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Q9V9J3 (SRC42_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Tyrosine-protein kinase Src42A

EC=2.7.10.2
Alternative name(s):
Tyrosine-protein kinase Src41
Short name=Dsrc41
Gene names
Name:Src42A
Synonyms:Src41, TK5
ORF Names:CG44128
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Essential for correct eye morphogenesis (ommatidial R7 neuron formation), this requires the Ras1/MAPK signal transduction pathway. May be involved in the regulation of cytoskeleton organization and cell-cell contacts in developing ommatidia. Ref.1

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Tissue specificity

Ubiquitous in early embryos, in stages 13-16 expression is seen in visceral mesoderm, hindgut, brain, anal pads and ventral ganglions. In larvae, expression is in CNS, wing disk, leg disk and photoreceptor precursors in the eye-antenna disks posterior to the morphogenetic furrow. Ref.1

Developmental stage

In early embryos expression is very low, expression increases during embryogenesis. Also expressed in larvae and pupae. Ref.1

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Transferase
Tyrosine-protein kinase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Traceable author statement PubMed 12147138. Source: FlyBase

actin filament bundle assembly

Inferred from mutant phenotype PubMed 16831834. Source: FlyBase

adherens junction organization

Inferred from mutant phenotype PubMed 18305002. Source: FlyBase

apoptotic cell clearance

Inferred from mutant phenotype PubMed 18432193. Source: FlyBase

compound eye development

Inferred from mutant phenotype Ref.1. Source: FlyBase

dorsal closure

Inferred from mutant phenotype PubMed 10634792PubMed 16831834. Source: FlyBase

dorsal closure, spreading of leading edge cells

Inferred from mutant phenotype PubMed 15857910. Source: FlyBase

epithelial cell-cell adhesion

Inferred from mutant phenotype PubMed 18305002. Source: FlyBase

imaginal disc fusion, thorax closure

Inferred from mutant phenotype PubMed 15857910. Source: FlyBase

imaginal disc-derived wing morphogenesis

Inferred from mutant phenotype PubMed 16648592. Source: FlyBase

negative regulation of epidermal growth factor receptor signaling pathway

Inferred from genetic interaction PubMed 10075855. Source: FlyBase

negative regulation of synaptic growth at neuromuscular junction

Inferred from genetic interaction PubMed 18925939. Source: FlyBase

open tracheal system development

Inferred from mutant phenotype PubMed 16469972PubMed 18305002. Source: FlyBase

peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 12014990. Source: FlyBase

protein phosphorylation

Inferred from direct assay PubMed 12014990. Source: FlyBase

salivary gland morphogenesis

Inferred from mutant phenotype PubMed 17507403. Source: FlyBase

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from genetic interaction PubMed 10075855. Source: FlyBase

tricarboxylic acid cycle

Inferred from direct assay PubMed 18042644. Source: FlyBase

   Cellular_componentadherens junction

Inferred from direct assay PubMed 18305002. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine kinase activity

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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 517517Tyrosine-protein kinase Src42A
PRO_0000088139

Regions

Domain63 – 12462SH3
Domain130 – 22293SH2
Domain248 – 504257Protein kinase
Nucleotide binding254 – 2629ATP By similarity UniProtKB P08631

Sites

Active site3701Proton acceptor By similarity UniProtKB P08631
Binding site2761ATP By similarity UniProtKB P08631

Experimental info

Sequence conflict651A → V in BAA07705. Ref.1
Sequence conflict3761V → I in AAB19907. Ref.5
Sequence conflict3761V → I in CAA05746. Ref.6
Sequence conflict381 – 3866GNIVKI → SNVVKM in AAB19907. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9V9J3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 1EF196E4D7AE61E9

FASTA51759,069
        10         20         30         40         50         60 
MGNCLTTQKG EPDKPADRIK LDDPPTIGVG VGVPQIPMPS HAGQPPEQIR PVPQIPESET 

