EzCatDB: T00256
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DB codeT00256
CATH domainDomain 12.30.30.40 : SH3 type barrels.
Domain 23.30.505.10 : SHC Adaptor Protein
Domain 3-.-.-.-
E.C.2.7.10.2

CATH domainRelated DB codes (homologues)
2.30.30.40 : SH3 type barrels.M00183,M00043,M00130,M00304,M00335
3.30.505.10 : SHC Adaptor ProteinM00183,M00043,M00130,M00148,M00304,M00333,M00339,M00344,T00221

Enzyme Name
UniProtKBKEGG

P06241
Protein nameTyrosine-protein kinase Fynnon-specific protein-tyrosine kinase
ABL
ABL1
ABL2
ABLL
ACK1
ACK2
AGMX1
ARG
ATK
ATP:protein-tyrosine O-phosphotransferase (ambiguous)
BLK
Bmk
BMX
BRK
Bruton's tyrosine kinase
Bsk
BTK
BTKL
CAKb
Cdgip
CHK
CSK
CTK
CYL
cytoplasmic protein tyrosine kinase
EMT
ETK
Fadk
FAK
FAK2
FER
Fert1/2
FES
FGR
focal adhesion kinase
FPS
FRK
FYN
HCK
HCTK
HYL
IMD1
ITK
IYK
JAK1
JAK2
JAK3
Janus kinase 1
Janus kinase 2
Janus kinase 3
JTK1
JTK9
L-JAK
LCK
LSK
LYN
MATK
Ntk
p60c-src protein tyrosine kinase
PKB
protein-tyrosine kinase (ambiguous)
PSCTK
PSCTK1
PSCTK2
PSCTK4
PSCTK5
PTK2
PTK2B
PTK6
PYK2
RAFTK
RAK
Rlk
Sik
SLK
SRC
SRC2
SRK
SRM
SRMS
STD
SYK
SYN
Tck
TEC
TNK1
Tsk
TXK
TYK2
TYK3
YES1
YK2
ZAP70
SynonymsEC 2.7.10.2
Proto-oncogene Syn
Proto-oncogene c-Fyn
Src-like kinase
SLK
p59-Fyn
RefSeqNP_002028.1 (Protein)
NM_002037.5 (DNA/RNA sequence)
NP_694592.1 (Protein)
NM_153047.3 (DNA/RNA sequence)
NP_694593.1 (Protein)
NM_153048.3 (DNA/RNA sequence)
PfamPF07714 (Pkinase_Tyr)
PF00017 (SH2)
PF00018 (SH3_1)
[Graphical view]


UniProtKB:Accession NumberP06241
Entry nameFYN_HUMAN
ActivityATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
SubunitAssociates through its SH3 domain, to the p85 subunit of phosphatidylinositol 3-kinase. Interacts with the FYN-binding protein (FYB). Interacts with phosphorylated TOM1L1. Interacts with CD79A upon activation of the B-cell antigen receptor which increases FYN activity (By similarity). Interacts with PAG1. Interacts (via SH3 domain) with HEV ORF3 protein.
Subcellular locationCell membrane. Note=Present and active in lipid rafts. Present in cell body and along the process of mature and developing oligodendroyctes.
CofactorManganese.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00034C00002C00585C00008C01167
CompoundManganeseATP[Protein]-L-tyrosineADP[Protein]-L-tyrosine phosphate
Typeheavy metalamine group,nucleotidearomatic ring (only carbon atom),peptide/proteinamine group,nucleotidearomatic ring (only carbon atom),peptide/protein,phosphate group/phosphate ion
ChEBI18291
35154
15422

16761

PubChem23930
5957

6022

             
1a0nBUnboundUnboundUnboundUnboundUnbound
1avzCUnboundUnboundBound:TYR 120(chain B)UnboundUnbound
1azgBUnboundUnboundUnboundUnboundUnbound
1efnAUnboundUnboundBound:TYR 120(chain B)UnboundUnbound
1efnCUnboundUnboundBound:TYR 120(chain D)UnboundUnbound
1fynAUnboundUnboundBound:TYR 4(chain B)UnboundUnbound
1m27CUnboundUnboundUnboundUnboundUnbound
1nyfAUnboundUnboundUnboundUnboundUnbound
1nygAUnboundUnboundUnboundUnboundUnbound
1shfAUnboundUnboundUnboundUnboundUnbound
1shfBUnboundUnboundUnboundUnboundUnbound
1g83A01UnboundUnboundUnboundUnboundUnbound
1g83B01UnboundUnboundUnboundUnboundUnbound
1aotFUnboundUnboundUnboundUnboundBound:PTR(chain P)
1aouFUnboundUnboundUnboundUnboundBound:PTR(chain P)
1g83A02UnboundUnboundUnboundUnboundUnbound
1g83B02UnboundUnboundUnboundUnboundUnbound

Active-site residues
pdbcomment
         
1a0nB 
1avzC 
1azgB 
1efnAmutant R96I
1efnCmutant R96I
1fynA 
1m27C 
1nyfA 
1nygA 
1shfA 
1shfB 
1g83A01 
1g83B01 
1aotFmutant C97S, C98S, C104S
1aouF 
1g83A02 
1g83B02 


