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Protein

Protein enhancer of sevenless 2B

Gene

drk

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

Functioni

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.2 Publications

GO - Molecular functioni

  1. sevenless binding Source: FlyBase
  2. SH3/SH2 adaptor activity Source: UniProtKB
  3. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. actin filament organization Source: FlyBase
  2. activation of JNKK activity Source: UniProtKB
  3. anterior/posterior axis specification, embryo Source: FlyBase
  4. associative learning Source: FlyBase
  5. embryonic development via the syncytial blastoderm Source: FlyBase
  6. imaginal disc-derived wing morphogenesis Source: FlyBase
  7. negative regulation of epidermal growth factor-activated receptor activity Source: FlyBase
  8. olfactory learning Source: FlyBase
  9. positive regulation of MAPK cascade Source: FlyBase
  10. positive regulation of R7 cell differentiation Source: FlyBase
  11. Ras protein signal transduction Source: FlyBase
  12. regulation of cell shape Source: FlyBase
  13. sevenless signaling pathway Source: FlyBase
  14. short-term memory Source: FlyBase
  15. TORC1 signaling Source: FlyBase
  16. torso signaling pathway Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Enzyme and pathway databases

ReactomeiREACT_273499. SOS-mediated signalling.
REACT_275007. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_282671. Regulation of actin dynamics for phagocytic cup formation.
REACT_283177. Spry regulation of FGF signaling.
REACT_284157. SHC1 events in ERBB2 signaling.
REACT_285373. NCAM signaling for neurite out-growth.
REACT_285422. Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
REACT_288287. Regulation of KIT signaling.
REACT_290285. FCERI mediated MAPK activation.
REACT_295632. PI3K events in ERBB2 signaling.
REACT_295853. Signal attenuation.
REACT_299068. GAB1 signalosome.
REACT_302538. SHC-mediated signalling.
REACT_303547. FRS2-mediated cascade.
REACT_305576. DAP12 signaling.
REACT_307287. GRB2 events in EGFR signaling.
REACT_308878. Constitutive PI3K/AKT Signaling in Cancer.
REACT_310046. Signalling to RAS.
REACT_312280. Negative regulation of FGFR signaling.
REACT_313058. SHC1 events in EGFR signaling.
REACT_313187. Tie2 Signaling.
REACT_316445. Regulation of signaling by CBL.
REACT_318075. PI-3K cascade.
REACT_318440. SHC-mediated cascade.
REACT_321995. SHC1 events in ERBB4 signaling.
REACT_334486. Signaling by SCF-KIT.
REACT_336401. Interleukin-3, 5 and GM-CSF signaling.
REACT_338876. EGFR downregulation.
REACT_339689. PIP3 activates AKT signaling.
REACT_342034. GRB2 events in ERBB2 signaling.
REACT_343362. Constitutive Signaling by EGFRvIII.
REACT_345845. PI3K Cascade.
REACT_350001. GRB2:SOS provides linkage to MAPK signaling for Integrins.
REACT_352090. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_352851. Signaling by FGFR1 fusion mutants.
REACT_352911. EGFR Transactivation by Gastrin.
REACT_354287. Signaling by FGFR mutants.
SignaLinkiQ08012.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:drk
Synonyms:E(sev)2B
ORF Names:CG6033
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0004638. drk.

Subcellular locationi

  1. Membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. nucleoplasm Source: FlyBase
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi49 – 491P → L: Inactivates the SH3 domain. Abolishes binding to Dab; when associated with R-199. 1 Publication
Mutagenesisi67 – 671R → H in Su(sevs11)R1 mutant; ommatidial cell development obstruction. 1 Publication
Mutagenesisi85 – 851R → K: Disrupts the SH2 domain. Does not affect binding to Dab. 1 Publication
Mutagenesisi106 – 1061H → Y in E(sev)2B mutant; ommatidial cell development obstruction. 1 Publication
Mutagenesisi199 – 1991G → R: Disrupts the SH3 domain. Abolishes binding to Dab; when associated with L-49. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Protein enhancer of sevenless 2BPRO_0000088210Add
BLAST

Proteomic databases

PaxDbiQ08012.
PRIDEiQ08012.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ08012.

Interactioni

Subunit structurei

Interacts with autophosphorylated sev via SH2 domain and Sos, Dos and Dab via SH3 domains. Binds to tyrosine phosphorylated Dab via the SH2 domain.4 Publications

Protein-protein interaction databases

BioGridi62256. 27 interactions.
DIPiDIP-21223N.
IntActiQ08012. 4 interactions.
MINTiMINT-242311.

