T00256
type: Enzyme
cath: SH3 type barrels.
cath: SHC Adaptor Protein
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/-.-.-.-
ec: https://purl.uniprot.org/enzyme/2.7.10.2
uniprot: P06241
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 enzyme: ATK
kegg enzyme: ATP:protein-tyrosine O-phosphotransferase (ambiguous)
kegg enzyme: BLK
kegg enzyme: Bmk
kegg enzyme: BMX
kegg enzyme: BRK
kegg enzyme: Bruton's tyrosine kinase
kegg enzyme: Bsk
kegg enzyme: BTK
kegg enzyme: BTKL
kegg enzyme: CAKb
kegg enzyme: Cdgip
kegg enzyme: CHK
kegg enzyme: CSK
kegg enzyme: CTK
kegg enzyme: CYL
kegg enzyme: cytoplasmic protein tyrosine kinase
kegg enzyme: EMT
kegg enzyme: ETK
kegg enzyme: Fadk
kegg enzyme: FAK
kegg enzyme: FAK2
kegg cofactor: Manganese
kegg substrate: ATP
kegg substrate: [Protein]-L-tyrosine
kegg product: ADP
kegg product: [Protein]-L-tyrosine phosphate
pdb: 1a0nB
pdb: 1avzC
pdb: 1azgB
pdb: 1efnA
pdb: 1efnC
pdb: 1fynA
pdb: 1m27C
pdb: 1nyfA
pdb: 1nygA
pdb: 1shfA
pdb: 1shfB
pdb: 1g83A01
pdb: 1g83B01
pdb: 1aotF
pdb: 1aouF
pdb: 1g83A02
pdb: 1g83B02
references: Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin.
references: High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides.
references: Interaction of peptides derived from the Fas ligand with the Fyn-SH3 domain.
references: Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase.
references: Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain.
references: Physical and functional interaction of Nef with Lck. HIV-1 Nef-induced T-cell signaling defects.
references: The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase.
references: Solution structure and peptide binding of the SH3 domain from human Fyn.
references: The SH3 domain of Itk/Emt binds to proline-rich sequences in the cytoplasmic domain of the T cell costimulatory receptor CD28.
references: The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling.
references: The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity.
references: Dot far-western blot analysis of relative binding affinities of the Src homology 3 domains of Efs and its related proteins.
references: Nef proteins of distinct HIV-1 or -2 isolates differ in their binding properties for HCK: isolation of a novel Nef binding factor with characteristics of an adaptor protein.
references: Proline residues in CD28 and the Src homology (SH)3 domain of Lck are required for T cell costimulation.
references: Activation of Vav by Nef induces cytoskeletal rearrangements and downstream effector functions.
references: HIV-2 and SIV nef proteins target different Src family SH3 domains than does HIV-1 Nef because of a triple amino acid substitution.
references: The role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases.
references: A mechanism for combinatorial regulation of electrical activity: Potassium channel subunits capable of functioning as Src homology 3-dependent adaptors.
references: SH3-SH2 domain orientation in Src kinases: NMR studies of Fyn.
references: Binding of SAP SH2 domain to FynT SH3 domain reveals a novel mechanism of receptor signalling in immune regulation.
comment: The E.C. was transferred from 2.7.1.112 to 2.7.10.2. ADP/ATP could be compatible with other Nucleoside diphosphate/Nucleoside triphosphate. This enzyme is composed of SH3 domain, SH2 domain and protein kinase domain. Although the structures of SH3 and SH2 domains have been determined, the catalytic domain of this enzyme has not been solved.

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

Manganese
type: KeggCofactor
references: KEGG:C00034
compound type: heavy metal
references: CHEBI:18291
references: CHEBI:35154
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

1efnA
type: Pdb
references: 1efn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1efn
comment: mutant R96I

1efnC
type: Pdb
references: 1efn
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1efn
comment: mutant R96I

1aotF
type: Pdb
references: 1aot
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1aot
comment: mutant C97S, C98S, C104S

Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF SH3 DOMAIN.
medline id: 93327750
references: http://www.ncbi.nlm.nih.gov/pubmed/7687536
journal: EMBO J
volume: 12
pages: 2617-24
published year: 1993
authors:
  item: Noble ME
  item: Musacchio A
  item: Saraste M
  item: Courtneidge SA
  item: Wierenga RK
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P06241

High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 80-141.
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: P06241

Interaction of peptides derived from the Fas ligand with the Fyn-SH3 domain.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7589480
journal: FEBS Lett
volume: 373
pages: 265-8
published year: 1995
authors:
  item: Hane M
  item: Lowin B
  item: Peitsch M
  item: Becker K
  item: Tschopp J

Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase.
type: BibliographicResource
comment: STRUCTURE BY NMR.
medline id: 97121261
references: http://www.ncbi.nlm.nih.gov/pubmed/8961927
journal: Biochemistry
volume: 35
pages: 15646-53
published year: 1996
authors:
  item: Renzoni DA
  item: Pugh DJ
  item: Siligardi G
  item: Das P
  item: Morton CJ
  item: Rossi C
  item: Waterfield MD
  item: Campbell ID
  item: Ladbury JE
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P06241

Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 84-140 IN COMPLEX WITH NEF.
medline id: 96279837
references: http://www.ncbi.nlm.nih.gov/pubmed/8681387
journal: Cell
volume: 85
pages: 931-42
published year: 1996
authors:
  item: Lee CH
  item: Saksela K
  item: Mirza UA
  item: Chait BT
  item: Kuriyan J
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P06241

