ELM Details - LIG_SH3

LIG_SH3_1

Functional site class:	SH3 ligand
Functional site description:	This motif is involved in protein-protein interaction mediated by SH3 domains
ELM(s):	LIG_SH3_3, LIG_SH3_4, LIG_SH3_1, LIG_SH3_2, LIG_SH3_5
LIG_SH3_1 description:	This is the motif recognized by class I SH3 domains
Pattern:	[RKY]..P..P
Present in taxon(s):	Homo sapiens Fungi/Metazoa group Bos taurus Mus musculus Rattus norvegicus Gallus gallus Saccharomyces cerevisiae
Not represented in taxon(s):

See instances for LIG_SH3_1

Abstract

SH3 (Src Homolgy 3) domains are small protein modules of about 50-60 residues. It is found in proteins involved in several biological processes as diverse as signal transduction pathways, cytoskeleton organization, membrane traffic or organelle assembly. SH3 domains bind to proline-rich peptides that form a left-handed polyproline type II helix (PPII) in one of two opposite orientations. Ligand orientation depends on the position of the positive residue in the target peptide. Peptides that bind in a type I orientation contain the consensus R/KXXPXXP, while the type II orientation conform to the PXXPXR/K consensus

Selected references

Brown MT, Andrade J, Radhakrishna H, Donaldson JG, Cooper JA, Randazzo PA

ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src.

Mol Cell Biol 1998 Dec;18(12) : 7038-51.

PMID: 9819391

Cicchetti P, Mayer BJ, Thiel G, Baltimore D

Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho.

Science 1992 Aug 7;257(5071) : 803-6.

PMID: 1379745

Evangelista M, Klebl BM, Tong AH, Webb BA, Leeuw T, Leberer E, Whiteway M, Thomas DY, Boone C

A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex.

J Cell Biol 2000 Jan 24;148(2) : 353-62.

PMID: 10648568

Hansson H, Smith CI, Hard T

Both proline-rich sequences in the TH region of Bruton's tyrosine kinase stabilize intermolecular interactions with the SH3 domain.

FEBS Lett 2001 Nov 9;508(1) : 11-5.

PMID: 11707259

Kapeller R, Prasad KV, Janssen O, Hou W, Schaffhausen BS, Rudd CE, Cantley LC

Identification of two SH3-binding motifs in the regulatory subunit of phosphatidylinositol 3-kinase.

J Biol Chem 1994 Jan 21;269(3) : 1927-33.

PMID: 8294442

Kay BK, Williamson MP, Sudol M

The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains.

FASEB J 2000 Feb;14(2) : 231-41.

PMID: 10657980

Lee G, Newman ST, Gard DL, Band H, Panchamoorthy G

Tau interacts with src-family non-receptor tyrosine kinases.

J Cell Sci 1998 Nov;111() : 3167-77.

PMID: 9763511

Mayer BJ

SH3 domains: complexity in moderation.

J Cell Sci 2001 Apr;114() : 1253-63.

PMID: 11256992

Pellicena P, Miller WT

Processive phosphorylation of p130Cas by Src depends on SH3-polyproline interactions.

J Biol Chem 2001 Jul 27;276(30) : 28190-6.

PMID: 11389136

Plemper RK, Hammond AL, Cattaneo R

Measles virus envelope glycoproteins hetero-oligomerize in the endoplasmic reticulum.

J Biol Chem 2001 Nov 23;276(47) : 44239-46.

PMID: 11535597

Ren R, Mayer BJ, Cicchetti P, Baltimore D

Identification of a ten-amino acid proline-rich SH3 binding site.

Science 1993 Feb 19;259(5098) : 1157-61.

PMID: 8438166

Richard S, Yu D, Blumer KJ, Hausladen D, Olszowy MW, Connelly PA, Shaw AS

Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1.

Mol Cell Biol 1995 Jan;15(1) : 186-97.

PMID: 7799925

Shen Z, Batzer A, Koehler JA, Polakis P, Schlessinger J, Lydon NB, Moran MF

Evidence for SH3 domain directed binding and phosphorylation of Sam68 by Src.

Oncogene 1999 Aug 19;18(33) : 4647-53.

PMID: 10467411

Suzuki A, Kadota N, Hara T, Nakagami Y, Izumi T, Takenawa T, Sabe H, Endo T

Meltrin alpha cytoplasmic domain interacts with SH3 domains of Src and Grb2 and is phosphorylated by v-Src.

