P00520 (ABL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase ABL1
EC=2.7.10.2

Alternative name(s):
Abelson murine leukemia viral oncogene homolog 1
Abelson tyrosine-protein kinase 1
Proto-oncogene c-Abl
p150

Gene names

Name:	Abl1
Synonyms:	Abl

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1123 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-191' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. Ref.11 Ref.12 Ref.13 Ref.18 Ref.19 Ref.20 Ref.22 Ref.24 Ref.25 Ref.27 Ref.33
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.30 Ref.33 Ref.35
Cofactor	Magnesium or manganese.
Enzyme regulation	Stabilized in the inactive form by an association between the SH3 domain and the SH2-TK linker region, interactions of the N-terminal cap, and contributions from an N-terminal myristoyl group and phospholipids. Activated by autophosphorylation as well as by SRC-family kinase-mediated phosphorylation By similarity. Activated by RIN1 binding to the SH2 and SH3 domains. Also stimulated by cell death inducers and DNA-damage By similarity. Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant phosphoinositide known to regulate cytoskeletal and membrane proteins, inhibits also the tyrosine kinase activity. Inhibited by imatinib mesylate (Gleevec). Ref.13 Ref.24 Ref.25 Ref.30 Ref.31 Ref.35
Subunit structure	Interacts with INPPL1/SHIP2. Interacts with SORBS1 following insulin stimulation. Found in a trimolecular complex containing CDK5 and CABLES1. Interacts with CABLES1 and PSTPIP1. Interacts with ZDHHC16. Interacts with the 14-3-3 proteins, YWHAB, YWHAE, YWHAG, YWHAH, SFN AND YWHAZ; the interaction with 14-3-3 proteins requires phosphorylation on Thr-734 and sequesters ABL1 into the cytoplasm. Interacts (via SH3 domain) with CASP9; the interaction is direct and increases in the response of cells to genotoxic stress and ABL1/c-Abl activation By similarity. Interacts with ABI1, ABI2, BCR, CRK, FYN, LYN, PSMA7 RAD9A, RAD51, RAD52, TP73 and WASF3. A complex made of ABL1, CTTN and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement By similarity. Interacts with ITGB1, HCK and FGR. Ref.15 Ref.16 Ref.18 Ref.21 Ref.24 Ref.27
Subcellular location	Cytoplasm › cytoskeleton. Nucleus. Mitochondrion. Note: The myristoylated c-ABL protein is reported to be nuclear. Sequestered into the cytoplasm through interaction with 14-3-3 proteins By similarity. Localizes to mitochondria in response to oxidative stress. Ref.13 Ref.14 Ref.19
Tissue specificity	Widely expressed.
Post-translational modification	Acetylated at Lys-710 by EP300 which promotes the cytoplasmic translocation By similarity. Phosphorylation at Tyr-70 by members of the SRC family of kinases disrupts SH3 domain-based autoinhibitory interactions and intermolecular associations, such as that with ABI1, and also enhances kinase activity By similarity. Phosphorylation at Tyr-226 and Tyr-393 correlate with increased activity By similarity. DNA damage-induced activation of ABL1 requires the function of ATM and Ser-446 phosphorylation. Phosphorylation at Thr-547 and Ser-569 has been attributed to a CDC2-associated kinase and is coupled to cell division. Phosphorylation at Ser-618 and Ser-619 by PAK2 increases binding to CRK and reduces binding to ABI1 By similarity. Phosphorylation on Thr-734 is required for binding 14-3-3 proteins for cytoplasmic translocation By similarity. Phosphorylated by PDGFRB and PRKDC. Ref.7 Ref.10 Ref.13 Ref.24 Ref.25 Ref.27 Ref.30 Ref.35 Polyubiquitinated. Polyubiquitination of ABL1 leads to degradation By similarity. Isoform IV is myristoylated on Gly-2.
Disruption phenotype	Mutants are born with the expected Mendelian frequency, but fail to thrive and most die within three weeks after birth. Most mutants are runted, and have atrophied thymuses with severe thymocyte deficiency. Mutants that survive to weaning age are most often runted, and about half of them show lymphopenia. They display a major reduction in the number of pre-B and immature B-cell classes in bone marrow with a wide variation between individuals, but essentially normal mature B-cell levels. Mutants are highly susceptible to infections. Ref.8 Ref.9
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.

