SIAH2

E3 ubiquitin-protein ligase SIAH2 is an enzyme that in humans is encoded by the SIAH2 gene.[5][6]

SIAH2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 5H9M
Identifiers
Aliases	SIAH2, hSiah2, siah E3 ubiquitin protein ligase 2
External IDs	OMIM: 602213 MGI: 108062 HomoloGene: 21053 GeneCards: SIAH2
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3q25.1 Start 150,741,125 bp[1] End 150,763,477 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3 D|3 28.68 cM Start 58,674,938 bp[2] End 58,692,400 bp[2]
Gene ontology Molecular function • GO:0001106 transcription corepressor activity • zinc ion binding • metal ion binding • GO:0001948 protein binding • ubiquitin conjugating enzyme binding • transferase activity • ubiquitin-protein transferase activity • GO:1904264, GO:1904822, GO:0090622, GO:0090302 ubiquitin protein ligase activity Cellular component • cytoplasm • cytosol • intracellular membrane-bounded organelle • nucleoplasm • neuronal cell body • early endosome • neuron projection • cell nucleus Biological process • cellular protein metabolic process • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process • small GTPase mediated signal transduction • regulation of protein ubiquitination • negative regulation of extrinsic apoptotic signaling pathway • negative regulation of apoptotic process • cellular protein catabolic process • axon guidance • multicellular organism development • protein ubiquitination • cell cycle • negative regulation of canonical Wnt signaling pathway • apoptotic process • negative regulation of nucleic acid-templated transcription • protein polyubiquitination • protein deubiquitination • ubiquitin-dependent protein catabolic process • negative regulation of netrin-activated signaling pathway • proteasome-mediated ubiquitin-dependent protein catabolic process • regulation of circadian rhythm • rhythmic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6478	20439
Ensembl	ENSG00000181788	ENSMUSG00000036432
UniProt	O43255	Q06986
RefSeq (mRNA)	NM_005067	NM_009174
RefSeq (protein)	NP_005058	NP_033200
Location (UCSC)	Chr 3: 150.74 – 150.76 Mb	Chr 3: 58.67 – 58.69 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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.[6]

Interactions

SIAH2 has been shown to interact with PEG10,[7] Synaptophysin,[8] PEG3[9] and VAV1.[10]

References

1. GRCh38: Ensembl release 89: ENSG00000181788 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000036432 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Hu G, Zhang S, Vidal M, Baer JL, Xu T, Fearon ER (October 1997). "Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway". Genes & Development. 11 (20): 2701–14. doi:10.1101/gad.11.20.2701. PMC 316613. PMID 9334332.
6. "Entrez Gene: SIAH2 seven in absentia homolog 2 (Drosophila)".
7. Okabe H, Satoh S, Furukawa Y, Kato T, Hasegawa S, Nakajima Y, Yamaoka Y, Nakamura Y (June 2003). "Involvement of PEG10 in human hepatocellular carcinogenesis through interaction with SIAH1". Cancer Research. 63 (12): 3043–8. PMID 12810624.
8. Wheeler TC, Chin LS, Li Y, Roudabush FL, Li L (March 2002). "Regulation of synaptophysin degradation by mammalian homologues of seven in absentia". The Journal of Biological Chemistry. 277 (12): 10273–82. doi:10.1074/jbc.M107857200. PMID 11786535.
9. Relaix F, Wei XJ, Li W, Pan J, Lin Y, Bowtell DD, Sassoon DA, Wu X (February 2000). "Pw1/Peg3 is a potential cell death mediator and cooperates with Siah1a in p53-mediated apoptosis". Proceedings of the National Academy of Sciences of the United States of America. 97 (5): 2105–10. doi:10.1073/pnas.040378897. PMC 15761. PMID 10681424.
10. 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". Molecular and Cellular Biology. 19 (5): 3798–807. doi:10.1128/mcb.19.5.3798. PMC 84217. PMID 10207103.

Further reading

• Maruyama K, Sugano S (January 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 (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 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, Valentine V, Look AT, Fearon ER (November 1997). "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 (January 1999). "Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins". Molecular and Cellular Biology. 19 (1): 724–32. doi:10.1128/mcb.19.1.724. PMC 83929. PMID 9858595.
• 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". Molecular and Cellular Biology. 19 (5): 3798–807. doi:10.1128/mcb.19.5.3798. PMC 84217. PMID 10207103.
• Relaix F, Wei XJ, Li W, Pan J, Lin Y, Bowtell DD, Sassoon DA, Wu X (February 2000). "Pw1/Peg3 is a potential cell death mediator and cooperates with Siah1a in p53-mediated apoptosis". Proceedings of the National Academy of Sciences of the United States of America. 97 (5): 2105–10. doi:10.1073/pnas.040378897. PMC 15761. PMID 10681424.
• Joensuu T, Hämäläinen R, Lehesjoki AE, de la Chapelle A, Sankila EM (February 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 (May 2001). "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses". Molecular Cell. 7 (5): 915–26. doi:10.1016/S1097-2765(01)00242-8. PMID 11389839.
• Boehm J, He Y, Greiner A, Staudt L, Wirth T (August 2001). "Regulation of BOB.1/OBF.1 stability by SIAH". The EMBO Journal. 20 (15): 4153–62. doi:10.1093/emboj/20.15.4153. PMC 149152. PMID 11483518.
• Wheeler TC, Chin LS, Li Y, Roudabush FL, Li L (March 2002). "Regulation of synaptophysin degradation by mammalian homologues of seven in absentia". The Journal of Biological Chemistry. 277 (12): 10273–82. doi:10.1074/jbc.M107857200. PMID 11786535.
• Kutsenko AS, Gizatullin RZ, Al-Amin AN, Wang F, Kvasha SM, Podowski RM, Matushkin YG, Gyanchandani A, Muravenko OV, Levitsky VG, Kolchanov NA, Protopopov AI, Kashuba VI, Kisselev LL, Wasserman W, Wahlestedt C, Zabarovsky ER (July 2002). "NotI flanking sequences: a tool for gene discovery and verification of the human genome". Nucleic Acids Research. 30 (14): 3163–70. doi:10.1093/nar/gkf428. PMC 135748. PMID 12136098.
• Habelhah H, Frew IJ, Laine A, Janes PW, Relaix F, Sassoon D, Bowtell DD, Ronai Z (November 2002). "Stress-induced decrease in TRAF2 stability is mediated by Siah2". The EMBO Journal. 21 (21): 5756–65. doi:10.1093/emboj/cdf576. PMC 131073. PMID 12411493.
• Okabe H, Satoh S, Furukawa Y, Kato T, Hasegawa S, Nakajima Y, Yamaoka Y, Nakamura Y (June 2003). "Involvement of PEG10 in human hepatocellular carcinogenesis through interaction with SIAH1". Cancer Research. 63 (12): 3043–8. PMID 12810624.
• Fanelli M, Fantozzi A, De Luca P, Caprodossi S, Matsuzawa S, Lazar MA, Pelicci PG, Minucci S (February 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". The Journal of Biological Chemistry. 279 (7): 5374–9. doi:10.1074/jbc.M306407200. PMID 14645235.
• Germani A, Prabel A, Mourah S, Podgorniak MP, Di Carlo A, Ehrlich R, Gisselbrecht S, Varin-Blank N, Calvo F, Bruzzoni-Giovanelli H (December 2003). "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.
• Nakayama K, Frew IJ, Hagensen M, Skals M, Habelhah H, Bhoumik A, Kadoya T, Erdjument-Bromage H, Tempst P, Frappell PB, Bowtell DD, Ronai Z (June 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.