Structurei

Secondary structure

1
211
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Beta strandi13 – 164Combined sources
Beta strandi23 – 297Combined sources
Turni31 – 333Combined sources
Beta strandi36 – 416Combined sources
Beta strandi44 – 507Combined sources
Beta strandi53 – 553Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A36NMR-A1-59[»]
2A37NMR-A1-59[»]
2AZSNMR-A1-59[»]
2AZVNMR-A1-59[»]
ProteinModelPortaliQ08012.
SMRiQ08012. Positions 1-211.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08012.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5858SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini60 – 15192SH2PROSITE-ProRule annotationAdd
BLAST
Domaini152 – 21160SH3 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the GRB2/sem-5/DRK family.Curated
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 2 SH3 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiNOG298780.
GeneTreeiENSGT00550000074482.
InParanoidiQ08012.
KOiK04364.
OMAiRFQDSVQ.
OrthoDBiEOG75F4F6.
PhylomeDBiQ08012.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08012-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAIAKHDFS ATADDELSFR KTQILKILNM EDDSNWYRAE LDGKEGLIPS
60 70 80 90 100
NYIEMKNHDW YYGRITRADA EKLLSNKHEG AFLIRISESS PGDFSLSVKC
110 120 130 140 150
PDGVQHFKVL RDAQSKFFLW VVKFNSLNEL VEYHRTASVS RSQDVKLRDM
160 170 180 190 200
IPEEMLVQAL YDFVPQESGE LDFRRGDVIT VTDRSDENWW NGEIGNRKGI
210
FPATYVTPYH S
Length:211
Mass (Da):24,435
Last modified:February 1, 1995 - v1
Checksum:iA1D0614AF358F3C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA46444.
RefSeqiNP_476858.1. NM_057510.4.
NP_725302.1. NM_165994.2.
NP_725303.1. NM_165995.2.
NP_725304.1. NM_165996.2.
NP_725306.1. NM_165998.2.
UniGeneiDm.3707.

Genome annotation databases

EnsemblMetazoaiFBtr0087694; FBpp0086813; FBgn0004638.
FBtr0087695; FBpp0086814; FBgn0004638.
FBtr0087696; FBpp0086815; FBgn0004638.
FBtr0087697; FBpp0086816; FBgn0004638.
FBtr0087698; FBpp0086817; FBgn0004638.
GeneIDi36497.
KEGGidme:Dmel_CG6033.
UCSCiCG6033-RC. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA46444.
RefSeqiNP_476858.1. NM_057510.4.
NP_725302.1. NM_165994.2.
NP_725303.1. NM_165995.2.
NP_725304.1. NM_165996.2.
NP_725306.1. NM_165998.2.
UniGeneiDm.3707.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A36NMR-A1-59[»]
2A37NMR-A1-59[»]
2AZSNMR-A1-59[»]
2AZVNMR-A1-59[»]
ProteinModelPortaliQ08012.
SMRiQ08012. Positions 1-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62256. 27 interactions.
DIPiDIP-21223N.
IntActiQ08012. 4 interactions.
MINTiMINT-242311.

Proteomic databases

PaxDbiQ08012.
PRIDEiQ08012.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087694; FBpp0086813; FBgn0004638.
FBtr0087695; FBpp0086814; FBgn0004638.
FBtr0087696; FBpp0086815; FBgn0004638.
FBtr0087697; FBpp0086816; FBgn0004638.
FBtr0087698; FBpp0086817; FBgn0004638.
GeneIDi36497.
KEGGidme:Dmel_CG6033.
UCSCiCG6033-RC. d. melanogaster.

Organism-specific databases

CTDi36497.
FlyBaseiFBgn0004638. drk.

Phylogenomic databases

eggNOGiNOG298780.
GeneTreeiENSGT00550000074482.
InParanoidiQ08012.
KOiK04364.
OMAiRFQDSVQ.
OrthoDBiEOG75F4F6.
PhylomeDBiQ08012.

Enzyme and pathway databases

ReactomeiREACT_273499. SOS-mediated signalling.
REACT_275007. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_282671. Regulation of actin dynamics for phagocytic cup formation.
REACT_283177. Spry regulation of FGF signaling.
REACT_284157. SHC1 events in ERBB2 signaling.
REACT_285373. NCAM signaling for neurite out-growth.
REACT_285422. Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
REACT_288287. Regulation of KIT signaling.
REACT_290285. FCERI mediated MAPK activation.
REACT_295632. PI3K events in ERBB2 signaling.
REACT_295853. Signal attenuation.
REACT_299068. GAB1 signalosome.
REACT_302538. SHC-mediated signalling.
REACT_303547. FRS2-mediated cascade.
REACT_305576. DAP12 signaling.
REACT_307287. GRB2 events in EGFR signaling.
REACT_308878. Constitutive PI3K/AKT Signaling in Cancer.
REACT_310046. Signalling to RAS.
REACT_312280. Negative regulation of FGFR signaling.
REACT_313058. SHC1 events in EGFR signaling.
REACT_313187. Tie2 Signaling.
REACT_316445. Regulation of signaling by CBL.
REACT_318075. PI-3K cascade.
REACT_318440. SHC-mediated cascade.
REACT_321995. SHC1 events in ERBB4 signaling.
REACT_334486. Signaling by SCF-KIT.
REACT_336401. Interleukin-3, 5 and GM-CSF signaling.
REACT_338876. EGFR downregulation.
REACT_339689. PIP3 activates AKT signaling.
REACT_342034. GRB2 events in ERBB2 signaling.
REACT_343362. Constitutive Signaling by EGFRvIII.
REACT_345845. PI3K Cascade.
REACT_350001. GRB2:SOS provides linkage to MAPK signaling for Integrins.
REACT_352090. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_352851. Signaling by FGFR1 fusion mutants.
REACT_352911. EGFR Transactivation by Gastrin.
REACT_354287. Signaling by FGFR mutants.
SignaLinkiQ08012.

Miscellaneous databases

ChiTaRSidrk. fly.
EvolutionaryTraceiQ08012.
GenomeRNAii36497.
NextBioi798864.
PROiQ08012.

Gene expression databases

BgeeiQ08012.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 2 hits.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. "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.

Entry informationi

Entry nameiDRK_DROME
AccessioniPrimary (citable) accession number: Q08012
Secondary accession number(s): A4UZF9, Q0E989, Q9V6Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 29, 2015
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.