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P00528

- SRC64_DROME

UniProt

P00528 - SRC64_DROME

Protein

Tyrosine-protein kinase Src64B

Gene

Src64B

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 3 (01 Jun 2001)
      Previous versions | rss
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    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: UniProtKB-EC
    3. protein binding Source: IntAct
    4. protein tyrosine kinase activity Source: FlyBase

    GO - Biological processi

    1. actin cytoskeleton organization Source: FlyBase
    2. adherens junction organization Source: FlyBase
    3. cellularization Source: FlyBase
    4. dorsal closure Source: FlyBase
    5. epithelial cell-cell adhesion Source: FlyBase
    6. female germline ring canal formation Source: FlyBase
    7. female germline ring canal formation, actin assembly Source: FlyBase
    8. female germline ring canal stabilization Source: FlyBase
    9. filtration diaphragm assembly Source: FlyBase
    10. germarium-derived egg chamber formation Source: FlyBase
    11. germarium-derived female germ-line cyst encapsulation Source: FlyBase
    12. JNK cascade Source: FlyBase
    13. karyosome formation Source: FlyBase
    14. learning or memory Source: FlyBase
    15. long-term memory Source: FlyBase
    16. mushroom body development Source: FlyBase
    17. negative regulation of synaptic growth at neuromuscular junction Source: FlyBase
    18. olfactory learning Source: FlyBase
    19. oogenesis Source: FlyBase
    20. open tracheal system development Source: FlyBase
    21. ovarian fusome organization Source: FlyBase
    22. ovarian nurse cell to oocyte transport Source: FlyBase
    23. parallel actin filament bundle assembly Source: FlyBase
    24. peptidyl-tyrosine phosphorylation Source: FlyBase
    25. positive regulation of protein kinase activity Source: FlyBase
    26. protein phosphorylation Source: FlyBase
    27. regulation of actin polymerization or depolymerization Source: FlyBase
    28. salivary gland morphogenesis Source: FlyBase

    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.
    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. germline ring canal Source: FlyBase

    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.

    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.
    GeneTreeiENSGT00640000091347.
    InParanoidiP00528.
    KOiK05704.
    OMAiKQGSRFP.
    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

    MGNKCCSKRQ DQELALAYPT GGYKKSDYTF GQTHINSSGG GNMGGVLGQK    50
    HNNGGSLDSR YTPDPNHRGP LKIGGKGGVD IIRPRTTPTG VPGVVLKRVV 100
    VALYDYKSRD ESDLSFMKGD RMEVIDDTES DWWRVVNLTT RQEGLIPLNF 150
    VAEERSVNSE DWFFENVLRK EADKLLLAEE NPRGTFLVRP SEHNPNGYSL 200
    SVKDWEDGRG YHVKHYRIKP LDNGGYYIAT NQTFPSLQAL VMAYSKNALG 250
    LCHILSRPCP KPQPQMWDLG PELRDKYEIP RSEIQLLRKL GRGNFGEVFY 300
    GKWRNSIDVA VKTLREGTMS TAAFLQEAAI MKKFRHNRLV ALYAVCSQEE 350
    PIYIVQEYMS KGSLLDFLRE GDGRYLHFED LIYIATQVAS GMEYLESKQL 400
    IHRDLAARNV LIGENNVAKI CDFGLARVIA DDEYCPKQGS RFPVKWTAPE 450
    AIIYGKFSIK SDVWSYGILL MELFTYGQVP YPGMHSREVI ENIERGFRMP 500
    KPTNHYFPDN IYQLLLQCWD AVPEKRPTFE FLNHYFESFS VTSEVPYREV 550
    QD 552
    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:
    EMBL
    GenBank
    DDBJ
    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_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.
    UniGeneiDm.1531.

    Genome annotation databases

    EnsemblMetazoaiFBtr0073321; 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.
    GeneIDi48973.
    KEGGidme:Dmel_CG7524.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    RefSeqi NP_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.
    UniGenei Dm.1531.

    3D structure databases

    ProteinModelPortali P00528.
    SMRi P00528. Positions 101-548.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 71867. 47 interactions.
    DIPi DIP-17438N.
    IntActi P00528. 7 interactions.
    MINTi MINT-296972.
    STRINGi 7227.FBpp0099948.

    Proteomic databases

    PaxDbi P00528.
    PRIDEi P00528.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0073321 ; 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 .
    GeneIDi 48973.
    KEGGi dme:Dmel_CG7524.

    Organism-specific databases

    CTDi 48973.
    FlyBasei FBgn0262733. Src64B.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00640000091347.
    InParanoidi P00528.
    KOi K05704.
    OMAi KQGSRFP.
    OrthoDBi EOG7GTT2V.
    PhylomeDBi P00528.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 1994.
    SignaLinki P00528.

    Miscellaneous databases

    ChiTaRSi Src64B. drosophila.
    GenomeRNAii 48973.
    NextBioi 839596.

    Gene expression databases

    Bgeei P00528.

    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

    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: October 1, 2014
    This is version 164 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