SIAH2

Siah E3 ubiquitin protein ligase 2

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 transferase activity • protein binding • zinc ion binding • ligase activity • ubiquitin conjugating enzyme binding
Cellular component	• nucleoplasm • cytoplasm • early endosome • cytosol • neuron projection • neuronal cell body • intracellular membrane-bounded organelle
Biological process	• ubiquitin-dependent protein catabolic process • cell cycle • small GTPase mediated signal transduction • axon guidance • protein ubiquitination • regulation of protein ubiquitination • negative regulation of apoptotic process • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process • cellular protein catabolic process • negative regulation of canonical Wnt signaling pathway • negative regulation of nucleic acid-templated transcription • negative regulation of extrinsic apoptotic signaling pathway
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 3:
150.74 – 150.76 Mb

Chr 3:
58.67 – 58.69 Mb

PubMed search

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 (November 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.
1 2 "Entrez Gene: SIAH2 seven in absentia homolog 2 (Drosophila)".
↑ Okabe, Hiroshi; Satoh Seiji; Furukawa Yoichi; Kato Tatsushi; Hasegawa Suguru; Nakajima Yumi; Yamaoka Yoshio; Nakamura Yusuke (June 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 (March 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 (February 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.
↑ 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.

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.
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.
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.
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.
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.
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.
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.
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.

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SIAH2

Interactions

References

Further reading