Ontologies

Keywords
Biological process	Apoptosis Autophagy Cell adhesion DNA damage DNA repair Endocytosis
Cellular component	Cytoplasm Cytoskeleton Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding DNA-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Acetylation Lipoprotein Myristate Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage induced protein phosphorylation Inferred from electronic annotation. Source: Compara DNA repair Inferred from electronic annotation. Source: UniProtKB-KW actin cytoskeleton organization Inferred from direct assay Ref.18. Source: UniProtKB apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW autophagy Inferred from electronic annotation. Source: UniProtKB-KW cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW endocytosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of protein serine/threonine kinase activity Inferred from electronic annotation. Source: Compara peptidyl-tyrosine phosphorylation Inferred from direct assay PubMed 11390389Ref.13. Source: UniProtKB platelet-derived growth factor receptor signaling pathway Inferred from direct assay PubMed 20417104. Source: MGI positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of oxidoreductase activity Inferred from electronic annotation. Source: Compara positive regulation of peptidyl-tyrosine phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell cycle Inferred from direct assay PubMed 11809706. Source: MGI regulation of response to DNA damage stimulus Inferred from electronic annotation. Source: Compara signal transduction in response to DNA damage Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cell leading edge Inferred from direct assay PubMed 20417104. Source: MGI cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from sequence alignment PubMed 17101133. Source: MGI mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: Compara nucleus Inferred from direct assay Ref.14. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from direct assay Ref.13. Source: UniProtKB DNA binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from direct assay Ref.13. Source: UniProtKB manganese ion binding Inferred from direct assay Ref.13. Source: UniProtKB non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC proline-rich region binding Inferred from sequence or structural similarity. Source: UniProtKB protein tyrosine kinase activity Inferred from direct assay PubMed 11390389PubMed 15657060Ref.13. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDKN1B	P46527	2	EBI-914519,EBI-519280	From a different organism.
Dok1	P97465	4	EBI-914519,EBI-914917
Nck1	Q99M51	2	EBI-914519,EBI-642202

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform I (identifier: P00520-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform II (identifier: P00520-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MLEICLKLVGCKSKKGLSSSSSCYLE → MISFDLLSDELHLKLLVLDV

Isoform III (identifier: P00520-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MLEICLKLVGCKSKKGLSSSSSCYLE → MSQRWTYTKCRVQRDPALPFM

Isoform IV (identifier: P00520-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MLEICLKLVGCKSKKGLSSSSSCYLE → MGQQPGKVLGDQRRPSLPALHFIKGAGKRDSSRHGGPHCNVFVEH

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1123

1123

Tyrosine-protein kinase ABL1

PRO_0000088051

Regions

Domain

61 – 121

61

SH3

Domain

127 – 217

91

SH2

Domain

242 – 493

252

Protein kinase

Nucleotide binding

248 – 256

9

ATP Probable

Nucleotide binding

316 – 322

7

ATP Probable

Region

1 – 60

60

CAP

Region

863 – 961

99

DNA-binding

Region

945 – 1123

179

F-actin-binding By similarity

Motif

381 – 405

25

Kinase activation loop

Motif

605 – 609

5

Nuclear localization signal 1 Potential

Motif

708 – 714

7

Nuclear localization signal 2 Potential

Motif

761 – 768

8

Nuclear localization signal 3 Potential

Motif

1083 – 1093

11

Nuclear export signal

Compositional bias

18 – 22

5

Poly-Ser

Compositional bias

605 – 609

5

Poly-Lys

Compositional bias

804 – 1012

209

Pro-rich

Compositional bias

891 – 897

7

Poly-Pro

Sites

Active site

363

1

Proton acceptor By similarity

Binding site

271

1

ATP By similarity

Amino acid modifications

Modified residue

50

1

Phosphoserine By similarity

Modified residue

70

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

185

1

Phosphotyrosine By similarity

Modified residue

226

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

253

1

Phosphotyrosine By similarity

Modified residue

257

1

Phosphotyrosine By similarity

Modified residue

264

1

Phosphotyrosine By similarity

Modified residue

392

1

Phosphothreonine By similarity

Modified residue

393

1

Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases Ref.24 Ref.30

Modified residue

394

1

Phosphothreonine By similarity

Modified residue

446

1

Phosphoserine Ref.13

Modified residue

469

1

Phosphotyrosine By similarity

Modified residue

547

1

Phosphothreonine Ref.7

Modified residue

569

1

Phosphoserine Ref.7

Modified residue

613

1

Phosphothreonine By similarity

Modified residue

618

1

Phosphoserine; by PAK2 By similarity

Modified residue

619

1

Phosphoserine; by PAK2 By similarity

Modified residue

620

1

Phosphoserine By similarity

Modified residue

658

1

Phosphoserine By similarity

Modified residue

682

1

Phosphoserine By similarity

Modified residue

710

1

N6-acetyllysine; by EP300 By similarity

Modified residue

717

1

Phosphoserine By similarity

Modified residue

734

1

Phosphothreonine By similarity

Modified residue

803

1

Phosphoserine By similarity

Modified residue

807

1

Phosphoserine By similarity

Modified residue

812

1

Phosphothreonine By similarity

Modified residue

844

1

Phosphothreonine By similarity

Modified residue

909

1

Phosphoserine By similarity

Modified residue

911

1

Phosphoserine By similarity

Modified residue

927

1

Phosphoserine By similarity

Modified residue

970

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 26

26

MLEIC…SCYLE → MISFDLLSDELHLKLLVLDV in isoform II.

VSP_004959

Alternative sequence

1 – 26

26

MLEIC…SCYLE → MSQRWTYTKCRVQRDPALPF M in isoform III.

VSP_004958

Alternative sequence

1 – 26

26

MLEIC…SCYLE → MGQQPGKVLGDQRRPSLPAL HFIKGAGKRDSSRHGGPHCN VFVEH in isoform IV.

