P42684 (ABL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Abelson tyrosine-protein kinase 2
EC=2.7.10.2

Alternative name(s):
Abelson murine leukemia viral oncogene homolog 2
Abelson-related gene protein
Tyrosine-protein kinase ARG

Gene names

Name:	ABL2
Synonyms:	ABLL, ARG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1182 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Non-receptor tyrosine-protein kinase that plays an ABL1-overlapping role in key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion and receptor endocytosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like MYH10 (involved in movement); CTTN (involved in signaling); or TUBA1 and TUBB (microtubule subunits). Binds directly F-actin and regulates actin cytoskeletal structure through its F-actin-bundling activity. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as CRK, CRKL, DOK1 or ARHGAP35. Adhesion-dependent phosphorylation of ARHGAP35 promotes its association with RASA1, resulting in recruitment of ARHGAP35 to the cell periphery where it inhibits RHO. Phosphorylates multiple receptor tyrosine kinases like PDGFRB and other substrates which are involved in endocytosis regulation such as RIN1. In brain, may regulate neurotransmission by phosphorylating proteins at the synapse. ABL2 acts also as a regulator of multiple pathological signaling cascades during infection. Pathogens can highjack ABL2 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Ref.11 Ref.12 Ref.13 Ref.15 Ref.17
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 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. 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). Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant phosphoinositide known to regulate cytoskeletal and membrane proteins, inhibits the tyrosine kinase activity By similarity. Ref.10 Ref.11
Subunit structure	Interacts with PSMA7. Interacts with CTTN. Ref.11 Ref.13 Ref.30
Subcellular location	Cytoplasm › cytoskeleton.
Tissue specificity	Widely expressed.
Domain	Contains two distinct classes of F-actin-binding domains. Although both can bind F-actin, the 2 are required to bundle actin filaments By similarity. Ref.26
Post-translational modification	Phosphorylated at Tyr-261 by ABL1 in response to oxidative stress. Phosphorylated by PDGFRB By similarity. Ref.10 Ref.12 Polyubiquitinated. Polyubiquitination of ABL2 leads to degradation.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily. Contains 1 protein kinase domain. Contains 1 SH2 domain. Contains 1 SH3 domain.
Sequence caution	The sequence CAD98092.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
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 Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament bundle assembly Inferred from electronic annotation. Source: Compara axon guidance Traceable author statement. Source: Reactome cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cellular response to retinoic acid Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.11. Source: UniProtKB positive regulation of neuron projection development Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL positive regulation of oxidoreductase activity Inferred from direct assay PubMed 12893824. Source: BHF-UCL regulation of actin cytoskeleton reorganization Traceable author statement Ref.26. Source: UniProtKB regulation of autophagy Traceable author statement Ref.26. Source: UniProtKB regulation of cell adhesion Traceable author statement Ref.26. Source: UniProtKB regulation of cell motility Traceable author statement Ref.26. Source: UniProtKB regulation of endocytosis Traceable author statement Ref.26. Source: UniProtKB signal transduction Traceable author statement Ref.1. Source: ProtInc
Cellular_component	actin cytoskeleton Traceable author statement Ref.26. Source: UniProtKB cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW actin filament binding Traceable author statement Ref.26. Source: UniProtKB actin monomer binding Traceable author statement Ref.26. Source: UniProtKB magnesium ion binding Inferred from direct assay Ref.11. Source: UniProtKB manganese ion binding Inferred from direct assay Ref.11. Source: UniProtKB non-membrane spanning protein tyrosine kinase activity Traceable author statement Ref.26. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CRK	P46108	5	EBI-1102694,EBI-886
FYN	P06241	2	EBI-1102694,EBI-515315
GRB2	P62993	2	EBI-1102694,EBI-401755
NCK1	P16333	3	EBI-1102694,EBI-389883
PIK3R1	P27986	2	EBI-1102694,EBI-79464
PLCG1	P19174	4	EBI-1102694,EBI-79387
RIN1	Q13671	4	EBI-1102694,EBI-366017
SRC	P12931	2	EBI-1102694,EBI-621482

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P42684-1)

Also known as: IB; 1BLCTL;

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 2 (identifier: P42684-2)

Also known as: IA; 1ASCTL;

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MGQQVGRVGE...EGDKTGGSSP → MVLGTVLLPP...ASESALPDLT

Isoform 3 (identifier: P42684-3)

Also known as: IC; 1ALCTL;

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: MGQQVGRVGE...ETGFNIFTQH → MVLGTVLLPP...ASESALPDLT

Isoform 4 (identifier: P42684-4)

Also known as: 1ASCTS;

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MGQQVGRVGE...EGDKTGGSSP → MVLGTVLLPP...ASESALPDLT
     688-790: Missing.

Note: Contains a phosphotyrosine at position 647.

Isoform 5 (identifier: P42684-5)

Also known as: 1BLCTS;

The sequence of this isoform differs from the canonical sequence as follows:
     688-790: Missing.

Note: Contains a phosphotyrosine at position 683.

Isoform 6 (identifier: P42684-6)

Also known as: 1BSCTL;

The sequence of this isoform differs from the canonical sequence as follows:
     53-73: Missing.

Isoform 7 (identifier: P42684-7)

Also known as: 1BSCTS;

The sequence of this isoform differs from the canonical sequence as follows:
     53-73: Missing.
     688-790: Missing.

Note: Contains a phosphotyrosine at position 662.

Isoform 10 (identifier: P42684-10)

Also known as: 1ALCTS;

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: MGQQVGRVGE...ETGFNIFTQH → MVLGTVLLPP...ASESALPDLT
     688-790: Missing.

Note: Contains a phosphotyrosine at position 668.

