibleiQ24324. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
rlP404172EBI-671282,EBI-867790

Protein-protein interaction databases

BioGridi58322. 28 interactions.
DIPiDIP-29770N.
IntActiQ24324. 2 interactions.
MINTiMINT-8075402.
STRINGi7227.FBpp0071248.

Structurei

3D structure databases

ProteinModelPortaliQ24324.
SMRiQ24324. Positions 40-384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 364278Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0581. Eukaryota.
ENOG410XQ5A. LUCA.
GeneTreeiENSGT00760000119199.
InParanoidiQ24324.
KOiK04368.
OMAiSKMTKNK.
OrthoDBiEOG7HF1KZ.
PhylomeDBiQ24324.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q24324-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKNKLNLVL PPVNTEATVA AATVAPTPPF KTPSGTDTHS LLGKPKTSID
60 70 80 90 100
ALTETLEGLD MGDTERKRIK MFLSQKEKIG ELSDEDLEKL GELGSGNGGV
110 120 130 140 150
VMKVRHTHTH LIMARKLIHL EVKPAIKKQI LRELKVLHEC NFPHIVGFYG
160 170 180 190 200
AFYSDGEISI CMEYMDGGSL DLILKRAGRI PESILGRITL AVLKGLSYLR
210 220 230 240 250
DNHAIIHRDV KPSNILVNSS GEIKICDFGV SGQLIDSMAN SFVGTRSYMS
260 270 280 290 300
PERLQGTHYS VQSDIWSLGL SLVEMAIGMY PIPPPNTATL ESIFADNAEE
310 320 330 340 350
SGQPTDEPRA MAIFELLDYI VNEPPPKLEH KIFSTEFKDF VDICLKKQPD
360 370 380 390
ERADLKTLLS HPWIRKAELE EVDISGWVCK TMDLPPSTPK RNTSPN
Length:396
Mass (Da):43,870
Last modified:August 16, 2005 - v2
Checksum:i9245CED1DA750C33
GO

Sequence cautioni

The sequence BAA02925.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti394 – 3941S → L in strain: Reids2.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13782 Genomic DNA. Translation: BAA02925.1. Sequence problems.
AY135075 Genomic DNA. Translation: AAN17587.1.
AY135076 Genomic DNA. Translation: AAN17588.1.
AY135077 Genomic DNA. Translation: AAN17589.1.
AY135078 Genomic DNA. Translation: AAN17590.1.
AY135079 Genomic DNA. Translation: AAN17591.1.
AY135080 Genomic DNA. Translation: AAN17592.1.
AY135081 Genomic DNA. Translation: AAN17593.1.
AY135082 Genomic DNA. Translation: AAN17594.1.
AY135083 Genomic DNA. Translation: AAN17595.1.
AY135084 Genomic DNA. Translation: AAN17596.1.
AY135085 Genomic DNA. Translation: AAN17597.1.
AY135086 Genomic DNA. Translation: AAN17598.1.
AY135087 Genomic DNA. Translation: AAN17599.1.
AY135088 Genomic DNA. Translation: AAN17600.1.
AY135089 Genomic DNA. Translation: AAN17601.1.
AY135090 Genomic DNA. Translation: AAN17602.1.
AY135091 Genomic DNA. Translation: AAN17603.1.
AY135092 Genomic DNA. Translation: AAN17604.1.
AY135093 Genomic DNA. Translation: AAN17605.1.
AE014298 Genomic DNA. Translation: AAF46475.1.
AY058692 mRNA. Translation: AAL13921.1.
PIRiA45176.
RefSeqiNP_001285044.1. NM_001298115.1.
NP_511098.1. NM_078543.4.
UniGeneiDm.2620.

