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. 2014 May 14;7:39. doi: 10.3389/fnmol.2014.00039

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Copyright © 2014 Uren and Turnley.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Domain organization of the SOCS proteins. Each of the 8 SOCS proteins (SOCS1-7 and CIS) comprise a variable N-terminal region, a central Src Homology 2 (SH2) domain to recognize motifs containing phosphorylated tyrosine residues and a highly conserved C-terminal SOCS box to facilitate association with components of the ubiquitin ligase machinery such as elongin BC and cullin5. The kinase inhibitory region (KIR) (Sasaki et al., 1999; Yasukawa et al., 1999; Kershaw et al., 2013) within the extended SH2 subdomain (ESS) of SOCS1 and SOCS3 are denoted by an asterisk. The most closely related pairs of SOCS proteins according to amino acid sequence similarity are denoted on the right.