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InterPro: IPR001452 Src homology-3 domain

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UniProtKB
Matches:
7452 proteins
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IPR001452 SH3_domain
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Domain
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Found in IPR000108 Neutrophil cytosol factor 2
IPR000919 Neutrophil cytosol factor P40
IPR001655 Neutrophil cytosol factor 1
IPR001720 PI3 kinase, P85 regulatory subunit
IPR003005 Amphiphysin
IPR003017 Amphiphysin, isoform 1
IPR003023 Amphiphysin, isoform 2
IPR005417 Zona occludens protein
IPR005420 Zona occludens protein ZO-3
IPR005443 Voltage-dependent calcium channel, L-type, beta-1 subunit
IPR005444 Voltage-dependent calcium channel, L-type, beta-2 subunit
IPR008079 Voltage-dependent calcium channel, L-type, beta-3 subunit
IPR014536 Sorting nexin, Snx9 type
IPR014593 Uncharacterised conserved protein UCP034961, SH3-2
IPR015503 Cortactin
IPR015773 Tyrosine-protein kinase, non-receptor MATK
IPR015774 Tyrosine-protein kinase, non-receptor PTK6
IPR015778 Tyrosine-protein kinase, non-receptor Csk
IPR015827 Alpha-(1,6)-fucosyltransferase, eukaryotic type
IPR016231 Mitogen-activated protein kinase kinase kinase, 9/10/11
IPR016279 Phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma
IPR016313 Membrane-associated guanylate kinase (MAGUK) scaffold protein
IPR017304 Cytoplasmic, NCK
IPR020697 Tyrosine-protein kinase, non-receptor ITK/TSK
IPR020698 Tyrosine-protein kinase, non-receptor Btk29A
IPR020699 Tyrosine-protein kinase, non-receptor Srms
IPR020700 Tyrosine-protein kinase, non-receptor Abl
IPR020701 Tyrosine-protein kinase, non-receptor Src-1, nematode
IPR020702 Tyrosine-protein kinase, non-receptor FRK
IPR020703 Tyrosine-protein kinase, non-receptor Src64B
IPR020743 Tyrosine-protein kinase, non-receptor YES
IPR020744 Tyrosine-protein kinase, non-receptor Src
IPR020745 Tyrosine-protein kinase, non-receptor Fyn
IPR020746 Tyrosine-protein kinase, non-receptor Fgr
IPR020747 Tyrosine-protein kinase, non-receptor Lyn
IPR020748 Tyrosine-protein kinase, non-receptor Hck
IPR020749 Tyrosine-protein kinase, non-receptor Lck
IPR020750 Tyrosine-protein kinase, non-receptor Blk
IPR020753 Tyrosine-protein kinase, non-receptor Btk
IPR020755 Tyrosine-protein kinase, non-receptor Txk/Tec
Contains IPR011511 Variant SH3
IPR013315 Spectrin alpha chain, SH3 domain
IPR020473 Src homology-3, region
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp
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SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues [1, 2]. They are found in a great variety of intracellular or membrane-associated proteins [3, 4, 5] for example, in a variety of proteins with enzymatic activity, in adaptor proteins that lack catalytic sequences and in cytoskeletal 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 [6]. 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 [7].
