SIAH1

Seven in absentia homolog 1 (Drosophila), also known as SIAH1, is a human gene.

PBB_Summary
section_title =
summary_text = This gene encodes a protein that is a member of the seven in absentia homolog (SIAH) family. The protein is an E3 ligase and is involved in ubiquitination and proteasome-mediated degradation of specific proteins. The activity of this ubiquitin ligase has been implicated in the development of certain forms of Parkinson's disease, the regulation of the cellular response to hypoxia and induction of apoptosis. Alternative splicing results in several additional transcript variants, some encoding different isoforms and others that have not been fully characterized.cite web | title = Entrez Gene: SIAH1 seven in absentia homolog 1 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6477| accessdate = ]

References

PBB_Further_reading
citations =
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Nemani M, Linares-Cruz G, Bruzzoni-Giovanelli H, "et al." |title=Activation of the human homologue of the Drosophila sina gene in apoptosis and tumor suppression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 17 |pages= 9039–42 |year= 1996 |pmid= 8799150 |doi=
*cite journal | author=Hu G, Zhang S, Vidal M, "et al." |title=Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway. |journal=Genes Dev. |volume=11 |issue= 20 |pages= 2701–14 |year= 1997 |pmid= 9334332 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Hu G, Chung YL, Glover T, "et al." |title=Characterization of human homologs of the Drosophila seven in absentia (sina) gene. |journal=Genomics |volume=46 |issue= 1 |pages= 103–11 |year= 1998 |pmid= 9403064 |doi= 10.1006/geno.1997.4997
*cite journal | author=Matsuzawa S, Takayama S, Froesch BA, "et al." |title=p53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: suppression by BAG-1. |journal=EMBO J. |volume=17 |issue= 10 |pages= 2736–47 |year= 1998 |pmid= 9582267 |doi= 10.1093/emboj/17.10.2736
*cite journal | author=Block KL, Vornlocher HP, Hershey JW |title=Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3. |journal=J. Biol. Chem. |volume=273 |issue= 48 |pages= 31901–8 |year= 1998 |pmid= 9822659 |doi=
*cite journal | author=Hu G, Fearon ER |title=Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins. |journal=Mol. Cell. Biol. |volume=19 |issue= 1 |pages= 724–32 |year= 1999 |pmid= 9858595 |doi=
*cite journal | author=Relaix F, Wei X, Li W, "et al." |title=Pw1/Peg3 is a potential cell death mediator and cooperates with Siah1a in p53-mediated apoptosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 5 |pages= 2105–10 |year= 2000 |pmid= 10681424 |doi= 10.1073/pnas.040378897
*cite journal | author=Tanikawa J, Ichikawa-Iwata E, Kanei-Ishii C, "et al." |title=p53 suppresses the c-Myb-induced activation of heat shock transcription factor 3. |journal=J. Biol. Chem. |volume=275 |issue= 20 |pages= 15578–85 |year= 2000 |pmid= 10747903 |doi= 10.1074/jbc.M000372200
*cite journal | author=Medhioub M, Vaury C, Hamelin R, Thomas G |title=Lack of somatic mutation in the coding sequence of SIAH1 in tumors hemizygous for this candidate tumor suppressor gene. |journal=Int. J. Cancer |volume=87 |issue= 6 |pages= 794–7 |year= 2000 |pmid= 10956387 |doi=
*cite journal | author=Germani A, Bruzzoni-Giovanelli H, Fellous A, "et al." |title=SIAH-1 interacts with alpha-tubulin and degrades the kinesin Kid by the proteasome pathway during mitosis. |journal=Oncogene |volume=19 |issue= 52 |pages= 5997–6006 |year= 2001 |pmid= 11146551 |doi= 10.1038/sj.onc.1204002
*cite journal | author=Matsuzawa SI, Reed JC |title=Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses. |journal=Mol. Cell |volume=7 |issue= 5 |pages= 915–26 |year= 2001 |pmid= 11389839 |doi=
*cite journal | author=Liu J, Stevens J, Rote CA, "et al." |title=Siah-1 mediates a novel beta-catenin degradation pathway linking p53 to the adenomatous polyposis coli protein. |journal=Mol. Cell |volume=7 |issue= 5 |pages= 927–36 |year= 2001 |pmid= 11389840 |doi=
*cite journal | author=Tiedt R, Bartholdy BA, Matthias G, "et al." |title=The RING finger protein Siah-1 regulates the level of the transcriptional coactivator OBF-1. |journal=EMBO J. |volume=20 |issue= 15 |pages= 4143–52 |year= 2001 |pmid= 11483517 |doi= 10.1093/emboj/20.15.4143
*cite journal | author=Boehm J, He Y, Greiner A, "et al." |title=Regulation of BOB.1/OBF.1 stability by SIAH. |journal=EMBO J. |volume=20 |issue= 15 |pages= 4153–62 |year= 2001 |pmid= 11483518 |doi= 10.1093/emboj/20.15.4153
*cite journal | author=Susini L, Passer BJ, Amzallag-Elbaz N, "et al." |title=Siah-1 binds and regulates the function of Numb. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 26 |pages= 15067–72 |year= 2002 |pmid= 11752454 |doi= 10.1073/pnas.261571998
*cite journal | author=Wheeler TC, Chin LS, Li Y, "et al." |title=Regulation of synaptophysin degradation by mammalian homologues of seven in absentia. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10273–82 |year= 2002 |pmid= 11786535 |doi= 10.1074/jbc.M107857200
*cite journal | author=Maeda A, Yoshida T, Kusuzaki K, Sakai T |title=The characterization of the human Siah-1 promoter(1). |journal=FEBS Lett. |volume=512 |issue= 1-3 |pages= 223–6 |year= 2002 |pmid= 11852084 |doi=
*cite journal | author=Jarmuz A, Chester A, Bayliss J, "et al." |title=An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. |journal=Genomics |volume=79 |issue= 3 |pages= 285–96 |year= 2002 |pmid= 11863358 |doi= 10.1006/geno.2002.6718

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