Reviewed, UniProtKB/Swiss-Prot P42684 (ABL2_HUMAN)

Names and origin

Protein names

Recommended name:
    Tyrosine-protein kinase ABL2
    EC=2.7.10.2
Alternative name(s):
    Abelson murine leukemia viral oncogene homolog 2
    Abelson-related gene protein
    Tyrosine kinase ARG

Gene names

Name:	ABL2
Synonyms:	ABLL, ARG

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	1182 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. Ref.9
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). Ref.9
Subunit structure	Interacts with PSMA7.
Subcellular location	Cytoplasm › cytoskeleton.
Tissue specificity	Widely expressed.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22
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
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
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-tyrosine phosphorylation Ref.9 Inferred from direct assay. Source: UniProtKB positive regulation of oxidoreductase activity Inferred from direct assay. Source: UniProtKB signal transduction Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytosol Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Ref.9 Inferred from direct assay. Source: UniProtKB manganese ion binding Ref.9 Inferred from direct assay. Source: UniProtKB non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein binding Ref.9 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CRK	P46108	2	EBI-1102694,EBI-886
CRK	Q04929	1	EBI-1102694,EBI-1102801	From a different organism.
FYN	P06241	1	EBI-1102694,EBI-515315
GRB2	P62993	1	EBI-1102694,EBI-401755
NCK1	P16333	1	EBI-1102694,EBI-389883
PIK3R1	P27986	1	EBI-1102694,EBI-79464
PLCG1	P19174	2	EBI-1102694,EBI-79387
RIN1	Q13671	2	EBI-1102694,EBI-366017
SRC	P12931	1	EBI-1102694,EBI-621482

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform IB (identifier: P42684-1) 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 IA (identifier: P42684-2) The sequence of this isoform differs from the canonical sequence as follows:      1-73: MGQQVGRVGE...EGDKTGGSSP → MVLGTVLLPP...ASESALPDLT
Isoform IC (identifier: P42684-3) The sequence of this isoform differs from the canonical sequence as follows:      1-52: MGQQVGRVGE...ETGFNIFTQH → MVLGTVLLPP...ASESALPDLT
Isoform 4 (identifier: P42684-4) The sequence of this isoform differs from the canonical sequence as follows:      1-73: MGQQVGRVGE...EGDKTGGSSP → MVLGTVLLPP...ASESALPDLT      688-790: Missing.
Note: No experimental confirmation available.
Sequence annotation (Features)
	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
	Natural variant	12	1	S → T: dbSNP rs1318056.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 1182

1181

Tyrosine-protein kinase ABL2

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

2 – 106

105

CAP

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

71

1

Phosphoserine Ref.16

Modified residue

96

1

Phosphoserine

Modified residue

116

1

Phosphotyrosine Ref.17

Modified residue

203

1

Phosphoserine Ref.10 Ref.15 Ref.17

Modified residue

231

1

Phosphotyrosine Ref.17

Modified residue

272

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

275

1

Phosphoserine Ref.17

Modified residue

299

1

Phosphotyrosine By similarity

Modified residue

303

1

Phosphotyrosine By similarity

Modified residue

310

1

Phosphotyrosine Ref.8

Modified residue

439

1

Phosphotyrosine; by autocatalysis Ref.8 Ref.12 Ref.20

Modified residue

440

1

Phosphothreonine Ref.8

Modified residue

492

1

Phosphoserine By similarity

Modified residue

515

1

Phosphotyrosine Ref.8

Modified residue

602

1

Phosphoserine Ref.17

Modified residue

620

1

Phosphoserine Ref.17 Ref.18 Ref.19

Modified residue

631

1

Phosphoserine Ref.10 Ref.13 Ref.17 Ref.18 Ref.19

Modified residue

633

1

Phosphoserine Ref.18

Modified residue

655

1

Phosphoserine Ref.18

Modified residue

671

1

Phosphoserine Ref.17

Modified residue

683

1

Phosphotyrosine

Modified residue

718

1

Phosphotyrosine Ref.17

Modified residue

781

1

Phosphoserine

Modified residue

783

1

Phosphoserine Ref.13 Ref.19

Modified residue

784

1

Phosphothreonine

Modified residue

815

1

Phosphothreonine

Modified residue

817

1

Phosphoserine Ref.13 Ref.14 Ref.18 Ref.19 Ref.22

Modified residue

818

1

Phosphothreonine Ref.19

Modified residue

819

1

Phosphoserine Ref.19

Modified residue

820

1

Phosphoserine Ref.14 Ref.17 Ref.18 Ref.19 Ref.22

Modified residue

864

1

Phosphothreonine Ref.17

Modified residue

915

1

Phosphoserine Ref.17 Ref.18

Modified residue

936

1

Phosphoserine Ref.13 Ref.17 Ref.18 Ref.19 Ref.22

Modified residue

938

1

Phosphothreonine Ref.19

Lipidation

2

1

N-myristoyl glycine By similarity

Natural variations

Alternative sequence

1 – 73

73

MGQQV…GGSSP → MVLGTVLLPPNSYGRDQDTS LCCLCTEASESALPDLT in isoform 4.

VSP_021307

Alternative sequence

1 – 73

73

MGQQV…GGSSP → MVLGTVLLPPNTYGRDQDTS LCCLCTEASESALPDLT in isoform IA.

VSP_004961

Alternative sequence

1 – 52

52

MGQQV…IFTQH → MVLGTVLLPPNSYGRDQDTS LCCLCTEASESALPDLT in isoform IC.

VSP_017112

Alternative sequence

688 – 790

103

Missing in isoform 4.

