Reviewed, UniProtKB/Swiss-Prot P00522 (ABL_DROME)

Names and origin

Protein names

Recommended name:
    Tyrosine-protein kinase Abl
    EC=2.7.10.2
Alternative name(s):
    Abelson protein
      Short name=D-ash

Gene names

Name:	Abl
Synonyms:	ABL-1, Dash
ORF Names:	CG4032

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	1620 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subcellular location	Cytoplasm.
Tissue specificity	Arm and ena colocalize with Abl at adherens junctions throughout development.
Developmental stage	Expressed both maternally and zygotically.
Miscellaneous	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.
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 component	Cytoplasm
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	axon guidance Inferred from mutant phenotype. Source: FlyBase central nervous system development Inferred from genetic interaction. Source: FlyBase dorsal closure Ref.7 Inferred from mutant phenotype. Source: FlyBase peptidyl-tyrosine phosphorylation Inferred from mutant phenotype. Source: FlyBase regulation of actin polymerization or depolymerization Traceable author statement. Source: FlyBase regulation of cell shape Inferred from mutant phenotype. Source: FlyBase regulation of protein localization Inferred from direct assay. Source: FlyBase regulation of protein stability Inferred from mutant phenotype. Source: FlyBase ventral furrow formation Inferred from mutant phenotype. Source: FlyBase
Cellular component	apical cortex Inferred from direct assay. Source: FlyBase cell-cell junction Inferred from direct assay. Source: FlyBase cytosol Inferred from direct assay. Source: FlyBase extrinsic to plasma membrane Inferred from direct assay. Source: FlyBase muscle tendon junction Inferred from direct assay. Source: FlyBase
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB protein tyrosine kinase activity Ref.1 Inferred from direct assay. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ena	Q8T4F7	2	EBI-534090,EBI-466810
Lar	P16621	4	EBI-534090,EBI-668630
Ptp69D	P16620	1	EBI-534090,EBI-676392

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 1620	1620	Tyrosine-protein kinase Abl
Regions
	Domain	187 – 248	62	SH3
	Domain	254 – 346	93	SH2
	Domain	371 – 627	257	Protein kinase
	Nucleotide binding	377 – 385	9	ATP By similarity
	Compositional bias	2 – 92	91	Gly/Ser-rich
	Compositional bias	1056 – 1080	25	Pro-rich
Sites
	Active site	492	1	Proton acceptor By similarity
	Binding site	400	1	ATP By similarity
Amino acid modifications
	Modified residue	522	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	1497	1	Phosphotyrosine
Experimental info
	Sequence conflict	129 – 136	8	AASLLADA → RPLFWRI in AAA28934. Ref.1
	Sequence conflict	357 – 360	4	LSPE → ASAQ Ref.5
	Sequence conflict	628 – 631	4	ESSI → VGDV Ref.5
	Sequence conflict	1241 – 1243	3	AEP → RT in AAA28934. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P00522-1 [UniParc]. Last modified April 12, 2005. Version 3. Checksum: 14287B02CC8FE86B	FASTA	1,620	171,588
	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

References

	« Hide 'large scale' referencesShow '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: 2832740] [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: 10731132] [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. , 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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[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: 12537569] [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: 6317185] [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: 9635189] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[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: 11756472] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[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: 12973825] [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: 17372656] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1497, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
PIR	TVFFA. A28128.
RefSeq	NP_524843.2.
UniGene	Dm.5397
3D structure databases
HSSP	HSSP built from PDB template 1OPL based on UniProtKB P00519.
SMR	P00522. Positions 191-639.
ModBase	Search...
Protein-protein interaction databases
IntAct	P00522.
Genome annotation databases
Ensembl	CG4032. Drosophila melanogaster. [Contig view]
GeneID	45821.
NMPDR	fig|7227.3.peg.10185.
Organism-specific databases
FlyBase	FBgn0000017. Abl.
Phylogenomic databases
HOGENOM	P00522.
Gene expression databases
ArrayExpress	P00522.
GermOnline	CG4032. Drosophila melanogaster.
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]
Gene3D	G3DSA:3.30.505.10. SH2. 1 hit.
Pfam	PF07714. Pkinase_Tyr. 1 hit. PF00017. SH2. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00401. SH2DOMAIN. PR00452. SH3DOMAIN. PR00109. TYRKINASE.
ProDom	PD000001. Prot_kinase. 1 hit. PD000093. SH2. 1 hit. PD000066. SH3. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00808. FABD. 1 hit. SM00252. SH2. 1 hit. SM00326. SH3. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
PROSITE	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]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

ABL_DROME

Accession

Primary (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:	September 2, 2008
This is version 101 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project