TRAM1
TRAM1 (translocation associated membrane protein 1, also known as TRAM or TRAMP) is a multi-pass membrane protein of the mammalian endoplasmic reticulum. It influences glycosylation and helps secretory proteins cross the ER membrane, and it is co-opted by cytomegalovirus to evade immune detection. Browse Assay Genie's current range of TRAM1 research reagents below, or read on for the biology behind the target.
TRAM1 is a multi-pass membrane protein that forms part of the mammalian endoplasmic reticulum. According to the RefSeq summary, it influences glycosylation and facilitates the translocation of secretory proteins across the ER membrane. It does this by regulating which domains of the nascent polypeptide chain are visible to the cytosol during a translocational pause. This places TRAM1 at the point where newly synthesised proteins are threaded into the secretory pathway and modified.
The protein is encoded by the TRAM1 gene and belongs to the TRAM family. In HGNC classification it sits within the TLC domain containing group. UniProt records the protein as translocating chain-associated membrane protein 1, and it is localised to the endoplasmic reticulum membrane. The related family member TRAM2 is a natural point of comparison for studies of ER translocation. A rat ortholog, Tram1, is listed for comparative work.
TRAM1 also has a role in viral immune evasion. During cytomegalovirus infection, it participates in ER-to-cytosol retrotranslocation driven by the viral proteins US2 and US11. This leads to degradation of major histocompatibility complex (MHC) class I heavy chains. The resulting loss of MHC class I decreases immune detection by cytotoxic T-cells. Because the same protein acts in normal secretory protein handling and in this virus-driven pathway, the TRAM1 protein is of interest to researchers studying ER biology and host-pathogen interactions.
TRAM1 regulates which domains of a nascent polypeptide are exposed to the cytosol during a translocational pause, making it relevant to secretory protein biogenesis.
The RefSeq summary states that TRAM1 influences glycosylation, so it is studied in work on how nascent proteins are modified in the ER.
TRAM1 participates in US2- and US11-mediated retrotranslocation of MHC class I heavy chains, a route by which cytomegalovirus reduces immune detection.
ER-to-cytosol retrotranslocation and degradation of MHC class I heavy chains involves TRAM1, linking it to antigen presentation and cytotoxic T-cell recognition.
TRAM1 is an ER membrane protein that influences glycosylation and facilitates translocation of secretory proteins across the ER membrane. It regulates which domains of the nascent chain are visible to the cytosol during a translocational pause. It also participates in virus-induced retrotranslocation of MHC class I heavy chains.
The HGNC name is translocation associated membrane protein 1, and UniProt lists translocating chain-associated membrane protein 1. Aliases include TRAM and TRAMP. The protein belongs to the TRAM family, and TRAM2 is a related family member.
During cytomegalovirus infection, TRAM1 participates in US2- and US11-mediated retrotranslocation of MHC class I heavy chains from the ER to the cytosol. Their degradation reduces detection by cytotoxic T-cells. A rat ortholog, Tram1, is listed; check the datasheet of any product for its validated reactivity.
Other TRAM family members, ER translocation components and MHC class I pathway targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q15629; product specifications from Assay Genie datasheets.