Physical and functional interaction of Nef with Lck. HIV-1 Nef-induced T-cell signaling defects.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8626429
journal: J Biol Chem
volume: 271
pages: 6333-41
published year: 1996
authors:
  item: Collette Y
  item: Dutartre H
  item: Benziane A
  item: Ramos-Morales
  item: Benarous R
  item: Harris M
  item: Olive D

The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8599760
journal: Nat Struct Biol
volume: 3
pages: 340-5
published year: 1996
authors:
  item: Grzesiek S
  item: Bax A
  item: Clore GM
  item: Gronenborn AM
  item: Hu JS
  item: Kaufman J
  item: Palmer I
  item: Stahl SJ
  item: Wingfield PT

Solution structure and peptide binding of the SH3 domain from human Fyn.
type: BibliographicResource
comment: STRUCTURE BY NMR OF SH3 DOMAIN.
medline id: 96399716
references: http://www.ncbi.nlm.nih.gov/pubmed/8805554
journal: Structure
volume: 4
pages: 705-14
published year: 1996
authors:
  item: Morton CJ
  item: Pugh DJ
  item: Brown EL
  item: Kahmann JD
  item: Renzoni DA
  item: Campbell ID
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P06241

The SH3 domain of Itk/Emt binds to proline-rich sequences in the cytoplasmic domain of the T cell costimulatory receptor CD28.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9317120
journal: J Immunol
volume: 159
pages: 3220-9
published year: 1997
authors:
  item: Marengere LE
  item: Okkenhaug K
  item: Clavreul A
  item: Couez D
  item: Gibson S
  item: Mills GB
  item: Mak TW
  item: Rottapel R

The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/9351809
journal: Structure
volume: 5
pages: 1361-72
published year: 1997
authors:
  item: Arold S
  item: Franken P
  item: Strub MP
  item: Hoh F
  item: Benichou S
  item: Benarous R
  item: Dumas C
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity.
type: BibliographicResource
comment: STRUCTURE BY NMR OF SH2 DOMAIN.
medline id: 98035454
references: http://www.ncbi.nlm.nih.gov/pubmed/9351806
journal: Structure
volume: 5
pages: 1313-23
published year: 1997
authors:
  item: Mulhern TD
  item: Shaw GL
  item: Morton CJ
  item: Day AJ
  item: Campbell ID
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P06241

Dot far-western blot analysis of relative binding affinities of the Src homology 3 domains of Efs and its related proteins.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9750131
journal: Anal Biochem
volume: 262
pages: 185-92
published year: 1998
authors:
  item: Ohba T
  item: Ishino M
  item: Aoto H
  item: Sasaki T

Nef proteins of distinct HIV-1 or -2 isolates differ in their binding properties for HCK: isolation of a novel Nef binding factor with characteristics of an adaptor protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9656992
journal: Virology
volume: 246
pages: 45-52
published year: 1998
authors:
  item: Karn T
  item: Hock B
  item: Holtrich U
  item: Adamski M
  item: Strebhardt K
  item: Rubsamen-Waigmann H

Proline residues in CD28 and the Src homology (SH)3 domain of Lck are required for T cell costimulation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10430626
journal: J Exp Med
volume: 190
pages: 375-84
published year: 1999
authors:
  item: Holdorf AD
  item: Green JM
  item: Levin SD
  item: Denny MF
  item: Straus DB
  item: Link V
  item: Changelian PS
  item: Allen PM
  item: Shaw AS

Activation of Vav by Nef induces cytoskeletal rearrangements and downstream effector functions.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10394361
journal: Mol Cell
volume: 3
pages: 729-39
published year: 1999
authors:
  item: Fackler OT
  item: Luo W
  item: Geyer M
  item: Alberts AS
  item: Peterlin BM

HIV-2 and SIV nef proteins target different Src family SH3 domains than does HIV-1 Nef because of a triple amino acid substitution.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10660579
journal: J Biol Chem
volume: 275
pages: 4171-6
published year: 2000
authors:
  item: Collette Y
  item: Arold S
  item: Picard C
  item: Janvier K
  item: Benichou S
  item: Benarous R
  item: Olive D
  item: Dumas C

The role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11278857
journal: J Biol Chem
volume: 276
pages: 17199-205
published year: 2001
authors:
  item: Arold ST
  item: Ulmer TS
  item: Mulhern TD
  item: Werner JM
  item: Ladbury JE
  item: Campbell ID
  item: Noble ME
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

A mechanism for combinatorial regulation of electrical activity: Potassium channel subunits capable of functioning as Src homology 3-dependent adaptors.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11149959
journal: Proc Natl Acad Sci U S A
volume: 98
pages: 705-10
published year: 2001
authors:
  item: Nitabach MN
  item: Llamas DA
  item: Araneda RC
  item: Intile JL
  item: Thompson IJ
  item: Zhou YI
  item: Holmes TC

SH3-SH2 domain orientation in Src kinases: NMR studies of Fyn.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12121645
journal: Structure
volume: 10
pages: 901-11
published year: 2002
authors:
  item: Ulmer TS
  item: Werner JM
  item: Campbell ID

Binding of SAP SH2 domain to FynT SH3 domain reveals a novel mechanism of receptor signalling in immune regulation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12545173
journal: Nat Cell Biol
volume: 5
pages: 149-54
published year: 2003
authors:
  item: Latour S
  item: Roncagalli R
  item: Chen R
  item: Bakinowski M
  item: Shi X
  item: Schwartzberg PL
  item: Davidson D
  item: Veillette A

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