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PDB - click here
1a07 , 1a08 , 1a09 , 1a0n , 1a1a , 1a1b , 1a1c , 1a1e , 1ab2 , 1abo , 1abq , 1ad5 , 1aey , 1aoj , 1aot , 1aou , 1ark , 1avz , 1awj , 1awo , 1aww , 1awx , 1aze , 1azg , 1b07 , 1bb9 , 1bbz , 1bhf , 1bhh , 1bk2 , 1bkl , 1bkm , 1blj , 1blk , 1bm2 , 1bmb , 1bu1 , 1by1 , 1cf4 , 1cj1 , 1cka , 1ckb , 1csk , 1cwd , 1cwe , 1e6g , 1e6h , 1e7o , 1efn , 1f1w , 1f2f , 1fbz , 1fhs , 1fmk , 1fyn , 1fyr , 1g83 , 1gbq , 1gbr , 1gcp , 1gcq , 1gd5 , 1gfc , 1gfd , 1ghu , 1gl5 , 1gri , 1h3h , 1h6h , 1h8k , 1h92 , 1hcs , 1hct , 1hd3 , 1hjd , 1hsq , 1i07 , 1i0c , 1i1j , 1ijr , 1io6 , 1is0 , 1j3t , 1jeg , 1jo8 , 1jqq , 1ju5 , 1jwo , 1jxm , 1jxo , 1jyq , 1jyr , 1jyu , 1k0x , 1k1z , 1k4u , 1k76 , 1k9a , 1kc2 , 1kfz , 1kik , 1kjw , 1kq6 , 1ksw , 1kwa , 1lcj , 1lck , 1lkk , 1lkl , 1lui , 1luk , 1lum , 1lun , 1m27 , 1m30 , 1m3a , 1m3b , 1m3c , 1m8m , 1muz , 1mv0 , 1mv3 , 1n5z , 1neb , 1neg , 1ng2 , 1nlo , 1nlp , 1nm7 , 1nyf , 1nyg , 1nzl , 1nzv , 1o41 , 1o42 , 1o43 , 1o44 , 1o45 , 1o46 , 1o47 , 1o48 , 1o49 , 1o4a , 1o4b , 1o4c , 1o4d , 1o4e , 1o4f , 1o4g , 1o4h , 1o4i , 1o4j , 1o4k , 1o4l , 1o4m , 1o4n , 1o4o , 1o4p , 1o4q , 1o4r , 1o7k , 1oeb , 1oot , 1opk , 1opl , 1ov3 , 1p13 , 1pht , 1pks , 1pkt , 1pnj , 1prl , 1prm , 1pwt , 1q68 , 1q69 , 1qcf , 1qg1 , 1qkw , 1qkx , 1qly , 1qwe , 1qwf , 1r1p , 1r1q , 1r1s , 1ri9 , 1rja , 1rlp , 1rlq , 1s1n , 1sem , 1sha , 1shb , 1shd , 1shf , 1shg , 1skj , 1spk , 1spr , 1sps , 1srl , 1srm , 1ssh , 1t0h , 1t0j , 1t3l , 1t3s , 1tuc , 1tud , 1tze , 1u06 , 1u46 , 1u4d , 1u54 , 1u5s , 1udl , 1ue9 , 1uec , 1uff , 1ug1 , 1ugv , 1uhc , 1uhf , 1uj0 , 1ujy , 1uti , 1uue , 1va8 , 1vyt , 1vyu , 1w1f , 1w6x , 1w70 , 1wa7 , 1wfw , 1wi7 , 1wie , 1wlp , 1wx6 , 1wxu , 1wyx , 1x0n , 1x27 , 1x2q , 1x6b , 1y0m , 1y57 , 1ycs , 1yn8 , 1ynz , 1ywo , 1ywp , 1zbj , 1zfp , 1zlm , 1zsg , 1zuu , 1zx6 , 2a36 , 2a37 , 2abl , 2ak5 , 2aoa , 2aob , 2azs , 2azv , 2b86 , 2bz8 , 2c0i , 2c0o , 2c0t , 2cdt , 2csq , 2d0n , 2d1x , 2dfk , 2ejy , 2epd , 2esw , 2etz , 2eu0 , 2ev8 , 2eyv , 2eyw , 2eyy , 2f2v , 2fo0 , 2frw , 2fry , 2gbq , 2h46 , 2h5k , 2h8h , 2hck , 2hsp , 2huw , 2iim , 2j6f , 2j6k , 2j6o , 2j7i , 2js0 , 2jte , 2jyq , 2k3b , 2nuz , 2nwm , 2o2o , 2o2w , 2o31 , 2o88 , 2o9s , 2o9v , 2oaw , 2pni , 2ptk , 2rf0 , 2rn8 , 2rna , 2sem , 2src , 2v1r , 2vkn , 3c7i , 3gbq , 3hck , 3sem , 4gbq , 4hck , 5hck
Database linksHelp
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PROSITE doc: PDOC50002
PANDIT: PF00018
Blocks: IPB001452
Pfam Clan: CL0010.17
InteractionsHelp
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This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverageHelp
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Overlapping InterPro entriesHelp
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IPR001452 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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A2CG49 Kalirin