VSP_004960

Experimental info

Mutagenesis

112

1

P → S: Strongly reduced inhibition by GNF-2. Ref.35

Mutagenesis

128

1

Y → D: Strongly reduced inhibition by GNF-2. Ref.35

Mutagenesis

139

1

Y → C: Strongly reduced inhibition by GNF-2. Ref.35

Mutagenesis

226

1

Y → F: Minimal reduction in ability to autophosphorylate. Ref.24

Mutagenesis

229

1

S → P: Strongly reduced inhibition by GNF-2. Ref.35

Mutagenesis

271

1

K → M: Loss of kinase activity. Ref.24

Mutagenesis

315

1

T → I: Loss of inhibition by imatinib. Loss of inhibition by GNF-2. Ref.35

Mutagenesis

393

1

Y → F: Minimal reduction in ability to autophosphorylate. Ref.24

Mutagenesis

446

1

S → A: No effect on basal activity, but abolishes ionizing radiation-induced activation. Ref.13

Mutagenesis

464

1

C → Y: Loss of inhibition by GNF-2. Ref.35

Mutagenesis

465

1

P → S: Loss of inhibition by GNF-2. Ref.35

Mutagenesis

497

1

F → L: Strongly reduced inhibition by GNF-2. Ref.35

Mutagenesis

505

1

E → K: Loss of inhibition by GNF-2. Ref.35

Mutagenesis

506

1

V → L: Strongly reduced inhibition by GNF-2. Ref.35

Mutagenesis

1083

1

L → A: Loss of nuclear export.

Sequence conflict

184 – 187

4

LYVS → VGDW in AAB60451. Ref.4

Sequence conflict

184 – 187

4

LYVS → VGDW in AAB60450. Ref.4

Sequence conflict

782 – 786

5

PPRLV → LPGWL in AAA88241. Ref.1

Sequence conflict

987

1

D → G in BAC41088. Ref.2

Secondary structure

1

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1123

Helix Strand Turn

Details...

