Reviewed, UniProtKB/Swiss-Prot P00519 (ABL1_HUMAN)

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, JTK7

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1130 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.16 Ref.28
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) which is used for the treatment of chronic myeloid leukemia (CML). Inhibited by VX-680, an inhibitor that acts also on imanitib-resistant mutants. Ref.28 Ref.29
Subunit structure	Interacts with SORBS1 following insulin stimulation. Found in a trimolecular complex containing CDK5 and CABLES1. Interacts with CABLES1 and PSTPIP1. Interacts with ZDHHC16 By similarity. Interacts with INPPL1/SHIP2. 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.
Subcellular location	Cytoplasm › cytoskeleton. Nucleus. Note: Sequestered into the cytoplasm through interaction with 14-3-3 proteins. Ref.15 Isoform IB: Nucleus membrane; Lipid-anchor. Note: The myristoylated c-ABL protein is reported to be nuclear. Ref.15
Tissue specificity	Widely expressed.
Post-translational modification	Phosphorylated by PRKDC By similarity. DNA damage-induced activation of c-Abl requires the function of ATM and Ser-446 phosphorylation. Isoform IB is myristoylated on Gly-2. Phosphorylation on Thr-735 is required for binding 14-3-3 proteins for cytoplasmic translocation.
Involvement in disease	A chromosomal aberration involving ABL1 is a cause of chronic myeloid leukemia (CML) [MIM:608232]. Translocation t(9;22)(q34;q11) with BCR. The translocation produces a BCR-ABL found also in acute myeloid leukemia (AML) and acute lymphoblastic leukemia (ALL).
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 Membrane Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction resulting in induction of apoptosis Traceable author statement. Source: ProtInc actin cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW mismatch repair Traceable author statement. Source: ProtInc peptidyl-tyrosine phosphorylation Ref.16 Inferred from direct assay. Source: UniProtKB positive regulation of oxidoreductase activity Inferred from direct assay. Source: UniProtKB regulation of transcription involved in S-phase of mitotic cell cycle Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay. Source: MGI
Molecular function	ATP binding Ref.16 Inferred from direct assay. Source: UniProtKB DNA binding Non-traceable author statement. Source: UniProtKB magnesium ion binding Ref.16 Inferred from direct assay. Source: UniProtKB manganese ion binding Ref.16 Inferred from direct assay. Source: UniProtKB non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein C-terminus binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABI1	Q8IZP0	2	EBI-375543,EBI-375446
Abi1	Q8CBW3	1	EBI-375543,EBI-375511	From a different organism.