A7KAX9 Rho/Cdc42/Rac GTPase-activating protein RICS

O01761 Muscle M-line assembly protein unc-89

P13395 Spectrin alpha chain

P15891 Actin-binding protein

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013783 Immunoglobulin-like fold
IPR001251 Cellular retinaldehyde-binding/triple function, C-terminal
IPR017441 Protein kinase, ATP binding site
IPR017442 Serine/threonine-protein kinase-like domain
IPR008936 Rho GTPase activation protein
IPR007850 RCSD
IPR011009 Protein kinase-like domain
IPR008957 Fibronectin, type III-like fold
IPR018159 Spectrin/alpha-actinin
IPR000719 Protein kinase, catalytic domain
IPR002290 Serine/threonine-protein kinase domain
IPR013315 Spectrin alpha chain, SH3 domain
IPR003961 Fibronectin, type III
IPR002017 Spectrin repeat
IPR011993 Pleckstrin homology-type
IPR007110 Immunoglobulin-like
IPR003598 Immunoglobulin subtype 2
IPR011992 EF-hand-like domain
IPR003599 Immunoglobulin subtype
IPR002108 Actin-binding, cofilin/tropomyosin type
IPR002048 Calcium-binding EF-hand
IPR001849 Pleckstrin homology
IPR000219 Dbl homology (DH) domain
IPR001452 Src homology-3 domain
IPR000198 RhoGAP
IPR018247 EF-Hand 1, calcium-binding site
IPR008271 Serine/threonine-protein kinase, active site
IPR018249 EF-HAND 2
IPR000108 Neutrophil cytosol factor 2
IPR001683 Phox-like
IPR014837 EF-hand, Ca insensitive
IPR009134 Tyrosine-protein kinase, vascular endothelial growth factor receptor (VEGFR), N-terminal
IPR020473 Src homology-3, region
ModBase
SWISS-MODEL
PDB Chain
CATH Domain
SCOP Domain

PublicationsHelp
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1. Pawson T, Schlessingert J.
SH2 and SH3 domains.
Curr. Biol. 3 434-42 1993 [PubMed: 15335710]
http://dx.doi.org/10.1016/0960-9822(93)90350-W
2. Mayer BJ.
SH3 domains: complexity in moderation.
J. Cell. Sci. 114 1253-63 2001 [PubMed: 11256992]
http://jcs.biologists.org/cgi/content/abstract/114/7/1253
3. Musacchio A, Gibson T, Lehto VP, Saraste M.
SH3--an abundant protein domain in search of a function.
FEBS Lett. 307 55-61 1992 [PubMed: 1639195]
http://dx.doi.org/10.1016/0014-5793(92)80901-R
4. Mayer BJ, Baltimore D.
Signalling through SH2 and SH3 domains.
Trends Cell Biol. 3 8-13 1993 [PubMed: 14731533]
http://dx.doi.org/10.1016/0962-8924(93)90194-6
5. Pawson T.
Protein modules and signalling networks.
Nature 373 573-80 1995 [PubMed: 7531822]
http://dx.doi.org/10.1038/373573a0
6. Cowburn D, Kuriyan J.
Structures of SH2 and SH3 domains.
Curr. Opin. Struct. Biol. 3 828-37 1993
7. Morton CJ, Campbell ID.
SH3 domains. Molecular 'Velcro'.
Curr. Biol. 4 615-7 1994 [PubMed: 7953536]
http://dx.doi.org/10.1016/S0960-9822(00)00134-2

