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UniProtKB/Swiss-Prot entry P00522


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ABL_DROME
Primary accession number P00522
Secondary accession numbers Q95TV1 Q9VV86
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on April 12, 2005 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 102)
Name and origin of the protein
Protein name Tyrosine-protein kinase Abl
Synonyms EC 2.7.10.2
Abelson protein
D-ash
Gene name
Name: Abl
Synonyms: ABL-1, Dash
ORFNames: CG4032
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
PubMed=2832740 [NCBI, ExPASy, EBI, Israel, Japan]
Henkemeyer M.J., Bennett R.L., Gertler F.B., Hoffmann F.M.;
"DNA sequence, structure, and tyrosine kinase activity of the Drosophila melanogaster Abelson proto-oncogene homolog.";
Mol. Cell. Biol. 8:843-853(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-1620.
STRAIN=Berkeley;
TISSUE=Embryo;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-631.
DOI=10.1016/0092-8674(83)90172-1; PubMed=6317185 [NCBI, ExPASy, EBI, Israel, Japan]
Hoffmann F.M., Fresco L.D., Hoffman-Falk H., Shilo B.-Z.;
"Nucleotide sequences of the Drosophila src and abl homologs: conservation and variability in the src family oncogenes.";
Cell 35:393-401(1983).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1016/S0960-9822(98)70249-0; PubMed=9635189 [NCBI, ExPASy, EBI, Israel, Japan]
Loureiro J., Peifer M.;
"Roles of Armadillo, a Drosophila catenin, during central nervous system development.";
Curr. Biol. 8:622-632(1998).
[7]
FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1083/jcb.200105102; PubMed=11756472 [NCBI, ExPASy, EBI, Israel, Japan]
Grevengoed E.E., Loureiro J.J., Jesse T.L., Peifer M.;
"Abelson kinase regulates epithelial morphogenesis in Drosophila.";
J. Cell Biol. 155:1185-1198(2001).
[8]
FUNCTION.
DOI=10.1002/neu.10232; PubMed=12973825 [NCBI, ExPASy, EBI, Israel, Japan]
Hsouna A., Kim Y.-S., VanBerkum M.F.A.;
"Abelson tyrosine kinase is required to transduce midline repulsive cues.";
J. Neurobiol. 57:15-30(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1497, AND MASS SPECTROMETRY.
DOI=10.1039/b617545g; PubMed=17372656 [NCBI, ExPASy, EBI, Israel, Japan]
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M19692; AAA28934.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19690; AAA28934.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19691; AAA28934.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014296; AAF49431.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY058497; AAL13726.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K01042; AAA28443.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A28128; TVFFA.
RefSeq NP_524843.2; -.
UniGene Dm.5397
3D structure databases
HSSP P00519; 1OPL. [HSSP ENTRY / PDB]
SMR P00522; 191-639.
ModBase P00522.
Protein-protein interaction databases
IntAct P00522; -.
Organism-specific databases
FlyBase FBgn0000017; Abl.
Gene expression databases
ArrayExpress P00522; -.
GermOnline CG4032; Drosophila melanogaster.
Ontologies
GO
GO:0045179; Cellular component: apical cortex (inferred from direct assay from FlyBase).
GO:0005911; Cellular component: cell-cell junction (inferred from direct assay from FlyBase).
GO:0005829; Cellular component: cytosol (inferred from direct assay from FlyBase).
GO:0019897; Cellular component: extrinsic to plasma membrane (inferred from direct assay from FlyBase).
