STEAP4 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | STEAP4 , STAMP2, TIARP, TNFAIP9, STEAP4 metalloreductase, SchLAH | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 611098 MGI: 1923560 HomoloGene: 36422 GeneCards: STEAP4 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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STEAP family member 4 is a protein that in humans is encoded by the STEAP4 gene. [5]
The protein encoded by this gene belongs to the STEAP (six transmembrane epithelial antigen of prostate) family, and resides in the golgi apparatus. It functions as a metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+), using NAD(+) as acceptor. Studies in mice and human suggest that this gene may be involved in adipocyte development and metabolism, and may contribute to the normal biology of the prostate cell, as well as prostate cancer progression. Alternatively spliced transcript variants encoding different isoforms have been found for this gene
Yang Huanming, also known as Henry Yang, is a Chinese biologist, businessman and one of China's leading genetics researchers. He is Chairman and co-founder of the Beijing Genomics Institute, formerly of the Chinese Academy of Sciences. He was elected as member of the Chinese Academy of Sciences in 2007, a foreign academician of Indian National Science Academy in 2009, a member of the German National Academy of Sciences in 2012, and foreign associate of the US National Academy of Science in 2014.
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Trafficking protein particle complex subunit 2 (TRAPPC2) also known as MBP-1-interacting protein 2A (MIP-2A) is a protein that in humans is encoded by the TRAPPC2 gene. A processed pseudogene of this gene is located on chromosome 19, and other pseuodogenes of it are found on chromosome 8 and the Y chromosome. Two transcript variants encoding the same protein have been found for this gene.
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YedZ of E. coli has been examined topologically and has 6 transmembrane segments (TMSs) with both the N- and C-termini localized to the cytoplasm. von Rozycki et al. 2004 identified homologues of YedZ in bacteria and animals. YedZ homologues exhibit conserved histidyl residues in their transmembrane domains that may function in heme binding. Some of the homologues encoded in the genomes of various bacteria have YedZ domains fused to transport, electron transfer and biogenesis proteins. One of the animal homologues is the 6 TMS epithelial plasma membrane antigen of the prostate (STAMP1) that is over-expressed in prostate cancer. Some animal homologues have YedZ domains fused C-terminal to homologues of NADP oxidoreductases.
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.