Isoform 8 (identifier: P42684-8)

The sequence of this isoform differs from the canonical sequence as follows:
     53-73: Missing.
     550-564: EEVAEELGRAASSSS → EVLLHCANQTCITL
     565-1182: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1182

1182

Abelson tyrosine-protein kinase 2

PRO_0000088052

Regions

Domain

107 – 167

61

SH3

Domain

173 – 263

91

SH2

Domain

288 – 539

252

Protein kinase

Nucleotide binding

294 – 302

9

ATP By similarity

Nucleotide binding

362 – 368

7

ATP By similarity

Region

1 – 106

106

CAP

Region

694 – 930

237

F-actin-binding By similarity

Region

1020 – 1182

163

F-actin-binding By similarity

Motif

427 – 451

25

Kinase activation loop By similarity

Motif

658 – 660

3

Nuclear localization signal Potential

Compositional bias

561 – 564

4

Poly-Ser

Compositional bias

732 – 739

8

Poly-Gly

Compositional bias

843 – 1055

213

Pro-rich

Compositional bias

984 – 988

5

Poly-Pro

Sites

Active site

409

1

Proton acceptor By similarity

Binding site

317

1

ATP By similarity

Amino acid modifications

Modified residue

261

1

Phosphotyrosine; by ABL1 and autocatalysis Ref.12

Modified residue

272

1

Phosphotyrosine; by autocatalysis Ref.10

Modified residue

275

1

Phosphoserine Ref.20

Modified residue

439

1

Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases Ref.10

Modified residue

568

1

Phosphotyrosine; by autocatalysis Ref.10

Modified residue

620

1

Phosphoserine Ref.21

Modified residue

631

1

Phosphoserine Ref.21 Ref.25 Ref.27

Modified residue

633

1

Phosphoserine Ref.21

Modified residue

655

1

Phosphoserine Ref.21

Modified residue

683

1

Phosphotyrosine; by autocatalysis Ref.10 Ref.23

Modified residue

718

1

Phosphotyrosine Ref.23

Modified residue

817

1

Phosphoserine Ref.16 Ref.21

Modified residue

820

1

Phosphoserine Ref.21 Ref.24

Modified residue

915

1

Phosphoserine Ref.20

Modified residue

936

1

Phosphoserine Ref.21 Ref.24 Ref.25

Lipidation

2

1

N-myristoyl glycine By similarity

Natural variations

Alternative sequence

1 – 73

73

MGQQV…GGSSP → MVLGTVLLPPNSYGRDQDTS LCCLCTEASESALPDLT in isoform 2 and isoform 4.

VSP_004961

Alternative sequence

1 – 52

52

MGQQV…IFTQH → MVLGTVLLPPNSYGRDQDTS LCCLCTEASESALPDLT in isoform 3 and isoform 10.

VSP_017112

Alternative sequence

53 – 73

21

Missing in isoform 6, isoform 7 and isoform 8.

VSP_041772

Alternative sequence

550 – 564

15

EEVAE…ASSSS → EVLLHCANQTCITL in isoform 8.

VSP_041773

Alternative sequence

565 – 1182

618

Missing in isoform 8.

VSP_041774

Alternative sequence

688 – 790

103

Missing in isoform 4, isoform 5, isoform 7 and isoform 10.

VSP_021308

Natural variant

78

1

R → H. Ref.31
Corresponds to variant rs55655202 [ dbSNP | Ensembl ].

VAR_055411

Natural variant

99

1

E → Q Somatic mutation in a breast cancer sample. Ref.31

VAR_055412

Natural variant

519

1

R → I Somatic mutation in a lung squamous cell carcinoma. Ref.31

VAR_055413

Natural variant

769

1

T → S. Ref.31
Corresponds to variant rs55892721 [ dbSNP | Ensembl ].

VAR_055414

Natural variant

930

1

K → R. Ref.5 Ref.31
Corresponds to variant rs17277288 [ dbSNP | Ensembl ].

VAR_029232

Natural variant

946

1

V → M. Ref.5
Corresponds to variant rs28913889 [ dbSNP | Ensembl ].

VAR_029233

Natural variant

996

1

P → R. Ref.5 Ref.31
Corresponds to variant rs28913890 [ dbSNP | Ensembl ].

VAR_029234

Natural variant

1085

1

S → N. Ref.5
Corresponds to variant rs28913891 [ dbSNP | Ensembl ].

VAR_029235

Natural variant

1101

1

T → A. Ref.5
Corresponds to variant rs28913892 [ dbSNP | Ensembl ].

VAR_029236

Isoform 4:

Natural variant

12

1

S → T.
Corresponds to variant rs1318056 [ dbSNP | Ensembl ].

Experimental info

Sequence conflict

343 – 344

2

NL → TI no nucleotide entry Ref.9

Sequence conflict

435

1

T → I in AK311045. Ref.3

Sequence conflict

981

1

K → R in CAD98092. Ref.4

Secondary structure

1

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1182

Helix Strand Turn

Details...