GO:0005927; Cellular component: muscle tendon junction (inferred from direct assay from FlyBase).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004713; Molecular function: protein tyrosine kinase activity (inferred from direct assay from FlyBase).
GO:0007411; Biological process: axon guidance (inferred from mutant phenotype from FlyBase).
GO:0007417; Biological process: central nervous system development (inferred from genetic interaction from FlyBase).
GO:0007391; Biological process: dorsal closure (inferred from mutant phenotype from FlyBase).
GO:0018108; Biological process: peptidyl-tyrosine phosphorylation (inferred from mutant phenotype from FlyBase).
GO:0008064; Biological process: regulation of actin polymerization or depolymerization (traceable author statement from FlyBase).
GO:0008360; Biological process: regulation of cell shape (inferred from mutant phenotype from FlyBase).
GO:0032880; Biological process: regulation of protein localization (inferred from direct assay from FlyBase).
GO:0031647; Biological process: regulation of protein stability (inferred from mutant phenotype from FlyBase).
GO:0007370; Biological process: ventral furrow formation (inferred from mutant phenotype from FlyBase).
QuickGo view.
Family and domain databases
InterPro IPR015015; F_actin_bd.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR000980; SH2.
IPR001452; SH3.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
Graphical view of domain structure.
Gene3D G3DSA:3.30.505.10; SH2; 1.
Pfam PF07714; Pkinase_Tyr; 1.
PF00017; SH2; 1.
PF00018; SH3_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00401; SH2DOMAIN.
PR00452; SH3DOMAIN.
PR00109; TYRKINASE.
ProDom PD000001; Prot_kinase; 1.
PD000093; SH2; 1.
PD000066; SH3; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00808; FABD; 1.
SM00252; SH2; 1.
SM00326; SH3; 1.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS50001; SH2; 1.
PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P00522.
ProtoNet P00522.
Genome annotation databases
Ensembl CG4032; Drosophila melanogaster. [Contig view]
GeneID 45821; -.
NMPDR fig|7227.3.peg.10185; -.
Phylogenomic databases
HOGENOM P00522; -.
Other
NextBio 838372; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein; SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1620  1620     Tyrosine-protein kinase Abl. PRO_0000088054
DOMAIN   187    248  62     SH3. 
DOMAIN   254    346  93     SH2. 
DOMAIN   371    627  257     Protein kinase. 
NP_BIND   377    385  9     ATP (By similarity). 
COMPBIAS   2     92  91     Gly/Ser-rich. 
COMPBIAS   1056   1080  25     Pro-rich. 
ACT_SITE   492    492        Proton acceptor (By similarity). 
BINDING   400    400        ATP (By similarity). 
MOD_RES   522    522        Phosphotyrosine; by autocatalysis (By similarity). 
MOD_RES   1497   1497        Phosphotyrosine. 
CONFLICT   129    136        AASLLADA -> RPLFWRI (in Ref. 1; AAA28934). 
CONFLICT   357    360        LSPE -> ASAQ (in Ref. 5). 
CONFLICT   628    631        ESSI -> VGDV (in Ref. 5). 
CONFLICT   1241   1243        AEP -> RT (in Ref. 1; AAA28934). 
Sequence information
Length: 1620 AA [This is the length of the unprocessed precursor] Molecular weight: 171588 Da [This is the MW of the unprocessed precursor] CRC64: 14287B02CC8FE86B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGAQQGKDRG AHSGGGGSGA PVSCIGLSSS PVASVSPHCI SSSSGVSSAP LGGGSTLRGS 

