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P00522

- ABL_DROME

UniProt

P00522 - ABL_DROME

Protein

Tyrosine-protein kinase Abl

Gene

Abl

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 158 (01 Oct 2014)
      Sequence version 3 (12 Apr 2005)
      Previous versions | rss
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    Functioni

    Arm and Abl proteins function cooperatively at adherens junctions in both the CNS and epidermis; critical for embryonic epithelial morphogenesis regulating cell shape changes and cell migration. Plays a critical role in transducing embryonic midline repulsive cues; may regulate cytoskeletal dynamics underlying a growth cone's response to midline cues. The ability of pCC/MP2 axons to correctly interpret midline repulsive cues and stay on the ipsilateral side is dependent on the strength of both Slit/robo and Abl-dependent signaling pathways.3 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 PublicationPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei400 – 4001ATPPROSITE-ProRule annotation
    Active sitei492 – 4921Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi377 – 3859ATPPROSITE-ProRule annotation
    Nucleotide bindingi445 – 4517ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. axon guidance Source: FlyBase
    2. axon midline choice point recognition Source: FlyBase
    3. axonogenesis Source: FlyBase
    4. central nervous system development Source: FlyBase
    5. compound eye development Source: FlyBase
    6. cytoplasmic transport, nurse cell to oocyte Source: FlyBase
    7. dorsal closure Source: FlyBase
    8. epithelial cell morphogenesis Source: FlyBase
    9. morphogenesis of an epithelium Source: FlyBase
    10. motor neuron axon guidance Source: FlyBase
    11. negative regulation of synaptic growth at neuromuscular junction Source: FlyBase
    12. neuron migration Source: FlyBase
    13. peptidyl-tyrosine phosphorylation Source: FlyBase
    14. photoreceptor cell axon guidance Source: FlyBase
    15. planar cell polarity pathway involved in axis elongation Source: FlyBase
    16. positive regulation of protein export from nucleus Source: FlyBase
    17. protein phosphorylation Source: FlyBase
    18. regulation of actin polymerization or depolymerization Source: FlyBase
    19. regulation of cell shape Source: FlyBase
    20. regulation of protein localization Source: FlyBase
    21. regulation of protein stability Source: FlyBase
    22. ventral cord development Source: FlyBase
    23. ventral furrow formation Source: FlyBase

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 1994.
    ReactomeiREACT_180258. Factors involved in megakaryocyte development and platelet production.
    REACT_181315. Regulation of actin dynamics for phagocytic cup formation.
    SignaLinkiP00522.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Abl (EC:2.7.10.2)
    Alternative name(s):
    D-ash
    Protein abelson
    Gene namesi
    Name:Abl
    Synonyms:ABL-1, Dash
    ORF Names:CG4032
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0000017. Abl.

    Subcellular locationi

    GO - Cellular componenti

    1. adherens junction Source: FlyBase
    2. apical cortex Source: FlyBase
    3. axon Source: FlyBase
    4. cell-cell junction Source: FlyBase
    5. cell cortex Source: FlyBase
    6. cytoplasm Source: FlyBase
    7. cytosol Source: FlyBase
    8. extrinsic component of plasma membrane Source: FlyBase
    9. muscle tendon junction Source: FlyBase

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Both loss- and gain-of-function mutants exhibit neurons within the pCC/MP2 pathway that incorrectly project across the midline. Loss of Abl disrupts cell migration and cell shape changes during dorsal closure.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 16201620Tyrosine-protein kinase AblPRO_0000088054Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei522 – 5221Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1497 – 14971Phosphotyrosine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP00522.

    Expressioni

    Tissue specificityi

    Arm and ena colocalize with Abl at adherens junctions throughout development.2 Publications

    Developmental stagei

    Expressed both maternally and zygotically.1 Publication

    Gene expression databases

    BgeeiP00522.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    enaQ8T4F72EBI-534090,EBI-466810
    LarP166214EBI-534090,EBI-668630

    Protein-protein interaction databases

    BioGridi69904. 15 interactions.
    IntActiP00522. 4 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP00522.
    SMRiP00522. Positions 172-639.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini187 – 24862SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini254 – 34693SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini371 – 627257Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi510 – 53425Kinase activation loopBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 9291Gly/Ser-richAdd
    BLAST
    Compositional biasi1056 – 108025Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL 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.
    InParanoidiP00522.
    KOiK06619.
    OrthoDBiEOG7GTT2V.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR015015. F-actin_binding.
    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]
    PfamiPF08919. F_actin_bind. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00808. FABD. 1 hit.
    SM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 2 hits.
    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.

