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Protein

Tyrosine-protein kinase Src64B

Gene

Src64B

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

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei312 – 3121ATPPROSITE-ProRule annotation
Active sitei404 – 4041Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi290 – 2989ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. non-membrane spanning protein tyrosine kinase activity Source: GO_Central
  3. protein tyrosine kinase activity Source: FlyBase
  4. receptor binding Source: GO_Central

GO - Biological processi

  1. actin cytoskeleton organization Source: FlyBase
  2. adherens junction organization Source: FlyBase
  3. axon guidance Source: FlyBase
  4. cell migration Source: GO_Central
  5. cellularization Source: FlyBase
  6. dorsal closure Source: FlyBase
  7. epithelial cell-cell adhesion Source: FlyBase
  8. female germline ring canal formation Source: FlyBase
  9. female germline ring canal formation, actin assembly Source: FlyBase
  10. female germline ring canal stabilization Source: FlyBase
  11. filtration diaphragm assembly Source: FlyBase
  12. germarium-derived egg chamber formation Source: FlyBase
  13. germarium-derived female germ-line cyst encapsulation Source: FlyBase
  14. innate immune response Source: GO_Central
  15. JNK cascade Source: FlyBase
  16. karyosome formation Source: FlyBase
  17. learning or memory Source: FlyBase
  18. long-term memory Source: FlyBase
  19. mushroom body development Source: FlyBase
  20. negative regulation of synaptic growth at neuromuscular junction Source: FlyBase
  21. olfactory learning Source: FlyBase
  22. oogenesis Source: FlyBase
  23. open tracheal system development Source: FlyBase
  24. ovarian fusome organization Source: FlyBase
  25. ovarian nurse cell to oocyte transport Source: FlyBase
  26. parallel actin filament bundle assembly Source: FlyBase
  27. peptidyl-tyrosine autophosphorylation Source: GO_Central
  28. peptidyl-tyrosine phosphorylation Source: FlyBase
  29. positive regulation of protein kinase activity Source: FlyBase
  30. protein phosphorylation Source: FlyBase
  31. regulation of actin polymerization or depolymerization Source: FlyBase
  32. regulation of cell proliferation Source: GO_Central
  33. salivary gland morphogenesis Source: FlyBase
  34. transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
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.
ReactomeiREACT_180238. Spry regulation of FGF signaling.
REACT_180243. Regulation of signaling by CBL.
REACT_181975. GAB1 signalosome.
REACT_182056. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_204973. p130Cas linkage to MAPK signaling for integrins.
REACT_210116. Signaling by ERBB2.
REACT_213859. Signaling by SCF-KIT.
REACT_214005. Signaling by EGFR.
REACT_214284. NCAM signaling for neurite out-growth.
REACT_221889. Platelet sensitization by LDL.
REACT_222212. DCC mediated attractive signaling.
REACT_225247. Fc epsilon receptor (FCERI) signaling.
REACT_229887. Integrin alphaIIb beta3 signaling.
REACT_232187. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_236136. Recycling pathway of L1.
REACT_238518. EPHB-mediated forward signaling.
REACT_239954. Ephrin signaling.
REACT_241128. EPH-ephrin mediated repulsion of cells.
REACT_246078. p38MAPK events.
REACT_250894. EPHA-mediated growth cone collapse.
REACT_252605. VEGFA-VEGFR2 Pathway.
REACT_255277. ADP signalling through P2Y purinoceptor 1.
REACT_256780. Sema3A PAK dependent Axon repulsion.
REACT_256915. Nephrin interactions.
REACT_260350. EPH-Ephrin signaling.
REACT_261064. Regulation of KIT signaling.
REACT_268975. GP1b-IX-V activation signalling.
REACT_269976. CRMPs in Sema3A signaling.
REACT_271373. Thrombin signalling through proteinase activated receptors (PARs).
REACT_34513. DSCAM interactions.
REACT_86289. Netrin mediated repulsion signals.
SignaLinkiP00528.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Src64B (EC:2.7.10.2)
Short name:
Dsrc64
Gene namesi
Name:Src64B
Synonyms:Src1
ORF Names:CG7524
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0262733. Src64B.

Subcellular locationi

GO - Cellular componenti

  1. extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  2. germline ring canal Source: FlyBase
  3. plasma membrane Source: FlyBase
Complete GO annotation...

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 552552Tyrosine-protein kinase Src64BPRO_0000088140Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei434 – 4341Phosphotyrosine; by autocatalysisBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP00528.
PRIDEiP00528.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

Abundant in embryos and pupae, rare in larvae and adults.1 Publication

Gene expression databases

BgeeiP00528.
ExpressionAtlasiP00528. differential.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
sloQ037203EBI-87092,EBI-426805

Protein-protein interaction databases

BioGridi71867. 47 interactions.
DIPiDIP-17438N.
IntActiP00528. 7 interactions.
MINTiMINT-296972.
STRINGi7227.FBpp0099948.

Structurei

3D structure databases

ProteinModelPortaliP00528.
SMRiP00528. Positions 101-548.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 15662SH3PROSITE-ProRule annotationAdd
BLAST
Domaini162 – 25998SH2PROSITE-ProRule annotationAdd
BLAST
Domaini284 – 537254Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
InParanoidiP00528.
KOiK05704.
OMAiYIATNQT.
OrthoDBiEOG7GTT2V.
PhylomeDBiP00528.

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.

P00528-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNKCCSKRQ DQELALAYPT GGYKKSDYTF GQTHINSSGG GNMGGVLGQK
60 70 80 90 100
HNNGGSLDSR YTPDPNHRGP LKIGGKGGVD IIRPRTTPTG VPGVVLKRVV
110 120 130 140 150
VALYDYKSRD ESDLSFMKGD RMEVIDDTES DWWRVVNLTT RQEGLIPLNF
160 170 180 190 200
VAEERSVNSE DWFFENVLRK EADKLLLAEE NPRGTFLVRP SEHNPNGYSL
210 220 230 240 250
SVKDWEDGRG YHVKHYRIKP LDNGGYYIAT NQTFPSLQAL VMAYSKNALG
260 270 280 290 300
LCHILSRPCP KPQPQMWDLG PELRDKYEIP RSEIQLLRKL GRGNFGEVFY
310 320 330 340 350
GKWRNSIDVA VKTLREGTMS TAAFLQEAAI MKKFRHNRLV ALYAVCSQEE
360 370 380 390 400
PIYIVQEYMS KGSLLDFLRE GDGRYLHFED LIYIATQVAS GMEYLESKQL
410 420 430 440 450
IHRDLAARNV LIGENNVAKI CDFGLARVIA DDEYCPKQGS RFPVKWTAPE
460 470 480 490 500
AIIYGKFSIK SDVWSYGILL MELFTYGQVP YPGMHSREVI ENIERGFRMP
510 520 530 540 550
KPTNHYFPDN IYQLLLQCWD AVPEKRPTFE FLNHYFESFS VTSEVPYREV

QD
Length:552
Mass (Da):63,003
Last modified:June 1, 2001 - v3
Checksum:i4A63CF4F16562864
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021A → S in AAA28913 (PubMed:2996778).Curated
Sequence conflicti261 – 27212KPQPQ…DLGPE → ASLPQTAAPDVGFGPQ in AAA28489 (PubMed:6317185).CuratedAdd
BLAST
Sequence conflicti286 – 2872LL → VV in AAA28489 (PubMed:6317185).Curated
Sequence conflicti290 – 2901L → V in AAA28489 (PubMed:6317185).Curated
Sequence conflicti293 – 2931G → R in AAA28489 (PubMed:6317185).Curated
Sequence conflicti316 – 3161E → A in AAA28489 (PubMed:6317185).Curated
Sequence conflicti366 – 3661D → N in AAA28489 (PubMed:6317185).Curated
Sequence conflicti373 – 3731G → D in AAA28489 (PubMed:6317185).Curated
Sequence conflicti384 – 3852IA → MH in AAA28489 (PubMed:6317185).Curated
Sequence conflicti389 – 3902AS → TT in AAA28489 (PubMed:6317185).Curated
Sequence conflicti393 – 3931E → K in AAA28489 (PubMed:6317185).Curated
Sequence conflicti400 – 4001L → V in AAA28489 (PubMed:6317185).Curated
Sequence conflicti406 – 4072AA → TT in AAA28489 (PubMed:6317185).Curated
Sequence conflicti435 – 4351C → R in AAA28489 (PubMed:6317185).Curated
Sequence conflicti460 – 4601K → E in CAA05754 (PubMed:9731193).Curated
Sequence conflicti471 – 4711M → T in AAA28489 (PubMed:6317185).Curated
Sequence conflicti484 – 4841M → L in AAA28489 (PubMed:6317185).Curated
Sequence conflicti507 – 5071F → L in AAA28489 (PubMed:6317185).Curated
Sequence conflicti536 – 5361F → L in AAA28489 (PubMed:6317185).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_001014561.1. NM_001014561.2.
NP_001014562.1. NM_001014562.3.
NP_001014563.1. NM_001014563.3.
NP_001014564.1. NM_001014564.3.
NP_001189051.1. NM_001202122.1.
NP_001246628.1. NM_001259699.2.
NP_001246629.1. NM_001259700.2.
NP_524934.2. NM_080195.4.
UniGeneiDm.1531.

Genome annotation databases

EnsemblMetazoaiFBtr0073321; FBpp0073177; FBgn0262733.
FBtr0100504; FBpp0099944; FBgn0262733.
FBtr0100505; FBpp0099946; FBgn0262733.
FBtr0100507; FBpp0099947; FBgn0262733.
FBtr0100508; FBpp0099948; FBgn0262733.
FBtr0302594; FBpp0291750; FBgn0262733.
FBtr0304989; FBpp0293526; FBgn0262733.
FBtr0304990; FBpp0293527; FBgn0262733.
GeneIDi48973.
KEGGidme:Dmel_CG7524.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_001014561.1. NM_001014561.2.
NP_001014562.1. NM_001014562.3.
NP_001014563.1. NM_001014563.3.
NP_001014564.1. NM_001014564.3.
NP_001189051.1. NM_001202122.1.
NP_001246628.1. NM_001259699.2.
NP_001246629.1. NM_001259700.2.
NP_524934.2. NM_080195.4.
UniGeneiDm.1531.

3D structure databases

ProteinModelPortaliP00528.
SMRiP00528. Positions 101-548.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi71867. 47 interactions.
DIPiDIP-17438N.
IntActiP00528. 7 interactions.
MINTiMINT-296972.
STRINGi7227.FBpp0099948.

Proteomic databases

PaxDbiP00528.
PRIDEiP00528.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0073321; FBpp0073177; FBgn0262733.
FBtr0100504; FBpp0099944; FBgn0262733.
FBtr0100505; FBpp0099946; FBgn0262733.
FBtr0100507; FBpp0099947; FBgn0262733.
FBtr0100508; FBpp0099948; FBgn0262733.
FBtr0302594; FBpp0291750; FBgn0262733.
FBtr0304989; FBpp0293526; FBgn0262733.
FBtr0304990; FBpp0293527; FBgn0262733.
GeneIDi48973.
KEGGidme:Dmel_CG7524.

Organism-specific databases

CTDi48973.
FlyBaseiFBgn0262733. Src64B.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
InParanoidiP00528.
KOiK05704.
OMAiYIATNQT.
OrthoDBiEOG7GTT2V.
PhylomeDBiP00528.

Enzyme and pathway databases

BRENDAi2.7.10.2. 1994.
ReactomeiREACT_180238. Spry regulation of FGF signaling.
REACT_180243. Regulation of signaling by CBL.
REACT_181975. GAB1 signalosome.
REACT_182056. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_204973. p130Cas linkage to MAPK signaling for integrins.
REACT_210116. Signaling by ERBB2.
REACT_213859. Signaling by SCF-KIT.
REACT_214005. Signaling by EGFR.
REACT_214284. NCAM signaling for neurite out-growth.
REACT_221889. Platelet sensitization by LDL.
REACT_222212. DCC mediated attractive signaling.
REACT_225247. Fc epsilon receptor (FCERI) signaling.
REACT_229887. Integrin alphaIIb beta3 signaling.
REACT_232187. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_236136. Recycling pathway of L1.
REACT_238518. EPHB-mediated forward signaling.
REACT_239954. Ephrin signaling.
REACT_241128. EPH-ephrin mediated repulsion of cells.
REACT_246078. p38MAPK events.
REACT_250894. EPHA-mediated growth cone collapse.
REACT_252605. VEGFA-VEGFR2 Pathway.
REACT_255277. ADP signalling through P2Y purinoceptor 1.
REACT_256780. Sema3A PAK dependent Axon repulsion.
REACT_256915. Nephrin interactions.
REACT_260350. EPH-Ephrin signaling.
REACT_261064. Regulation of KIT signaling.
REACT_268975. GP1b-IX-V activation signalling.
REACT_269976. CRMPs in Sema3A signaling.
REACT_271373. Thrombin signalling through proteinase activated receptors (PARs).
REACT_34513. DSCAM interactions.
REACT_86289. Netrin mediated repulsion signals.
SignaLinkiP00528.

Miscellaneous databases

ChiTaRSiSrc64B. fly.
GenomeRNAii48973.
NextBioi839596.

Gene expression databases

BgeeiP00528.
ExpressionAtlasiP00528. differential.

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]
ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiSRC64_DROME
AccessioniPrimary (citable) accession number: P00528
Secondary accession number(s): A4V1H7, O18372, Q9VZA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 169 of the entry and version 3 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

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.