Beta strand

171 – 177

7

Helix

180 – 188

9

Beta strand

194 – 203

10

Beta strand

206 – 212

7

Beta strand

217 – 220

4

Beta strand

226 – 228

3

Helix

241 – 250

10

Beta strand

255 – 257

3

Beta strand

280 – 282

3

Helix

285 – 287

3

Beta strand

288 – 293

6

Helix

294 – 297

4

Beta strand

300 – 307

8

Helix

308 – 310

3

Beta strand

312 – 318

7

Helix

326 – 337

12

Beta strand

347 – 351

5

Beta strand

353 – 356

4

Beta strand

358 – 362

5

Helix

369 – 375

7

Turn

378 – 380

3

Helix

383 – 402

20

Helix

412 – 414

3

Beta strand

415 – 417

3

Helix

419 – 421

3

Beta strand

423 – 425

3

Beta strand

435 – 437

3

Beta strand

438 – 440

3

Helix

449 – 451

3

Helix

454 – 459

6

Helix

464 – 479

16

Helix

491 – 493

3

Helix

494 – 499

6

Helix

512 – 521

10

Helix

526 – 528

3

Helix

532 – 545

14

Helix

1069 – 1071

3

Turn

1076 – 1078

3

Helix

1080 – 1083

4

Helix

1086 – 1099

14

Helix

1106 – 1123

18

Helix

1124 – 1126

3

Helix

1130 – 1152

23

Beta strand

1155 – 1158

4

Helix

1165 – 1181

17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (IB) (1BLCTL) [UniParc]. Last modified November 1, 1995. Version 1. Checksum: ED93869BC2B14FAA	FASTA	1,182	128,343
	10 20 30 40 50 60 MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TTETGFNIFT QHDHFASCVE 70 80 90 100 110 120 DGFEGDKTGG SSPEALHRPY GCDVEPQALN EAIRWSSKEN LLGATESDPN LFVALYDFVA 130 140 150 160 170 180 SGDNTLSITK GEKLRVLGYN QNGEWSEVRS KNGQGWVPSN YITPVNSLEK HSWYHGPVSR 190 200 210 220 230 240 SAAEYLLSSL INGSFLVRES ESSPGQLSIS LRYEGRVYHY RINTTADGKV YVTAESRFST 250 260 270 280 290 300 LAELVHHHST VADGLVTTLH YPAPKCNKPT VYGVSPIHDK WEMERTDITM KHKLGGGQYG 310 320 330 340 350 360 EVYVGVWKKY SLTVAVKTLK EDTMEVEEFL KEAAVMKEIK HPNLVQLLGV CTLEPPFYIV 370 380 390 400 410 420 TEYMPYGNLL DYLRECNREE VTAVVLLYMA TQISSAMEYL EKKNFIHRDL AARNCLVGEN 430 440 450 460 470 480 HVVKVADFGL SRLMTGDTYT AHAGAKFPIK WTAPESLAYN TFSIKSDVWA FGVLLWEIAT 490 500 510 520 530 540 YGMSPYPGID LSQVYDLLEK GYRMEQPEGC PPKVYELMRA CWKWSPADRP SFAETHQAFE 550 560 570 580 590 600 TMFHDSSISE EVAEELGRAA SSSSVVPYLP RLPILPSKTR TLKKQVENKE NIEGAQDATE 610 620 630 640 650 660 NSASSLAPGF IRGAQASSGS PALPRKQRDK SPSSLLEDAK ETCFTRDRKG GFFSSFMKKR 670 680 690 700 710 720 NAPTPPKRSS SFREMENQPH KKYELTGNFS SVASLQHADG FSFTPAQQEA NLVPPKCYGG 730 740 750 760 770 780 SFAQRNLCND DGGGGGGSGT AGGGWSGITG FFTPRLIKKT LGLRAGKPTA SDDTSKPFPR 790 800 810 820 830 840 SNSTSSMSSG LPEQDRMAMT LPRNCQRSKL QLERTVSTSS QPEENVDRAN DMLPKKSEES 850 860 870 880 890 900 AAPSRERPKA KLLPRGATAL PLRTPSGDLA ITEKDPPGVG VAGVAAAPKG KEKNGGARLG 910 920 930 940 950 960 MAGVPEDGEQ PGWPSPAKAA PVLPTTHNHK VPVLISPTLK HTPADVQLIG TDSQGNKFKL 970 980 990 1000 1010 1020 LSEHQVTSSG DKDRPRRVKP KCAPPPPPVM RLLQHPSICS DPTEEPTALT AGQSTSETQE 1030 1040 1050 1060 1070 1080 GGKKAALGAV PISGKAGRPV MPPPQVPLPT SSISPAKMAN GTAGTKVALR KTKQAAEKIS 1090 1100 1110 1120 1130 1140 ADKISKEALL ECADLLSSAL TEPVPNSQLV DTGHQLLDYC SGYVDCIPQT RNKFAFREAV 1150 1160 1170 1180 SKLELSLQEL QVSSAAAGVP GTNPVLNNLL SCVQEISDVV QR
	Isoform 2 (IA) (1ASCTL) [UniParc]. Checksum: EB47F5DE7CFDAE67	FASTA	1,146	124,560
	10 20 30 40 50 60 MVLGTVLLPP NSYGRDQDTS LCCLCTEASE SALPDLTEAL HRPYGCDVEP QALNEAIRWS 70 80 90 100 110 120 SKENLLGATE SDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNQNGEWS EVRSKNGQGW 130 140 150 160 170 180 VPSNYITPVN SLEKHSWYHG PVSRSAAEYL LSSLINGSFL VRESESSPGQ LSISLRYEGR 190 200 210 220 230 240 VYHYRINTTA DGKVYVTAES RFSTLAELVH HHSTVADGLV TTLHYPAPKC NKPTVYGVSP 250 260 270 280 290 300 IHDKWEMERT DITMKHKLGG GQYGEVYVGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM 310 320 330 340 350 360 KEIKHPNLVQ LLGVCTLEPP FYIVTEYMPY GNLLDYLREC NREEVTAVVL LYMATQISSA 370 380 390 400 410 420 MEYLEKKNFI HRDLAARNCL VGENHVVKVA DFGLSRLMTG DTYTAHAGAK FPIKWTAPES 430 440 450 460 470 480 LAYNTFSIKS DVWAFGVLLW EIATYGMSPY PGIDLSQVYD LLEKGYRMEQ PEGCPPKVYE 490 500 510 520 530 540 LMRACWKWSP ADRPSFAETH QAFETMFHDS SISEEVAEEL GRAASSSSVV PYLPRLPILP 550 560 570 580 590 600 SKTRTLKKQV ENKENIEGAQ DATENSASSL APGFIRGAQA SSGSPALPRK QRDKSPSSLL 610 620 630 640 650 660 EDAKETCFTR DRKGGFFSSF MKKRNAPTPP KRSSSFREME NQPHKKYELT GNFSSVASLQ 670 680 690 700 710 720 HADGFSFTPA QQEANLVPPK CYGGSFAQRN LCNDDGGGGG GSGTAGGGWS GITGFFTPRL 730 740 750 760 770 780 IKKTLGLRAG KPTASDDTSK PFPRSNSTSS MSSGLPEQDR MAMTLPRNCQ RSKLQLERTV 790 800 810 820 830 840 STSSQPEENV DRANDMLPKK SEESAAPSRE RPKAKLLPRG ATALPLRTPS GDLAITEKDP 850 860 870 880 890 900 PGVGVAGVAA APKGKEKNGG ARLGMAGVPE DGEQPGWPSP AKAAPVLPTT HNHKVPVLIS 910 920 930 940 950 960 PTLKHTPADV QLIGTDSQGN KFKLLSEHQV TSSGDKDRPR RVKPKCAPPP PPVMRLLQHP 970 980 990 1000 1010 1020 SICSDPTEEP TALTAGQSTS ETQEGGKKAA LGAVPISGKA GRPVMPPPQV PLPTSSISPA 1030 1040 1050 1060 1070 1080 KMANGTAGTK VALRKTKQAA EKISADKISK EALLECADLL SSALTEPVPN SQLVDTGHQL 1090 1100 1110 1120 1130 1140 LDYCSGYVDC IPQTRNKFAF REAVSKLELS LQELQVSSAA AGVPGTNPVL NNLLSCVQEI SDVVQR
	Isoform 3 (IC) (1ALCTL) [UniParc]. Checksum: 0E3923FE9EEEAFEC	FASTA	1,167	126,684
	10 20 30 40 50 60 MVLGTVLLPP NSYGRDQDTS LCCLCTEASE SALPDLTDHF ASCVEDGFEG DKTGGSSPEA 70 80 90 100 110 120 LHRPYGCDVE PQALNEAIRW SSKENLLGAT ESDPNLFVAL YDFVASGDNT LSITKGEKLR 130 140 150 160 170 180 VLGYNQNGEW SEVRSKNGQG WVPSNYITPV NSLEKHSWYH GPVSRSAAEY LLSSLINGSF 190 200 210 220 230 240 LVRESESSPG QLSISLRYEG RVYHYRINTT ADGKVYVTAE SRFSTLAELV HHHSTVADGL 250 260 270 280 290 300 VTTLHYPAPK CNKPTVYGVS PIHDKWEMER TDITMKHKLG GGQYGEVYVG VWKKYSLTVA 310 320 330 340 350 360 VKTLKEDTME VEEFLKEAAV MKEIKHPNLV QLLGVCTLEP PFYIVTEYMP YGNLLDYLRE 370 380 390 400 410 420 CNREEVTAVV LLYMATQISS AMEYLEKKNF IHRDLAARNC LVGENHVVKV ADFGLSRLMT 430 440 450 460 470 480 GDTYTAHAGA KFPIKWTAPE SLAYNTFSIK SDVWAFGVLL WEIATYGMSP YPGIDLSQVY 490 500 510 520 530 540 DLLEKGYRME QPEGCPPKVY ELMRACWKWS PADRPSFAET HQAFETMFHD SSISEEVAEE 550 560 570 580 590 600 LGRAASSSSV VPYLPRLPIL PSKTRTLKKQ VENKENIEGA QDATENSASS LAPGFIRGAQ 610 620 630 640 650 660 ASSGSPALPR KQRDKSPSSL LEDAKETCFT RDRKGGFFSS FMKKRNAPTP PKRSSSFREM 670 680 690 700 710 720 ENQPHKKYEL TGNFSSVASL QHADGFSFTP AQQEANLVPP KCYGGSFAQR NLCNDDGGGG 730 740 750 760 770 780 GGSGTAGGGW SGITGFFTPR LIKKTLGLRA GKPTASDDTS KPFPRSNSTS SMSSGLPEQD 790 800 810 820 830 840 RMAMTLPRNC QRSKLQLERT VSTSSQPEEN VDRANDMLPK KSEESAAPSR ERPKAKLLPR 850 860 870 880 890 900 GATALPLRTP SGDLAITEKD PPGVGVAGVA AAPKGKEKNG GARLGMAGVP EDGEQPGWPS 910 920 930 940 950 960 PAKAAPVLPT THNHKVPVLI SPTLKHTPAD VQLIGTDSQG NKFKLLSEHQ VTSSGDKDRP 970 980 990 1000 1010 1020 RRVKPKCAPP PPPVMRLLQH PSICSDPTEE PTALTAGQST SETQEGGKKA ALGAVPISGK 1030 1040 1050 1060 1070 1080 AGRPVMPPPQ VPLPTSSISP AKMANGTAGT KVALRKTKQA AEKISADKIS KEALLECADL 1090 1100 1110 1120 1130 1140 LSSALTEPVP NSQLVDTGHQ LLDYCSGYVD CIPQTRNKFA FREAVSKLEL SLQELQVSSA 1150 1160 AAGVPGTNPV LNNLLSCVQE ISDVVQR
	Isoform 4 (1ASCTS) [UniParc]. Checksum: 973C4751FD7E13F9	FASTA	1,043	114,159
	10 20 30 40 50 60 MVLGTVLLPP NSYGRDQDTS LCCLCTEASE SALPDLTEAL HRPYGCDVEP QALNEAIRWS 70 80 90 100 110 120 SKENLLGATE SDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNQNGEWS EVRSKNGQGW 130 140 150 160 170 180 VPSNYITPVN SLEKHSWYHG PVSRSAAEYL LSSLINGSFL VRESESSPGQ LSISLRYEGR 190 200 210 220 230 240 VYHYRINTTA DGKVYVTAES RFSTLAELVH HHSTVADGLV TTLHYPAPKC NKPTVYGVSP 250 260 270 280 290 300 IHDKWEMERT DITMKHKLGG GQYGEVYVGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM 310 320 330 340 350 360 KEIKHPNLVQ LLGVCTLEPP FYIVTEYMPY GNLLDYLREC NREEVTAVVL LYMATQISSA 370 380 390 400 410 420 MEYLEKKNFI HRDLAARNCL VGENHVVKVA DFGLSRLMTG DTYTAHAGAK FPIKWTAPES 430 440 450 460 470 480 LAYNTFSIKS DVWAFGVLLW EIATYGMSPY PGIDLSQVYD LLEKGYRMEQ PEGCPPKVYE 490 500 510 520 530 540 LMRACWKWSP ADRPSFAETH QAFETMFHDS SISEEVAEEL GRAASSSSVV PYLPRLPILP 550 560 570 580 590 600 SKTRTLKKQV ENKENIEGAQ DATENSASSL APGFIRGAQA SSGSPALPRK QRDKSPSSLL 610 620 630 640 650 660 EDAKETCFTR DRKGGFFSSF MKKRNAPTPP KRSSSFREME NQPHKKYELT GLPEQDRMAM 670 680 690 700 710 720 TLPRNCQRSK LQLERTVSTS SQPEENVDRA NDMLPKKSEE SAAPSRERPK AKLLPRGATA 730 740 750 760 770 780 LPLRTPSGDL AITEKDPPGV GVAGVAAAPK GKEKNGGARL GMAGVPEDGE QPGWPSPAKA 790 800 810 820 830 840 APVLPTTHNH KVPVLISPTL KHTPADVQLI GTDSQGNKFK LLSEHQVTSS GDKDRPRRVK 850 860 870 880 890 900 PKCAPPPPPV MRLLQHPSIC SDPTEEPTAL TAGQSTSETQ EGGKKAALGA VPISGKAGRP 910 920 930 940 950 960 VMPPPQVPLP TSSISPAKMA NGTAGTKVAL RKTKQAAEKI SADKISKEAL LECADLLSSA 970 980 990 1000 1010 1020 LTEPVPNSQL VDTGHQLLDY CSGYVDCIPQ TRNKFAFREA VSKLELSLQE LQVSSAAAGV 1030 1040 PGTNPVLNNL LSCVQEISDV VQR
