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P00528 (SRC64_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 161. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase Src64B

Short name=Dsrc64
EC=2.7.10.2
Gene names
Name:Src64B
Synonyms:Src1
ORF Names:CG7524
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in the development of neural tissue and smooth muscle. Ref.1

Catalytic activity

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

Tissue specificity

After the first 8 hours of development, accumulates almost exclusively in neural tissues such as the brain, ventral nerve chord, and eye-antennal disks, and in differentiating smooth muscle. Ref.1

Developmental stage

Abundant in embryos and pupae, rare in larvae and adults. 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
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJNK cascade

Traceable author statement PubMed 12147138. Source: FlyBase

actin cytoskeleton organization

Inferred from mutant phenotype PubMed 15979065. Source: FlyBase

adherens junction organization

Inferred from mutant phenotype PubMed 18305002. Source: FlyBase

cellularization

Inferred from mutant phenotype PubMed 14736750. Source: FlyBase

dorsal closure

Traceable author statement PubMed 12147138. Source: FlyBase

epithelial cell-cell adhesion

Inferred from mutant phenotype PubMed 18305002. Source: FlyBase

female germline ring canal formation

Inferred from mutant phenotype PubMed 16775001PubMed 9655810. Source: FlyBase

female germline ring canal formation, actin assembly

Inferred from mutant phenotype PubMed 11854310. Source: FlyBase

female germline ring canal stabilization

Inferred from mutant phenotype PubMed 9655810. Source: FlyBase

germarium-derived egg chamber formation

Inferred from mutant phenotype PubMed 16775001. Source: FlyBase

germarium-derived female germ-line cyst encapsulation

Inferred from mutant phenotype PubMed 16775001. Source: FlyBase

karyosome formation

Inferred from mutant phenotype PubMed 15979065. Source: FlyBase

learning or memory

Inferred from mutant phenotype PubMed 12593794. Source: FlyBase

long-term memory

Inferred from mutant phenotype PubMed 21490205. Source: FlyBase

mushroom body development

Inferred from mutant phenotype PubMed 14608664. Source: FlyBase

negative regulation of synaptic growth at neuromuscular junction

Inferred from genetic interaction PubMed 18925939. Source: FlyBase

olfactory learning

Inferred from mutant phenotype PubMed 12593794. Source: FlyBase

oogenesis

Inferred from mutant phenotype PubMed 15979065. Source: FlyBase

open tracheal system development

Inferred from mutant phenotype PubMed 18305002. Source: FlyBase

ovarian fusome organization

Inferred from mutant phenotype PubMed 15979065. Source: FlyBase

ovarian nurse cell to oocyte transport

Inferred from mutant phenotype PubMed 15979065. Source: FlyBase

parallel actin filament bundle assembly

Inferred from mutant phenotype PubMed 11854310. Source: FlyBase

peptidyl-tyrosine phosphorylation

Inferred from genetic interaction PubMed 12014990. Source: FlyBase

positive regulation of protein kinase activity

Inferred from mutant phenotype PubMed 20154139. Source: FlyBase

protein phosphorylation

Non-traceable author statement PubMed 10908587. Source: FlyBase

regulation of actin polymerization or depolymerization

Inferred from mutant phenotype PubMed 11854310. Source: FlyBase

salivary gland morphogenesis

Inferred from mutant phenotype PubMed 17507403. Source: FlyBase

   Cellular_componentgermline ring canal

Inferred from direct assay PubMed 16775001. 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

Inferred from sequence or structural similarity Ref.1. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

sloQ037203EBI-87092,EBI-426805

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 552552Tyrosine-protein kinase Src64B
PRO_0000088140

Regions

Domain95 – 15662SH3
Domain162 – 25998SH2
Domain284 – 537254Protein kinase
Nucleotide binding290 – 2989ATP By similarity

Sites

Active site4041Proton acceptor By similarity
Binding site3121ATP By similarity

Amino acid modifications

Modified residue4341Phosphotyrosine; by autocatalysis By similarity

Experimental info

Sequence conflict1021A → S in AAA28913. Ref.1
Sequence conflict261 – 27212KPQPQ…DLGPE → ASLPQTAAPDVGFGPQ in AAA28489. Ref.5
Sequence conflict286 – 2872LL → VV in AAA28489. Ref.5
Sequence conflict2901L → V in AAA28489. Ref.5
Sequence conflict2931G → R in AAA28489. Ref.5
Sequence conflict3161E → A in AAA28489. Ref.5
Sequence conflict3661D → N in AAA28489. Ref.5
Sequence conflict3731G → D in AAA28489. Ref.5
Sequence conflict384 – 3852IA → MH in AAA28489. Ref.5
Sequence conflict389 – 3902AS → TT in AAA28489. Ref.5
Sequence conflict3931E → K in AAA28489. Ref.5
Sequence conflict4001L → V in AAA28489. Ref.5
Sequence conflict406 – 4072AA → TT in AAA28489. Ref.5
Sequence conflict4351C → R in AAA28489. Ref.5
Sequence conflict4601K → E in CAA05754. Ref.6
Sequence conflict4711M → T in AAA28489. Ref.5
Sequence conflict4841M → L in AAA28489. Ref.5
Sequence conflict5071F → L in AAA28489. Ref.5
Sequence conflict5361F → L in AAA28489. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P00528 [UniParc].