ABR	Q12979	1	EBI-375543,EBI-489922
ACAP1	Q15027	1	EBI-375543,EBI-751746
AHSG	P02765	1	EBI-375543,EBI-1223374
AIRE	O43918	1	EBI-375543,EBI-1753081
AKAP6	Q13023	1	EBI-375543,EBI-1056102
APOL5	Q9BWW9	1	EBI-375543,EBI-1753592
ARHGEF11	O15085	1	EBI-375543,EBI-311099
ASAP1	Q9ULH1	1	EBI-375543,EBI-346622
ASB16	Q96NS5	1	EBI-375543,EBI-1751918
ATM	Q13315	1	EBI-375543,EBI-495465
BAZ2A	Q9UIF9	1	EBI-375543,EBI-934890
Bcar1	Q63767	1	EBI-375543,EBI-1176801	From a different organism.
BMP8B	P34820	1	EBI-375543,EBI-1752660
BRCA2	P51587	1	EBI-375543,EBI-79792
BRPF3	Q9ULD4	1	EBI-375543,EBI-1753470
C20orf46	Q9NUR3	1	EBI-375543,EBI-1753189
C6	P13671	1	EBI-375543,EBI-1753221
CAST	P20810	1	EBI-375543,EBI-1268770
CCKBR	P32239	1	EBI-375543,EBI-1753137
CD2AP	Q9Y5K6	1	EBI-375543,EBI-298152
CDC27	P30260	1	EBI-375543,EBI-994813
CDKL5	O76039	1	EBI-375543,EBI-1752465
CELSR3	Q9NYQ7	1	EBI-375543,EBI-308417
CENPA	P49450	1	EBI-375543,EBI-1751979
CHRD	Q9H2X0	1	EBI-375543,EBI-947551
CKAP5	Q14008	1	EBI-375543,EBI-310585
CNTFR	P26992	1	EBI-375543,EBI-743758
CNTNAP1	P78357	1	EBI-375543,EBI-1751903
COBRA1	Q8WX92	1	EBI-375543,EBI-347721
CRK	P46108	1	EBI-375543,EBI-886
CSMD2	Q7Z408	1	EBI-375543,EBI-1957312
CTAGE5	O15320	1	EBI-375543,EBI-1050253
CUL7	Q14999	1	EBI-375543,EBI-308606
CYP4F2	P78329	1	EBI-375543,EBI-1752413
DDX41	Q9UJV9	1	EBI-375543,EBI-1046350
DKKL1	Q9UK85	1	EBI-375543,EBI-1753048
DLGAP1	O14490	1	EBI-375543,EBI-1753207
DLGAP2	Q9P1A6	1	EBI-375543,EBI-1753397
DLGAP3	O95886	1	EBI-375543,EBI-1752541
DLGAP4	Q9Y2H0	1	EBI-375543,EBI-722139
DLX4	Q92988	1	EBI-375543,EBI-1752755
DNASE1L2	Q92874	1	EBI-375543,EBI-1751995
DNM1	Q05193	1	EBI-375543,EBI-713135
DNM2	P50570	1	EBI-375543,EBI-346547
DNM3	Q9UQ16	1	EBI-375543,EBI-1111783
DOCK3	Q8IZD9	1	EBI-375543,EBI-1752361
DUSP15	Q9H1R2	1	EBI-375543,EBI-1752795
EFNA5	P52803	1	EBI-375543,EBI-1753674
EFS	O43281	1	EBI-375543,EBI-718488
EPB41L3	Q9Y2J2	1	EBI-375543,EBI-310986
EPS15	P42566	1	EBI-375543,EBI-396684
F2RL2	O00254	1	EBI-375543,EBI-1751853
FAM110A	Q9BQ89	1	EBI-375543,EBI-1752811
FAM127A	O15255	1	EBI-375543,EBI-954396
FLNA	P21333	1	EBI-375543,EBI-350432
FLNC	Q14315	1	EBI-375543,EBI-489954
FOXF2	Q12947	1	EBI-375543,EBI-1752316
FYB	O15117	1	EBI-375543,EBI-1753267
FYN	P06241	1	EBI-375543,EBI-515315
G3BP2	Q9UN86	1	EBI-375543,EBI-1044298
GABBR1	Q9UBS5	1	EBI-375543,EBI-724156
GAD1	Q99259	1	EBI-375543,EBI-743184
GNS	P15586	1	EBI-375543,EBI-1752200
GPR45	Q9Y5Y3	1	EBI-375543,EBI-1751869
GRB2	P62993	1	EBI-375543,EBI-401755
GRIP2	Q9C0E4	1	EBI-375543,EBI-949557
GSTZ1	O43708	1	EBI-375543,EBI-748043
GSX2	Q9BZM3	1	EBI-375543,EBI-1753426
GTF2IRD1	Q9UHL9	1	EBI-375543,EBI-372530
GTF3A	Q92664	1	EBI-375543,EBI-1752104
HCN2	Q9UL51	1	EBI-375543,EBI-1751885
HCN4	Q9Y3Q4	1	EBI-375543,EBI-1753521
HEXA	P06865	1	EBI-375543,EBI-723519
HNRNPR	O43390	1	EBI-375543,EBI-713419
