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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

GO - Biological processi

  • actin cytoskeleton organization Source: FlyBase
  • adherens junction organization Source: FlyBase
  • axon guidance Source: FlyBase
  • cell differentiation Source: GO_Central
  • cell migration Source: GO_Central
  • cellularization Source: FlyBase
  • dorsal closure Source: FlyBase
  • epithelial cell-cell adhesion Source: FlyBase
  • female germline ring canal formation Source: FlyBase
  • female germline ring canal formation, actin assembly Source: FlyBase
  • female germline ring canal stabilization Source: FlyBase
  • filtration diaphragm assembly Source: FlyBase
  • germarium-derived egg chamber formation Source: FlyBase
  • germarium-derived female germ-line cyst encapsulation Source: FlyBase
  • innate immune response Source: GO_Central
  • JNK cascade Source: FlyBase
  • karyosome formation Source: FlyBase
  • learning or memory Source: FlyBase
  • long-term memory Source: FlyBase
  • mushroom body development Source: FlyBase
  • negative regulation of synaptic growth at neuromuscular junction Source: FlyBase
  • olfactory learning Source: FlyBase
  • oogenesis Source: FlyBase
  • open tracheal system development Source: FlyBase
  • ovarian fusome organization Source: FlyBase
  • ovarian nurse cell to oocyte transport Source: FlyBase
  • parallel actin filament bundle assembly Source: FlyBase
  • peptidyl-tyrosine autophosphorylation Source: GO_Central
  • peptidyl-tyrosine phosphorylation Source: FlyBase
  • positive regulation of protein kinase activity Source: FlyBase
  • protein phosphorylation Source: FlyBase
  • regulation of actin polymerization or depolymerization Source: FlyBase
  • regulation of cell proliferation Source: GO_Central
  • salivary gland morphogenesis Source: FlyBase
  • 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_279767. DCC mediated attractive signaling.
REACT_280149. Fc epsilon receptor (FCERI) signaling.
REACT_282444. GP1b-IX-V activation signalling.
REACT_283177. Spry regulation of FGF signaling.
REACT_285373. NCAM signaling for neurite out-growth.
REACT_285926. p38MAPK events.
REACT_286155. Netrin mediated repulsion signals.
REACT_288287. Regulation of KIT signaling.
REACT_291568. Ephrin signaling.
REACT_293578. ADP signalling through P2Y purinoceptor 1.
REACT_294512. Signaling by ERBB2.
REACT_299068. GAB1 signalosome.
REACT_302279. Thrombin signalling through proteinase activated receptors (PARs).
REACT_303345. EPHB-mediated forward signaling.
REACT_311282. p130Cas linkage to MAPK signaling for integrins.
REACT_312932. EPH-Ephrin signaling.
REACT_316445. Regulation of signaling by CBL.
REACT_318429. Integrin alphaIIb beta3 signaling.
REACT_319268. CRMPs in Sema3A signaling.
REACT_323102. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_323902. Nephrin interactions.
REACT_331500. EPH-ephrin mediated repulsion of cells.
REACT_331911. EPHA-mediated growth cone collapse.
REACT_334486. Signaling by SCF-KIT.
REACT_343793. Signaling by EGFR.
REACT_346571. VEGFA-VEGFR2 Pathway.
REACT_350001. GRB2:SOS provides linkage to MAPK signaling for Integrins.
REACT_352090. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_361821. CD209 (DC-SIGN) signaling.
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 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0262733. Src64B.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: FlyBase
  • extrinsic component of cytoplasmic side of plasma membrane Source: GO_Central
  • germline ring canal Source: FlyBase
  • 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.
GenevisibleiP00528. DM.

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.FBpp0293527.

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.FBpp0293527.

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_279767. DCC mediated attractive signaling.
REACT_280149. Fc epsilon receptor (FCERI) signaling.
REACT_282444. GP1b-IX-V activation signalling.
REACT_283177. Spry regulation of FGF signaling.
REACT_285373. NCAM signaling for neurite out-growth.
REACT_285926. p38MAPK events.
REACT_286155. Netrin mediated repulsion signals.
REACT_288287. Regulation of KIT signaling.
REACT_291568. Ephrin signaling.
REACT_293578. ADP signalling through P2Y purinoceptor 1.
REACT_294512. Signaling by ERBB2.
REACT_299068. GAB1 signalosome.
REACT_302279. Thrombin signalling through proteinase activated receptors (PARs).
REACT_303345. EPHB-mediated forward signaling.
REACT_311282. p130Cas linkage to MAPK signaling for integrins.
REACT_312932. EPH-Ephrin signaling.
REACT_316445. Regulation of signaling by CBL.
REACT_318429. Integrin alphaIIb beta3 signaling.
REACT_319268. CRMPs in Sema3A signaling.
REACT_323102. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_323902. Nephrin interactions.
REACT_331500. EPH-ephrin mediated repulsion of cells.
REACT_331911. EPHA-mediated growth cone collapse.
REACT_334486. Signaling by SCF-KIT.
REACT_343793. Signaling by EGFR.
REACT_346571. VEGFA-VEGFR2 Pathway.
REACT_350001. GRB2:SOS provides linkage to MAPK signaling for Integrins.
REACT_352090. Role of LAT2/NTAL/LAB on calcium mobilization.
REACT_361821. CD209 (DC-SIGN) signaling.
SignaLinkiP00528.

Miscellaneous databases

ChiTaRSiSrc64B. fly.
GenomeRNAii48973.
NextBioi839596.
PROiP00528.

Gene expression databases

BgeeiP00528.
ExpressionAtlasiP00528. differential.
GenevisibleiP00528. DM.

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: June 24, 2015
This is version 173 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.