Additional ReadingHelp
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Wu C, Ma MH, Brown KR, Geisler M, Li L, Tzeng E, Jia CY, Jurisica I, Li SS.
Systematic identification of SH3 domain-mediated human protein-protein interactions by peptide array target screening.
Proteomics 7 2007 1775-85 [PubMed: 17474147]
http://dx.doi.org/10.1002/pmic.200601006
Kong C, Su X, Chen PI, Stahl PD.
Rin1 interacts with signal-transducing adaptor molecule (STAM) and mediates epidermal growth factor receptor trafficking and degradation.
J. Biol. Chem. 282 2007 15294-301 [PubMed: 17403676]
http://dx.doi.org/10.1074/jbc.M611538200
Vallurupalli P, Hansen DF, Kay LE.
Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 11766-71 [PubMed: 18701719]
http://dx.doi.org/10.1073/pnas.0804221105
Taylor JD, Ababou A, Fawaz RR, Hobbs CJ, Williams MA, Ladbury JE.
Structure, dynamics, and binding thermodynamics of the v-Src SH2 domain: implications for drug design.
Proteins 73 2008 929-40 [PubMed: 18536014]
http://dx.doi.org/10.1002/prot.22119
Hake MJ, Choowongkomon K, Kostenko O, Carlin CR, Sonnichsen FD.
Specificity determinants of a novel Nck interaction with the juxtamembrane domain of the epidermal growth factor receptor.
Biochemistry 47 2008 3096-108 [PubMed: 18269246]
http://dx.doi.org/10.1021/bi701549a
Gushchina LV, Gabdulkhakov AG, Nikonov SV, Mateo PL, Filimonov VV.
Structural and thermodynamic studies of Bergerac-SH3 chimeras.
Biophys. Chem. 139 2009 106-15 [PubMed: 19042078]
http://dx.doi.org/10.1016/j.bpc.2008.10.011
Dimasi N.
Crystal structure of the C-terminal SH3 domain of the adaptor protein GADS in complex with SLP-76 motif peptide reveals a unique SH3-SH3 interaction.
Int. J. Biochem. Cell Biol. 39 2007 109-23 [PubMed: 17010654]
http://dx.doi.org/10.1016/j.biocel.2006.07.003
Mayer BJ, Hamaguchi M, Hanafusa H.
A novel viral oncogene with structural similarity to phospholipase C.
Nature 332 1988 272-5 [PubMed: 2450282]
http://dx.doi.org/10.1038/332272a0
Lee MF, Beauchamp RL, Beyer KS, Gusella JF, Ramesh V.
Magicin associates with the Src-family kinases and is phosphorylated upon CD3 stimulation.
Biochem. Biophys. Res. Commun. 348 2006 826-31 [PubMed: 16899217]
http://dx.doi.org/10.1016/j.bbrc.2006.07.126
Saito K, Chen M, Bard F, Chen S, Zhou H, Woodley D, Polischuk R, Schekman R, Malhotra V.
TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites.
Cell 136 2009 891-902 [PubMed: 19269366]
http://dx.doi.org/10.1016/j.cell.2008.12.025
Yun HM, Kim S, Kim HJ, Kostenis E, Kim JI, Seong JY, Baik JH, Rhim H.
The novel cellular mechanism of human 5-HT6 receptor through an interaction with Fyn.
J. Biol. Chem. 282 2007 5496-505 [PubMed: 17189269]
http://dx.doi.org/10.1074/jbc.M606215200
Kami K, Takeya R, Sumimoto H, Kohda D.
Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p.
EMBO J. 21 2002 4268-76 [PubMed: 12169629]
http://dx.doi.org/10.1093/emboj/cdf428
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