HOXC8	P31273	1	EBI-375543,EBI-1752118
KIFC2	Q96AC6	1	EBI-375543,EBI-724040
LIG3	P49916	1	EBI-375543,EBI-1753381
LRBA	P50851	1	EBI-375543,EBI-1052167
LRP2	P98164	1	EBI-375543,EBI-947916
LTBP2	Q14767	1	EBI-375543,EBI-1546118
MAP4K1	Q92918	1	EBI-375543,EBI-881
MED14	O60244	1	EBI-375543,EBI-394489
MEPE	Q9NQ76	1	EBI-375543,EBI-1753293
MKI67	P46013	1	EBI-375543,EBI-876367
NAP5	O14513	1	EBI-375543,EBI-1752508
NBEA	Q8NFP9	1	EBI-375543,EBI-723014
NCK1	P16333	1	EBI-375543,EBI-389883
NCKIPSD	Q9NZQ3	1	EBI-375543,EBI-957585
NEK8	Q86SG6	1	EBI-375543,EBI-1752987
NFASC	O94856	1	EBI-375543,EBI-1751948
NFS1	Q9Y697	1	EBI-375543,EBI-1751791
NKX2-1	P43699	1	EBI-375543,EBI-1391923
NOTCH3	Q9UM47	1	EBI-375543,EBI-1236377
NPVF	Q9HCQ7	1	EBI-375543,EBI-1753111
NXPH3	O95157	1	EBI-375543,EBI-1752913
OGN	P20774	1	EBI-375543,EBI-1753690
ORC1L	Q13415	1	EBI-375543,EBI-374847
OSBPL5	Q9H0X9	1	EBI-375543,EBI-1753005
P2RX7	Q99572	1	EBI-375543,EBI-1753251
PAX3	P23760	1	EBI-375543,EBI-1167564
PCDHA7	Q9UN72	1	EBI-375543,EBI-1753660
PDIA2	Q13087	1	EBI-375543,EBI-1752525
PIK3R1	P27986	1	EBI-375543,EBI-79464
PKD1	P98161	1	EBI-375543,EBI-1752013
PLCG1	P19174	1	EBI-375543,EBI-79387
POLD1	P28340	1	EBI-375543,EBI-716569
PPP3CA	Q08209	1	EBI-375543,EBI-352922
PRICKLE3	O43900	1	EBI-375543,EBI-1751761
PRX	Q9BXM0	1	EBI-375543,EBI-1753064
PTPN4	P29074	1	EBI-375543,EBI-710431
RAPGEF1	Q13905	1	EBI-375543,EBI-976876
RGS20	O76081	1	EBI-375543,EBI-1052678
RIMS1	Q86UR5	1	EBI-375543,EBI-1043236
RIN1	Q13671	3	EBI-375543,EBI-366017
RIN3	Q8TB24	1	EBI-375543,EBI-1570523
RPP38	P78345	1	EBI-375543,EBI-366493
RTN4	Q9NQC3	1	EBI-375543,EBI-715945
SCARF2	Q96GP6	1	EBI-375543,EBI-1752088
SEMA7A	O75326	1	EBI-375543,EBI-1753538
SEPN1	Q9NZV5	1	EBI-375543,EBI-1751965
SF3B4	Q15427	1	EBI-375543,EBI-348469
SFN	P31947	1	EBI-375543,EBI-476295
SHANK3	Q9BYB0	1	EBI-375543,EBI-1752330
SLC22A3	O75751	1	EBI-375543,EBI-1752674
SLC24A1	O60721	1	EBI-375543,EBI-1753504
SNX12	Q9UMY4	1	EBI-375543,EBI-1752602
SNX17	Q15036	1	EBI-375543,EBI-1752620
SNX3	O60493	1	EBI-375543,EBI-727209
SNX8	Q9Y5X2	1	EBI-375543,EBI-1752557
SORBS1	Q9BX66	2	EBI-375543,EBI-433642
SOS2	Q07890	1	EBI-375543,EBI-298181
SP1	P08047	1	EBI-375543,EBI-298336
SRC	P12931	1	EBI-375543,EBI-621482
ST5	P78524	1	EBI-375543,EBI-962633
SUV39H2	Q9H5I1	1	EBI-375543,EBI-723127
SYNJ2	O15056	1	EBI-375543,EBI-310513
TERF1	P54274-2	1	EBI-375543,EBI-711018
TGOLN2	O43493	1	EBI-375543,EBI-1752146
TMPO	P42167	1	EBI-375543,EBI-455283
TRIM39	Q9HCM9	1	EBI-375543,EBI-739510
TSKS	Q9UJT2	1	EBI-375543,EBI-852101
TULP4	Q9NRJ4	1	EBI-375543,EBI-1753487
UHMK1	Q8TAS1	1	EBI-375543,EBI-1753608
VPREB1	P12018	1	EBI-375543,EBI-1753454
VPS13A	Q96RL7	1	EBI-375543,EBI-1752583
WBP7	Q9UMN6	1	EBI-375543,EBI-765774
WNK2	Q9Y3S1	1	EBI-375543,EBI-948521
YWHAZ	P63104	1	EBI-375543,EBI-347088

