The protein encoded by this gene belongs to a family of ankyrin repeat proteins that, along with four other protein families, contain a C-terminal SOCS box motif. Growing evidence suggests that the SOCS box, similar to the F-box, acts as a bridge between specific substrate-binding domains and the more generic proteins that comprise a large family of E3 ubiquitin protein ligases. Alternatively spliced transcript variants have been identified for this gene.
ASB-8 (ankyrin repeat and SOCS box-containing 8) is a 288 amino acid member of the ASB family that contains one SOCS box domain and four ANK repeats. Localized to the cytoplasm, ASB-8 functions as a substrate-recognition component of an E3 ubiquitin-protein ligase complex and, working in conjunction with other proteins, plays a role in the ubiquitination and subsequent proteasomal degradation of target proteins. The highest level of ASB-8 expression has been detected in skeletal muscle. ASB-8 is also expressed in heart, brain, placenta, liver, kidney and pancreas.
A synthesized peptide derived from human ASB9.
A synthesized peptide derived from human ASBT, corresponding to a region within C-terminal amino acids.
A synthesized peptide derived from human ASC2, corresponding to a region within N-terminal amino acids.
This gene encodes a subunit of the activating signal cointegrator 1 (ASC-1) complex. The ASC-1 complex is a transcriptional coactivator that plays an important role in gene transactivation by multiple transcription factors including activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and serum response factor (SRF). The encoded protein contains an N-terminal KH-type RNA-binding motif which is required for AP-1 transactivation by the ASC-1 complex. Mutations in this gene are associated with Barrett esophagus and esophageal adenocarcinoma. Alternatively spliced transcripts encoding multiple isoforms have been observed for this gene.
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