VSP_021308

Natural variant

78

1

R → H: dbSNP rs55655202. Ref.25

VAR_055411

Natural variant

99

1

E → Q Somatic mutation in a breast cancer sample. Ref.25

VAR_055412

Natural variant

519

1

R → I Somatic mutation in a lung squamous cell carcinoma. Ref.25

VAR_055413

Natural variant

769

1

T → S: dbSNP rs55892721. Ref.25

VAR_055414

Natural variant

930

1

K → R: dbSNP rs17277288. Ref.25 Ref.3

VAR_029232

Natural variant

946

1

V → M: dbSNP rs28913889. Ref.3

VAR_029233

Natural variant

996

1

P → R: dbSNP rs28913890. Ref.25 Ref.3

VAR_029234

Natural variant

1085

1

S → N: dbSNP rs28913891. Ref.3

VAR_029235

Natural variant

1101

1

T → A: dbSNP rs28913892. Ref.3

VAR_029236

Experimental info

Sequence conflict

343 – 344

2

NL → TI Ref.7

Sequence conflict

981

1

K → R in CAD98092. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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

Sequences

	Sequence		Length	Mass (Da)
	Isoform IB [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 IA. Checksum: 472FE7CB2CB9BE15	FASTA	1,146	124,574
	10 20 30 40 50 60 MVLGTVLLPP NTYGRDQDTS 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 IC. 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. 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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2198571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS IA AND IB).
[2]	"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: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Uterine endothelium.
[3]	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.
[4]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[6]	"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 IC). Tissue: Brain.
[7]	"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: 3787260] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 343-469.
[8]	"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-310; TYR-439; THR-440 AND TYR-515, MASS SPECTROMETRY.
[9]	"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: 15886098] [Abstract] Cited for: INTERACTION WITH RIN1, FUNCTION, ENZYME REGULATION.
[10]	"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-203 AND SER-631, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"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: 16678104] [Abstract] Cited for: FUNCTION, INTERACTION WITH PSMA7.
[12]	"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-439, MASS SPECTROMETRY.
[13]	"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-631; SER-783; SER-817 AND SER-936, MASS SPECTROMETRY.
[14]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817 AND SER-820, MASS SPECTROMETRY.
[15]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, MASS SPECTROMETRY.
[16]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, MASS SPECTROMETRY.
[17]	"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 TYR-116; SER-203; TYR-231; SER-275; SER-602; SER-620; SER-631; SER-671; TYR-718; SER-820; THR-864; SER-915 AND SER-936, MASS SPECTROMETRY.
[18]	"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-620; SER-631; SER-633; SER-655; SER-817; SER-820; SER-915 AND SER-936, MASS SPECTROMETRY.
[19]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620; SER-631; SER-783; SER-817; THR-818; SER-819; SER-820; SER-936 AND THR-938, MASS SPECTROMETRY.
[20]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[21]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-620; SER-631; TYR-683; TYR-718; SER-781; THR-784; THR-815; SER-817; SER-819; SER-820 AND SER-936, MASS SPECTROMETRY.
[22]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817; SER-820 AND SER-936, MASS SPECTROMETRY. Tissue: T-cell.
[23]	"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.
[24]	"The crystal structure of human ABL2 in complex with Gleevec." Structural genomics consortium (SGC) Submitted (APR-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 279-546 IN COMPLEX WITH GLEEVEC.
[25]	"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 [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.
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.
IPI00383728.
IPI00719587.
IPI00745593.

PIR

A35962.
B35962.

RefSeq

NP_001129472.1.
NP_001129473.1.
NP_001161711.1.
NP_005149.4.
NP_009298.1.

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	[»]
3GVU	X-ray	2.05	A	279-546	[»]
3HMI	X-ray	1.65	A	279-546	[»]

SMR

P42684. Positions 108-558.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-91N.

IntAct

P42684. 16 interactions.

STRING

P42684.

PTM databases

PhosphoSite

P42684.

Proteomic databases

PRIDE

P42684.

Genome annotation databases

Ensembl

ENST00000367623; ENSP00000356595; ENSG00000143322; Homo sapiens. [Genome view]

GeneID

27.

KEGG

hsa:27.

UCSC

uc001gmg.2. human.
uc001gmh.2. human.
uc001gmi.2. human.
uc001gmj.2. human.

Organism-specific databases

CTD

27.

GeneCards

GC01M177339.

H-InvDB

HIX0001374.

HGNC

HGNC:77. ABL2.

HPA

CAB017106.
HPA001866.

MIM

164690. gene.

PharmGKB

PA24414.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11298.

HOGENOM

HBG446901.

HOVERGEN

P42684.

InParanoid

P42684.

OMA

QEANLVP.

OrthoDB

EOG937V10.

Enzyme and pathway databases

BRENDA

2.7.10.2. 247.

Reactome

REACT_18266. Axon guidance.

Gene expression databases

ArrayExpress

P42684.

Bgee

P42684.

CleanEx

HS_ABL2.

Genevestigator

P42684.

GermOnline

ENSG00000143322. Homo sapiens.

Family and domain databases

InterPro

IPR015015. F-actin_binding.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR020700. Tyr_kinase_non-rcpt_Abl.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
[Graphical view]

Gene3D

G3DSA:3.30.505.10. SH2. 1 hit.

PANTHER

PTHR23256:SF144. Tyr_kinase_non-rcpt_Abl. 1 hit.
PTHR23256. Tyr_prot_kinase. 1 hit.

Pfam

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

PRINTS

PR00401. SH2DOMAIN.

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.

NextBio

89.

SOURCE

Search...

Entry information

Entry name

ABL2_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	February 9, 2010
This is version 118 of the entry and version 1 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.