        70         80         90        100        110        120 
AGANAKIFVA LYDYDARTDE DLSFRKGEHL EILNDTQGDW WLARSKKTRS EGYIPSNYVA 

       130        140        150        160        170        180 
KLKSIEAEPW YFRKIKRIEA EKKLLLPENE HGAFLIRDSE SRHNDYSLSV RDGDTVKHYR 

       190        200        210        220        230        240 
IRQLDEGGFF IARRTTFRTL QELVEHYSKD SDGLCVNLCK PCVQIEKPVT EGLSHRTRDQ 

       250        260        270        280        290        300 
WEIDRTSLKF VRKLGSGQFG DVWEGLWNNT TPVAIKTLKS GTMDPKDFLA EAQIMKKLRH 

       310        320        330        340        350        360 
TKLIQLYAVC TVEEPIYIIT ELMKHGSLLE YLQAIAGKGR SLKMQTLIDM AAQIAAGMAY 

       370        380        390        400        410        420 
LESQNYIHRD LAARNVLVGD GNIVKIADFG LARLIKEDEY EARVGARFPI KWTAPEAANY 

       430        440        450        460        470        480 
SKFSIKSDVW SFGILLTELV TYGRIPYPGM TNAEVLTQVE HGYRMPQPPN CEPRLYEIML 

       490        500        510 
ECWHKDPMRR PTFETLQWKL EDFYTSDQSD YKEAQAY 

« Hide

References

« Hide 'large scale' references
[1]"Regulation of cell-cell contacts in developing Drosophila eyes by Dsrc41, a new, close relative of vertebrate c-src."
Takahashi F., Endo S., Kojima T., Saigo K.
Genes Dev. 10:1645-1656(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: Canton-S.
Tissue: Pupae.
[2]"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.
[3]"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.
[4]"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.
[5]"Identification of seven novel protein-tyrosine kinase genes of Drosophila by the polymerase chain reaction."
Shishido E., Emori Y., Saigo K.
FEBS Lett. 289:235-238(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 374-428.
[6]"Sampling the genomic pool of protein tyrosine kinase genes using the polymerase chain reaction with genomic DNA."
Oates A.C., Wollberg P., Achen M.G., Wilks A.F.
Biochem. Biophys. Res. Commun. 249:660-667(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-427.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D42125 mRNA. Translation: BAA07705.1.
AE013599 Genomic DNA. Translation: AAF57295.1.
AY058652 mRNA. Translation: AAL13881.1.
S55977 Genomic DNA. Translation: AAB19907.1.
AJ002911 Genomic DNA. Translation: CAA05746.1.
RefSeqNP_476849.1. NM_057501.4.
UniGeneDm.4134.

3D structure databases

ProteinModelPortalQ9V9J3.
SMRQ9V9J3. Positions 37-515.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid61430. 26 interactions.
DIPDIP-22220N.
IntActQ9V9J3. 2 interactions.
MINTMINT-333459.
STRING7227.FBpp0085321.

Proteomic databases

PaxDbQ9V9J3.
PRIDEQ9V9J3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085967; FBpp0085320; FBgn0004603.
FBtr0085968; FBpp0085321; FBgn0004603.
GeneID35524.
KEGGdme:Dmel_CG44128.

Organism-specific databases

CTD35524.
FlyBaseFBgn0264959. Src42A.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00640000091347.
InParanoidQ9V9J3.
KOK08892.
OMAVSHYTKT.
PhylomeDBQ9V9J3.

Enzyme and pathway databases

BRENDA2.7.10.2. 1994.
SignaLinkQ9V9J3.

Gene expression databases

BgeeQ9V9J3.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSrc42A. drosophila.
GenomeRNAi35524.
NextBio793845.

Entry information

Entry nameSRC42_DROME
AccessionPrimary (citable) accession number: Q9V9J3
Secondary accession number(s): O18369 expand/collapse secondary AC list , Q0E9P0, Q26297, Q94879
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 120 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

Drosophila

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