references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF SH3 DOMAIN.
Medline ID93327750
PubMed ID7687536
JournalEMBO J
Year1993
Volume12
Pages2617-24
AuthorsNoble ME, Musacchio A, Saraste M, Courtneidge SA, Wierenga RK
TitleCrystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin.
Related PDB1shf
Related UniProtKBP06241
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 80-141.
Medline ID95393198
PubMed ID7664083
JournalNat Struct Biol
Year1994
Volume1
Pages546-51
AuthorsMusacchio A, Saraste M, Wilmanns M
TitleHigh-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides.
Related PDB1fyn
Related UniProtKBP06241
[3]
PubMed ID7589480
JournalFEBS Lett
Year1995
Volume373
Pages265-8
AuthorsHane M, Lowin B, Peitsch M, Becker K, Tschopp J
TitleInteraction of peptides derived from the Fas ligand with the Fyn-SH3 domain.
[4]
CommentsSTRUCTURE BY NMR.
Medline ID97121261
PubMed ID8961927
JournalBiochemistry
Year1996
Volume35
Pages15646-53
AuthorsRenzoni DA, Pugh DJ, Siligardi G, Das P, Morton CJ, Rossi C, Waterfield MD, Campbell ID, Ladbury JE
TitleStructural 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.
Related PDB1a0n,1azg
Related UniProtKBP06241
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 84-140 IN COMPLEX WITH NEF.
Medline ID96279837
PubMed ID8681387
JournalCell
Year1996
Volume85
Pages931-42
AuthorsLee CH, Saksela K, Mirza UA, Chait BT, Kuriyan J
TitleCrystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain.
Related PDB1efn
Related UniProtKBP06241
[6]
PubMed ID8626429
JournalJ Biol Chem
Year1996
Volume271
Pages6333-41
AuthorsCollette Y, Dutartre H, Benziane A, Ramos-Morales, Benarous R, Harris M, Olive D
TitlePhysical and functional interaction of Nef with Lck. HIV-1 Nef-induced T-cell signaling defects.
[7]
PubMed ID8599760
JournalNat Struct Biol
Year1996
Volume3
Pages340-5
AuthorsGrzesiek S, Bax A, Clore GM, Gronenborn AM, Hu JS, Kaufman J, Palmer I, Stahl SJ, Wingfield PT
TitleThe 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.
[8]
CommentsSTRUCTURE BY NMR OF SH3 DOMAIN.
Medline ID96399716
PubMed ID8805554
JournalStructure
Year1996
Volume4
Pages705-14
AuthorsMorton CJ, Pugh DJ, Brown EL, Kahmann JD, Renzoni DA, Campbell ID
TitleSolution structure and peptide binding of the SH3 domain from human Fyn.
Related PDB1nyf,1nyg
Related UniProtKBP06241
[9]
PubMed ID9317120
JournalJ Immunol
Year1997
Volume159
Pages3220-9
AuthorsMarengere LE, Okkenhaug K, Clavreul A, Couez D, Gibson S, Mills GB, Mak TW, Rottapel R
TitleThe SH3 domain of Itk/Emt binds to proline-rich sequences in the cytoplasmic domain of the T cell costimulatory receptor CD28.
[10]
CommentsX-ray crystallography
PubMed ID9351809
JournalStructure
Year1997
Volume5
Pages1361-72
AuthorsArold S, Franken P, Strub MP, Hoh F, Benichou S, Benarous R, Dumas C
TitleThe 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.
Related PDB1avz
[11]
CommentsSTRUCTURE BY NMR OF SH2 DOMAIN.
Medline ID98035454
PubMed ID9351806
JournalStructure
Year1997
Volume5
Pages1313-23
AuthorsMulhern TD, Shaw GL, Morton CJ, Day AJ, Campbell ID
TitleThe SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity.
Related PDB1aot,1aou
Related UniProtKBP06241
[12]
PubMed ID9750131
JournalAnal Biochem
Year1998
Volume262
Pages185-92
AuthorsOhba T, Ishino M, Aoto H, Sasaki T
TitleDot far-western blot analysis of relative binding affinities of the Src homology 3 domains of Efs and its related proteins.
[13]
PubMed ID9656992
JournalVirology
Year1998
Volume246
Pages45-52
AuthorsKarn T, Hock B, Holtrich U, Adamski M, Strebhardt K, Rubsamen-Waigmann H
TitleNef 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.
[14]
PubMed ID10430626
JournalJ Exp Med
Year1999
Volume190
Pages375-84
AuthorsHoldorf AD, Green JM, Levin SD, Denny MF, Straus DB, Link V, Changelian PS, Allen PM, Shaw AS
TitleProline residues in CD28 and the Src homology (SH)3 domain of Lck are required for T cell costimulation.
[15]
PubMed ID10394361
JournalMol Cell
Year1999
Volume3
Pages729-39
AuthorsFackler OT, Luo W, Geyer M, Alberts AS, Peterlin BM
TitleActivation of Vav by Nef induces cytoskeletal rearrangements and downstream effector functions.
[16]
PubMed ID10660579
JournalJ Biol Chem
Year2000
Volume275
Pages4171-6
AuthorsCollette Y, Arold S, Picard C, Janvier K, Benichou S, Benarous R, Olive D, Dumas C
TitleHIV-2 and SIV nef proteins target different Src family SH3 domains than does HIV-1 Nef because of a triple amino acid substitution.
[17]
PubMed ID11278857
JournalJ Biol Chem
Year2001
Volume276
Pages17199-205
AuthorsArold ST, Ulmer TS, Mulhern TD, Werner JM, Ladbury JE, Campbell ID, Noble ME
TitleThe role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases.
Related PDB1g83
[18]
PubMed ID11149959
JournalProc Natl Acad Sci U S A
Year2001
Volume98
Pages705-10
AuthorsNitabach MN, Llamas DA, Araneda RC, Intile JL, Thompson IJ, Zhou YI, Holmes TC
TitleA mechanism for combinatorial regulation of electrical activity: Potassium channel subunits capable of functioning as Src homology 3-dependent adaptors.
[19]
PubMed ID12121645
JournalStructure
Year2002
Volume10
Pages901-11
AuthorsUlmer TS, Werner JM, Campbell ID
TitleSH3-SH2 domain orientation in Src kinases: NMR studies of Fyn.
[20]
PubMed ID12545173
JournalNat Cell Biol
Year2003
Volume5
Pages149-54
AuthorsLatour S, Roncagalli R, Chen R, Bakinowski M, Shi X, Schwartzberg PL, Davidson D, Veillette A
TitleBinding of SAP SH2 domain to FynT SH3 domain reveals a novel mechanism of receptor signalling in immune regulation.

comments
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.

createdupdated
2004-03-032009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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