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform IA (identifier: P00519-1)

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 IB (identifier: P00519-2)

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

Note: The myristoylated c-ABL protein is reported to be nuclear. Ref.15 Myristoylated on Gly-2.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1130

1130

Proto-oncogene tyrosine-protein kinase ABL1

PRO_0000088050

Regions

Domain

61 – 121

61

SH3

Domain

127 – 217

91

SH2

Domain

242 – 493

252

Protein kinase

Nucleotide binding

248 – 256

9

ATP

Nucleotide binding

316 – 322

7

ATP

Region

1 – 60

60

CAP

Motif

381 – 405

25

Kinase activation loop

Motif

605 – 609

5

Nuclear localization signal Potential

Compositional bias

18 – 22

5

Poly-Ser

Compositional bias

605 – 609

5

Poly-Lys

Compositional bias

782 – 1019

238

Pro-rich

Compositional bias

897 – 903

7

Poly-Pro

Sites

Active site

363

1

Proton acceptor By similarity

Binding site

271

1

ATP

Site

26 – 27

2

Breakpoint for translocation to form BCR-ABL oncogene

Amino acid modifications

Modified residue

50

1

Phosphoserine Ref.29 Ref.20

Modified residue

185

1

Phosphotyrosine Ref.20 Ref.13 Ref.18

Modified residue

226

1

Phosphotyrosine; by autocatalysis Ref.13

Modified residue

253

1

Phosphotyrosine Ref.13

Modified residue

257

1

Phosphotyrosine Ref.13

Modified residue

264

1

Phosphotyrosine Ref.13

Modified residue

393

1

Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases Ref.20 Ref.13

Modified residue

394

1

Phosphothreonine Ref.13

Modified residue

446

1

Phosphoserine By similarity

Modified residue

469

1

Phosphotyrosine Ref.13

Modified residue

569

1

Phosphoserine Ref.20 Ref.17 Ref.19 Ref.21

Modified residue

613

1

Phosphothreonine Ref.20

Modified residue

620

1

Phosphoserine Ref.20

Modified residue

659

1

Phosphoserine Ref.20

Modified residue

683

1

Phosphoserine Ref.20 Ref.17

Modified residue

718

1

Phosphoserine Ref.20

Modified residue

735

1

Phosphothreonine Ref.15

Modified residue

781

1

Phosphothreonine Ref.20

Modified residue

805

1

Phosphoserine Ref.20 Ref.17

Modified residue

809

1

Phosphoserine Ref.20 Ref.17

Modified residue

814

1

Phosphothreonine Ref.20

Modified residue

844

1

Phosphothreonine Ref.20 Ref.21

Modified residue

852

1

Phosphothreonine Ref.20 Ref.21

Modified residue

917

1

Phosphoserine Ref.20 Ref.21

Modified residue

919

1

Phosphoserine Ref.20

Modified residue

936

1

Phosphoserine Ref.20

Modified residue

949

1

Phosphoserine Ref.17

Modified residue

977

1

Phosphoserine Ref.20

Natural variations

Alternative sequence

1 – 26

26

MLEIC…SCYLE → MGQQPGKVLGDQRRPSLPAL HFIKGAGKKESSRHGGPHCN VFVEH in isoform IB.

VSP_004957

Natural variant

47

1

R → G in a lung large cell carcinoma sample; somatic mutation. Ref.33

VAR_032676

Natural variant

140

1

L → P: dbSNP rs1064152. Ref.1

VAR_051692

Natural variant

166

1

R → K in a melanoma sample; somatic mutation. Ref.33

VAR_032677

Natural variant

247

1

K → R: dbSNP rs34549764.

VAR_051693

Natural variant

706

1

G → V

VAR_025043

Natural variant

810

1

P → L

VAR_032678

Natural variant

852

1

T → P

VAR_025044

Natural variant

900

1

P → S

VAR_025045

Natural variant

968

1

S → P: dbSNP rs1064165.

VAR_051694

Natural variant

972

1

S → L: dbSNP rs2229067. Ref.33 Ref.4

VAR_025046

Experimental info

Mutagenesis

735

1

T → A: Abolishes phosphorylation. Loss of binding YWHAS and YWHAZ. Localizes to the nucleus. No effect on kinase activity. Ref.15

Sequence conflict

159

1

G → S in AAA51561. Ref.1

Sequence conflict

424 – 425

2

AF → GK Ref.9

Sequence conflict

445

1

L → R in AAA51561. Ref.1

Sequence conflict

459

1

E → K in AAA51561. Ref.1

Sequence conflict

520

1

S → T in AAA51561. Ref.1

Sequence conflict

719

1

A → V in AAA51561. Ref.1

Sequence conflict

837

1

G → E in CAA34438. Ref.2

Sequence conflict

837

1

G → W in AAA51561. Ref.1

Sequence conflict

863

1

G → R in AAA51561. Ref.1

Sequence conflict

894

1

R → K in AAA51561. Ref.1

Sequence conflict

917 – 919

3

SPS → RPG in AAA51561. Ref.1

Sequence conflict

952

1

G → A in AAA51561. Ref.1

Sequence conflict

967 – 968

2

QS → HP in AAA51561. Ref.1

Sequence conflict

982

1

P → PL in AAA51561. Ref.1

Sequence conflict

1022

1

Missing in AAA51561. Ref.1

Sequence conflict

1045

1

R → G in AAA51561. Ref.1

Sequence conflict

1103

1

T → S in AAA51561. Ref.1

Secondary structure

1

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1130

Helix Strand Turn

Details...

