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Q9V9J3

- SRC42_DROME

UniProt

Q9V9J3 - SRC42_DROME

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Protein
Tyrosine-protein kinase Src42A
Gene
Src42A, Src41, TK5, CG44128
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei276 – 2761ATP By similarityBy similarity
Active sitei370 – 3701Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi254 – 2629ATP By similarityBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  3. protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. JNK cascade Source: FlyBase
  2. actin filament bundle assembly Source: FlyBase
  3. adherens junction organization Source: FlyBase
  4. apoptotic cell clearance Source: FlyBase
  5. cell migration Source: FlyBase
  6. compound eye development Source: FlyBase
  7. dorsal closure Source: FlyBase
  8. dorsal closure, spreading of leading edge cells Source: FlyBase
  9. epithelial cell-cell adhesion Source: FlyBase
  10. imaginal disc fusion, thorax closure Source: FlyBase
  11. imaginal disc-derived wing morphogenesis Source: FlyBase
  12. negative regulation of epidermal growth factor receptor signaling pathway Source: FlyBase
  13. negative regulation of synaptic growth at neuromuscular junction Source: FlyBase
  14. open tracheal system development Source: FlyBase
  15. peptidyl-tyrosine phosphorylation Source: FlyBase
  16. protein phosphorylation Source: FlyBase
  17. salivary gland morphogenesis Source: FlyBase
  18. transmembrane receptor protein tyrosine kinase signaling pathway Source: FlyBase
  19. tricarboxylic acid cycle Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 1994.
SignaLinkiQ9V9J3.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Src42A (EC:2.7.10.2)
Alternative name(s):
Tyrosine-protein kinase Src41
Short name:
Dsrc41
Gene namesi
Name:Src42A
Synonyms:Src41, TK5
ORF Names:CG44128
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0264959. Src42A.

Subcellular locationi

GO - Cellular componenti

  1. adherens junction Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 517517Tyrosine-protein kinase Src42A
PRO_0000088139Add
BLAST

Proteomic databases

PaxDbiQ9V9J3.
PRIDEiQ9V9J3.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

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

Gene expression databases

BgeeiQ9V9J3.

Interactioni

Protein-protein interaction databases

BioGridi61430. 27 interactions.
DIPiDIP-22220N.
IntActiQ9V9J3. 2 interactions.
MINTiMINT-333459.
STRINGi7227.FBpp0085321.

Structurei

3D structure databases

ProteinModelPortaliQ9V9J3.
SMRiQ9V9J3. Positions 37-515.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 12462SH3
Add
BLAST
Domaini130 – 22293SH2
Add
BLAST
Domaini248 – 504257Protein kinase
Add
BLAST

Sequence similaritiesi

Contains 1 SH2 domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00640000091347.
InParanoidiQ9V9J3.
KOiK08892.
OMAiVSHYTKT.
PhylomeDBiQ9V9J3.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. 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]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. 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]

Sequencei

Sequence statusi: Complete.

Q9V9J3-1 [UniParc]FASTAAdd to Basket

« Hide

MGNCLTTQKG EPDKPADRIK LDDPPTIGVG VGVPQIPMPS HAGQPPEQIR    50
PVPQIPESET AGANAKIFVA LYDYDARTDE DLSFRKGEHL EILNDTQGDW 100
WLARSKKTRS EGYIPSNYVA KLKSIEAEPW YFRKIKRIEA EKKLLLPENE 150
HGAFLIRDSE SRHNDYSLSV RDGDTVKHYR IRQLDEGGFF IARRTTFRTL 200
QELVEHYSKD SDGLCVNLCK PCVQIEKPVT EGLSHRTRDQ WEIDRTSLKF 250
VRKLGSGQFG DVWEGLWNNT TPVAIKTLKS GTMDPKDFLA EAQIMKKLRH 300
TKLIQLYAVC TVEEPIYIIT ELMKHGSLLE YLQAIAGKGR SLKMQTLIDM 350
AAQIAAGMAY LESQNYIHRD LAARNVLVGD GNIVKIADFG LARLIKEDEY 400
EARVGARFPI KWTAPEAANY SKFSIKSDVW SFGILLTELV TYGRIPYPGM 450
TNAEVLTQVE HGYRMPQPPN CEPRLYEIML ECWHKDPMRR PTFETLQWKL 500
EDFYTSDQSD YKEAQAY 517
Length:517
Mass (Da):59,069
Last modified:May 1, 2000 - v1
Checksum:i1EF196E4D7AE61E9
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651A → V in BAA07705. 1 Publication
Sequence conflicti376 – 3761V → I in AAB19907. 1 Publication
Sequence conflicti376 – 3761V → I in CAA05746. 1 Publication
Sequence conflicti381 – 3866GNIVKI → SNVVKM in AAB19907. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_476849.1. NM_057501.4.
UniGeneiDm.4134.

Genome annotation databases

EnsemblMetazoaiFBtr0085967; FBpp0085320; FBgn0004603.
FBtr0085968; FBpp0085321; FBgn0004603.
GeneIDi35524.
KEGGidme:Dmel_CG44128.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi NP_476849.1. NM_057501.4.
UniGenei Dm.4134.

3D structure databases

ProteinModelPortali Q9V9J3.
SMRi Q9V9J3. Positions 37-515.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 61430. 27 interactions.
DIPi DIP-22220N.
IntActi Q9V9J3. 2 interactions.
MINTi MINT-333459.
STRINGi 7227.FBpp0085321.

Proteomic databases

PaxDbi Q9V9J3.
PRIDEi Q9V9J3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0085967 ; FBpp0085320 ; FBgn0004603 .
FBtr0085968 ; FBpp0085321 ; FBgn0004603 .
GeneIDi 35524.
KEGGi dme:Dmel_CG44128.

Organism-specific databases

CTDi 35524.
FlyBasei FBgn0264959. Src42A.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00640000091347.
InParanoidi Q9V9J3.
KOi K08892.
OMAi VSHYTKT.
PhylomeDBi Q9V9J3.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 1994.
SignaLinki Q9V9J3.

Miscellaneous databases

ChiTaRSi Src42A. drosophila.
GenomeRNAii 35524.
NextBioi 793845.

Gene expression databases

Bgeei Q9V9J3.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR011009. 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 ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. 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.

Entry informationi

Entry nameiSRC42_DROME
AccessioniPrimary (citable) accession number: Q9V9J3
Secondary accession number(s): O18369
, Q0E9P0, Q26297, Q94879
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 122 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