Beta strand

65 – 70

6

Beta strand

76 – 79

4

Beta strand

87 – 93

7

Beta strand

97 – 103

7

Beta strand

108 – 112

5

Helix

113 – 115

3

Beta strand

116 – 121

6

Helix

122 – 124

3

Beta strand

128 – 131

4

Helix

134 – 140

7

Helix

141 – 143

3

Beta strand

148 – 153

6

Beta strand

155 – 157

3

Beta strand

161 – 167

7

Beta strand

170 – 175

6

Beta strand

184 – 187

4

Beta strand

192 – 194

3

Helix

195 – 202

8

Beta strand

209 – 211

3

Beta strand

226 – 228

3

Beta strand

230 – 233

4

Helix

239 – 241

3

Beta strand

242 – 248

7

Helix

249 – 251

3

Beta strand

255 – 261

7

Helix

262 – 264

3

Beta strand

266 – 273

8

Beta strand

275 – 278

4

Helix

280 – 292

13

Beta strand

301 – 305

5

Beta strand

307 – 316

10

Helix

323 – 329

7

Turn

332 – 334

3

Helix

337 – 357

21

Beta strand

359 – 362

4

Helix

366 – 368

3

Beta strand

369 – 371

3

Helix

373 – 375

3

Beta strand

377 – 379

3

Helix

384 – 386

3

Beta strand

390 – 396

7

Beta strand

399 – 401

3

Helix

403 – 405

3

Helix

408 – 413

6

Helix

418 – 433

16

Beta strand

439 – 442

4

Helix

445 – 447

3

Helix

448 – 453

6

Helix

466 – 475

10

Helix

480 – 482

3

Helix

486 – 509

24

Sequences

	Sequence		Length	Mass (Da)
	Isoform I [UniParc]. Last modified February 15, 2005. Version 3. Checksum: BD48ADE8557AE95C	FASTA	1,123	122,673
	10 20 30 40 50 60 MLEICLKLVG CKSKKGLSSS SSCYLEEALQ RPVASDFEPQ GLSEAARWNS KENLLAGPSE 70 80 90 100 110 120 NDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNHNGEWC EAQTKNGQGW VPSNYITPVN 130 140 150 160 170 180 SLEKHSWYHG PVSRNAAEYL LSSGINGSFL VRESESSPGQ RSISLRYEGR VYHYRINTAS 190 200 210 220 230 240 DGKLYVSSES RFNTLAELVH HHSTVADGLI TTLHYPAPKR NKPTIYGVSP NYDKWEMERT 250 260 270 280 290 300 DITMKHKLGG GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ 310 320 330 340 350 360 LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVSAVVL LYMATQISSA MEYLEKKNFI 370 380 390 400 410 420 HRDLAARNCL VGENHLVKVA DFGLSRLMTG DTYTAHAGAK FPIKWTAPES LAYNKFSIKS 430 440 450 460 470 480 DVWAFGVLLW EIATYGMSPY PGIDLSQVYE LLEKDYRMER PEGCPEKVYE LMRACWQWNP 490 500 510 520 530 540 SDRPSFAEIH QAFETMFQES SISDEVEKEL GKRGTRGGAG SMLQAPELPT KTRTCRRAAE 550 560 570 580 590 600 QKDAPDTPEL LHTKGLGESD ALDSEPAVSP LLPRKERGPP DGSLNEDERL LPRDRKTNLF 610 620 630 640 650 660 SALIKKKKKM APTPPKRSSS FREMDGQPDR RGASEDDSRE LCNGPPALTS DAAEPTKSPK 670 680 690 700 710 720 ASNGAGVPNG AFREPGNSGF RSPHMWKKSS TLTGSRLAAA EEESGMSSSK RFLRSCSASC 730 740 750 760 770 780 MPHGARDTEW RSVTLPRDLP SAGKQFDSST FGGHKSEKPA LPRKRTSESR SEQVAKSTAM 790 800 810 820 830 840 PPPRLVKKNE EAAEEGFKDT ESSPGSSPPS LTPKLLRRQV TASPSSGLSH KEEATKGSAS 850 860 870 880 890 900 GMGTPATAEP APPSNKVGLS KASSEEMRVR RHKHSSESPG RDKGRLAKLK PAPPPPPACT 910 920 930 940 950 960 GKAGKPAQSP SQEAGEAGGP TKTKCTSLAM DAVNTDPTKA GPPGEGLRKP VPPSVPKPQS 970 980 990 1000 1010 1020 TAKPPGTPTS PVSTPSTAPA PSPLAGDQQP SSAAFIPLIS TRVSLRKTRQ PPERIASGTI 1030 1040 1050 1060 1070 1080 TKGVVLDSTE ALCLAISRNS EQMASHSAVL EAGKNLYTFC VSYVDSIQQM RNKFAFREAI 1090 1100 1110 1120 NKLESNLREL QICPATASSG PAATQDFSKL LSSVKEISDI VRR
	Isoform II [UniParc]. Checksum: 002F9D346307028A	FASTA	1,117	122,179
	10 20 30 40 50 60 MISFDLLSDE LHLKLLVLDV EALQRPVASD FEPQGLSEAA RWNSKENLLA GPSENDPNLF 70 80 90 100 110 120 VALYDFVASG DNTLSITKGE KLRVLGYNHN GEWCEAQTKN GQGWVPSNYI TPVNSLEKHS 130 140 150 160 170 180 WYHGPVSRNA AEYLLSSGIN GSFLVRESES SPGQRSISLR YEGRVYHYRI NTASDGKLYV 190 200 210 220 230 240 SSESRFNTLA ELVHHHSTVA DGLITTLHYP APKRNKPTIY GVSPNYDKWE MERTDITMKH 250 260 270 280 290 300 KLGGGQYGEV YEGVWKKYSL TVAVKTLKED TMEVEEFLKE AAVMKEIKHP NLVQLLGVCT 310 320 330 340 350 360 REPPFYIITE FMTYGNLLDY LRECNRQEVS AVVLLYMATQ ISSAMEYLEK KNFIHRDLAA 370 380 390 400 410 420 RNCLVGENHL VKVADFGLSR LMTGDTYTAH AGAKFPIKWT APESLAYNKF SIKSDVWAFG 430 440 450 460 470 480 VLLWEIATYG MSPYPGIDLS QVYELLEKDY RMERPEGCPE KVYELMRACW QWNPSDRPSF 490 500 510 520 530 540 AEIHQAFETM FQESSISDEV EKELGKRGTR GGAGSMLQAP ELPTKTRTCR RAAEQKDAPD 550 560 570 580 590 600 TPELLHTKGL GESDALDSEP AVSPLLPRKE RGPPDGSLNE DERLLPRDRK TNLFSALIKK 610 620 630 640 650 660 KKKMAPTPPK RSSSFREMDG QPDRRGASED DSRELCNGPP ALTSDAAEPT KSPKASNGAG 670 680 690 700 710 720 VPNGAFREPG NSGFRSPHMW KKSSTLTGSR LAAAEEESGM SSSKRFLRSC SASCMPHGAR 730 740 750 760 770 780 DTEWRSVTLP RDLPSAGKQF DSSTFGGHKS EKPALPRKRT SESRSEQVAK STAMPPPRLV 790 800 810 820 830 840 KKNEEAAEEG FKDTESSPGS SPPSLTPKLL RRQVTASPSS GLSHKEEATK GSASGMGTPA 850 860 870 880 890 900 TAEPAPPSNK VGLSKASSEE MRVRRHKHSS ESPGRDKGRL AKLKPAPPPP PACTGKAGKP 910 920 930 940 950 960 AQSPSQEAGE AGGPTKTKCT SLAMDAVNTD PTKAGPPGEG LRKPVPPSVP KPQSTAKPPG 970 980 990 1000 1010 1020 TPTSPVSTPS TAPAPSPLAG DQQPSSAAFI PLISTRVSLR KTRQPPERIA SGTITKGVVL 1030 1040 1050 1060 1070 1080 DSTEALCLAI SRNSEQMASH SAVLEAGKNL YTFCVSYVDS IQQMRNKFAF REAINKLESN 1090 1100 1110 LRELQICPAT ASSGPAATQD FSKLLSSVKE ISDIVRR