Helix

49 – 53

5

Helix

58 – 60

3

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

Beta strand

142 – 144

3

Beta strand

148 – 153

6

Beta strand

155 – 157

3

Beta strand

161 – 167

7

Beta strand

170 – 178

9

Beta strand

184 – 187

4

Beta strand

192 – 194

3

Helix

195 – 204

10

Beta strand

209 – 211

3

Helix

239 – 241

3

Beta strand

242 – 248

7

Helix

249 – 251

3

Beta strand

254 – 261

8

Helix

262 – 264

3

Beta strand

266 – 272

7

Helix

280 – 290

11

Beta strand

301 – 305

5

Beta strand

307 – 310

4

Beta strand

312 – 316

5

Helix

323 – 329

7

Turn

332 – 334

3

Helix

337 – 357

21

Helix

366 – 368

3

Beta strand

369 – 371

3

Helix

373 – 375

3

Beta strand

377 – 379

3

Beta strand

389 – 391

3

Helix

403 – 405

3

Helix

408 – 413

6

Helix

418 – 433

16

Helix

445 – 447

3

Helix

448 – 453

6

Helix

466 – 475

10

Helix

480 – 482

3

Helix

486 – 509

24

Turn

510 – 512

3

Helix

1029 – 1045

17

Turn

1046 – 1048

3

Helix

1053 – 1070

18

Helix

1071 – 1073

3

Helix

1080 – 1097

18

Beta strand

1101 – 1104

4

Beta strand

1106 – 1108

3

Helix

1115 – 1128

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform IA [UniParc]. Last modified January 24, 2006. Version 4. Checksum: 85FE6C1C0E483EA2	FASTA	1,130	122,873
	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 NKPTVYGVSP NYDKWEMERT 250 260 270 280 290 300 DITMKHKLGG GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ 310 320 330 340 350 360 LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVNAVVL 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 GKQGVRGAVS TLLQAPELPT KTRTSRRAAE 550 560 570 580 590 600 HRDTTDVPEM PHSKGQGESD PLDHEPAVSP LLPRKERGPP EGGLNEDERL LPKDKKTNLF 610 620 630 640 650 660 SALIKKKKKT APTPPKRSSS FREMDGQPER RGAGEEEGRD ISNGALAFTP LDTADPAKSP 670 680 690 700 710 720 KPSNGAGVPN GALRESGGSG FRSPHLWKKS STLTSSRLAT GEEEGGGSSS KRFLRSCSAS 730 740 750 760 770 780 CVPHGAKDTE WRSVTLPRDL QSTGRQFDSS TFGGHKSEKP ALPRKRAGEN RSDQVTRGTV 790 800 810 820 830 840 TPPPRLVKKN EEAADEVFKD IMESSPGSSP PNLTPKPLRR QVTVAPASGL PHKEEAGKGS 850 860 870 880 890 900 ALGTPAAAEP VTPTSKAGSG APGGTSKGPA EESRVRRHKH SSESPGRDKG KLSRLKPAPP 910 920 930 940 950 960 PPPAASAGKA GGKPSQSPSQ EAAGEAVLGA KTKATSLVDA VNSDAAKPSQ PGEGLKKPVL 970 980 990 1000 1010 1020 PATPKPQSAK PSGTPISPAP VPSTLPSASS ALAGDQPSST AFIPLISTRV SLRKTRQPPE 1030 1040 1050 1060 1070 1080 RIASGAITKG VVLDSTEALC LAISRNSEQM ASHSAVLEAG KNLYTFCVSY VDSIQQMRNK 1090 1100 1110 1120 1130 FAFREAINKL ENNLRELQIC PATAGSGPAA TQDFSKLLSS VKEISDIVQR
	Isoform IB. Checksum: DF9D4512F78FFE52	FASTA	1,149	124,955
	10 20 30 40 50 60 MGQQPGKVLG DQRRPSLPAL HFIKGAGKKE 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 KPTVYGVSPN YDKWEMERTD ITMKHKLGGG QYGEVYEGVW KKYSLTVAVK TLKEDTMEVE 310 320 330 340 350 360 EFLKEAAVMK EIKHPNLVQL LGVCTREPPF YIITEFMTYG NLLDYLRECN RQEVNAVVLL 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 KQGVRGAVST 550 560 570 580 590 600 LLQAPELPTK TRTSRRAAEH RDTTDVPEMP HSKGQGESDP LDHEPAVSPL LPRKERGPPE 610 620 630 640 650 660 GGLNEDERLL PKDKKTNLFS ALIKKKKKTA PTPPKRSSSF REMDGQPERR GAGEEEGRDI 670 680 690 700 710 720 SNGALAFTPL DTADPAKSPK PSNGAGVPNG ALRESGGSGF RSPHLWKKSS TLTSSRLATG 730 740 750 760 770 780 EEEGGGSSSK RFLRSCSASC VPHGAKDTEW RSVTLPRDLQ STGRQFDSST FGGHKSEKPA 790 800 810 820 830 840 LPRKRAGENR SDQVTRGTVT PPPRLVKKNE EAADEVFKDI MESSPGSSPP NLTPKPLRRQ 850 860 870 880 890 900 VTVAPASGLP HKEEAGKGSA LGTPAAAEPV TPTSKAGSGA PGGTSKGPAE ESRVRRHKHS 910 920 930 940 950 960 SESPGRDKGK LSRLKPAPPP PPAASAGKAG GKPSQSPSQE AAGEAVLGAK TKATSLVDAV 970 980 990 1000 1010 1020 NSDAAKPSQP GEGLKKPVLP ATPKPQSAKP SGTPISPAPV PSTLPSASSA LAGDQPSSTA 1030 1040 1050 1060 1070 1080 FIPLISTRVS LRKTRQPPER IASGAITKGV VLDSTEALCL AISRNSEQMA SHSAVLEAGK 1090 1100 1110 1120 1130 1140 NLYTFCVSYV DSIQQMRNKF AFREAINKLE NNLRELQICP ATAGSGPAAT QDFSKLLSSV KEISDIVQR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Alternative splicing of RNAs transcribed from the human abl gene and from the bcr-abl fused gene." Shtivelman E., Lifshitz B., Gale R.P., Roe B.A., Canaani E. Cell 47:277-284(1986) [PubMed: 3021337] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IA), ALTERNATIVE SPLICING, VARIANT PRO-140.
