SIAH2

Seven in absentia homolog 2 (Drosophila), also known as SIAH2, is a human gene.cite web | title = Entrez Gene: SIAH2 seven in absentia homolog 2 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6478| accessdate = ]

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 regulating cellular response to hypoxia.cite web | title = Entrez Gene: SIAH2 seven in absentia homolog 2 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6478| accessdate = ]

References

Further reading

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=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |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=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=Germani A, Romero F, Houlard M, "et al." |title=hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling pathways. |journal=Mol. Cell. Biol. |volume=19 |issue= 5 |pages= 3798–807 |year= 1999 |pmid= 10207103 |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=Joensuu T, Hämäläinen R, Lehesjoki AE, "et al." |title=A sequence-ready map of the Usher syndrome type III critical region on chromosome 3q. |journal=Genomics |volume=63 |issue= 3 |pages= 409–16 |year= 2000 |pmid= 10704288 |doi= 10.1006/geno.1999.6096
*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=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=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=Kutsenko AS, Gizatullin RZ, Al-Amin AN, "et al." |title=NotI flanking sequences: a tool for gene discovery and verification of the human genome. |journal=Nucleic Acids Res. |volume=30 |issue= 14 |pages= 3163–70 |year= 2002 |pmid= 12136098 |doi=
*cite journal | author=Habelhah H, Frew IJ, Laine A, "et al." |title=Stress-induced decrease in TRAF2 stability is mediated by Siah2. |journal=EMBO J. |volume=21 |issue= 21 |pages= 5756–65 |year= 2002 |pmid= 12411493 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Okabe H, Satoh S, Furukawa Y, "et al." |title=Involvement of PEG10 in human hepatocellular carcinogenesis through interaction with SIAH1. |journal=Cancer Res. |volume=63 |issue= 12 |pages= 3043–8 |year= 2003 |pmid= 12810624 |doi=
*cite journal | author=Fanelli M, Fantozzi A, De Luca P, "et al." |title=The coiled-coil domain is the structural determinant for mammalian homologues of Drosophila Sina-mediated degradation of promyelocytic leukemia protein and other tripartite motif proteins by the proteasome. |journal=J. Biol. Chem. |volume=279 |issue= 7 |pages= 5374–9 |year= 2004 |pmid= 14645235 |doi= 10.1074/jbc.M306407200
*cite journal | author=Germani A, Prabel A, Mourah S, "et al." |title=SIAH-1 interacts with CtIP and promotes its degradation by the proteasome pathway. |journal=Oncogene |volume=22 |issue= 55 |pages= 8845–51 |year= 2004 |pmid= 14654780 |doi= 10.1038/sj.onc.1206994
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Nakayama K, Frew IJ, Hagensen M, "et al." |title=Siah2 regulates stability of prolyl-hydroxylases, controls HIF1alpha abundance, and modulates physiological responses to hypoxia. |journal=Cell |volume=117 |issue= 7 |pages= 941–52 |year= 2004 |pmid= 15210114 |doi= 10.1016/j.cell.2004.06.001

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