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Q08012 (DRK_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Protein enhancer of sevenless 2B

Short name=Protein E(sev)2B
Alternative name(s):
Downstream of receptor kinase
SH2-SH3 adapter protein drk
Gene names
Name:drk
Synonyms:E(sev)2B
ORF Names:CG6033
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for proper signaling by sevenless. May act to stimulate the ability of Sos to catalyze Ras1 activation by linking sevenless and Sos in a signaling complex. Ref.1 Ref.2

Subunit structure

Interacts with autophosphorylated sev via SH2 domain and Sos, Dos and Dab via SH3 domains. Binds to tyrosine phosphorylated Dab via the SH2 domain. Ref.1 Ref.2 Ref.7 Ref.8

Subcellular location

Membrane; Peripheral membrane protein Ref.2.

Tissue specificity

Found mainly in the developing eye and in the antennal disk. Also observed in other imaginal disks tested and in the embryo.

Sequence similarities

Belongs to the GRB2/sem-5/DRK family.

Contains 1 SH2 domain.

Contains 2 SH3 domains.

Ontologies

Keywords
   Cellular componentMembrane
   DomainRepeat
SH2 domain
SH3 domain
   Molecular functionTransducer
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRas protein signal transduction

Inferred from physical interaction Ref.2. Source: FlyBase

actin filament organization

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

activation of JNKK activity

Non-traceable author statement Ref.1Ref.2. Source: UniProtKB

anterior/posterior axis specification, embryo

Traceable author statement PubMed 10494038. Source: FlyBase

associative learning

Inferred from mutant phenotype PubMed 19244537. Source: FlyBase

embryonic development via the syncytial blastoderm

Inferred from mutant phenotype PubMed 8978055. Source: FlyBase

imaginal disc-derived wing morphogenesis

Inferred from mutant phenotype PubMed 16648592. Source: FlyBase

negative regulation of epidermal growth factor-activated receptor activity

Inferred from genetic interaction PubMed 21340027. Source: FlyBase

olfactory learning

Inferred from mutant phenotype PubMed 19244537. Source: FlyBase

positive regulation of R7 cell differentiation

Inferred from genetic interaction PubMed 20980384. Source: FlyBase

positive regulation of signal transduction

Inferred from physical interaction Ref.2. Source: GOC

regulation of cell shape

Inferred from mutant phenotype PubMed 14527345. Source: FlyBase

sevenless signaling pathway

Inferred from genetic interaction Ref.2. Source: FlyBase

short-term memory

Inferred from mutant phenotype PubMed 19244537. Source: FlyBase

torso signaling pathway

Traceable author statement PubMed 10494038. Source: FlyBase

   Cellular_componentplasma membrane

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionSH3/SH2 adaptor activity

Non-traceable author statement Ref.1Ref.2. Source: UniProtKB

sevenless binding

Inferred from physical interaction Ref.2. Source: FlyBase

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Protein enhancer of sevenless 2B
PRO_0000088210

Regions

Domain1 – 5858SH3 1
Domain60 – 15192SH2
Domain152 – 21160SH3 2

Experimental info

Mutagenesis491P → L: Inactivates the SH3 domain. Abolishes binding to Dab; when associated with R-199. Ref.7
Mutagenesis671R → H in Su(sevs11)R1 mutant; ommatidial cell development obstruction. Ref.2
Mutagenesis851R → K: Disrupts the SH2 domain. Does not affect binding to Dab. Ref.7
Mutagenesis1061H → Y in E(sev)2B mutant; ommatidial cell development obstruction. Ref.2
Mutagenesis1991G → R: Disrupts the SH3 domain. Abolishes binding to Dab; when associated with L-49. Ref.7

Secondary structure

............... 211
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08012 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: A1D0614AF358F3C0

FASTA21124,435
        10         20         30         40         50         60 
MEAIAKHDFS ATADDELSFR KTQILKILNM EDDSNWYRAE LDGKEGLIPS NYIEMKNHDW 

        70         80         90        100        110        120 
YYGRITRADA EKLLSNKHEG AFLIRISESS PGDFSLSVKC PDGVQHFKVL RDAQSKFFLW 

       130        140        150        160        170        180 
VVKFNSLNEL VEYHRTASVS RSQDVKLRDM IPEEMLVQAL YDFVPQESGE LDFRRGDVIT 

