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Tyrosine-protein kinase Abl (EC 2.7.10.2) (D-ash) (Protein abelson)

 ABL_DROME               Reviewed;        1620 AA.
P00522; Q95TV1; Q9VV86;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
12-APR-2005, sequence version 3.
12-SEP-2018, entry version 197.
RecName: Full=Tyrosine-protein kinase Abl;
EC=2.7.10.2;
AltName: Full=D-ash;
AltName: Full=Protein abelson;
Name=Abl; Synonyms=ABL-1, Dash; ORFNames=CG4032;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND
DEVELOPMENTAL STAGE.
PubMed=2832740; DOI=10.1128/MCB.8.2.843;
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;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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; DOI=10.1186/gb-2002-3-12-research0080;
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.
PubMed=6317185; DOI=10.1016/0092-8674(83)90172-1;
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, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=9635189; DOI=10.1016/S0960-9822(98)70249-0;
Loureiro J., Peifer M.;
"Roles of Armadillo, a Drosophila catenin, during central nervous
system development.";
Curr. Biol. 8:622-632(1998).
[7]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=11756472; DOI=10.1083/jcb.200105102;
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.
PubMed=12973825; DOI=10.1002/neu.10232;
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 IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=17372656; DOI=10.1039/b617545g;
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).
-!- 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.
{ECO:0000269|PubMed:11756472, ECO:0000269|PubMed:12973825,
ECO:0000269|PubMed:9635189}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:2832740}.
-!- INTERACTION:
Q8T4F7:ena; NbExp=2; IntAct=EBI-534090, EBI-466810;
P16621:Lar; NbExp=4; IntAct=EBI-534090, EBI-668630;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Arm and ena colocalize with Abl at adherens
junctions throughout development. {ECO:0000269|PubMed:11756472,
ECO:0000269|PubMed:9635189}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
{ECO:0000269|PubMed:2832740}.
-!- 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.
{ECO:0000269|PubMed:11756472, ECO:0000269|PubMed:9635189}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. ABL subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAA28934.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAL13726.1; Type=Frameshift; Positions=323; Evidence={ECO:0000305};
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EMBL; M19692; AAA28934.1; ALT_SEQ; Genomic_DNA.
EMBL; M19690; AAA28934.1; JOINED; Genomic_DNA.
EMBL; M19691; AAA28934.1; JOINED; Genomic_DNA.
EMBL; AE014296; AAF49431.2; -; Genomic_DNA.
EMBL; AY058497; AAL13726.1; ALT_FRAME; mRNA.
EMBL; K01042; AAA28443.1; -; Genomic_DNA.
PIR; A28128; TVFFA.
RefSeq; NP_001287085.1; NM_001300156.1.
RefSeq; NP_524843.2; NM_080104.3.
UniGene; Dm.5397; -.
ProteinModelPortal; P00522; -.
SMR; P00522; -.
BioGrid; 69904; 40.
IntAct; P00522; 8.
STRING; 7227.FBpp0303166; -.
iPTMnet; P00522; -.
PaxDb; P00522; -.
PRIDE; P00522; -.
EnsemblMetazoa; FBtr0075357; FBpp0075116; FBgn0000017.
EnsemblMetazoa; FBtr0345369; FBpp0311523; FBgn0000017.
GeneID; 45821; -.
KEGG; dme:Dmel_CG4032; -.
CTD; 45821; -.
FlyBase; FBgn0000017; Abl.
eggNOG; KOG4278; Eukaryota.
eggNOG; COG0515; LUCA.
InParanoid; P00522; -.
KO; K06619; -.
OMA; NMFQESS; -.
OrthoDB; EOG091G0D46; -.
BRENDA; 2.7.10.2; 1994.
Reactome; R-DME-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-DME-375170; CDO in myogenesis.
Reactome; R-DME-428890; Role of ABL in ROBO-SLIT signaling.
Reactome; R-DME-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-DME-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
SignaLink; P00522; -.
GenomeRNAi; 45821; -.
PRO; PR:P00522; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0000017; Expressed in 23 organ(s), highest expression level in head.
ExpressionAtlas; P00522; baseline and differential.
Genevisible; P00522; DM.
GO; GO:0005912; C:adherens junction; TAS:FlyBase.
GO; GO:0045179; C:apical cortex; IDA:FlyBase.
GO; GO:0030424; C:axon; IDA:FlyBase.
GO; GO:0005938; C:cell cortex; IDA:FlyBase.
GO; GO:0005911; C:cell-cell junction; IDA:FlyBase.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005829; C:cytosol; IDA:FlyBase.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:FlyBase.
GO; GO:0005927; C:muscle tendon junction; IDA:FlyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:FlyBase.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:FlyBase.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0003401; P:axis elongation; IMP:FlyBase.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0016199; P:axon midline choice point recognition; IMP:FlyBase.
