M00130
type: Enzyme
rlcp: p1162
cath: SH3 type barrels.
cath: SHC Adaptor Protein
cath: Phosphorylase Kinase; domain 1
cath: Transferase(Phosphotransferase); domain 1
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/-.-.-.-
ec: https://purl.uniprot.org/enzyme/2.7.10.2
uniprot: P00520
uniprot: P00519
kegg enzyme: non-specific protein-tyrosine kinase
kegg enzyme: ABL
kegg enzyme: ABL1
kegg enzyme: ABL2
kegg enzyme: ABLL
kegg enzyme: ACK1
kegg enzyme: ACK2
kegg enzyme: AGMX1
kegg enzyme: ARG
kegg cofactor: Magnesium
kegg substrate: ATP
kegg substrate: [Protein]-L-tyrosine
kegg product: ADP
kegg product: [Protein]-L-tyrosine phosphate
pdb: 2ablA01
pdb: 1opkA01
pdb: 1oplA01
pdb: 1awoA
pdb: 1bbzA
pdb: 1bbzC
pdb: 1bbzE
pdb: 1bbzG
pdb: 1ju5C
pdb: 1aboA
pdb: 1aboB
pdb: 1abqA
pdb: 2ablA02
pdb: 1opkA02
pdb: 1oplA02
pdb: 1oplB02
pdb: 1opkA03
pdb: 1oplA03
pdb: 1oplB03
pdb: 1fpuA01
pdb: 1fpuB01
pdb: 1iepA01
pdb: 1iepB01
pdb: 1m52A01
pdb: 1m52B01
pdb: 1opjA01
pdb: 1opjB01
pdb: 1opkA04
pdb: 1oplA04
pdb: 1oplB04
pdb: 1fpuA02
pdb: 1fpuB02
pdb: 1iepA02
pdb: 1iepB02
pdb: 1m52A02
pdb: 1m52B02
pdb: 1opjA02
pdb: 1opjB02
active site residues resources: P00520
active site residues resources: P00519
references: Three-dimensional solution structure of the src homology 2 domain of c-abl.
references: Secondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR spectroscopy in solution.
references: High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides.
references: The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct.
references: Intramolecular interactions of the regulatory domains of the Bcr-Abl kinase reveal a novel control mechanism.
references: Crystal structure of the abl-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactions.
references: The substrate specificity of the catalytic domain of Abl plays an important role in directing phosphorylation of the adaptor protein Crk.
references: Regulation of the hTERT telomerase catalytic subunit by the c-Abl tyrosine kinase.
references: c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines.
references: Structural mechanism for STI-571 inhibition of abelson tyrosine kinase.
references: Phosphorylation and structure-based functional studies reveal a positive and a negative role for the activation loop of the c-Abl tyrosine kinase.
references: Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571).
references: Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide.
references: A myristoyl/phosphotyrosine switch regulates c-Abl.
references: Structural basis for the autoinhibition of c-Abl tyrosine kinase.
comment: The E.C. was transferred from 2.7.1.112 to 2.7.10.2. This enzyme is composed of the N-terminal poly-Ser region, SH3 domain, SH2 domain, protein kinase domain, nuclear localization signal region with poly-Lys, and Pro-rich domain. The PDB structure, 2abl, corresponds to the SH3 and SH2 domains, whilst the structure, 1fpu, corresponds to the kinase domain. (1opk and 1opl cover from the SH3 domain to the kinase domain.) The structures of the C-terminal domains have not been determined yet. Altough the catalytic mechanism of this enzyme has not been discussed yet, it can be similar to that of its homologous enzymes (see M00129) due to the complete conservation of active site residues.