Oncogene 2000 Nov 30;19(51) : 5842-50.

PMID: 11127814

Tu Y, Kucik DF, Wu C

Identification and kinetic analysis of the interaction between Nck-2 and DOCK180.

FEBS Lett 2001 Mar 2;491(3) : 193-9.

PMID: 11240126

Westphal RS, Soderling SH, Alto NM, Langeberg LK, Scott JD

Scar/WAVE-1, a Wiskott-Aldrich syndrome protein, assembles an actin-associated multi-kinase scaffold.

EMBO J 2000 Sep 1;19(17) : 4589-600.

PMID: 10970852

Yuan ZM, Huang Y, Ishiko T, Nakada S, Utsugisawa T, Kharbanda S, Wang R, Sung P, Shinohara A, Weichselbaum R, Kufe D

Regulation of Rad51 function by c-Abl in response to DNA damage.

J Biol Chem 1998 Feb 13;273(7) : 3799-802.

PMID: 9461559

Yuan ZM, Shioya H, Ishiko T, Sun X, Gu J, Huang YY, Lu H, Kharbanda S, Weichselbaum R, Kufe D

p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage.

Nature 1999 Jun 24;399(6738) : 814-7.

PMID: 10391251

Zamora-Leon SP, Lee G, Davies P, Shafit-Zagardo B

Binding of Fyn to MAP-2c through an SH3 binding domain. Regulation of the interaction by ERK2.

J Biol Chem 2001 Oct 26;276(43) : 39950-8.

PMID: 11546790

de Mendez I, Homayounpour N, Leto TL

Specificity of p47phox SH3 domain interactions in NADPH oxidase assembly and activation.

Mol Cell Biol 1997 Apr;17(4) : 2177-85.

PMID: 9121467

This ELM has been assigned the following Gene Ontology (GO) terms for biological process, cellular component and molecular function.

Biological Process

  cell growth and/or maintenance

GO:0008150

  cell communication

GO:0007154

  signal transduction

GO:0007165

Cellular Component

  plasma membrane

GO:0005886

  focal adhesion

GO:0005925

  cytosol

GO:0005829

Molecular Function

  Binding

GO:0005488

  protein binding

GO:0005515

  protein domain specific binding

GO:0019904

  SH3-domain binding

GO:0017124

Instances for LIG_SH3_1

Sequence	Position	Subsequence (Click for evidence information)	PDB	Gene Name	Protein Description	Organism
P85A_HUMAN	88-94	SPPTPKPRPPRPLPVAPG	-	Name=PIK3R1; Synonyms=GRB1;	Phosphatidylinositol 3-kinase regulatory subunit alpha (PI3-kinase p85 subunit alpha) (PtdIns-3-kinase p85-alpha) (PI3K).	Homo sapiens (Human).
TAU_HUMAN	546-552	KVAVVRTPPKSPSSAKSR	-	Name=MAPT; Synonyms=MAPTL, MTBT1, TAU;	Microtubule-associated protein tau (Neurofibrillary tangle protein) (Paired helical filament-tau) (PHF-tau).	Homo sapiens (Human).
BTK_HUMAN	186-192	HRKTKKPLPPTPEEDQIL	-	Name=BTK; Synonyms=AGMX1, ATK, BPK;	Tyrosine-protein kinase BTK (EC 2.7.10.2) (Bruton tyrosine kinase) (Agammaglobulinaemia tyrosine kinase) (ATK) (B-cell progenitor kinase) (BPK).	Homo sapiens (Human).
BTK_HUMAN	200-206	DQILKKPLPPEPAAAPVS	-	Name=BTK; Synonyms=AGMX1, ATK, BPK;	Tyrosine-protein kinase BTK (EC 2.7.10.2) (Bruton tyrosine kinase) (Agammaglobulinaemia tyrosine kinase) (ATK) (B-cell progenitor kinase) (BPK).	Homo sapiens (Human).
RAD51_HUMAN	315-321	RICKIYDSPCLPEAEAMF	-	Name=RAD51; Synonyms=RAD51A, RECA;	DNA repair protein RAD51 homolog 1 (hRAD51) (HsRAD51).	Homo sapiens (Human).