	Isoform 5 (1BLCTS) [UniParc]. Checksum: 9916652E5DB8F74D	FASTA	1,079	117,942
	10 20 30 40 50 60 MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TTETGFNIFT QHDHFASCVE 70 80 90 100 110 120 DGFEGDKTGG SSPEALHRPY GCDVEPQALN EAIRWSSKEN LLGATESDPN LFVALYDFVA 130 140 150 160 170 180 SGDNTLSITK GEKLRVLGYN QNGEWSEVRS KNGQGWVPSN YITPVNSLEK HSWYHGPVSR 190 200 210 220 230 240 SAAEYLLSSL INGSFLVRES ESSPGQLSIS LRYEGRVYHY RINTTADGKV YVTAESRFST 250 260 270 280 290 300 LAELVHHHST VADGLVTTLH YPAPKCNKPT VYGVSPIHDK WEMERTDITM KHKLGGGQYG 310 320 330 340 350 360 EVYVGVWKKY SLTVAVKTLK EDTMEVEEFL KEAAVMKEIK HPNLVQLLGV CTLEPPFYIV 370 380 390 400 410 420 TEYMPYGNLL DYLRECNREE VTAVVLLYMA TQISSAMEYL EKKNFIHRDL AARNCLVGEN 430 440 450 460 470 480 HVVKVADFGL SRLMTGDTYT AHAGAKFPIK WTAPESLAYN TFSIKSDVWA FGVLLWEIAT 490 500 510 520 530 540 YGMSPYPGID LSQVYDLLEK GYRMEQPEGC PPKVYELMRA CWKWSPADRP SFAETHQAFE 550 560 570 580 590 600 TMFHDSSISE EVAEELGRAA SSSSVVPYLP RLPILPSKTR TLKKQVENKE NIEGAQDATE 610 620 630 640 650 660 NSASSLAPGF IRGAQASSGS PALPRKQRDK SPSSLLEDAK ETCFTRDRKG GFFSSFMKKR 670 680 690 700 710 720 NAPTPPKRSS SFREMENQPH KKYELTGLPE QDRMAMTLPR NCQRSKLQLE RTVSTSSQPE 730 740 750 760 770 780 ENVDRANDML PKKSEESAAP SRERPKAKLL PRGATALPLR TPSGDLAITE KDPPGVGVAG 790 800 810 820 830 840 VAAAPKGKEK NGGARLGMAG VPEDGEQPGW PSPAKAAPVL PTTHNHKVPV LISPTLKHTP 850 860 870 880 890 900 ADVQLIGTDS QGNKFKLLSE HQVTSSGDKD RPRRVKPKCA PPPPPVMRLL QHPSICSDPT 910 920 930 940 950 960 EEPTALTAGQ STSETQEGGK KAALGAVPIS GKAGRPVMPP PQVPLPTSSI SPAKMANGTA 970 980 990 1000 1010 1020 GTKVALRKTK QAAEKISADK ISKEALLECA DLLSSALTEP VPNSQLVDTG HQLLDYCSGY 1030 1040 1050 1060 1070 VDCIPQTRNK FAFREAVSKL ELSLQELQVS SAAAGVPGTN PVLNNLLSCV QEISDVVQR
	Isoform 6 (1BSCTL) [UniParc]. Checksum: A54046CDF6770B1C	FASTA	1,161	126,219
	10 20 30 40 50 60 MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TTETGFNIFT QHEALHRPYG 70 80 90 100 110 120 CDVEPQALNE AIRWSSKENL LGATESDPNL FVALYDFVAS GDNTLSITKG EKLRVLGYNQ 130 140 150 160 170 180 NGEWSEVRSK NGQGWVPSNY ITPVNSLEKH SWYHGPVSRS AAEYLLSSLI NGSFLVRESE 190 200 210 220 230 240 SSPGQLSISL RYEGRVYHYR INTTADGKVY VTAESRFSTL AELVHHHSTV ADGLVTTLHY 250 260 270 280 290 300 PAPKCNKPTV YGVSPIHDKW EMERTDITMK HKLGGGQYGE VYVGVWKKYS LTVAVKTLKE 310 320 330 340 350 360 DTMEVEEFLK EAAVMKEIKH PNLVQLLGVC TLEPPFYIVT EYMPYGNLLD YLRECNREEV 370 380 390 400 410 420 TAVVLLYMAT QISSAMEYLE KKNFIHRDLA ARNCLVGENH VVKVADFGLS RLMTGDTYTA 430 440 450 460 470 480 HAGAKFPIKW TAPESLAYNT FSIKSDVWAF GVLLWEIATY GMSPYPGIDL SQVYDLLEKG 490 500 510 520 530 540 YRMEQPEGCP PKVYELMRAC WKWSPADRPS FAETHQAFET MFHDSSISEE VAEELGRAAS 550 560 570 580 590 600 SSSVVPYLPR LPILPSKTRT LKKQVENKEN IEGAQDATEN SASSLAPGFI RGAQASSGSP 610 620 630 640 650 660 ALPRKQRDKS PSSLLEDAKE TCFTRDRKGG FFSSFMKKRN APTPPKRSSS FREMENQPHK 670 680 690 700 710 720 KYELTGNFSS VASLQHADGF SFTPAQQEAN LVPPKCYGGS FAQRNLCNDD GGGGGGSGTA 730 740 750 760 770 780 GGGWSGITGF FTPRLIKKTL GLRAGKPTAS DDTSKPFPRS NSTSSMSSGL PEQDRMAMTL 790 800 810 820 830 840 PRNCQRSKLQ LERTVSTSSQ PEENVDRAND MLPKKSEESA APSRERPKAK LLPRGATALP 850 860 870 880 890 900 LRTPSGDLAI TEKDPPGVGV AGVAAAPKGK EKNGGARLGM AGVPEDGEQP GWPSPAKAAP 910 920 930 940 950 960 VLPTTHNHKV PVLISPTLKH TPADVQLIGT DSQGNKFKLL SEHQVTSSGD KDRPRRVKPK 970 980 990 1000 1010 1020 CAPPPPPVMR LLQHPSICSD PTEEPTALTA GQSTSETQEG GKKAALGAVP ISGKAGRPVM 1030 1040 1050 1060 1070 1080 PPPQVPLPTS SISPAKMANG TAGTKVALRK TKQAAEKISA DKISKEALLE CADLLSSALT 1090 1100 1110 1120 1130 1140 EPVPNSQLVD TGHQLLDYCS GYVDCIPQTR NKFAFREAVS KLELSLQELQ VSSAAAGVPG 1150 1160 TNPVLNNLLS CVQEISDVVQ R
	Isoform 7 (1BSCTS) [UniParc]. Checksum: 28DCB354F9917898	FASTA	1,058	115,817