       190        200        210 
VTDRSDENWW NGEIGNRKGI FPATYVTPYH S 

« Hide

References

« Hide 'large scale' references
[1]"An SH3-SH2-SH3 protein is required for p21Ras1 activation and binds to sevenless and Sos proteins in vitro."
Simon M.A., Dodson G.S., Rubin G.M.
Cell 73:169-177(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SEV AND SOS.
Tissue: Eye.
[2]"A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos."
Olivier J.P., Raabe T., Henkemeyer M., Dickson B., Mbamalu G., Margolis B., Schlessinger J., Hafen E., Pawson T.
Cell 73:179-191(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SEV AND SOS, MUTAGENESIS OF ARG-67 AND HIS-106.
Tissue: Embryo.
[3]"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: Ann Arbor1, Ann Arbor16, Ann Arbor18, Ann Arbor20, Ann Arbor3, CA2, CT1, Georgia-5b, Kakamega-2, Kakamega-b1, Kakamega-b2, Kenya-HLa3, Kenya-HLa4, Kenya-HLa6, Kenya-LGC, M2, Makindu-1, Makindu-b1, Makindu-b5, PYR2, Reids2 and Sapporo.
[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]"Disabled is a putative adaptor protein that functions during signaling by the sevenless receptor tyrosine kinase."
Le N., Simon M.A.
Mol. Cell. Biol. 18:4844-4854(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB, MUTAGENESIS OF PRO-49; ARG-85 AND GLY-199.
[8]"SH3 domain-mediated binding of the Drk protein to Dos is an important step in signaling of Drosophila receptor tyrosine kinases."
Feller S.M., Wecklein H., Lewitzky M., Kibler E., Raabe T.
Mech. Dev. 116:129-139(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DOS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L12446 mRNA. Translation: AAA28898.1.
L13173 mRNA. No translation available.
AY135053 Genomic DNA. Translation: AAN17564.1.
AY135054 Genomic DNA. Translation: AAN17565.1.
AY135055 Genomic DNA. Translation: AAN17566.1.
AY135056 Genomic DNA. Translation: AAN17567.1.
AY135057 Genomic DNA. Translation: AAN17568.1.
AY135058 Genomic DNA. Translation: AAN17569.1.
AY135059 Genomic DNA. Translation: AAN17570.1.
AY135060 Genomic DNA. Translation: AAN17571.1.
AY135061 Genomic DNA. Translation: AAN17572.1.
AY135062 Genomic DNA. Translation: AAN17573.1.
AY135063 Genomic DNA. Translation: AAN17574.1.
AY135064 Genomic DNA. Translation: AAN17575.1.
AY135065 Genomic DNA. Translation: AAN17576.1.
AY135066 Genomic DNA. Translation: AAN17577.1.
AY135067 Genomic DNA. Translation: AAN17578.1.
AY135068 Genomic DNA. Translation: AAN17579.1.
AY135069 Genomic DNA. Translation: AAN17580.1.
AY135070 Genomic DNA. Translation: AAN17581.1.
AY135071 Genomic DNA. Translation: AAN17582.1.
AY135072 Genomic DNA. Translation: AAN17583.1.
AY135073 Genomic DNA. Translation: AAN17584.1.
AY135074 Genomic DNA. Translation: AAN17585.1.
AE013599 Genomic DNA. Translation: AAF58368.1.
AE013599 Genomic DNA. Translation: AAM68582.1.
AE013599 Genomic DNA. Translation: AAM68583.1.
AE013599 Genomic DNA. Translation: AAM68584.1.
AE013599 Genomic DNA. Translation: AAM68585.1.
AY061142 mRNA. Translation: AAL28690.1.
PIRA46444.
RefSeqNP_476858.1. NM_057510.3.
NP_725302.1. NM_165994.1.
NP_725303.1. NM_165995.1.
NP_725304.1. NM_165996.1.
NP_725305.1. NM_165997.1.
NP_725306.1. NM_165998.1.
UniGeneDm.3707.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A36NMR-A1-59[»]
2A37NMR-A1-59[»]
2AZSNMR-A1-59[»]
2AZVNMR-A1-59[»]
ProteinModelPortalQ08012.
SMRQ08012. Positions 1-211.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid62256. 27 interactions.
DIPDIP-21223N.
IntActQ08012. 4 interactions.
MINTMINT-242311.

Proteomic databases

PaxDbQ08012.
PRIDEQ08012.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0087693; FBpp0086812; FBgn0004638.
FBtr0087694; FBpp0086813; FBgn0004638.
FBtr0087695; FBpp0086814; FBgn0004638.
FBtr0087696; FBpp0086815; FBgn0004638.
FBtr0087697; FBpp0086816; FBgn0004638.
FBtr0087698; FBpp0086817; FBgn0004638.
GeneID36497.
KEGGdme:Dmel_CG6033.
UCSCCG6033-RC. d. melanogaster.

Organism-specific databases

CTD36497.
FlyBaseFBgn0004638. drk.

Phylogenomic databases

eggNOGNOG298780.
GeneTreeENSGT00550000074482.
InParanoidQ08012.
KOK04364.
OMAVETKFVQ.
OrthoDBEOG75F4F6.
PhylomeDBQ08012.

Enzyme and pathway databases

SignaLinkQ08012.

Gene expression databases

BgeeQ08012.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 2 hits.
SSF55550. SSF55550. 1 hit.
PROSITEPS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSdrk. drosophila.
EvolutionaryTraceQ08012.
GenomeRNAi36497.
NextBio798864.
PROQ08012.

Entry information

Entry nameDRK_DROME
AccessionPrimary (citable) accession number: Q08012
Secondary accession number(s): A4UZF9, Q0E989, Q9V6Q5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 131 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

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