SH3 type barrels.
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.30.30.40

SHC Adaptor Protein
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.505.10

Phosphorylase Kinase; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.200.20

Transferase(Phosphotransferase); domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/1.10.510.10
catalytic domain: index.html

Magnesium
type: KeggCofactor
references: KEGG:C00305
compound type: divalent metal (Ca2+, Mg2+)
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

ATP
type: KeggSubstrate
references: KEGG:C00002
compound type: amine group
compound type: nucleotide
references: CHEBI:15422
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

[Protein]-L-tyrosine
type: KeggSubstrate
references: KEGG:C00585
compound type: aromatic ring (only carbon atom)
compound type: peptide/protein

ADP
type: KeggProduct
references: KEGG:C00008
compound type: amine group
compound type: nucleotide
references: CHEBI:16761
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

[Protein]-L-tyrosine phosphate
type: KeggProduct
references: KEGG:C01167
compound type: aromatic ring (only carbon atom)
compound type: peptide/protein
compound type: phosphate group/phosphate ion

1opkA04
type: Pdb
references: 1opk
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1opk
catalytic residue: ;ARG 386
cofactor binding residue: ASN 387;ASP 400(Magnesium binding)
modified residue: TYR 412(auto-Phosphorylation)
comment: mutant D382N

1oplA04
type: Pdb
references: 1opl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1opl
catalytic residue: ;ARG 386
cofactor binding residue: ASN 387;ASP 400(Magnesium binding)
modified residue: TYR 412(auto-Phosphorylation)
comment: mutant D382N

1oplB04
type: Pdb
references: 1opl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1opl
catalytic residue: ;ARG 386
cofactor binding residue: ASN 387;ASP 400(Magnesium binding)
modified residue: TYR 412(auto-Phosphorylation)
comment: mutant D382N

1fpuA02
type: Pdb
references: 1fpu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fpu
catalytic residue: ASP 363;ARG 367
cofactor binding residue: ASN 368;ASP 381(Magnesium binding)
modified residue: TYR 393(auto-Phosphorylation)

1fpuB02
type: Pdb
references: 1fpu
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fpu
catalytic residue: ASP 363;ARG 367
cofactor binding residue: ASN 368;ASP 381(Magnesium binding)
modified residue: TYR 393(auto-Phosphorylation)

1iepA02
type: Pdb
references: 1iep
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iep
catalytic residue: ASP 363;ARG 367
cofactor binding residue: ASN 368;ASP 381(Magnesium binding)
modified residue: TYR 393(auto-Phosphorylation)

1iepB02
type: Pdb
references: 1iep
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1iep
catalytic residue: ASP 363;ARG 367
cofactor binding residue: ASN 368;ASP 381(Magnesium binding)
modified residue: TYR 393(auto-Phosphorylation)

1m52A02
type: Pdb
references: 1m52
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1m52
catalytic residue: ASP 363;ARG 367
cofactor binding residue: ASN 368;ASP 381(Magnesium binding)
modified residue: TYR 393(auto-Phosphorylation)

1m52B02
type: Pdb
references: 1m52
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1m52
catalytic residue: ASP 363;ARG 367
cofactor binding residue: ASN 368;ASP 381(Magnesium binding)
modified residue: TYR 393(auto-Phosphorylation)

1opjA02
type: Pdb
references: 1opj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1opj
catalytic residue: ASP 382;ARG 386
cofactor binding residue: ASN 387;ASP 400(Magnesium binding)
modified residue: TYR 412(auto-Phosphorylation)

1opjB02
type: Pdb
references: 1opj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1opj
catalytic residue: ASP 382;ARG 386
cofactor binding residue: ASN 387;ASP 400(Magnesium binding)
modified residue: TYR 412(auto-Phosphorylation)

Three-dimensional solution structure of the src homology 2 domain of c-abl.
type: BibliographicResource
comment: STRUCTURE BY NMR OF SH2 DOMAIN.
medline id: 92370689
references: http://www.ncbi.nlm.nih.gov/pubmed/1505033
journal: Cell
volume: 70
pages: 697-704
published year: 1992
authors:
  item: Overduin M
  item: Rios CB
  item: Mayer BJ
  item: Baltimore D
  item: Cowburn D
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00519

Secondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR spectroscopy in solution.
type: BibliographicResource
comment: STRUCTURE BY NMR OF SH2 DOMAIN.
medline id: 93101588
references: http://www.ncbi.nlm.nih.gov/pubmed/1281542
journal: Proc Natl Acad Sci U S A
volume: 89
pages: 11673-7
published year: 1992
authors:
  item: Overduin M
  item: Mayer B
  item: Rios CB
  item: Baltimore D
  item: Cowburn D
references: P00519

High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 61-121.
medline id: 95393198
references: http://www.ncbi.nlm.nih.gov/pubmed/7664083
journal: Nat Struct Biol
volume: 1
pages: 546-51
published year: 1994
authors:
  item: Musacchio A
  item: Saraste M
  item: Wilmanns M
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00520

The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct.
type: BibliographicResource
comment: STRUCTURE BY NMR OF SH3 DOMAIN.
medline id: 96131878
references: http://www.ncbi.nlm.nih.gov/pubmed/8590002
journal: Structure
volume: 3
pages: 1075-86
published year: 1995
authors:
  item: Gosser YQ
  item: Zheng J
  item: Overduin M
  item: Mayer BJ
  item: Cowburn D
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00519

Intramolecular interactions of the regulatory domains of the Bcr-Abl kinase reveal a novel control mechanism.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 57-218.
medline id: 96398698
references: http://www.ncbi.nlm.nih.gov/pubmed/8805596
journal: Structure
volume: 4
pages: 1105-14
published year: 1996
authors:
  item: Nam HJ
  item: Haser WG
  item: Roberts TM
  item: Frederick CA
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00519

Crystal structure of the abl-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactions.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 64-121.
medline id: 98365516
references: http://www.ncbi.nlm.nih.gov/pubmed/9698566
journal: J Mol Biol
volume: 281
pages: 513-21
published year: 1998
authors:
  item: Pisabarro MT
  item: Serrano L
  item: Wilmanns M
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00519

The substrate specificity of the catalytic domain of Abl plays an important role in directing phosphorylation of the adaptor protein Crk.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11080615
journal: Cell Signal
volume: 12
pages: 637-43
published year: 2000
authors:
  item: Amoui M
  item: Miller WT

Regulation of the hTERT telomerase catalytic subunit by the c-Abl tyrosine kinase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10837221
journal: Curr Biol
volume: 10
pages: 568-75
published year: 2000
authors:
  item: Kharbanda S
  item: Kumar V
  item: Dhar S
  item: Pandey P
  item: Chen C
  item: Majumder P
  item: Yuan ZM
  item: Whang Y
  item: Strauss W
  item: Pandita TK
  item: Weaver D
  item: Kufe D

c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10964922
journal: J Biol Chem
volume: 275
pages: 35631-7
published year: 2000
authors:
  item: Brasher BB
  item: Van Etten RA

Structural mechanism for STI-571 inhibition of abelson tyrosine kinase.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 223-515.
medline id: 20446271
references: http://www.ncbi.nlm.nih.gov/pubmed/10988075
journal: Science
volume: 289
pages: 1938-42
published year: 2000
authors:
  item: Schindler T
  item: Bornmann W
  item: Pellicena P
  item: Miller WT
  item: Clarkson B
  item: Kuriyan J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P00519

Phosphorylation and structure-based functional studies reveal a positive and a negative role for the activation loop of the c-Abl tyrosine kinase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11781820
journal: Oncogene
volume: 20
pages: 8075-84
published year: 2001
authors:
  item: Dorey K
  item: Engen JR
  item: Kretzschmar J
  item: Wilm M
  item: Neubauer G
  item: Schindler T
  item: Superti-Furga G

Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571).
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12154025
journal: Cancer Res
volume: 62
pages: 4236-43
published year: 2002
authors:
  item: Nagar B
  item: Bornmann WG
  item: Pellicena P
  item: Schindler T
  item: Veach DR
  item: Miller WT
  item: Clarkson B
  item: Kuriyan J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12384576
journal: Proc Natl Acad Sci U S A
volume: 99
pages: 14053-8
published year: 2002
authors:
  item: Donaldson LW
  item: Gish G
  item: Pawson T
  item: Kay LE
  item: Forman-Kay JD
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

A myristoyl/phosphotyrosine switch regulates c-Abl.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12654250
journal: Cell
volume: 112
pages: 845-57
published year: 2003
authors:
  item: Hantschel O
  item: Nagar B
  item: Guettler S
  item: Kretzschmar J
  item: Dorey K
  item: Kuriyan J
  item: Superti-Furga G