[2]	"Nucleotide sequence analysis of human abl and bcr-abl cDNAs." Fainstein E., Einat M., Gokkel E., Marcelle C., Croce C.M., Gale R.P., Canaani E. Oncogene 4:1477-1481(1989) [PubMed: 2687768] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IA). Tissue: Fibroblast.
[3]	"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] (ISOFORMS IA AND IB). Tissue: Lung.
[4]	NIEHS SNPs program Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-706; PRO-852; SER-900 AND LEU-972.
[5]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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 IB). Tissue: Cerebellum.
[8]	"A new fused transcript in Philadelphia chromosome positive acute lymphocytic leukaemia." Fainstein E., Marcelle C., Rosner A., Canaani E., Gale R.P., Dreazen O., Smith S.D., Croce C.M. Nature 330:386-388(1987) [PubMed: 2825022] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-40, SUBCELLULAR COMPONENT.
[9]	"Homology between phosphotyrosine acceptor site of human c-abl and viral oncogene products." Groffen J., Heisterkamp N., Reynolds F.H. Jr., Stephenson J.R. Nature 304:167-169(1983) [PubMed: 6191223] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 360-426.
[10]	"Sequence analysis of the mutation at codon 834 and the sequence variation of codon 837 of c-abl gene." Inokuchi K., Futaki M., Dan K., Nomura T. Leukemia 8:343-344(1994) [PubMed: 7545908] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 825-845.
[11]	"N-terminal mutations activate the leukemogenic potential of the myristoylated form of c-abl." Jackson P., Baltimore D. EMBO J. 8:449-456(1989) [PubMed: 2542016] [Abstract] Cited for: MYRISTOYLATION (ISOFORM IB).
[12]	"A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells." Wisniewski D., Strife A., Swendeman S., Erdjument-Bromage H., Geromanos S., Kavanaugh W.M., Tempst P., Clarkson B. Blood 93:2707-2720(1999) [PubMed: 10194451] [Abstract] Cited for: INTERACTION WITH INPPL1.
[13]	"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry." Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C. Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed: 12522270] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185; TYR-226; TYR-253; TYR-257; TYR-264; TYR-393; THR-394 AND TYR-469, MASS SPECTROMETRY.
[14]	"Cloning, mapping, and characterization of the human sorbin and SH3 domain containing 1 (SORBS1) gene: a protein associated with c-Abl during insulin signaling in the hepatoma cell line Hep3B." Lin W.-H., Huang C.-J., Liu M.-W., Chang H.-M., Chen Y.-J., Tai T.-Y., Chuang L.-M. Genomics 74:12-20(2001) [PubMed: 11374898] [Abstract] Cited for: INTERACTION WITH SORBS1.
[15]	"JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage." Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y. Nat. Cell Biol. 7:278-285(2005) [PubMed: 15696159] [Abstract] Cited for: INTERACTION WITH YWHAB; YWHAE; YWHAG; YWHAH; SFN AND YWHAZ, PHOSPHORYLATION AT THR-735, MASS SPECTROMETRY, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-735.
[16]	"Protein binding and signaling properties of RIN1 suggest a unique effector function." Han L., Wong D., Dhaka A., Afar D.E.H., White M., Xie W., Herschman H., Witte O., Colicelli J. Proc. Natl. Acad. Sci. U.S.A. 94:4954-4959(1997) [PubMed: 9144171] [Abstract] Cited for: INTERACTION WITH RIN1, FUNCTION.
[17]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; SER-683; SER-805; SER-809 AND SER-949, MASS SPECTROMETRY. Tissue: Epithelium.
[18]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185, MASS SPECTROMETRY.
[19]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, MASS SPECTROMETRY.
[20]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; TYR-185; TYR-393; SER-569; THR-613; SER-620; SER-659; SER-683; SER-718; THR-781; SER-805; SER-809; THR-814; THR-844; THR-852; SER-917; SER-919; SER-936 AND SER-977, MASS SPECTROMETRY.
[21]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; THR-844; THR-852 AND SER-917, MASS SPECTROMETRY.
[22]	"Three-dimensional solution structure of the src homology 2 domain of c-abl." Overduin M., Rios C.B., Mayer B.J., Baltimore D., Cowburn D. Cell 70:697-704(1992) [PubMed: 1505033] [Abstract] Cited for: STRUCTURE BY NMR OF SH2 DOMAIN.
[23]	"Secondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR spectroscopy in solution." Overduin M., Mayer B.J., Rios C.B., Baltimore D., Cowburn D. Proc. Natl. Acad. Sci. U.S.A. 89:11673-11677(1992) [PubMed: 1281542] [Abstract] Cited for: STRUCTURE BY NMR OF SH2 DOMAIN.
[24]	"Homology modeling of the Abl-SH3 domain." Pisabarro M.T., Ortiz A.R., Serrano L., Wade R.C. Proteins 20:203-215(1994) [PubMed: 7892170] [Abstract] Cited for: 3D-STRUCTURE MODELING OF SH3 DOMAIN.
[25]	"The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct." Gosser Y.Q., Zheng J., Overduin M., Mayer B.J., Cowburn D. Structure 3:1075-1086(1995) [PubMed: 8590002] [Abstract] Cited for: STRUCTURE BY NMR OF SH3 DOMAIN.
[26]	"Crystal structure of the abl-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactions." Pisabarro M.T., Serrano L., Wilmanns M. J. Mol. Biol. 281:513-521(1998) [PubMed: 9698566] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 64-121.
[27]	"Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide." Donaldson L.W., Gish G., Pawson T., Kay L.E., Forman-Kay J.D. Proc. Natl. Acad. Sci. U.S.A. 99:14053-14058(2002) [PubMed: 12384576] [Abstract] Cited for: STRUCTURE BY NMR OF 62-122 IN COMPLEX WITH CRK.
[28]	"Structure of the kinase domain of an imatinib-resistant Abl mutant in complex with the Aurora kinase inhibitor VX-680." Young M.A., Shah N.P., Chao L.H., Seeliger M., Milanov Z.V., Biggs W.H. III, Treiber D.K., Patel H.K., Zarrinkar P.P., Lockhart D.J., Sawyers C.L., Kuriyan J. Cancer Res. 66:1007-1014(2006) [PubMed: 16424036] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 229-513 OF MUTANT PRO-396 IN COMPLEX WITH INHIBITOR VX-680, FUNCTION, ENZYME REGULATION.
[29]	"Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase." Nagar B., Hantschel O., Seeliger M., Davies J.M., Weis W.I., Superti-Furga G., Kuriyan J. Mol. Cell 21:787-798(2006) [PubMed: 16543148] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 38-512, MASS SPECTROMETRY, MYRISTOYLATION OF N-TERMINUS (ISOFORM IB), PHOSPHORYLATION AT SER-50, AUTOINHIBITION MECHANISM, ENZYME REGULATION.
[30]	"A Src-like inactive conformation in the abl tyrosine kinase domain." Levinson N.M., Kuchment O., Shen K., Young M.A., Koldobskiy M., Karplus M., Cole P.A., Kuriyan J. PLoS Biol. 4:E144-E144(2006) [PubMed: 16640460] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 229-512 IN COMPLEXES WITH ATP-PEPTIDE CONJUGATE, CONFORMATION CHANGES DURING ACTIVATION.
[31]	"Structural biology contributions to the discovery of drugs to treat chronic myelogenous leukaemia." Cowan-Jacob S.W., Fendrich G., Floersheimer A., Furet P., Liebetanz J., Rummel G., Rheinberger P., Centeleghe M., Fabbro D., Manley P.W. Acta Crystallogr. D 63:80-93(2007) [PubMed: 17164530] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 229-500 IN COMPLEXES WITH IMANITIB AND WITH THE INHIBITORS NVP-AEG082; NVP-AFN941; NVP-AFG210 AND PD180970.
[32]	"Crystallization by capillary counter-diffusion and structure determination of the N114A mutant of the SH3 domain of Abl tyrosine kinase complexed with a high-affinity peptide ligand." Camara-Artigas A., Palencia A., Martinez J.C., Luque I., Gavira J.A., Garcia-Ruiz J.M. Acta Crystallogr. D 63:646-652(2007) [PubMed: 17452790] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 64-121 OF MUTANT ALA-114 IN COMPLEX WITH PROLINE-RICH PEPTIDE.
[33]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS GLY-47; LYS-166; VAL-706; LEU-810 AND LEU-972.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