    P00522-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAQQGKDRG AHSGGGGSGA PVSCIGLSSS PVASVSPHCI SSSSGVSSAP     50
    LGGGSTLRGS RIKSSSSGVA SGSGSGGGGG GSGSGLSQRS GGHKDARCNP 100
    TVGLNIFTEH NEALLQSRPL PHIPAGSTAA SLLADAAELQ QHQQDSGGLG 150
    LQGSSLGGGH SSTTSVFESA HRWTSKENLL APGPEEDDPQ LFVALYDFQA 200
    GGENQLSLKK GEQVRILSYN KSGEWCEAHS DSGNVGWVPS NYVTPLNSLE 250
    KHSWYHGPIS RNAAEYLLSS GINGSFLVRE SESSPGQRSI SLRYEGRVYH 300
    YRISEDPDGK VFVTQEAKFN TLAELVHHHS VPHEGHGLIT PLLYPAPKQN 350
    KPTVFPLSPE PDEWEICRTD IMMKHKLGGG QYGEVYEAVW KRYGNTVAVK 400
    TLKEDTMALK DFLEEAAIMK EMKHPNLVQL IGVCTREPPF YIITEFMSHG 450
    NLLDFLRSAG RETLDAVALL YMATQIASGM SYLESRNYIH RDLAARNCLV 500
    GDNKLVKVAD FGLARLMRDD TYTAHAGAKF PIKWTAPEGL AYNKFSTKSD 550
    VWAFGVLLWE IATYGMSPYP AIDLTDVYHK LDKGYRMERP PGCPPEVYDL 600
    MRQCWQWDAT DRPTFKSIHH ALEHMFQESS ITEAVEKQLN ANATSASSSA 650
    PSTSGVATGG GATTTTAASG CASSSSATAS LSLTPQMVKK GLPGGQALTP 700
    NAHHNDPHQQ QASTPMSETG STSTKLSTFS SQGKGNVQMR RTTNKQGKQA 750
    PAPPKRTSLL SSSRDSTYRE EDPANARCNF IDDLSTNGLA RDINSLTQRY 800
    DSETDPAADP DTDATGDSLE QSLSQVIAAP VTNKMQHSLH SGGGGGGIGP 850
    RSSQQHSSFK RPTGTPVMGN RGLETRQSKR SQLHSQAPGP GPPSTQPHHG 900
    NNGVVTSAHP ITVGALDVMN VKQVVNRYGT LPKGARIGAY LDSLEDSSEA 950
    APALPATAPS LPPANGHATP PAARLNPKAS PIPPQQMIRS NSSGGVTMQN 1000
    NAAASLNKLQ RHRTTTEGTM MTFSSFRAGG SSSSPKRSAS GVASGVQPAL 1050
    ANLEFPPPPL DLPPPPEEFE GGPPPPPPAP ESAVQAIQQH LHAQLPNNGN 1100
    ISNGNGTNNN DSSHNDVSNI APSVEEASSR FGVSLRKREP STDSCSSLGS 1150
    PPEDLKEKLI TEIKAAGKDT APASHLANGS GIAVVDPVSL LVTELAESMN 1200
    LPKPPPQQQQ KLTNGNSTGS GFKAQLKKVE PKKMSAPMPK AEPANTIIDF 1250
    KAHLRRVDKE KEPATPAPAP ATVAVANNAN CNTTGTLNRK EDGSKKFSQA 1300
    MQKTEIKIDV TNSNVEADAG AAGEGDLGKR RSTGSINSLK KLWEQQPPAP 1350
    DYATSTILQQ QPSVVNGGGT PNAQLSPKYG MKSGAINTVG TLPAKLGNKQ 1400
    PPAAPPPPPP NCTTSNSSTT SISTSSRDCT SRQQASSTIK TSHSTQLFTD 1450
    DEEQSHTEGL GSGGQGSADM TQSLYEQKPQ IQQKPAVPHK PTKLTIYATP 1500
    IAKLTEPASS ASSTQISRES ILELVGLLEG SLKHPVNAIA GSQWLQLSDK 1550
    LNILHNSCVI FAENGAMPPH SKFQFRELVT RVEAQSQHLR SAGSKNVQDN 1600
    ERLVAEVGQS LRQISNALNR 1620
    Length:1,620
    Mass (Da):171,588
    Last modified:April 12, 2005 - v3
    Checksum:i14287B02CC8FE86B
    GO