	Isoform III [UniParc]. Checksum: AB3B4510AE8C5C38	FASTA	1,118	122,480
	10 20 30 40 50 60 MSQRWTYTKC RVQRDPALPF MEALQRPVAS DFEPQGLSEA ARWNSKENLL AGPSENDPNL 70 80 90 100 110 120 FVALYDFVAS GDNTLSITKG EKLRVLGYNH NGEWCEAQTK NGQGWVPSNY ITPVNSLEKH 130 140 150 160 170 180 SWYHGPVSRN AAEYLLSSGI NGSFLVRESE SSPGQRSISL RYEGRVYHYR INTASDGKLY 190 200 210 220 230 240 VSSESRFNTL AELVHHHSTV ADGLITTLHY PAPKRNKPTI YGVSPNYDKW EMERTDITMK 250 260 270 280 290 300 HKLGGGQYGE VYEGVWKKYS LTVAVKTLKE DTMEVEEFLK EAAVMKEIKH PNLVQLLGVC 310 320 330 340 350 360 TREPPFYIIT EFMTYGNLLD YLRECNRQEV SAVVLLYMAT QISSAMEYLE KKNFIHRDLA 370 380 390 400 410 420 ARNCLVGENH LVKVADFGLS RLMTGDTYTA HAGAKFPIKW TAPESLAYNK FSIKSDVWAF 430 440 450 460 470 480 GVLLWEIATY GMSPYPGIDL SQVYELLEKD YRMERPEGCP EKVYELMRAC WQWNPSDRPS 490 500 510 520 530 540 FAEIHQAFET MFQESSISDE VEKELGKRGT RGGAGSMLQA PELPTKTRTC RRAAEQKDAP 550 560 570 580 590 600 DTPELLHTKG LGESDALDSE PAVSPLLPRK ERGPPDGSLN EDERLLPRDR KTNLFSALIK 610 620 630 640 650 660 KKKKMAPTPP KRSSSFREMD GQPDRRGASE DDSRELCNGP PALTSDAAEP TKSPKASNGA 670 680 690 700 710 720 GVPNGAFREP GNSGFRSPHM WKKSSTLTGS RLAAAEEESG MSSSKRFLRS CSASCMPHGA 730 740 750 760 770 780 RDTEWRSVTL PRDLPSAGKQ FDSSTFGGHK SEKPALPRKR TSESRSEQVA KSTAMPPPRL 790 800 810 820 830 840 VKKNEEAAEE GFKDTESSPG SSPPSLTPKL LRRQVTASPS SGLSHKEEAT KGSASGMGTP 850 860 870 880 890 900 ATAEPAPPSN KVGLSKASSE EMRVRRHKHS SESPGRDKGR LAKLKPAPPP PPACTGKAGK 910 920 930 940 950 960 PAQSPSQEAG EAGGPTKTKC TSLAMDAVNT DPTKAGPPGE GLRKPVPPSV PKPQSTAKPP 970 980 990 1000 1010 1020 GTPTSPVSTP STAPAPSPLA GDQQPSSAAF IPLISTRVSL RKTRQPPERI ASGTITKGVV 1030 1040 1050 1060 1070 1080 LDSTEALCLA ISRNSEQMAS HSAVLEAGKN LYTFCVSYVD SIQQMRNKFA FREAINKLES 1090 1100 1110 NLRELQICPA TASSGPAATQ DFSKLLSSVK EISDIVRR
	Isoform IV [UniParc]. Checksum: 7A9DB9E772EAF05F	FASTA	1,142	124,769
	10 20 30 40 50 60 MGQQPGKVLG DQRRPSLPAL HFIKGAGKRD SSRHGGPHCN VFVEHEALQR PVASDFEPQG 70 80 90 100 110 120 LSEAARWNSK ENLLAGPSEN DPNLFVALYD FVASGDNTLS ITKGEKLRVL GYNHNGEWCE 130 140 150 160 170 180 AQTKNGQGWV PSNYITPVNS LEKHSWYHGP VSRNAAEYLL SSGINGSFLV RESESSPGQR 190 200 210 220 230 240 SISLRYEGRV YHYRINTASD GKLYVSSESR FNTLAELVHH HSTVADGLIT TLHYPAPKRN 250 260 270 280 290 300 KPTIYGVSPN YDKWEMERTD ITMKHKLGGG QYGEVYEGVW KKYSLTVAVK TLKEDTMEVE 310 320 330 340 350 360 EFLKEAAVMK EIKHPNLVQL LGVCTREPPF YIITEFMTYG NLLDYLRECN RQEVSAVVLL 370 380 390 400 410 420 YMATQISSAM EYLEKKNFIH RDLAARNCLV GENHLVKVAD FGLSRLMTGD TYTAHAGAKF 430 440 450 460 470 480 PIKWTAPESL AYNKFSIKSD VWAFGVLLWE IATYGMSPYP GIDLSQVYEL LEKDYRMERP 490 500 510 520 530 540 EGCPEKVYEL MRACWQWNPS DRPSFAEIHQ AFETMFQESS ISDEVEKELG KRGTRGGAGS 550 560 570 580 590 600 MLQAPELPTK TRTCRRAAEQ KDAPDTPELL HTKGLGESDA LDSEPAVSPL LPRKERGPPD 610 620 630 640 650 660 GSLNEDERLL PRDRKTNLFS ALIKKKKKMA PTPPKRSSSF REMDGQPDRR GASEDDSREL 670 680 690 700 710 720 CNGPPALTSD AAEPTKSPKA SNGAGVPNGA FREPGNSGFR SPHMWKKSST LTGSRLAAAE 730 740 750 760 770 780 EESGMSSSKR FLRSCSASCM PHGARDTEWR SVTLPRDLPS AGKQFDSSTF GGHKSEKPAL 790 800 810 820 830 840 PRKRTSESRS EQVAKSTAMP PPRLVKKNEE AAEEGFKDTE SSPGSSPPSL TPKLLRRQVT 850 860 870 880 890 900 ASPSSGLSHK EEATKGSASG MGTPATAEPA PPSNKVGLSK ASSEEMRVRR HKHSSESPGR 910 920 930 940 950 960 DKGRLAKLKP APPPPPACTG KAGKPAQSPS QEAGEAGGPT KTKCTSLAMD AVNTDPTKAG 970 980 990 1000 1010 1020 PPGEGLRKPV PPSVPKPQST AKPPGTPTSP VSTPSTAPAP SPLAGDQQPS SAAFIPLIST 1030 1040 1050 1060 1070 1080 RVSLRKTRQP PERIASGTIT KGVVLDSTEA LCLAISRNSE QMASHSAVLE AGKNLYTFCV 1090 1100 1110 1120 1130 1140 SYVDSIQQMR NKFAFREAIN KLESNLRELQ ICPATASSGP AATQDFSKLL SSVKEISDIV RR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of testis-derived c-abl cDNAs: implications for testis-specific transcription and abl oncogene activation." Oppi C., Shore S.K., Reddy E.P. Proc. Natl. Acad. Sci. U.S.A. 84:8200-8204(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I). Tissue: Testis.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I). Strain: ICR. Tissue: Embryo.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IV). Strain: C57BL/6. Tissue: Brain.
[4]	"Sequence and analysis of the human ABL gene, the BCR gene, and regions involved in the Philadelphia chromosomal translocation." Chissoe S.L., Bodenteich A., Wang Y.-F., Wang Y.-P., Burian D., Clifton S.W., Crabtree J., Freeman A., Iyer K., Jian L., Ma Y., McLaury H.-J., Pan H.-Q., Sarhan O.H., Toth S., Wang Z., Zhang G., Heisterkamp N., Groffen J., Roe B.A. Genomics 27:67-82(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-187 (ISOFORMS I; II; III AND IV).
[5]	"The mouse c-abl locus: molecular cloning and characterization." Wang J.Y.J., Ledley F., Goff S., Lee R., Groner Y., Baltimore D. Cell 36:349-356(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-182.
[6]	"Four murine c-abl mRNAs arise by usage of two transcriptional promoters and alternative splicing." Bernards A., Paskind M., Baltimore D. Oncogene 2:297-304(1988) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING.
[7]	"Differential phosphorylation of c-Abl in cell cycle determined by cdc2 kinase and phosphatase activity." Kipreos E.T., Wang J.Y. Science 248:217-220(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-547 AND SER-569.
[8]	"Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene." Tybulewicz V.L., Crawford C.E., Jackson P.K., Bronson R.T., Mulligan R.C. Cell 65:1153-1163(1991) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[9]	"Mice homozygous for the ablm1 mutation show poor viability and depletion of selected B and T cell populations." Schwartzberg P.L., Stall A.M., Hardin J.D., Bowdish K.S., Humaran T., Boast S., Harbison M.L., Robertson E.J., Goff S.P. Cell 65:1165-1175(1991) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[10]	"Cell cycle-regulated binding of c-Abl tyrosine kinase to DNA." Kipreos E.T., Wang J.Y. Science 256:382-385(1992) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING, DOMAIN, PHOSPHORYLATION.
[11]	"c-Abl kinase regulates the protein binding activity of c-Crk." Feller S.M., Knudsen B., Hanafusa H. EMBO J. 13:2341-2351(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases." Mayer B.J., Hirai H., Sakai R. Curr. Biol. 5:296-305(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Functional interaction between DNA-PK and c-Abl in response to DNA damage." Kharbanda S., Pandey P., Jin S., Inoue S., Bharti A., Yuan Z.-M., Weichselbaum R., Weaver D., Kufe D. Nature 386:732-735(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-446, MUTAGENESIS OF SER-446.
[14]	"Nuclear-cytoplasmic shuttling of C-ABL tyrosine kinase." Taagepera S., McDonald D., Loeb J.E., Whitaker L.L., McElroy A.K., Wang J.Y., Hope T.J. Proc. Natl. Acad. Sci. U.S.A. 95:7457-7462(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[15]	"Cables links Cdk5 and c-Abl and facilitates Cdk5 tyrosine phosphorylation, kinase upregulation, and neurite outgrowth." Zukerberg L.R., Patrick G.N., Nikolic M., Humbert S., Wu C.-L., Lanier L.M., Gertler F.B., Vidal M., Van Etten R.A., Tsai L.-H. Neuron 26:633-646(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A TRIMOLECULAR COMPLEX WITH CDK5 AND CABLES1, INTERACTION WITH CABLES1. Tissue: Brain.
[16]	"Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation." Cong F., Spencer S., Cote J.F., Wu Y., Tremblay M.L., Lasky L.A., Goff S.P. Mol. Cell 6:1413-1423(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PSTPIP1.
[17]	"Regulation of cell death by the Abl tyrosine kinase." Wang J.Y. Oncogene 19:5643-5650(2000) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[18]	"Inhibition of cell migration by Abl family tyrosine kinases through uncoupling of Crk-CAS complexes." Kain K.H., Klemke R.L. J. Biol. Chem. 276:16185-16192(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CRK, FUNCTION.
[19]	"Targeting of the c-Abl tyrosine kinase to mitochondria in the necrotic cell death response to oxidative stress." Kumar S., Bharti A., Mishra N.C., Raina D., Kharbanda S., Saxena S., Kufe D. J. Biol. Chem. 276:17281-17285(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[20]	"The beta-amyloid precursor protein APP is tyrosine-phosphorylated in cells expressing a constitutively active form of the Abl protoncogene." Zambrano N., Bruni P., Minopoli G., Mosca R., Molino D., Russo C., Schettini G., Sudol M., Russo T. J. Biol. Chem. 276:19787-19792(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[21]	"Aph2, a protein with a zf-DHHC motif, interacts with c-Abl and has pro-apoptotic activity." Li B., Cong F., Tan C.P., Wang S.X., Goff S.P. J. Biol. Chem. 277:28870-28876(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ZDHHC16.
[22]	"Interaction between UV-damaged DNA binding activity proteins and the c-Abl tyrosine kinase." Cong F., Tang J., Hwang B.J., Vuong B.Q., Chu G., Goff S.P. J. Biol. Chem. 277:34870-34878(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[23]	"Regulation of F-actin-dependent processes by the Abl family of tyrosine kinases." Woodring P.J., Hunter T., Wang J.Y. J. Cell Sci. 116:2613-2626(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[24]	"Two distinct phosphorylation pathways have additive effects on Abl family kinase activation." Tanis K.Q., Veach D., Duewel H.S., Bornmann W.G., Koleske A.J. Mol. Cell. Biol. 23:3884-3896(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH CRK, AUTOPHOSPHORYLATION AT TYR-226 AND TYR-393, MUTAGENESIS OF TYR-226; LYS-271 AND TYR-393.
