LIG_SH3_1
Accession: | |
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Functional site class: | SH3 ligand |
Functional site description: | This motif is involved in protein-protein interaction mediated by SH3 domains. |
ELMs with same func. site: | LIG_SH3_1 LIG_SH3_2 LIG_SH3_3 LIG_SH3_4 LIG_SH3_5 |
ELM Description: | This is the motif recognized by class I SH3 domains |
Pattern: | [RKY]..P..P |
Pattern Probability: | 0.0012370 |
Present in taxons: | Bos taurus Gallus gallus Homo sapiens Mus musculus Opisthokonta Rattus norvegicus Saccharomyces cerevisiae |
Interaction Domain: |
SH3_1 (PF00018)
SH3 domain
(Stochiometry: 1 : 1)
|
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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. |

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Identification of a protein that binds to the SH3 region of Abl and is
similar to Bcr and GAP-rho.
Cicchetti P, Mayer BJ, Thiel G, Baltimore D
Science 1992 Aug 7; 257 (5071), 803-6
PMID: 1379745
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Association of p62, a multifunctional SH2- and SH3-domain-binding protein,
with src family tyrosine kinases, Grb2, and phospholipase C gamma-1.
Richard S, Yu D, Blumer KJ, Hausladen D, Olszowy MW, Connelly PA, Shaw AS
Mol Cell Biol 1995 Jan; 15 (1), 186-97
PMID: 7799925
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Identification of two SH3-binding motifs in the regulatory subunit of
phosphatidylinositol 3-kinase.
Kapeller R, Prasad KV, Janssen O, Hou W, Schaffhausen BS, Rudd CE, Cantley LC
J Biol Chem 1994 Jan 21; 269 (3), 1927-33
PMID: 8294442
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Identification of a ten-amino acid proline-rich SH3 binding site.
Ren R, Mayer BJ, Cicchetti P, Baltimore D
Science 1993 Feb 19; 259 (5098), 1157-61
PMID: 8438166
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Specificity of p47phox SH3 domain interactions in NADPH oxidase assembly
and activation.
de Mendez I, Homayounpour N, Leto TL
Mol Cell Biol 1997 Apr; 17 (4), 2177-85
PMID: 9121467
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Regulation of Rad51 function by c-Abl in response to DNA damage.
Yuan ZM, Huang Y, Ishiko T, Nakada S, Utsugisawa T, Kharbanda S, Wang R, Sung P, Shinohara A, Weichselbaum R, Kufe D
J Biol Chem 1998 Feb 13; 273 (7), 3799-802
PMID: 9461559
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Tau interacts with src-family non-receptor tyrosine kinases.
Lee G, Newman ST, Gard DL, Band H, Panchamoorthy G
J Cell Sci 1998 Nov; 111, 3167-77
PMID: 9763511
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ASAP1, a phospholipid-dependent arf GTPase-activating protein that
associates with and is phosphorylated by Src.
Brown MT, Andrade J, Radhakrishna H, Donaldson JG, Cooper JA, Randazzo PA
Mol Cell Biol 1998 Dec; 18 (12), 7038-51
PMID: 9819391
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p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA
damage.
Yuan ZM, Shioya H, Ishiko T, Sun X, Gu J, Huang YY, Lu H, Kharbanda S, Weichselbaum R, Kufe D
Nature 1999 Jun 24; 399 (6738), 814-7
PMID: 10391251
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Evidence for SH3 domain directed binding and phosphorylation of Sam68 by
Src.
Shen Z, Batzer A, Koehler JA, Polakis P, Schlessinger J, Lydon NB, Moran MF
Oncogene 1999 Aug 19; 18 (33), 4647-53
PMID: 10467411
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A role for myosin-I in actin assembly through interactions with Vrp1p,
Bee1p, and the Arp2/3 complex.
Evangelista M, Klebl BM, Tong AH, Webb BA, Leeuw T, Leberer E, Whiteway M, Thomas DY, Boone C
J Cell Biol 2000 Jan 24; 148 (2), 353-62
PMID: 10648568
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The importance of being proline: the interaction of proline-rich motifs in
signaling proteins with their cognate domains.
