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P00522 (ABL_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase Abl

EC=2.7.10.2
Alternative name(s):
D-ash
Protein abelson
Gene names
Name:Abl
Synonyms:ABL-1, Dash
ORF Names:CG4032
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1620 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.1

Subcellular location

Cytoplasm.

Tissue specificity

Arm and ena colocalize with Abl at adherens junctions throughout development. Ref.6 Ref.7

Developmental stage

Expressed both maternally and zygotically. Ref.1

Disruption phenotype

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. Ref.6 Ref.7

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Sequence caution

The sequence AAA28934.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAL13726.1 differs from that shown. Reason: Frameshift at position 323.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon midline choice point recognition

Inferred from mutant phenotype Ref.8. Source: FlyBase

compound eye development

Inferred from genetic interaction PubMed 19217428. Source: FlyBase

cytoplasmic transport, nurse cell to oocyte

Inferred from mutant phenotype PubMed 19576200. Source: FlyBase

dorsal closure

Inferred from mutant phenotype Ref.7. Source: FlyBase

epithelial cell morphogenesis

Inferred from mutant phenotype Ref.7. Source: FlyBase

motor neuron axon guidance

Inferred from mutant phenotype PubMed 17568577. Source: FlyBase

negative regulation of synaptic growth at neuromuscular junction

Inferred from mutant phenotype PubMed 19675132. Source: FlyBase

neuron migration

Inferred from mutant phenotype PubMed 21726548. Source: FlyBase

photoreceptor cell axon guidance

Inferred from mutant phenotype PubMed 19217428. Source: FlyBase

planar cell polarity pathway involved in axis elongation

Inferred from mutant phenotype PubMed 22340496. Source: FlyBase

positive regulation of protein export from nucleus

Inferred from mutant phenotype PubMed 19217428. Source: FlyBase

regulation of actin polymerization or depolymerization

Traceable author statement PubMed 12231351. Source: FlyBase

regulation of cell shape

Inferred from mutant phenotype PubMed 14527345PubMed 17202187. Source: FlyBase

regulation of protein stability

Inferred from mutant phenotype PubMed 17804420. Source: FlyBase

ventral cord development

Inferred from mutant phenotype PubMed 19217428. Source: FlyBase

ventral furrow formation

Inferred from mutant phenotype PubMed 17202187. Source: FlyBase

   Cellular_componentapical cortex

Inferred from direct assay PubMed 17202187. Source: FlyBase

axon

Inferred from direct assay PubMed 2175256. Source: FlyBase

cell-cell junction

Inferred from direct assay PubMed 1295746. Source: FlyBase

cytosol

Inferred from direct assay PubMed 17804420. Source: FlyBase

extrinsic component of plasma membrane

Inferred from direct assay PubMed 1295746. Source: FlyBase

muscle tendon junction

Inferred from direct assay PubMed 1295746. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from direct assay PubMed 2175256. Source: FlyBase

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16201620Tyrosine-protein kinase Abl
PRO_0000088054

Regions

Domain187 – 24862SH3
Domain254 – 34693SH2
Domain371 – 627257Protein kinase
Nucleotide binding377 – 3859ATP By similarity
Nucleotide binding445 – 4517ATP By similarity
Motif510 – 53425Kinase activation loop By similarity
Compositional bias2 – 9291Gly/Ser-rich
Compositional bias1056 – 108025Pro-rich

Sites

Active site4921Proton acceptor By similarity
Binding site4001ATP By similarity

Amino acid modifications

Modified residue5221Phosphotyrosine; by autocatalysis By similarity
Modified residue14971Phosphotyrosine Ref.9

Experimental info

Sequence conflict129 – 1368AASLLADA → RPLFWRI in AAA28934. Ref.1
Sequence conflict357 – 3604LSPE → ASAQ Ref.5
Sequence conflict628 – 6314ESSI → VGDV Ref.5
Sequence conflict1241 – 12433AEP → RT in AAA28934. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P00522 [UniParc].

Last modified April 12, 2005. Version 3.
Checksum: 14287B02CC8FE86B

FASTA1,620171,588
        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 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
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.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRTVFFA. A28128.
RefSeqNP_524843.2. NM_080104.3.
UniGeneDm.5397.

3D structure databases

ProteinModelPortalP00522.
SMRP00522. Positions 172-639.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid69904. 15 interactions.
IntActP00522. 4 interactions.

Proteomic databases

PaxDbP00522.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0075357; FBpp0075116; FBgn0000017.
GeneID45821.
KEGGdme:Dmel_CG4032.

Organism-specific databases

CTD45821.
FlyBaseFBgn0000017. Abl.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00640000091347.
InParanoidP00522.
KOK06619.
OrthoDBEOG7GTT2V.

Enzyme and pathway databases

BRENDA2.7.10.2. 1994.
SignaLinkP00522.

Gene expression databases

BgeeP00522.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR015015. 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]
PfamPF08919. F_actin_bind. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00808. FABD. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. 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]
ProtoNetSearch...

Other

GenomeRNAi45821.
NextBio838372.
PROP00522.

Entry information

Entry nameABL_DROME
AccessionPrimary (citable) accession number: P00522
Secondary accession number(s): Q95TV1, Q9VV86
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 12, 2005
Last modified: March 19, 2014
This is version 152 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase