Reviewed, UniProtKB/Swiss-Prot P00520 (ABL1_MOUSE)

Names and origin

Protein names

Recommended name:
    Proto-oncogene tyrosine-protein kinase ABL1
    EC=2.7.10.2
Alternative name(s):
    Abelson murine leukemia viral oncogene homolog 1
    c-ABL
    p150

Gene names

Name:	Abl1
Synonyms:	Abl

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	1123 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Regulates cytoskeleton remodeling during cell differentiation, cell division and cell adhesion. Localizes to dynamic actin structures, and phosphorylates CRK and CRKL, DOK1, and other proteins controlling cytoskeleton dynamics. Regulates DNA repair potentially by activating the proapoptotic pathway when the DNA damage is too severe to be repaired. Ref.7 Ref.11 Ref.13
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
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 amino-terminal cap, and contributions from an amino-terminal myristoyl group and phospholipids. Activated by autophosphorylation as well as by SRC-family kinase-mediated phosphorylation. Activated by RIN1 binding to the SH2 and SH3 domains. Inhibited by imatinib mesylate (Gleevec). Ref.7 Ref.13
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-735' and, sequesters ABL1 into the cytoplasm By similarity.
Subcellular location	Cytoplasm › cytoskeleton. Nucleus. Note: The myristoylated c-ABL protein is reported to be nuclear. Sequestered into the cytoplasm through interaction with 14-3-3 proteins By similarity.
Tissue specificity	Widely expressed.
Post-translational modification	DNA damage-induced activation of c-Abl requires the function of ATM and Ser-446 phosphorylation. Phosphorylated by PRKDC. Isoform IV is myristoylated on Gly-2 By similarity.
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	Cell adhesion
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	actin cytoskeleton organization Ref.11 Inferred from direct assay. Source: UniProtKB cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-tyrosine phosphorylation Ref.7 Inferred from direct assay. Source: UniProtKB regulation of cell cycle Inferred from direct assay. Source: MGI
Cellular component	cytoplasm Ref.8 Inferred from direct assay. Source: UniProtKB cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Ref.8 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Ref.7 Inferred from direct assay. Source: UniProtKB magnesium ion binding Ref.7 Inferred from direct assay. Source: UniProtKB manganese ion binding Ref.7 Inferred from direct assay. Source: UniProtKB non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein domain specific binding Inferred from physical interaction. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDKN1B	P46527	1	EBI-914519,EBI-519280	From a different organism.
Dok1	P97465	3	EBI-914519,EBI-914917
Nck1	Q99M51	1	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

Proto-oncogene 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 By similarity

Region

1 – 60

60

CAP

Motif

605 – 609

5

Nuclear localization signal Potential

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

Amino acid modifications

Modified residue

50

1

Phosphoserine By similarity

Modified residue

185

1

Phosphotyrosine By similarity

Modified residue

226

1

Phosphotyrosine 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

393

1

Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases Ref.13

Modified residue

394

1

Phosphothreonine By similarity

Modified residue

446

1

Phosphoserine Ref.7

Modified residue

469

1

Phosphotyrosine By similarity

Modified residue

569

1

Phosphoserine By similarity

Modified residue

613

1

Phosphothreonine 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

717

1

Phosphoserine 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

226

1

Y → F: Minimal reduction in ability to autophosphorylate. Ref.13

Mutagenesis

271

1

K → M: Loss of kinase activity. Ref.13

Mutagenesis

393

1

Y → F: Minimal reduction in ability to autophosphorylate. Ref.13

Mutagenesis

446

1

S → A: No effect on basal activity, but abolishes ionizing radiation-induced activation. Ref.7

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

87 – 93

7

Beta strand

97 – 104

8

Beta strand

107 – 112

6

Helix

113 – 115

3

Beta strand

116 – 118

3

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

Helix

239 – 241

3

Beta strand

242 – 247

6

Turn

249 – 252

4

Beta strand

254 – 261

8

Helix

262 – 264

3

Beta strand

267 – 275

9

Turn

277 – 279

3

Helix

280 – 291

12

Beta strand

301 – 305

5

Beta strand

307 – 316

10

Helix

323 – 329

7

Turn

332 – 334

3

Helix

337 – 356

20

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 – 412

5

Helix

418 – 433

16

Helix

445 – 447

3

Helix

448 – 453

6

Helix

466 – 475

10

Helix

480 – 482

3

Helix

486 – 496

11

Helix

502 – 509

8

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. 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. 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. 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

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[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: 3317402] [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: 16141072] [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: 15489334] [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: 7665185] [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: 6319018] [Abstract] Cited for: NUCLEOTIDE SEQUENCE 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: 3283651] [Abstract] Cited for: ALTERNATIVE SPLICING.
[7]	"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: 9109492] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCALIZATION, PHOSPHORYLATION AT SER-446, MUTAGENESIS OF SER-446.
[8]	"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: 9636171] [Abstract] Cited for: SUBCELLULAR LOCALIZATION.
[9]	"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: 10896159] [Abstract] Cited for: IDENTIFICATION IN A TRIMOLECULAR COMPLEX WITH CDK5 AND CABLES1, INTERACTION WITH CABLES1. Tissue: Brain.
[10]	"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: 11163214] [Abstract] Cited for: INTERACTION WITH PSTPIP1.
[11]	"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: 11279004] [Abstract] Cited for: INTERACTION WITH CRK, FUNCTION.
[12]	"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: 12021275] [Abstract] Cited for: INTERACTION WITH ZDHHC16.
[13]	"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: 12748290] [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.
[14]	"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: 7664083] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 61-121.
[15]	"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: 10988075] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 229-515.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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_033724.2.

UniGene

Mm.1318

3D structure databases

PDBPDBe

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	[»]

SMR

P00520. Positions 1017-1123.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00520. 5 interactions.

PTM databases

PhosphoSite

P00520.

Genome annotation databases

Ensembl

ENSMUSG00000026842. Mus musculus. [Contig view]

GeneID

11350.

Organism-specific databases

MGI

MGI:87859. Abl1.

Phylogenomic databases

HOVERGEN

P00520.

OMA

P00520. GAFRESG.

Enzyme and pathway databases

BRENDA

2.7.10.2. 244.

Gene expression databases

ArrayExpress

P00520.

Bgee

P00520.

CleanEx

MM_ABL1.

GermOnline

ENSMUSG00000026842. Mus musculus.

Family and domain databases

InterPro

IPR015015. F-actin_binding.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
[Graphical view]

Gene3D

G3DSA:3.30.505.10. SH2. 1 hit.

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.

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]

ProtoNet

Search...

Other Resources

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:	June 16, 2009
This is version 133 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)