Kay BK, Williamson MP, Sudol M
FASEB J 2000 Feb; 14 (2), 231-41
PMID: 10657980
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Scar/WAVE-1, a Wiskott-Aldrich syndrome protein, assembles an
actin-associated multi-kinase scaffold.
Westphal RS, Soderling SH, Alto NM, Langeberg LK, Scott JD
EMBO J 2000 Sep 1; 19 (17), 4589-600
PMID: 10970852
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Meltrin alpha cytoplasmic domain interacts with SH3 domains of Src and
Grb2 and is phosphorylated by v-Src.
Suzuki A, Kadota N, Hara T, Nakagami Y, Izumi T, Takenawa T, Sabe H, Endo T
Oncogene 2000 Nov 30; 19 (51), 5842-50
PMID: 11127814
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Identification and kinetic analysis of the interaction between Nck-2 and
DOCK180.
Tu Y, Kucik DF, Wu C
FEBS Lett 2001 Mar 2; 491 (3), 193-9
PMID: 11240126
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SH3 domains: complexity in moderation.
Mayer BJ
J Cell Sci 2001 Apr; 114, 1253-63
PMID: 11256992
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Processive phosphorylation of p130Cas by Src depends on SH3-polyproline
interactions.
Pellicena P, Miller WT
J Biol Chem 2001 Jul 27; 276 (30), 28190-6
PMID: 11389136
-
Measles virus envelope glycoproteins hetero-oligomerize in the endoplasmic
reticulum.
Plemper RK, Hammond AL, Cattaneo R
J Biol Chem 2001 Nov 23; 276 (47), 44239-46
PMID: 11535597
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Binding of Fyn to MAP-2c through an SH3 binding domain. Regulation of the
interaction by ERK2.
Zamora-Leon SP, Lee G, Davies P, Shafit-Zagardo B
J Biol Chem 2001 Oct 26; 276 (43), 39950-8
PMID: 11546790
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Both proline-rich sequences in the TH region of Bruton's tyrosine kinase
stabilize intermolecular interactions with the SH3 domain.
Hansson H, Smith CI, Hard T
FEBS Lett 2001 Nov 9; 508 (1), 11-5
PMID: 11707259


(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Acc., Gene-, Name | Start | End | Subsequence | Logic | #Ev. | Organism | Notes |
---|---|---|---|---|---|---|---|
B7UM88 espF B7UM88_ECO27 |
169 | 175 | VSFKPTRQAPPPPTSGQASG | TP | 7 | Escherichia coli O127:H6 str. E2348/69 | |
B7UM88 espF B7UM88_ECO27 |
122 | 128 | VNFKPTRPAPPPPTSGQASG | TP | 9 | Escherichia coli O127:H6 str. E2348/69 | |
B7UM88 espF B7UM88_ECO27 |
75 | 81 | TSFTPSRPAPPPPTSGQASG | TP | 9 | Escherichia coli O127:H6 str. E2348/69 | |
Q06609 RAD51 RAD51_HUMAN |
315 | 321 | TRICKIYDSPCLPEAEAMFA | TP | 3 | Homo sapiens (Human) | |
P10636 MAPT TAU_HUMAN |
547 | 553 | KKVAVVRTPPKSPSSAKSRL | TP | 1 | Homo sapiens (Human) | |
Q06187 BTK BTK_HUMAN |
200 | 206 | EDQILKKPLPPEPAAAPVST | TP | 1 | Homo sapiens (Human) | |
Q06187 BTK BTK_HUMAN |
186 | 192 | SHRKTKKPLPPTPEEDQILK | TP | 1 | Homo sapiens (Human) | |
P27986 PIK3R1 P85A_HUMAN |
88 | 94 | ISPPTPKPRPPRPLPVAPGS | TP | 2 | Homo sapiens (Human) |
Please cite:
The Eukaryotic Linear Motif resource: 2022 release.
(PMID:34718738)
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement