SIAH2

From Wikipedia, the free encyclopedia

Seven in absentia homolog 2 (Drosophila)

Identifiers

SIAH2; hSiah2

External IDs

OMIM: 602213 MGI: 108062 HomoloGene: 21053

Gene ontology
Molecular Function:	• transcription corepressor activity • protein binding • zinc ion binding • ligase activity • metal ion binding
Cellular Component:	• nucleus • cytoplasm
Biological Process:	• ubiquitin-dependent protein catabolic process • ubiquitin cycle • apoptosis • cell cycle • small GTPase mediated signal transduction • multicellular organismal development

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_005067 (mRNA)
NP_005058 (protein)

XM_993621 (mRNA)
XP_998715 (protein)

Location

n/a

Chr 3: 58.76 - 58.78 Mb

Pubmed search

[1]

[2]

Seven in absentia homolog 2 (Drosophila), also known as SIAH2, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: SIAH2 seven in absentia homolog 2 (Drosophila).

[edit] Further reading

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Hu G, Zhang S, Vidal M, et al. (1997). "Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway.". Genes Dev. 11 (20): 2701–14. PMID 9334332.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Hu G, Chung YL, Glover T, et al. (1998). "Characterization of human homologs of the Drosophila seven in absentia (sina) gene.". Genomics 46 (1): 103–11. doi:10.1006/geno.1997.4997. PMID 9403064.
Hu G, Fearon ER (1999). "Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins.". Mol. Cell. Biol. 19 (1): 724–32. PMID 9858595.
Germani A, Romero F, Houlard M, et al. (1999). "hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling pathways.". Mol. Cell. Biol. 19 (5): 3798–807. PMID 10207103.
Relaix F, Wei X, Li W, et al. (2000). "Pw1/Peg3 is a potential cell death mediator and cooperates with Siah1a in p53-mediated apoptosis.". Proc. Natl. Acad. Sci. U.S.A. 97 (5): 2105–10. doi:10.1073/pnas.040378897. PMID 10681424.
Joensuu T, Hämäläinen R, Lehesjoki AE, et al. (2000). "A sequence-ready map of the Usher syndrome type III critical region on chromosome 3q.". Genomics 63 (3): 409–16. doi:10.1006/geno.1999.6096. PMID 10704288.
Matsuzawa SI, Reed JC (2001). "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses.". Mol. Cell 7 (5): 915–26. PMID 11389839.
Boehm J, He Y, Greiner A, et al. (2001). "Regulation of BOB.1/OBF.1 stability by SIAH.". EMBO J. 20 (15): 4153–62. doi:10.1093/emboj/20.15.4153. PMID 11483518.
Wheeler TC, Chin LS, Li Y, et al. (2002). "Regulation of synaptophysin degradation by mammalian homologues of seven in absentia.". J. Biol. Chem. 277 (12): 10273–82. doi:10.1074/jbc.M107857200. PMID 11786535.
Kutsenko AS, Gizatullin RZ, Al-Amin AN, et al. (2002). "NotI flanking sequences: a tool for gene discovery and verification of the human genome.". Nucleic Acids Res. 30 (14): 3163–70. PMID 12136098.
Habelhah H, Frew IJ, Laine A, et al. (2002). "Stress-induced decrease in TRAF2 stability is mediated by Siah2.". EMBO J. 21 (21): 5756–65. PMID 12411493.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Okabe H, Satoh S, Furukawa Y, et al. (2003). "Involvement of PEG10 in human hepatocellular carcinogenesis through interaction with SIAH1.". Cancer Res. 63 (12): 3043–8. PMID 12810624.
Fanelli M, Fantozzi A, De Luca P, et al. (2004). "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.". J. Biol. Chem. 279 (7): 5374–9. doi:10.1074/jbc.M306407200. PMID 14645235.
Germani A, Prabel A, Mourah S, et al. (2004). "SIAH-1 interacts with CtIP and promotes its degradation by the proteasome pathway.". Oncogene 22 (55): 8845–51. doi:10.1038/sj.onc.1206994. PMID 14654780.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Nakayama K, Frew IJ, Hagensen M, et al. (2004). "Siah2 regulates stability of prolyl-hydroxylases, controls HIF1alpha abundance, and modulates physiological responses to hypoxia.". Cell 117 (7): 941–52. doi:10.1016/j.cell.2004.06.001. PMID 15210114.