GO; GO:0007409; P:axonogenesis; IGI:FlyBase.
GO; GO:0021785; P:branchiomotor neuron axon guidance; IMP:CACAO.
GO; GO:0007417; P:central nervous system development; IGI:FlyBase.
GO; GO:0007268; P:chemical synaptic transmission; IMP:CACAO.
GO; GO:0048749; P:compound eye development; IGI:FlyBase.
GO; GO:0007303; P:cytoplasmic transport, nurse cell to oocyte; IMP:FlyBase.
GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
GO; GO:0003382; P:epithelial cell morphogenesis; IMP:FlyBase.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007611; P:learning or memory; IMP:CACAO.
GO; GO:0002009; P:morphogenesis of an epithelium; NAS:FlyBase.
GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
GO; GO:0010977; P:negative regulation of neuron projection development; IMP:CACAO.
GO; GO:0045886; P:negative regulation of synaptic growth at neuromuscular junction; IMP:FlyBase.
GO; GO:0001764; P:neuron migration; IMP:FlyBase.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:FlyBase.
GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:CACAO.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:FlyBase.
GO; GO:0046777; P:protein autophosphorylation; IDA:FlyBase.
GO; GO:0006468; P:protein phosphorylation; NAS:FlyBase.
GO; GO:0008064; P:regulation of actin polymerization or depolymerization; TAS:FlyBase.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase.
GO; GO:0032880; P:regulation of protein localization; IDA:FlyBase.
GO; GO:0031647; P:regulation of protein stability; IMP:FlyBase.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
GO; GO:0007419; P:ventral cord development; IMP:FlyBase.
GO; GO:0007370; P:ventral furrow formation; IMP:FlyBase.
CDD; cd09935; SH2_ABL; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR033221; ABL1.
InterPro; IPR035837; ABL_SH2.
InterPro; IPR015015; F-actin_binding.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
PANTHER; PTHR24418:SF88; PTHR24418:SF88; 1.
Pfam; PF08919; F_actin_bind; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00808; FABD; 1.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 2.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
Phosphoprotein; Reference proteome; SH2 domain; SH3 domain;
Transferase; Tyrosine-protein kinase.
CHAIN 1 1620 Tyrosine-protein kinase Abl.
/FTId=PRO_0000088054.
DOMAIN 187 248 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 254 346 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 371 627 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 377 385 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 445 451 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 510 534 Kinase activation loop. {ECO:0000250}.
COMPBIAS 2 92 Gly/Ser-rich.
COMPBIAS 1056 1080 Pro-rich.
ACT_SITE 492 492 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 400 400 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 522 522 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 1497 1497 Phosphotyrosine.
{ECO:0000269|PubMed:17372656}.
CONFLICT 129 136 AASLLADA -> RPLFWRI (in Ref. 1;
AAA28934). {ECO:0000305}.
CONFLICT 357 360 LSPE -> ASAQ (in Ref. 5). {ECO:0000305}.
CONFLICT 628 631 ESSI -> VGDV (in Ref. 5). {ECO:0000305}.
CONFLICT 1241 1243 AEP -> RT (in Ref. 1; AAA28934).
{ECO:0000305}.
SEQUENCE 1620 AA; 171588 MW; 14287B02CC8FE86B CRC64;
MGAQQGKDRG AHSGGGGSGA PVSCIGLSSS PVASVSPHCI SSSSGVSSAP LGGGSTLRGS
RIKSSSSGVA SGSGSGGGGG GSGSGLSQRS GGHKDARCNP TVGLNIFTEH NEALLQSRPL
PHIPAGSTAA SLLADAAELQ QHQQDSGGLG LQGSSLGGGH SSTTSVFESA HRWTSKENLL
