SIAH2

Seven in absentia homolog 2 (Drosophila)

Identifiers

SIAH2; hSiah2

External IDs

OMIM: 602213 MGI: 108062 HomoloGene: 21053 GeneCards: SIAH2 Gene

6.3.2.-

Gene Ontology
Molecular function	• transcription corepressor activity • ubiquitin-protein ligase activity • zinc ion binding • ligase activity • metal ion binding
Cellular component	• nucleus • cytoplasm • cytosol
Biological process	• ubiquitin-dependent protein catabolic process • apoptosis • cell cycle • small GTPase mediated signal transduction • multicellular organismal development • axon guidance • cellular protein catabolic process • negative regulation of canonical Wnt receptor signaling pathway
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 3:
150.46 – 150.48 Mb

Chr 3:
58.48 – 58.5 Mb

PubMed search

[1]

[2]

E3 ubiquitin-protein ligase SIAH2 is an enzyme that in humans is encoded by the SIAH2 gene.^[1]^[2]

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.^[2]

Interactions

SIAH2 has been shown to interact with PEG10,^[3] Synaptophysin,^[4] PEG3^[5] and VAV1.^[6]

References

^ Hu G, Zhang S, Vidal M, Baer JL, Xu T, Fearon ER (Nov 1997). "Mammalian homologs of seven in absentia regulate DCC via the ubiquitin–proteasome pathway". Genes Dev 11 (20): 2701–14. doi:10.1101/gad.11.20.2701. PMC 316613. PMID 9334332. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=316613.
^ ^a ^b "Entrez Gene: SIAH2 seven in absentia homolog 2 (Drosophila)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6478.
^ Okabe, Hiroshi; Satoh Seiji, Furukawa Yoichi, Kato Tatsushi, Hasegawa Suguru, Nakajima Yumi, Yamaoka Yoshio, Nakamura Yusuke (Jun. 2003). "Involvement of PEG10 in human hepatocellular carcinogenesis through interaction with SIAH1". Cancer Res. (United States) 63 (12): 3043–8. ISSN 0008-5472. PMID 12810624.
^ Wheeler, Tiffany C; Chin Lih-Shen, Li Yankun, Roudabush Francine L, Li Lian (Mar. 2002). "Regulation of synaptophysin degradation by mammalian homologues of seven in absentia". J. Biol. Chem. (United States) 277 (12): 10273–82. doi:10.1074/jbc.M107857200. ISSN 0021-9258. PMID 11786535.
^ Relaix, F; Wei X j, Li W, Pan J, Lin Y, Bowtell D D, Sassoon D A, Wu X (Feb. 2000). "Pw1/Peg3 is a potential cell death mediator and cooperates with Siah1a in p53-mediated apoptosis". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (5): 2105–10. doi:10.1073/pnas.040378897. ISSN 0027-8424. PMC 15761. PMID 10681424. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=15761.
^ Germani, A; Romero F, Houlard M, Camonis J, Gisselbrecht S, Fischer S, Varin-Blank N (May. 1999). "hSiah2 Is a New Vav Binding Protein Which Inhibits Vav-Mediated Signaling Pathways". Mol. Cell. Biol. (UNITED STATES) 19 (5): 3798–807. ISSN 0270-7306. PMC 84217. PMID 10207103. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84217.

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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
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. doi:10.1016/S0378-1119(97)00411-3. 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. PMC 83929. PMID 9858595. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=83929.
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. PMC 84217. PMID 10207103. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=84217.
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. PMC 15761. PMID 10681424. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=15761.
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. doi:10.1016/S1097-2765(01)00242-8. 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. PMC 149152. PMID 11483518. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=149152.
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. doi:10.1093/nar/gkf428. PMC 135748. PMID 12136098. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=135748.
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. doi:10.1093/emboj/cdf576. PMC 131073. PMID 12411493. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=131073.
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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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.

SIAH2

Interactions

References

Further reading