CGP resequencing studies

NIEHS-SNPs

Wikipedia

Abl entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

M14752 mRNA. Translation: AAA51561.1.
X16416 mRNA. Translation: CAA34438.1.
U07563 Genomic DNA. Translation: AAB60394.1.
U07563, U07561 Genomic DNA. Translation: AAB60393.1.
DQ145721 Genomic DNA. Translation: AAZ38718.1.
AL359092, AL161733 Genomic DNA. Translation: CAM45752.1.
AL161733 Genomic DNA. Translation: CAM45754.1.
AL161733, AL359092 Genomic DNA. Translation: CAM45756.1.
CH471090 Genomic DNA. Translation: EAW87948.1.
BC117451 mRNA. Translation: AAI17452.1.
S69223 Genomic DNA. Translation: AAD14034.1.

IPI

IPI00216969.
IPI00221171.

PIR

TVHUA. S08519.

RefSeq

NP_005148.2.
NP_009297.2.

UniGene

Hs.431048

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AB2	NMR	-	A	120-220	[»]
1ABL	model	-	A	65-121	[»]
1AWO	NMR	-	A	65-119	[»]
1BBZ	X-ray	1.65	A/C/E/G	64-121	[»]
1JU5	NMR	-	C	62-121	[»]
1OPL	X-ray	3.42	A/B	27-512	[»]
1ZZP	NMR	-	A	1007-1130	[»]
2ABL	X-ray	2.50	A	57-218	[»]
2E2B	X-ray	2.20	A/B	229-515	[»]
2F4J	X-ray	1.91	A	229-513	[»]
2FO0	X-ray	2.27	A	38-512	[»]
2G1T	X-ray	1.80	A/B/C/D	229-512	[»]
2G2F	X-ray	2.70	A/B	229-512	[»]
2G2H	X-ray	2.00	A/B	229-512	[»]
2G2I	X-ray	3.12	A/B	229-512	[»]
2GQG	X-ray	2.40	A/B	229-500	[»]
2HIW	X-ray	2.20	A/B	230-512	[»]
2HYY	X-ray	2.40	A/B/C/D	228-500	[»]
2HZ0	X-ray	2.10	A/B	228-497	[»]
2HZ4	X-ray	2.80	A/B/C	228-500	[»]
2HZI	X-ray	1.70	A/B	229-500	[»]
2O88	X-ray	1.75	A/B	64-121	[»]
2V7A	X-ray	2.50	A/B	229-512	[»]
3CS9	X-ray	2.21	A/B/C/D	229-500	[»]
3EG0	X-ray	2.30	A	60-121	[»]
3EG1	X-ray	1.85	A/B	60-121	[»]
3EG2	X-ray	1.80	A	60-121	[»]
3EG3	X-ray	1.40	A	60-121	[»]
3EGU	X-ray	2.25	A	60-121	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1042N.

IntAct

P00519. 160 interactions.

STRING

P00519.

PTM databases

PhosphoSite

P00519.

Proteomic databases

PRIDE

P00519.

Genome annotation databases

Ensembl

ENST00000318560; ENSP00000323315; ENSG00000097007; Homo sapiens. [Genome view]
ENST00000372348; ENSP00000361423; ENSG00000097007; Homo sapiens. [Genome view]
ENST00000393293; ENSP00000376971; ENSG00000097007; Homo sapiens. [Genome view]
ENST00000426772; ENSP00000406308; ENSG00000097007; Homo sapiens. [Genome view]
ENST00000438426; ENSP00000407756; ENSG00000097007; Homo sapiens. [Genome view]
ENST00000444970; ENSP00000400412; ENSG00000097007; Homo sapiens. [Genome view]

GeneID

25.

KEGG

hsa:25.

UCSC

uc004bzw.1. human.

Organism-specific databases

CTD

25.

GeneCards

GC09P132579.

H-InvDB

HIX0008474.

HGNC

HGNC:76. ABL1.

HPA

CAB002686.
HPA027251.
HPA027280.

MIM

189980. gene.
608232. phenotype.

Orphanet

521. Chronic myeloid leukemia.

PharmGKB

PA24413.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P00519.

OMA

GAFRESG.

Enzyme and pathway databases

BRENDA

2.7.10.2. 247.

Pathway_Interaction_DB

lis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development.
trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
pdgfrbpathway. PDGFR-beta signaling pathway.
telomerasepathway. Regulation of Telomerase.

Reactome

REACT_18266. Axon guidance.

Gene expression databases

ArrayExpress

P00519.

Bgee

P00519.

CleanEx

HS_ABL1.

Genevestigator

P00519.

GermOnline

ENSG00000097007. Homo sapiens.

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

DrugBank

DB00171. Adenosine triphosphate.
DB01254. Dasatinib.
DB00619. Imatinib.

NextBio

79.

PMAP-CutDB

P00519.

SOURCE

Search...

Entry information

Entry name

ABL1_HUMAN

Accession

Primary (citable) accession number: P00519
Secondary accession number(s): A3KFJ3 , Q13869, Q13870, Q16133, Q17R61, Q45F09

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 24, 2006
Last modified:	November 3, 2009
This is version 151 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.