    Sequence cautioni

    The sequence AAL13726.1 differs from that shown. Reason: Frameshift at position 323.
    The sequence AAA28934.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti129 – 1368AASLLADA → RPLFWRI in AAA28934. (PubMed:2832740)Curated
    Sequence conflicti357 – 3604LSPE → ASAQ(PubMed:6317185)Curated
    Sequence conflicti628 – 6314ESSI → VGDV(PubMed:6317185)Curated
    Sequence conflicti1241 – 12433AEP → RT in AAA28934. (PubMed:2832740)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19692, M19690, M19691 Genomic DNA. Translation: AAA28934.1. Sequence problems.
    AE014296 Genomic DNA. Translation: AAF49431.2.
    AY058497 mRNA. Translation: AAL13726.1. Frameshift.
    K01042 Genomic DNA. Translation: AAA28443.1.
    PIRiA28128. TVFFA.
    RefSeqiNP_524843.2. NM_080104.3.
    UniGeneiDm.5397.

    Genome annotation databases

    EnsemblMetazoaiFBtr0075357; FBpp0075116; FBgn0000017.
    GeneIDi45821.
    KEGGidme:Dmel_CG4032.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19692 , M19690 , M19691 Genomic DNA. Translation: AAA28934.1 . Sequence problems.
    AE014296 Genomic DNA. Translation: AAF49431.2 .
    AY058497 mRNA. Translation: AAL13726.1 . Frameshift.
    K01042 Genomic DNA. Translation: AAA28443.1 .
    PIRi A28128. TVFFA.
    RefSeqi NP_524843.2. NM_080104.3.
    UniGenei Dm.5397.

    3D structure databases

    ProteinModelPortali P00522.
    SMRi P00522. Positions 172-639.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 69904. 15 interactions.
    IntActi P00522. 4 interactions.

    Proteomic databases

    PaxDbi P00522.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0075357 ; FBpp0075116 ; FBgn0000017 .
    GeneIDi 45821.
    KEGGi dme:Dmel_CG4032.

    Organism-specific databases

    CTDi 45821.
    FlyBasei FBgn0000017. Abl.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00640000091347.
    InParanoidi P00522.
    KOi K06619.
    OrthoDBi EOG7GTT2V.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 1994.
    Reactomei REACT_180258. Factors involved in megakaryocyte development and platelet production.
    REACT_181315. Regulation of actin dynamics for phagocytic cup formation.
    SignaLinki P00522.

    Miscellaneous databases

    GenomeRNAii 45821.
    NextBioi 838372.
    PROi P00522.

    Gene expression databases

    Bgeei P00522.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR015015. F-actin_binding.
    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 PF08919. F_actin_bind. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00808. FABD. 1 hit.
    SM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 2 hits.
    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. "DNA sequence, structure, and tyrosine kinase activity of the Drosophila melanogaster Abelson proto-oncogene homolog."
      Henkemeyer M.J., Bennett R.L., Gertler F.B., Hoffmann F.M.
      Mol. Cell. Biol. 8:843-853(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, 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] OF 61-1620.
      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 357-631.
    6. "Roles of Armadillo, a Drosophila catenin, during central nervous system development."
      Loureiro J., Peifer M.
      Curr. Biol. 8:622-632(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    7. "Abelson kinase regulates epithelial morphogenesis in Drosophila."
      Grevengoed E.E., Loureiro J.J., Jesse T.L., Peifer M.
      J. Cell Biol. 155:1185-1198(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    8. "Abelson tyrosine kinase is required to transduce midline repulsive cues."
      Hsouna A., Kim Y.-S., VanBerkum M.F.A.
      J. Neurobiol. 57:15-30(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
      Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
      Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1497, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiABL_DROME
    AccessioniPrimary (citable) accession number: P00522
    Secondary accession number(s): Q95TV1, Q9VV86
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: April 12, 2005
    Last modified: October 1, 2014
    This is version 158 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