Rabbit anti-Human TRIM11 Polyclonal Antibody

Uniprot Id

Q96F44

Target Species

Human

Target Name

TRIM11

Target Full Name

E3 ubiquitin-protein ligase TRIM11

Target Function

E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle.

Target Subcellular Location

Cytoplasm. Nucleus.

Target Protein Families

TRIM/RBCC family

Target Tissue Specificity

Ubiquitous.

Target Research Area

Immunology

Target Synonyms

BIA 1; BIA1; E3 ubiquitin protein ligase TRIM11; E3 ubiquitin-protein ligase TRIM11; Protein BIA1; RING finger protein 92; RING type E3 ubiquitin transferase TRIM11; RNF 92; RNF92; TRI11_HUMAN; Trim 11; TRIM11; Tripartite motif containing 11; tripartite motif protein 11; Tripartite motif-containing protein 11

Target Background

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein localizes to the nucleus and the cytoplasm. Its function has not been identified.