	10 20 30 40 50 60 MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TTETGFNIFT QHEALHRPYG 70 80 90 100 110 120 CDVEPQALNE AIRWSSKENL LGATESDPNL FVALYDFVAS GDNTLSITKG EKLRVLGYNQ 130 140 150 160 170 180 NGEWSEVRSK NGQGWVPSNY ITPVNSLEKH SWYHGPVSRS AAEYLLSSLI NGSFLVRESE 190 200 210 220 230 240 SSPGQLSISL RYEGRVYHYR INTTADGKVY VTAESRFSTL AELVHHHSTV ADGLVTTLHY 250 260 270 280 290 300 PAPKCNKPTV YGVSPIHDKW EMERTDITMK HKLGGGQYGE VYVGVWKKYS LTVAVKTLKE 310 320 330 340 350 360 DTMEVEEFLK EAAVMKEIKH PNLVQLLGVC TLEPPFYIVT EYMPYGNLLD YLRECNREEV 370 380 390 400 410 420 TAVVLLYMAT QISSAMEYLE KKNFIHRDLA ARNCLVGENH VVKVADFGLS RLMTGDTYTA 430 440 450 460 470 480 HAGAKFPIKW TAPESLAYNT FSIKSDVWAF GVLLWEIATY GMSPYPGIDL SQVYDLLEKG 490 500 510 520 530 540 YRMEQPEGCP PKVYELMRAC WKWSPADRPS FAETHQAFET MFHDSSISEE VAEELGRAAS 550 560 570 580 590 600 SSSVVPYLPR LPILPSKTRT LKKQVENKEN IEGAQDATEN SASSLAPGFI RGAQASSGSP 610 620 630 640 650 660 ALPRKQRDKS PSSLLEDAKE TCFTRDRKGG FFSSFMKKRN APTPPKRSSS FREMENQPHK 670 680 690 700 710 720 KYELTGLPEQ DRMAMTLPRN CQRSKLQLER TVSTSSQPEE NVDRANDMLP KKSEESAAPS 730 740 750 760 770 780 RERPKAKLLP RGATALPLRT PSGDLAITEK DPPGVGVAGV AAAPKGKEKN GGARLGMAGV 790 800 810 820 830 840 PEDGEQPGWP SPAKAAPVLP TTHNHKVPVL ISPTLKHTPA DVQLIGTDSQ GNKFKLLSEH 850 860 870 880 890 900 QVTSSGDKDR PRRVKPKCAP PPPPVMRLLQ HPSICSDPTE EPTALTAGQS TSETQEGGKK 910 920 930 940 950 960 AALGAVPISG KAGRPVMPPP QVPLPTSSIS PAKMANGTAG TKVALRKTKQ AAEKISADKI 970 980 990 1000 1010 1020 SKEALLECAD LLSSALTEPV PNSQLVDTGH QLLDYCSGYV DCIPQTRNKF AFREAVSKLE 1030 1040 1050 LSLQELQVSS AAAGVPGTNP VLNNLLSCVQ EISDVVQR
	Isoform 10 (1ALCTS) [UniParc]. Checksum: AF67137EC553DFE7	FASTA	1,064	116,283
	10 20 30 40 50 60 MVLGTVLLPP NSYGRDQDTS LCCLCTEASE SALPDLTDHF ASCVEDGFEG DKTGGSSPEA 70 80 90 100 110 120 LHRPYGCDVE PQALNEAIRW SSKENLLGAT ESDPNLFVAL YDFVASGDNT LSITKGEKLR 130 140 150 160 170 180 VLGYNQNGEW SEVRSKNGQG WVPSNYITPV NSLEKHSWYH GPVSRSAAEY LLSSLINGSF 190 200 210 220 230 240 LVRESESSPG QLSISLRYEG RVYHYRINTT ADGKVYVTAE SRFSTLAELV HHHSTVADGL 250 260 270 280 290 300 VTTLHYPAPK CNKPTVYGVS PIHDKWEMER TDITMKHKLG GGQYGEVYVG VWKKYSLTVA 310 320 330 340 350 360 VKTLKEDTME VEEFLKEAAV MKEIKHPNLV QLLGVCTLEP PFYIVTEYMP YGNLLDYLRE 370 380 390 400 410 420 CNREEVTAVV LLYMATQISS AMEYLEKKNF IHRDLAARNC LVGENHVVKV ADFGLSRLMT 430 440 450 460 470 480 GDTYTAHAGA KFPIKWTAPE SLAYNTFSIK SDVWAFGVLL WEIATYGMSP YPGIDLSQVY 490 500 510 520 530 540 DLLEKGYRME QPEGCPPKVY ELMRACWKWS PADRPSFAET HQAFETMFHD SSISEEVAEE 550 560 570 580 590 600 LGRAASSSSV VPYLPRLPIL PSKTRTLKKQ VENKENIEGA QDATENSASS LAPGFIRGAQ 610 620 630 640 650 660 ASSGSPALPR KQRDKSPSSL LEDAKETCFT RDRKGGFFSS FMKKRNAPTP PKRSSSFREM 670 680 690 700 710 720 ENQPHKKYEL TGLPEQDRMA MTLPRNCQRS KLQLERTVST SSQPEENVDR ANDMLPKKSE 730 740 750 760 770 780 ESAAPSRERP KAKLLPRGAT ALPLRTPSGD LAITEKDPPG VGVAGVAAAP KGKEKNGGAR 790 800 810 820 830 840 LGMAGVPEDG EQPGWPSPAK AAPVLPTTHN HKVPVLISPT LKHTPADVQL IGTDSQGNKF 850 860 870 880 890 900 KLLSEHQVTS SGDKDRPRRV KPKCAPPPPP VMRLLQHPSI CSDPTEEPTA LTAGQSTSET 910 920 930 940 950 960 QEGGKKAALG AVPISGKAGR PVMPPPQVPL PTSSISPAKM ANGTAGTKVA LRKTKQAAEK 970 980 990 1000 1010 1020 ISADKISKEA LLECADLLSS ALTEPVPNSQ LVDTGHQLLD YCSGYVDCIP QTRNKFAFRE 1030 1040 1050 1060 AVSKLELSLQ ELQVSSAAAG VPGTNPVLNN LLSCVQEISD VVQR
	Isoform 8 [UniParc]. Checksum: 89E988F0EFF2ABCF	FASTA	542	60,864
	10 20 30 40 50 60 MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TTETGFNIFT QHEALHRPYG 70 80 90 100 110 120 CDVEPQALNE AIRWSSKENL LGATESDPNL FVALYDFVAS GDNTLSITKG EKLRVLGYNQ 130 140 150 160 170 180 NGEWSEVRSK NGQGWVPSNY ITPVNSLEKH SWYHGPVSRS AAEYLLSSLI NGSFLVRESE 190 200 210 220 230 240 SSPGQLSISL RYEGRVYHYR INTTADGKVY VTAESRFSTL AELVHHHSTV ADGLVTTLHY 250 260 270 280 290 300 PAPKCNKPTV YGVSPIHDKW EMERTDITMK HKLGGGQYGE VYVGVWKKYS LTVAVKTLKE 310 320 330 340 350 360 DTMEVEEFLK EAAVMKEIKH PNLVQLLGVC TLEPPFYIVT EYMPYGNLLD YLRECNREEV 370 380 390 400 410 420 TAVVLLYMAT QISSAMEYLE KKNFIHRDLA ARNCLVGENH VVKVADFGLS RLMTGDTYTA 430 440 450 460 470 480 HAGAKFPIKW TAPESLAYNT FSIKSDVWAF GVLLWEIATY GMSPYPGIDL SQVYDLLEKG 490 500 510 520 530 540 YRMEQPEGCP PKVYELMRAC WKWSPADRPS FAETHQAFET MFHDSSISEV LLHCANQTCI TL

