InterPro : IPR001452

Name  SH3 domain Short Name  SH3_domain
Type  Domain Description  SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues [, ]. They are found in a great variety of intracellular or membrane-associated proteins [, , ]for example, in a variety of proteins with enzymatic activity, in adaptor proteins, such as fodrin and yeast actin binding protein ABP-1.The SH3 domain has a characteristic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices. The surface of the SH3-domain bears a flat, hydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions. The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins, altering their subcellular location and mediating the assembly of large multiprotein complexes [].The crystal structure of the SH3 domain of the cytoskeletal protein spectrin, and the solution structures of SH3 domains of phospholipase C (PLC-y) and phosphatidylinositol 3-kinase p85 alpha-subunit, have been determined [, , ]. In spite of relatively limited sequence similarity, their overall structures are similar. The domains belong to the alpha+beta structural class, with 5 to 8 beta-strands forming 2 tightly-packed, anti-parallel beta-sheets arranged in a barrel-like structure, and intervening loops sometimes forming helices. Conserved aliphatic and aromatic residues form a hydrophobic core (A11, L23, A29, V34, W42, L52 and V59 in PLC-y []) and a hydrophobic pocket on the molecular surface (L12, F13, W53 and P55 in PLC-y). The conserved core is believed to stabilise the fold, while the pocket is thought to serve as a binding site for target proteins. Conserved carboxylic amino acids located in the loops, on the periphery of the pocket (D14 and E22), may be involved in protein-protein interactions via proline-rich regions. The N- and C-termini are packed in close proximity, indicating that they are independent structural modules.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

1 Child Features

Id Name Short Name Type
IPR029294 Helically-extended SH3 domain hSH3 Domain

2 Contains

Id Name Short Name Type
IPR011511 Variant SH3 domain SH3_2 Domain
IPR013315 Spectrin alpha chain, SH3 domain Spectrin_alpha_SH3 Domain

19 Found In

Id Name Short Name Type
IPR017304 Cytoplasmic protein NCK NCK Family
IPR001720 PI3 kinase, P85 regulatory subunit PI3kinase_P85 Family
IPR016313 Disks large 1 DLG1 Family
IPR003005 Amphiphysin Amphiphysin Family
IPR003017 Amphiphysin, isoform 1 Amphiphysin_1 Family
IPR003023 Amphiphysin 2 Amphiphysin_2 Family
IPR016231 Mitogen-activated protein (MAP) kinase kinase kinase, 9/10/11 MAPKKK9/10/11 Family
IPR016279 Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma PLC-gamma Family
IPR014536 Sorting nexin 9 subfamily Snx9_subfam Family
IPR014593 Uncharacterised conserved protein UCP034961, SH3-2 UCP034961_SH3_2 Family
IPR000919 Neutrophil cytosol factor P40 NCF_P40 Family
IPR005443 Voltage-dependent calcium channel, L-type, beta-1 subunit VDCC_L_b1su Family
IPR005444 Voltage-dependent calcium channel, L-type, beta-2 subunit VDCC_L_b2su Family
IPR008079 Voltage-dependent calcium channel, L-type, beta-3 subunit VDCC_L_b3su Family
IPR005417 Tight junction protein ZO ZO Family
IPR005420 Tight junction protein ZO-3 ZO-3 Family
IPR001655 Neutrophil cytosol factor 1 P47PHOX Family
IPR015503 Cortactin Cortactin Family
IPR015827 Alpha-(1,6)-fucosyltransferase, eukaryotic type Alpha1_6FUT_euk Family

0 Parent Features

9 Publications

First Author Title Year Journal Volume Pages
Pawson T SH2 and SH3 domains. 1993 Curr Biol 3 434-42
Pawson T Protein modules and signalling networks. 1995 Nature 373 573-80
Mayer BJ Signalling through SH2 and SH3 domains. 1993 Trends Cell Biol 3 8-13
Kohda D Solution structure of the SH3 domain of phospholipase C-gamma. 1993 Cell 72 953-60
Booker GW Solution structure and ligand-binding site of the SH3 domain of the p85 alpha subunit of phosphatidylinositol 3-kinase. 1993 Cell 73 813-22
Morton CJ SH3 domains. Molecular 'Velcro'. 1994 Curr Biol 4 615-7
Musacchio A SH3--an abundant protein domain in search of a function. 1992 FEBS Lett 307 55-61
Musacchio A Crystal structure of a Src-homology 3 (SH3) domain. 1992 Nature 359 851-5
Mayer BJ SH3 domains: complexity in moderation. 2001 J Cell Sci 114 1253-63



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)