APGPEEDDPQ LFVALYDFQA GGENQLSLKK GEQVRILSYN KSGEWCEAHS DSGNVGWVPS
NYVTPLNSLE KHSWYHGPIS RNAAEYLLSS GINGSFLVRE SESSPGQRSI SLRYEGRVYH
YRISEDPDGK VFVTQEAKFN TLAELVHHHS VPHEGHGLIT PLLYPAPKQN KPTVFPLSPE
PDEWEICRTD IMMKHKLGGG QYGEVYEAVW KRYGNTVAVK TLKEDTMALK DFLEEAAIMK
EMKHPNLVQL IGVCTREPPF YIITEFMSHG NLLDFLRSAG RETLDAVALL YMATQIASGM
SYLESRNYIH RDLAARNCLV GDNKLVKVAD FGLARLMRDD TYTAHAGAKF PIKWTAPEGL
AYNKFSTKSD VWAFGVLLWE IATYGMSPYP AIDLTDVYHK LDKGYRMERP PGCPPEVYDL
MRQCWQWDAT DRPTFKSIHH ALEHMFQESS ITEAVEKQLN ANATSASSSA PSTSGVATGG
GATTTTAASG CASSSSATAS LSLTPQMVKK GLPGGQALTP NAHHNDPHQQ QASTPMSETG
STSTKLSTFS SQGKGNVQMR RTTNKQGKQA PAPPKRTSLL SSSRDSTYRE EDPANARCNF
IDDLSTNGLA RDINSLTQRY DSETDPAADP DTDATGDSLE QSLSQVIAAP VTNKMQHSLH
SGGGGGGIGP RSSQQHSSFK RPTGTPVMGN RGLETRQSKR SQLHSQAPGP GPPSTQPHHG
NNGVVTSAHP ITVGALDVMN VKQVVNRYGT LPKGARIGAY LDSLEDSSEA APALPATAPS
LPPANGHATP PAARLNPKAS PIPPQQMIRS NSSGGVTMQN NAAASLNKLQ RHRTTTEGTM
MTFSSFRAGG SSSSPKRSAS GVASGVQPAL ANLEFPPPPL DLPPPPEEFE GGPPPPPPAP
ESAVQAIQQH LHAQLPNNGN ISNGNGTNNN DSSHNDVSNI APSVEEASSR FGVSLRKREP
STDSCSSLGS PPEDLKEKLI TEIKAAGKDT APASHLANGS GIAVVDPVSL LVTELAESMN
LPKPPPQQQQ KLTNGNSTGS GFKAQLKKVE PKKMSAPMPK AEPANTIIDF KAHLRRVDKE
KEPATPAPAP ATVAVANNAN CNTTGTLNRK EDGSKKFSQA MQKTEIKIDV TNSNVEADAG
AAGEGDLGKR RSTGSINSLK KLWEQQPPAP DYATSTILQQ QPSVVNGGGT PNAQLSPKYG
MKSGAINTVG TLPAKLGNKQ PPAAPPPPPP NCTTSNSSTT SISTSSRDCT SRQQASSTIK
TSHSTQLFTD DEEQSHTEGL GSGGQGSADM TQSLYEQKPQ IQQKPAVPHK PTKLTIYATP
IAKLTEPASS ASSTQISRES ILELVGLLEG SLKHPVNAIA GSQWLQLSDK LNILHNSCVI
FAENGAMPPH SKFQFRELVT RVEAQSQHLR SAGSKNVQDN ERLVAEVGQS LRQISNALNR


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10-782-55014 Cytoplasmic tyrosine-protein kinase BMX - EC 2.7.10.2; Bone marrow tyrosine kinase gene in chromosome X protein; Epithelial and endothelial tyrosine kinase; ETK; NTK38 N_A 0.001 mg
EIAAB13074 Eck,Epha2,Ephrin type-A receptor 2,Epithelial cell kinase,Mouse,Mus musculus,Myk2,Sek2,Tyrosine-protein kinase receptor ECK,Tyrosine-protein kinase receptor MPK-5,Tyrosine-protein kinase receptor SEK-
U1915m CLIA kit Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T
U1915m CLIA Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T
E1915m ELISA Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T
E1915m ELISA kit Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T
EIAAB44682 Dtk,Etk2_tyro3,Mouse,Mus musculus,Rse,TK19-2,Tyro3,Tyrosine-protein kinase DTK,Tyrosine-protein kinase receptor TYRO3,Tyrosine-protein kinase RSE
E1915h ELISA Agammaglobulinaemia tyrosine kinase,AGMX1,ATK,ATK,B-cell progenitor kinase,BPK,BPK,Bruton tyrosine kinase,BTK,Homo sapiens,Human,Tyrosine-protein kinase BTK 96T
E1915h ELISA kit Agammaglobulinaemia tyrosine kinase,AGMX1,ATK,ATK,B-cell progenitor kinase,BPK,BPK,Bruton tyrosine kinase,BTK,Homo sapiens,Human,Tyrosine-protein kinase BTK 96T
U1915h CLIA Agammaglobulinaemia tyrosine kinase,AGMX1,ATK,ATK,B-cell progenitor kinase,BPK,BPK,Bruton tyrosine kinase,BTK,Homo sapiens,Human,Tyrosine-protein kinase BTK 96T
U1915h CLIA kit Agammaglobulinaemia tyrosine kinase,AGMX1,ATK,ATK,B-cell progenitor kinase,BPK,BPK,Bruton tyrosine kinase,BTK,Homo sapiens,Human,Tyrosine-protein kinase BTK 96T
E0039m ELISA kit Fetal liver kinase 2,FL cytokine receptor,FLK-2,Flk-2,Flt3,FLT-3,Flt-3,Fms-like tyrosine kinase 3,Mouse,Mus musculus,Receptor-type tyrosine-protein kinase FLT3,Tyrosine-protein kinase recep 96T


 

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