SH3 Interactome Conserves General Function Over Specific Form

This data is supplementary material for:

SH3 Interactome Conserves General Function Over Specific Form

Xiaofeng Xin1*†, David Gfeller1*‡, Jackie Cheng2*, Raffi Tonikian1*, Lin Sun3¶, Ailan Guo4, Lianet Lopez1, Alevtina Pavlenco1, Adenrele Akintobi3, Yingnan Zhang5, Jean-Francois Rual6,7, Bridget Currell8, Somasekar Seshagiri8, Tong Hao6,7, Xinping Yang6,7, Yun A. Shen6,7, Kourosh Salehi-Ashtiani6,7, Jingjing Li1, Aaron T. Cheng2, Dryden Bouamalay2, Adrien Lugari9, David E. Hill6,7, Mark L. Grimes10, David G. Drubin2, Barth D. Grant3, Marc Vidal6,7, Charles Boone1§, Sachdev S. Sidhu1§, Gary D. Bader1,11§

Supplementary Information

* Supplementary Information

Supplementary Tables

Data

File Format

Each zip file contains a set of peptide files as shown in the example below. A peptide file describes a protein containing a specific domain, and provides known peptide ligands of this domain obtained by an experimental technique. These files can be directly loaded into the LOLA software, which can be used to visualize peptide sets as sequence logos and to create Logo Trees, or the BRAIN software, which is a Cytoscape plugin that can be used to search protein sequence databases for proteins that contain sequence patterns matching a set of peptides.

The peptide file consists of a Header Section that describes the protein and domain sequence, and a Peptide Section that lists and describes the peptide ligands.

The peptides have been aligned with MUSCLE (Nucl. Acids Res. (2004) 32 (5): 1792-1797) and all multiple alignments have been manually curated. For some domains (STAM-1 = C34G6.7 and HUM-1 = F29D10.4), the interacting peptides have bee split into two groups corresponding to Class I (RxxPxxP) and class II (PxxPxR) SH3 ligands.

Example:

Gene Name       B0303.7
Accession       Refseq:B0303.7
Organism        C. elegans
NCBITaxonomy    ID9606
Domain Number   1
Domain Type     SH3
Interpro ID     IPR001452
Technique       Phage Display High Valency
Domain sequence PSYSAPAISTPYGIAKFDYAPTQSDEMGLRIGDTVLISKKVDAEWFYGENQNQRTFGIVPSSYLDIKIPLKEAFTAL
PeptideName     Peptide CloneFrequency
1       GSEVPPVPPRPV    1
2       SLDPPPVPPRPV    1
3       ASARPPVPPRPL    1
4       SNLDHWQPGEPV    1
5       DMRAPPVPPRPD    1
6       XXXAPLPPPRPD    1
7       FQDVRIAPQVPA    1
8       APVAPEPPPRPH    1
9       SXIVPTVPPVPD    1
10      GQTAPPVPARPA    1
11      EGVAPPPPPRPV    1
12      FTTAPPVPPRPL    1
13      LGTAPPVPARPI    1
14      SEILPTIPPRPD    1
15      SGTPPPVPTRPD    1
16      VTEAPQVPPRPF    1
17      GETAPPVPPRPL    1
18      LPEPPPPPPRPV    1
19      LLDTPAVPTRPC    1
20      YGAAPPVPPRPV    1
21      QPKAPPVPVRPS    1
22      LLDTPAVPTRPC    1
23      GEYAPPVPPRPD    1
24      DITAPPPPPRPY    1
25      VRETPPVPARPA    1
26      SLDPPPVPPRPV    1
27      LDRVPPPPARPS    1
28      XGEAPPAPPRPG    1
29      VDAAPPVPQRPA    1
30      GATAPPVPPRPN    1
31      GDLPPPVPPRPS    1

Header Section

Describes the protein, domain, and experiment. Required fields are indicated with a *.

NOTE: This section is in a 2 column format. Field names must be separated from their values with a single TAB character. Multiple TABs, or spaces, are not accepted.

Peptide Section

Describes the experimentally determined peptide ligands. The peptide sequences must be in multiple alignment format. The sequences should contain no gaps, and should be padded with the X symbol on both sides, where required, such that all sequences have identical length.

NOTE: This section is in a 5-column format. Column headers and values must be separated with a single TAB character. Multiple TABs or spaces are not accepted.

Required fields are indicated with a *.

Author Information

1 The Donnelly Centre and the Department of Molecular Genetics, University of Toronto, Toronto, Ontario M5S 3E1, Canada

2 Department of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA 94720, USA

3 Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08854, USA

4 Cell Signaling Technology, Danvers, MA 01923, USA

5 Department of Early Discovery Biochemistry, Genentech, South San Francisco, CA 94080, USA

6 Center for Cancer Systems Biology (CCSB) and Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA

7 Department of Genetics, Harvard Medical School, Boston, MA 02115, USA

8 Department of Molecular Biology, Genentech, South San Francisco, CA 94080, USA

9 IMR Laboratory, UPR 3243, Institut de Microbiologie de la Méditérannée, CNRS and Aix-Marseille Université, 31 Chemin Joseph Aiguier, 13402 Marseille Cedex 20, France

10 Division of Biological Sciences, Center for Structural and Functional Neuroscience, The University of Montana, Missoula, MT 59812, USA

11 Department of Computer Science, University of Toronto, Toronto, ON M5S 2E4, Canada

* These authors contributed equally to this work.

† Present address: Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA

‡ Present address: Swiss Institute of Bioinformatics, Molecular Modelling, Génopode, CH-1015 Lausanne, Switzerland

¶ Present address: Department of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118, USA

§ To whom correspondence should be addressed. E-mail: sachdev.sidhu@utoronto.ca (S.S.S.); charlie.boone@utoronto.ca (C.B.); gary.bader@utoronto.ca (G.D.B.)

Data/SH3Worm (last edited 2013-03-13 12:49:25 by DavidGfeller)

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