TTYH2 gene is located at 17q24. The encoded human protein TTYH2 has 534 amino acids. The protein is characterized by five membrane-spanning domains and N-glycan modifications important for trafficking to the plasma membrane, where these proteins are oriented with the amino terminus located extracellularly and the carboxyl terminus located cytoplasmically. Consistent with Ca²⁺ dependence, both TTYH2 and TTYH3 contain an acidic-amino-acid cluster at the C-terminus, predicted to interact with Ca²⁺ ions. hTTY2 as a putative chloride ion channel plays a role in Ca²⁺ signal transduction. The protein may be involved in cell proliferation and cell aggregation.
|Basic Information of TTYH2|
|Protein Name||Protein tweety homolog 2 (hTTY2)|
|Gene Name||TTYH2, C17orf29|
|Organism||Homo sapiens (Human)|
Using comparative genomic hybridization, high-level amplification of 17q24-q25, the region containing TTYH2 has been found in adrenocortical tumors, brain metastases of solid tumors, and muscle-invasive bladder cancer. These findings could suggest that up-regulated TTYH2 gene expression might play an important role in the carcinogenesis of various cancers. Furthermore, TTYH2 functions as a cell surface receptor, and its up-regulation may give a growth advantage or metastatic ability to cancer cells.
Fig.1 Previously predicted membrane topology and structural features of Tweety family proteins. (He, 2008)
This article finds that the TTYH2 gene may play an important role in regulating both proliferating and metastatic potentials of colorectal cancer.
This article suggests that Nedd4-2 differentially interacts with and regulates TTYH1-3, which is important for understanding mechanisms controlling Tweety proteins in physiology and disease.
This article suggests that over-expression of TTYH2 in renal cell carcinoma may have an important role in kidney tumorigenesis.
This article reveals that ttyh1, ttyh2, and ttyh3 may play distinct roles throughout embryonic development.
This article suggests that N-glycosylation impacts on TTYH2 protein levels, ubiquitination and, to a lesser extent, on its cellular localization.
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