References

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[1]	"The complete coding sequence of arg defines the Abelson subfamily of cytoplasmic tyrosine kinases." Kruh G.D., Perego R., Miki T., Aaronson S.A. Proc. Natl. Acad. Sci. U.S.A. 87:5802-5806(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2).
[2]	"Eight full-length abelson related gene (Arg) isoforms are constitutively expressed in caki-1 cell line and cell distribution of two isoforms has been analyzed after transfection." Bianchi C., Torsello B., Angeloni V., Bombelli S., Soldi M., Invernizzi L., Brambilla P., Perego R.A. J. Cell. Biochem. 105:1219-1227(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6 AND 7), ALTERNATIVE SPLICING (ISOFORM 10), VARIANT THR-12 (ISOFORM 4).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Uterine endothelium.
[5]	NIEHS SNPs program Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-930; MET-946; ARG-996; ASN-1085 AND ALA-1101.
[6]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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].
[8]	"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 3). Tissue: Brain.
[9]	"A novel human gene closely related to the abl proto-oncogene." Kruh G.D., King C.R., Kraus M.H., Popescu N.C., Amsbaugh S.C., McBride W.O., Aaronson S.A. Science 234:1545-1548(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 343-469.
[10]	"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: AUTOPHOSPHORYLATION AT TYR-272; TYR-439; TYR-568 AND TYR-683, ENZYME REGULATION.
[11]	"RIN1 is an ABL tyrosine kinase activator and a regulator of epithelial-cell adhesion and migration." Hu H., Bliss J.M., Wang Y., Colicelli J. Curr. Biol. 15:815-823(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RIN1, FUNCTION, ENZYME REGULATION.
[12]	"Ubiquitination and degradation of the Arg tyrosine kinase is regulated by oxidative stress." Cao C., Li Y., Leng Y., Li P., Ma Q., Kufe D. Oncogene 24:2433-2440(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT TYR-261, UBIQUITINATION.
[13]	"Interaction between c-Abl and Arg tyrosine kinases and proteasome subunit PSMA7 regulates proteasome degradation." Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q., Cao C. Mol. Cell 22:317-327(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PSMA7.
[14]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[15]	"A critical role for cortactin phosphorylation by Abl-family kinases in PDGF-induced dorsal-wave formation." Boyle S.N., Michaud G.A., Schweitzer B., Predki P.F., Koleske A.J. Curr. Biol. 17:445-451(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Abl kinases regulate autophagy by promoting the trafficking and function of lysosomal components." Yogalingam G., Pendergast A.M. J. Biol. Chem. 283:35941-35953(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[18]	"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.
[19]	"How do Abl family kinases regulate cell shape and movement?" Hernandez S.E., Krishnaswami M., Miller A.L., Koleske A.J. Trends Cell Biol. 14:36-44(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND SER-915, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620; SER-631; SER-633; SER-655; SER-817; SER-820 AND SER-936, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"Emerging roles of Abl family tyrosine kinases in microbial pathogenesis." Backert S., Feller S.M., Wessler S. Trends Biochem. Sci. 33:80-90(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[23]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-718, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-668 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-647 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-683 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-662 (ISOFORM 7), MASS SPECTROMETRY.
[24]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820 AND SER-936, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 AND SER-936, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"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.
[27]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, MASS SPECTROMETRY.
[28]	"Solution structure of the human ABL2 SH2 domain." RIKEN structural genomics initiative (RSGI) Submitted (FEB-2008) to the PDB data bank Cited for: STRUCTURE BY NMR OF 163-268.
[29]	"Crystal structures of ABL-related gene (ABL2) in complex with imatinib, tozasertib (VX-680), and a type I inhibitor of the triazole carbothioamide class." Salah E., Ugochukwu E., Barr A.J., von Delft F., Knapp S., Elkins J.M. J. Med. Chem. 54:2359-2367(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 279-546 IN COMPLEXES WITH INHIBITORS.
[30]	"Lysozyme contamination facilitates crystallization of a heterotrimeric cortactin-Arg-lysozyme complex." Liu W., MacGrath S.M., Koleske A.J., Boggon T.J. Acta Crystallogr. F 68:154-158(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 563-579 IN COMPLEX WITH CTTN, INTERACTION WITH CTTN.
[31]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-78; GLN-99; ILE-519; SER-769; ARG-930 AND ARG-996, VARIANT [LARGE SCALE ANALYSIS] THR-12 (ISOFORM 4).
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