[25]	"Bidirectional signaling links the Abelson kinases to the platelet-derived growth factor receptor." Plattner R., Koleske A.J., Kazlauskas A., Pendergast A.M. Mol. Cell. Biol. 24:2573-2583(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION.
[26]	"Role of c-Abl in the DNA damage stress response." Shaul Y., Ben-Yehoyada M. Cell Res. 15:33-35(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[27]	"c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration." Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G., Berton G. FEBS Lett. 584:15-21(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF CELL MIGRATION, PHOSPHORYLATION, INTERACTION WITH ITGB1; HCK AND FGR.
[28]	"ABL tyrosine kinases: evolution of function, regulation, and specificity." Colicelli J. Sci. Signal. 3:RE6-RE6(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION, DOMAIN.
[29]	"High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides." Musacchio A., Saraste M., Wilmanns M. Nat. Struct. Biol. 1:546-551(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 61-121.
[30]	"Structural mechanism for STI-571 inhibition of Abelson tyrosine kinase." Schindler T., Bornmann W., Pellicena P., Miller W.T., Clarkson B., Kuriyan J. Science 289:1938-1942(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 229-515 IN COMPLEX WITH INHIBITOR STI-571, CATALYTIC ACTIVITY, ENZYME REGULATION, PHOSPHORYLATION AT TYR-393, ACTIVATION LOOP.
[31]	"Structural basis for the autoinhibition of c-Abl tyrosine kinase." Nagar B., Hantschel O., Young M.A., Scheffzek K., Veach D., Bornmann W., Clarkson B., Superti-Furga G., Kuriyan J. Cell 112:859-871(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 229-515, MYRISTOYLATION (ISOFORM IV), ENZYME REGULATION.
[32]	"Crystal structure of the T315I mutant of AbI kinase." Zhou T., Parillon L., Li F., Wang Y., Keats J., Lamore S., Xu Q., Shakespeare W., Dalgarno D., Zhu X. Chem. Biol. Drug Des. 70:171-181(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 229-515 OF WILD-TYPE AND MUTANT ILE-315 IN COMPLEX WITH INHIBITOR PPY-A.
[33]	"AP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently inhibits the T315I mutant and overcomes mutation-based resistance." O'Hare T., Shakespeare W.C., Zhu X., Eide C.A., Rivera V.M., Wang F., Adrian L.T., Zhou T., Huang W.S., Xu Q., Metcalf C.A. III, Tyner J.W., Loriaux M.M., Corbin A.S., Wardwell S., Ning Y., Keats J.A., Wang Y. , Sundaramoorthi R., Thomas M., Zhou D., Snodgrass J., Commodore L., Sawyer T.K., Dalgarno D.C., Deininger M.W., Druker B.J., Clackson T. Cancer Cell 16:401-412(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 229-515 OF MUTANT ILE-315 IN COMPLEX WITH INHIBITOR AP24534, CATALYTIC ACTIVITY, FUNCTION.
[34]	"Structural analysis of DFG-in and DFG-out dual Src-Abl inhibitors sharing a common vinyl purine template." Zhou T., Commodore L., Huang W.S., Wang Y., Sawyer T.K., Shakespeare W.C., Clackson T., Zhu X., Dalgarno D.C. Chem. Biol. Drug Des. 75:18-28(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) OF 115-401 IN COMPLEXES WITH INHIBITORS AP24283 AND AP24163.
[35]	"Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors." Zhang J., Adrian F.J., Jahnke W., Cowan-Jacob S.W., Li A.G., Iacob R.E., Sim T., Powers J., Dierks C., Sun F., Guo G.R., Ding Q., Okram B., Choi Y., Wojciechowski A., Deng X., Liu G., Fendrich G. , Strauss A., Vajpai N., Grzesiek S., Tuntland T., Liu Y., Bursulaya B., Azam M., Manley P.W., Engen J.R., Daley G.Q., Warmuth M., Gray N.S. Nature 463:501-506(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 115-401 IN COMPLEX WITH INHIBITORS IMATINIB AND GNF-2, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF PRO-112; TYR-128; TYR-139; SER-229; THR-315; CYS-464; PRO-465; PHE-497; GLU-505 AND VAL-506.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J02995 mRNA. Translation: AAA88241.1.
AK090095 mRNA. Translation: BAC41088.1.
BC059260 mRNA. Translation: AAH59260.1.
U14721, U14720 Genomic DNA. Translation: AAB60451.1.
U14721, U14720 Genomic DNA. Translation: AAB60450.1.
U14721, U13835 Genomic DNA. Translation: AAB60448.1.
U14721, U13835 Genomic DNA. Translation: AAB60449.1.
X07539 Genomic DNA. Translation: CAA30411.1.
X07539 Genomic DNA. Translation: CAA30412.1.
X07540 Genomic DNA. Translation: CAA30413.1.
X07541 Genomic DNA. Translation: CAA30414.1.
M12263 mRNA. Translation: AAA37136.1.
M12264 mRNA. Translation: AAA37137.1.
M12265 mRNA. Translation: AAA37138.1.
M12266 Genomic DNA. Translation: AAA37134.1.
K03228 mRNA. Translation: AAA37135.1.