Structural basis for the autoinhibition of c-Abl tyrosine kinase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12654251
journal: Cell
volume: 112
pages: 859-71
published year: 2003
authors:
  item: Nagar B
  item: Hantschel O
  item: Young MA
  item: Scheffzek K
  item: Veach D
  item: Bornmann W
  item: Clarkson B
  item: Superti-Furga G
  item: Kuriyan J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

ATK
type: KeggEnzyme

ATP:protein-tyrosine O-phosphotransferase (ambiguous)
type: KeggEnzyme

BLK
type: KeggEnzyme

Bmk
type: KeggEnzyme

BMX
type: KeggEnzyme

BRK
type: KeggEnzyme

Bruton's tyrosine kinase
type: KeggEnzyme

Bsk
type: KeggEnzyme

BTK
type: KeggEnzyme

BTKL
type: KeggEnzyme

CAKb
type: KeggEnzyme

Cdgip
type: KeggEnzyme

CHK
type: KeggEnzyme

CSK
type: KeggEnzyme

CTK
type: KeggEnzyme

CYL
type: KeggEnzyme

cytoplasmic protein tyrosine kinase
type: KeggEnzyme

EMT
type: KeggEnzyme

ETK
type: KeggEnzyme

Fadk
type: KeggEnzyme

FAK
type: KeggEnzyme

FAK2
type: KeggEnzyme

FER
type: KeggEnzyme

Fert1/2
type: KeggEnzyme

FES
type: KeggEnzyme

FGR
type: KeggEnzyme

focal adhesion kinase
type: KeggEnzyme

FPS
type: KeggEnzyme

FRK
type: KeggEnzyme

FYN
type: KeggEnzyme

HCK
type: KeggEnzyme

HCTK
type: KeggEnzyme

HYL
type: KeggEnzyme

IMD1
type: KeggEnzyme

ITK
type: KeggEnzyme

IYK
type: KeggEnzyme

JAK1
type: KeggEnzyme

JAK2
type: KeggEnzyme

JAK3
type: KeggEnzyme

Janus kinase 1
type: KeggEnzyme

Janus kinase 2
type: KeggEnzyme

Janus kinase 3
type: KeggEnzyme

JTK1
type: KeggEnzyme

JTK9
type: KeggEnzyme

L-JAK
type: KeggEnzyme

LCK
type: KeggEnzyme

LSK
type: KeggEnzyme

LYN
type: KeggEnzyme

MATK
type: KeggEnzyme

Ntk
type: KeggEnzyme

p60c-src protein tyrosine kinase
type: KeggEnzyme

PKB
type: KeggEnzyme

protein-tyrosine kinase (ambiguous)
type: KeggEnzyme

PSCTK
type: KeggEnzyme

PSCTK1
type: KeggEnzyme

PSCTK2
type: KeggEnzyme

PSCTK4
type: KeggEnzyme

PSCTK5
type: KeggEnzyme

PTK2
type: KeggEnzyme

PTK2B
type: KeggEnzyme

PTK6
type: KeggEnzyme

PYK2
type: KeggEnzyme

RAFTK
type: KeggEnzyme

RAK
type: KeggEnzyme

Rlk
type: KeggEnzyme

Sik
type: KeggEnzyme

SLK
type: KeggEnzyme

SRC
type: KeggEnzyme

SRC2
type: KeggEnzyme

SRK
type: KeggEnzyme

SRM
type: KeggEnzyme

SRMS
type: KeggEnzyme

STD
type: KeggEnzyme

SYK
type: KeggEnzyme

SYN
type: KeggEnzyme

Tck
type: KeggEnzyme

TEC
type: KeggEnzyme

TNK1
type: KeggEnzyme

Tsk
type: KeggEnzyme

TXK
type: KeggEnzyme

TYK2
type: KeggEnzyme

TYK3
type: KeggEnzyme

YES1
type: KeggEnzyme

YK2
type: KeggEnzyme

ZAP70
type: KeggEnzyme