CGP resequencing studies

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M35296 mRNA. Translation: AAA35553.1.
FJ542283 mRNA. Translation: ACK76601.1.
FJ542284 mRNA. Translation: ACK76602.1.
FJ542285 mRNA. Translation: ACK76603.1.
FJ542286 mRNA. Translation: ACK76604.1.
AK311045 mRNA. No translation available.
BX538317 mRNA. Translation: CAD98092.1. Different initiation.
DQ009672 Genomic DNA. Translation: AAY16984.1.
AL139132, AL359179, AL512326 Genomic DNA. Translation: CAH70921.1.
AL139132, AL359179, AL512326 Genomic DNA. Translation: CAH70925.1.
AL359179, AL139132, AL512326 Genomic DNA. Translation: CAI15584.1.
AL359179, AL139132, AL512326 Genomic DNA. Translation: CAI15585.1.
AL512326, AL359179, AL139132 Genomic DNA. Translation: CAI13566.1.
AL512326, AL359179, AL139132 Genomic DNA. Translation: CAI13570.1.
CH471067 Genomic DNA. Translation: EAW91040.1.
BC065912 mRNA. Translation: AAH65912.1.

IPI

IPI00329488.
IPI00719587.
IPI00745593.
IPI00914546.
IPI00954441.
IPI00954457.
IPI00954474.
IPI00954546.
IPI01025224.

PIR

A35962.
B35962.

RefSeq

NP_001129472.1. NM_001136000.2.
NP_001129473.1. NM_001136001.1.
NP_001161708.1. NM_001168236.1.
NP_001161709.1. NM_001168237.1.
NP_001161710.1. NM_001168238.1.
NP_001161711.1. NM_001168239.1.
NP_005149.4. NM_005158.4.
NP_009298.1. NM_007314.3.

UniGene

Hs.159472.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ECD	NMR	-	A	163-268	[»]
2KK1	NMR	-	A	1058-1182	[»]
2XYN	X-ray	2.81	A/B/C	279-546	[»]
3GVU	X-ray	2.05	A	279-546	[»]
3HMI	X-ray	1.65	A	279-546	[»]
3ULR	X-ray	1.65	C	563-579	[»]
4EIH	X-ray	1.20	A	165-273	[»]

ProteinModelPortal

P42684.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-91N.

IntAct

P42684. 17 interactions.

MINT

MINT-1347081.

STRING

9606.ENSP00000356595.

PTM databases

PhosphoSite

P42684.

Polymorphism databases

DMDM

1168268.

Proteomic databases

PaxDb

P42684.

PRIDE

P42684.

Protocols and materials databases

DNASU

27.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000344730; ENSP00000339209; ENSG00000143322.
ENST00000367623; ENSP00000356595; ENSG00000143322.
ENST00000392043; ENSP00000375897; ENSG00000143322.
ENST00000408940; ENSP00000386152; ENSG00000143322.
ENST00000502732; ENSP00000427562; ENSG00000143322.
ENST00000504405; ENSP00000426831; ENSG00000143322.
ENST00000507173; ENSP00000423413; ENSG00000143322.
ENST00000511413; ENSP00000424697; ENSG00000143322.
ENST00000512653; ENSP00000423578; ENSG00000143322.

GeneID

27.

KEGG

hsa:27.

UCSC

uc001gmg.4. human.
uc001gmi.4. human.
uc001gmj.4. human.
uc010pne.2. human.
uc010png.2. human.
uc010pnh.2. human.

Organism-specific databases

CTD

27.

GeneCards

GC01M179068.

HGNC

HGNC:77. ABL2.

HPA

CAB017106.
HPA001866.

MIM

164690. gene.

neXtProt

NX_P42684.

PharmGKB

PA24414.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG004162.

InParanoid

P42684.

KO

K08887.

OMA

PPKCYGG.

OrthoDB

EOG4NS39R.

Enzyme and pathway databases

BRENDA

2.7.10.2. 2681.

Reactome

REACT_111045. Developmental Biology.

SignaLink

P42684.

Gene expression databases

ArrayExpress

P42684.

Bgee

P42684.

CleanEx

HS_ABL2.

Genevestigator

P42684.

GermOnline

ENSG00000143322. Homo sapiens.

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.

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

P42684.

ChEMBL

CHEMBL4014.

ChiTaRS

ABL2. human.

DrugBank

DB00171. Adenosine triphosphate.
DB01254. Dasatinib.

EvolutionaryTrace

P42684.

GenomeRNAi

27.

NextBio

89.

SOURCE

Search...

Entry information

Entry name

ABL2_HUMAN

Accession

Primary (citable) accession number: P42684
Secondary accession number(s): A0M8X0 , B7UEF2, B7UEF3, B7UEF4, B7UEF5, Q5T0X6, Q5W0C5, Q6NZY6, Q7Z301

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 29, 2013
This is version 155 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.