IPI

IPI00227806.
IPI00227807.
IPI00314762.
IPI00453940.

PIR

A39962.
S00774.

RefSeq

NP_001106174.1. NM_001112703.1.
NP_033724.2. NM_009594.3.

UniGene

Mm.1318.
Mm.474779.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ABO	X-ray	2.00	A/B	61-121	[»]
1ABQ	X-ray	2.80	A	61-121	[»]
1FPU	X-ray	2.40	A/B	229-515	[»]
1IEP	X-ray	2.10	A/B	229-515	[»]
1M52	X-ray	2.60	A/B	229-515	[»]
1OPJ	X-ray	1.75	A/B	229-515	[»]
1OPK	X-ray	1.80	A	27-515	[»]
2HZN	X-ray	2.70	A	229-515	[»]
2QOH	X-ray	1.95	A/B	229-515	[»]
2Z60	X-ray	1.95	A	229-515	[»]
3DK3	X-ray	2.02	A/B	233-514	[»]
3DK6	X-ray	2.02	A/B	233-514	[»]
3DK7	X-ray	2.01	A/B	233-505	[»]
3IK3	X-ray	1.90	A/B	229-515	[»]
3K5V	X-ray	1.74	A/B	229-515	[»]
3KF4	X-ray	1.90	A/B	229-515	[»]
3KFA	X-ray	1.22	A/B	229-515	[»]
3MS9	X-ray	1.80	A/B	229-515	[»]
3MSS	X-ray	1.95	A/B/C/D	229-515	[»]
3OXZ	X-ray	2.20	A	229-511	[»]
3OY3	X-ray	1.95	A/B	229-511	[»]

ProteinModelPortal

P00520.

SMR

P00520. Positions 46-511, 1017-1123.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00520. 7 interactions.

MINT

MINT-85127.

PTM databases

PhosphoSite

P00520.

Proteomic databases

PaxDb

P00520.

PRIDE

P00520.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000028190; ENSMUSP00000028190; ENSMUSG00000026842.
ENSMUST00000075759; ENSMUSP00000075167; ENSMUSG00000026842.

GeneID

11350.

KEGG

mmu:11350.

UCSC

uc008jdz.2. mouse.

Organism-specific databases

CTD

25.

MGI

MGI:87859. Abl1.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00640000091347.

HOVERGEN

HBG004162.

KO

K06619.

OMA

GAFRESG.

OrthoDB

EOG40P460.

Enzyme and pathway databases

BRENDA

2.7.10.2. 3474.

Reactome

REACT_127416. Developmental Biology.
REACT_89750. Hemostasis.

Gene expression databases

ArrayExpress

P00520.

Bgee

P00520.

CleanEx

MM_ABL1.

Genevestigator

P00520.

GermOnline

ENSMUSG00000026842. Mus musculus.

Family and domain databases

Gene3D

3.30.505.10. 1 hit.

InterPro

IPR015015. F-actin_binding.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_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]

Pfam

PF08919. F_actin_bind. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00109. TYRKINASE.

SMART

SM00808. FABD. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50044. SH3. 1 hit.

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]

ProtoNet

Search...

Other

BindingDB

P00520.

ChEMBL

CHEMBL3099.

EvolutionaryTrace

P00520.

NextBio

278620.

SOURCE

Search...

Entry information

Entry name

ABL1_MOUSE

Accession

Primary (citable) accession number: P00520
Secondary accession number(s): P97896 , Q61252, Q61253, Q61254, Q61255, Q61256, Q61257, Q61258, Q61259, Q61260, Q61261, Q6PCM5, Q8C1X4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	February 15, 2005
Last modified:	May 1, 2013
This is version 176 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program