Genome annotation databases

EnsemblMetazoaiFBtr0071313; FBpp0071248; FBgn0010269.
GeneIDi31872.
KEGGidme:Dmel_CG15793.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13782 Genomic DNA. Translation: BAA02925.1. Sequence problems.
AY135075 Genomic DNA. Translation: AAN17587.1.
AY135076 Genomic DNA. Translation: AAN17588.1.
AY135077 Genomic DNA. Translation: AAN17589.1.
AY135078 Genomic DNA. Translation: AAN17590.1.
AY135079 Genomic DNA. Translation: AAN17591.1.
AY135080 Genomic DNA. Translation: AAN17592.1.
AY135081 Genomic DNA. Translation: AAN17593.1.
AY135082 Genomic DNA. Translation: AAN17594.1.
AY135083 Genomic DNA. Translation: AAN17595.1.
AY135084 Genomic DNA. Translation: AAN17596.1.
AY135085 Genomic DNA. Translation: AAN17597.1.
AY135086 Genomic DNA. Translation: AAN17598.1.
AY135087 Genomic DNA. Translation: AAN17599.1.
AY135088 Genomic DNA. Translation: AAN17600.1.
AY135089 Genomic DNA. Translation: AAN17601.1.
AY135090 Genomic DNA. Translation: AAN17602.1.
AY135091 Genomic DNA. Translation: AAN17603.1.
AY135092 Genomic DNA. Translation: AAN17604.1.
AY135093 Genomic DNA. Translation: AAN17605.1.
AE014298 Genomic DNA. Translation: AAF46475.1.
AY058692 mRNA. Translation: AAL13921.1.
PIRiA45176.
RefSeqiNP_001285044.1. NM_001298115.1.
NP_511098.1. NM_078543.4.
UniGeneiDm.2620.

3D structure databases

ProteinModelPortaliQ24324.
SMRiQ24324. Positions 40-384.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58322. 28 interactions.
DIPiDIP-29770N.
IntActiQ24324. 2 interactions.
MINTiMINT-8075402.
STRINGi7227.FBpp0071248.

Proteomic databases

PaxDbiQ24324.
PRIDEiQ24324.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071313; FBpp0071248; FBgn0010269.
GeneIDi31872.
KEGGidme:Dmel_CG15793.

Organism-specific databases

CTDi31872.
FlyBaseiFBgn0010269. Dsor1.

Phylogenomic databases

eggNOGiKOG0581. Eukaryota.
ENOG410XQ5A. LUCA.
GeneTreeiENSGT00760000119199.
InParanoidiQ24324.
KOiK04368.
OMAiSKMTKNK.
OrthoDBiEOG7HF1KZ.
PhylomeDBiQ24324.

Enzyme and pathway databases

BRENDAi2.4.1.222. 1994.
2.7.12.2. 1994.
ReactomeiR-DME-110056. MAPK3 (ERK1) activation.
R-DME-112411. MAPK1 (ERK2) activation.
R-DME-445144. Signal transduction by L1.
R-DME-5673000. RAF activation.
R-DME-5674135. MAP2K and MAPK activation.
R-DME-5674499. Negative feedback regulation of MAPK pathway.
SignaLinkiQ24324.

Miscellaneous databases

GenomeRNAii31872.
PROiQ24324.

Gene expression databases

BgeeiQ24324.
ExpressionAtlasiQ24324. differential.
GenevisibleiQ24324. DM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A protein kinase similar to MAP kinase activator acts downstream of the raf kinase in Drosophila."
    Tsuda L., Inoue Y.H., Yoo M.-A., Mizuno M., Hata M., Lim Y.-M., Adachi-Yamada T., Ryo H., Masamune Y., Nishida Y.
    Cell 72:407-414(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE.
  2. "Contrasting selection pressures on components of the Ras-mediated signal transduction pathway in Drosophila."
    Riley R.M., Jin W., Gibson G.
    Mol. Ecol. 12:1315-1323(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 5-17-88#b1, 5-17-88a#4, 5-17-88a#6, 5-17-88b#1, 5-17-88b#5, 7-21-88#b2, 7-21-88b#1, 7-21-88b#2, 7-21-88b#4, AA1, AA16, AA18, AA20, AA3, CA2, M2, PYR2, Reids2 and wild5b.
  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. "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.

Entry informationi

Entry nameiDSOR1_DROME
AccessioniPrimary (citable) accession number: Q24324
Secondary accession number(s): Q8ISE0, Q9W360
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 16, 2005
Last modified: June 8, 2016
This is version 138 of the entry and version 2 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

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 one 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.