        70         80         90        100        110        120 
RIKSSSSGVA SGSGSGGGGG GSGSGLSQRS GGHKDARCNP TVGLNIFTEH NEALLQSRPL 

       130        140        150        160        170        180 
PHIPAGSTAA SLLADAAELQ QHQQDSGGLG LQGSSLGGGH SSTTSVFESA HRWTSKENLL 

       190        200        210        220        230        240 
APGPEEDDPQ LFVALYDFQA GGENQLSLKK GEQVRILSYN KSGEWCEAHS DSGNVGWVPS 

       250        260        270        280        290        300 
NYVTPLNSLE KHSWYHGPIS RNAAEYLLSS GINGSFLVRE SESSPGQRSI SLRYEGRVYH 

       310        320        330        340        350        360 
YRISEDPDGK VFVTQEAKFN TLAELVHHHS VPHEGHGLIT PLLYPAPKQN KPTVFPLSPE 

       370        380        390        400        410        420 
PDEWEICRTD IMMKHKLGGG QYGEVYEAVW KRYGNTVAVK TLKEDTMALK DFLEEAAIMK 

       430        440        450        460        470        480 
EMKHPNLVQL IGVCTREPPF YIITEFMSHG NLLDFLRSAG RETLDAVALL YMATQIASGM 

       490        500        510        520        530        540 
SYLESRNYIH RDLAARNCLV GDNKLVKVAD FGLARLMRDD TYTAHAGAKF PIKWTAPEGL 

       550        560        570        580        590        600 
AYNKFSTKSD VWAFGVLLWE IATYGMSPYP AIDLTDVYHK LDKGYRMERP PGCPPEVYDL 

       610        620        630        640        650        660 
MRQCWQWDAT DRPTFKSIHH ALEHMFQESS ITEAVEKQLN ANATSASSSA PSTSGVATGG 

       670        680        690        700        710        720 
GATTTTAASG CASSSSATAS LSLTPQMVKK GLPGGQALTP NAHHNDPHQQ QASTPMSETG 

       730        740        750        760        770        780 
STSTKLSTFS SQGKGNVQMR RTTNKQGKQA PAPPKRTSLL SSSRDSTYRE EDPANARCNF 

       790        800        810        820        830        840 
IDDLSTNGLA RDINSLTQRY DSETDPAADP DTDATGDSLE QSLSQVIAAP VTNKMQHSLH 

       850        860        870        880        890        900 
SGGGGGGIGP RSSQQHSSFK RPTGTPVMGN RGLETRQSKR SQLHSQAPGP GPPSTQPHHG 

       910        920        930        940        950        960 
NNGVVTSAHP ITVGALDVMN VKQVVNRYGT LPKGARIGAY LDSLEDSSEA APALPATAPS 

       970        980        990       1000       1010       1020 
LPPANGHATP PAARLNPKAS PIPPQQMIRS NSSGGVTMQN NAAASLNKLQ RHRTTTEGTM 

      1030       1040       1050       1060       1070       1080 
MTFSSFRAGG SSSSPKRSAS GVASGVQPAL ANLEFPPPPL DLPPPPEEFE GGPPPPPPAP 

      1090       1100       1110       1120       1130       1140 
ESAVQAIQQH LHAQLPNNGN ISNGNGTNNN DSSHNDVSNI APSVEEASSR FGVSLRKREP 

      1150       1160       1170       1180       1190       1200 
STDSCSSLGS PPEDLKEKLI TEIKAAGKDT APASHLANGS GIAVVDPVSL LVTELAESMN 

      1210       1220       1230       1240       1250       1260 
LPKPPPQQQQ KLTNGNSTGS GFKAQLKKVE PKKMSAPMPK AEPANTIIDF KAHLRRVDKE 

      1270       1280       1290       1300       1310       1320 
KEPATPAPAP ATVAVANNAN CNTTGTLNRK EDGSKKFSQA MQKTEIKIDV TNSNVEADAG 

      1330       1340       1350       1360       1370       1380 
AAGEGDLGKR RSTGSINSLK KLWEQQPPAP DYATSTILQQ QPSVVNGGGT PNAQLSPKYG 

      1390       1400       1410       1420       1430       1440 
MKSGAINTVG TLPAKLGNKQ PPAAPPPPPP NCTTSNSSTT SISTSSRDCT SRQQASSTIK 

      1450       1460       1470       1480       1490       1500 
TSHSTQLFTD DEEQSHTEGL GSGGQGSADM TQSLYEQKPQ IQQKPAVPHK PTKLTIYATP 

      1510       1520       1530       1540       1550       1560 
IAKLTEPASS ASSTQISRES ILELVGLLEG SLKHPVNAIA GSQWLQLSDK LNILHNSCVI 

      1570       1580       1590       1600       1610       1620 
FAENGAMPPH SKFQFRELVT RVEAQSQHLR SAGSKNVQDN ERLVAEVGQS LRQISNALNR 

P00522 in FASTA format

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