Last modified June 1, 2001. Version 3.
Checksum: 4A63CF4F16562864

FASTA55263,003
        10         20         30         40         50         60 
MGNKCCSKRQ DQELALAYPT GGYKKSDYTF GQTHINSSGG GNMGGVLGQK HNNGGSLDSR 

        70         80         90        100        110        120 
YTPDPNHRGP LKIGGKGGVD IIRPRTTPTG VPGVVLKRVV VALYDYKSRD ESDLSFMKGD 

       130        140        150        160        170        180 
RMEVIDDTES DWWRVVNLTT RQEGLIPLNF VAEERSVNSE DWFFENVLRK EADKLLLAEE 

       190        200        210        220        230        240 
NPRGTFLVRP SEHNPNGYSL SVKDWEDGRG YHVKHYRIKP LDNGGYYIAT NQTFPSLQAL 

       250        260        270        280        290        300 
VMAYSKNALG LCHILSRPCP KPQPQMWDLG PELRDKYEIP RSEIQLLRKL GRGNFGEVFY 

       310        320        330        340        350        360 
GKWRNSIDVA VKTLREGTMS TAAFLQEAAI MKKFRHNRLV ALYAVCSQEE PIYIVQEYMS 

       370        380        390        400        410        420 
KGSLLDFLRE GDGRYLHFED LIYIATQVAS GMEYLESKQL IHRDLAARNV LIGENNVAKI 

       430        440        450        460        470        480 
CDFGLARVIA DDEYCPKQGS RFPVKWTAPE AIIYGKFSIK SDVWSYGILL MELFTYGQVP 

       490        500        510        520        530        540 
YPGMHSREVI ENIERGFRMP KPTNHYFPDN IYQLLLQCWD AVPEKRPTFE FLNHYFESFS 

       550 
VTSEVPYREV QD 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence and the tissue-specific expression of Drosophila c-src."
Simon M.A., Drees B., Kornberg T., Bishop J.M.
Cell 42:831-840(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[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]"Nucleotide sequences of the Drosophila src and abl homologs: conservation and variability in the src family oncogenes."
Hoffmann F.M., Fresco L.D., Hoffman-Falk H., Shilo B.-Z.
Cell 35:393-401(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 249-552.
[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 410-461.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11917 mRNA. Translation: AAA28913.1.
AE014296 Genomic DNA. Translation: AAF47922.1.
AE014296 Genomic DNA. Translation: AAX52734.1.
AE014296 Genomic DNA. Translation: AAX52735.1.
AE014296 Genomic DNA. Translation: AAX52736.1.
AE014296 Genomic DNA. Translation: AAX52737.1.
AY051781 mRNA. Translation: AAK93205.1.
K01043 Genomic DNA. Translation: AAA28489.1.
AJ002919 Genomic DNA. Translation: CAA05754.1.
RefSeqNP_001014561.1. NM_001014561.2.
NP_001014562.1. NM_001014562.3.
NP_001014563.1. NM_001014563.3.
NP_001014564.1. NM_001014564.3.
NP_001189050.1. NM_001202121.2.
NP_001189051.1. NM_001202122.1.
NP_001246628.1. NM_001259699.2.
NP_001246629.1. NM_001259700.2.
NP_524934.2. NM_080195.4.
UniGeneDm.1531.

3D structure databases

ProteinModelPortalP00528.
SMRP00528. Positions 101-548.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid71867. 47 interactions.
DIPDIP-17438N.
IntActP00528. 7 interactions.
MINTMINT-296972.
STRING7227.FBpp0099948.

Proteomic databases

PaxDbP00528.
PRIDEP00528.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0073321; FBpp0073177; FBgn0262733.
FBtr0100504; FBpp0099944; FBgn0262733.
FBtr0100505; FBpp0099946; FBgn0262733.
FBtr0100507; FBpp0099947; FBgn0262733.
FBtr0100508; FBpp0099948; FBgn0262733.
FBtr0302593; FBpp0291749; FBgn0262733.
FBtr0302594; FBpp0291750; FBgn0262733.
FBtr0304989; FBpp0293526; FBgn0262733.
FBtr0304990; FBpp0293527; FBgn0262733.
GeneID48973.
KEGGdme:Dmel_CG7524.

Organism-specific databases

CTD48973.
FlyBaseFBgn0262733. Src64B.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00640000091347.
InParanoidP00528.
KOK05704.
OMAKQGSRFP.
OrthoDBEOG7GTT2V.
PhylomeDBP00528.

Enzyme and pathway databases

BRENDA2.7.10.2. 1994.
SignaLinkP00528.

Gene expression databases

BgeeP00528.

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

ChiTaRSSrc64B. drosophila.
GenomeRNAi48973.
NextBio839596.

Entry information

Entry nameSRC64_DROME
AccessionPrimary (citable) accession number: P00528
Secondary accession number(s): A4V1H7, O18372, Q9VZA2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 161 of the entry and version 3 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