SIAH2: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''E3 ubiquitin-protein ligase SIAH2''' is an [[enzyme]] that in humans is encoded by the ''SIAH2'' [[gene]].<ref name="pmid9334332">{{cite journal | vauthors = Hu G, Zhang S, Vidal M, Baer JL, Xu T, Fearon ER | title = Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway | journal = Genes & Development | volume = 11 | issue = 20 | pages = 2701–14 | date = October 1997 | pmid = 9334332 | pmc = 316613 | doi = 10.1101/gad.11.20.2701 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SIAH2 seven in absentia homolog 2 (Drosophila)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6478| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Seven in absentia homolog 2 (Drosophila)
| HGNCid = 10858
| Symbol = SIAH2
| AltSymbols =; hSiah2
| OMIM = 602213
| ECnumber = 
| Homologene = 21053
| MGIid = 108062
| Function = {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016874 |text = ligase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6478
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_005058
    | Hs_RefseqmRNA = NM_005067
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 20439
    | Mm_Ensembl = ENSMUSG00000036432
    | Mm_RefseqmRNA = XM_993621
    | Mm_RefseqProtein = XP_998715
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 58762878
    | Mm_GenLoc_end = 58780317
    | Mm_Uniprot = Q3UEV2
  }}
}}
'''Seven in absentia homolog 2 (Drosophila)''', also known as '''SIAH2''', is a human [[gene]].<ref name="entrez">{{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 = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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 (medical)|hypoxia]].<ref name="entrez" />
{{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.<ref name="entrez">{{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 = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
SIAH2 has been shown to [[Protein-protein interaction|interact]] with [[PEG10]],<ref name=pmid12810624>{{cite journal | vauthors = Okabe H, Satoh S, Furukawa Y, Kato T, Hasegawa S, Nakajima Y, Yamaoka Y, Nakamura Y | title = Involvement of PEG10 in human hepatocellular carcinogenesis through interaction with SIAH1 | journal = Cancer Research | volume = 63 | issue = 12 | pages = 3043–8 | date = June 2003 | pmid = 12810624 }}</ref> [[Synaptophysin]],<ref name=pmid11786535>{{cite journal | vauthors = Wheeler TC, Chin LS, Li Y, Roudabush FL, Li L | title = Regulation of synaptophysin degradation by mammalian homologues of seven in absentia | journal = The Journal of Biological Chemistry | volume = 277 | issue = 12 | pages = 10273–82 | date = March 2002 | pmid = 11786535 | doi = 10.1074/jbc.M107857200 }}</ref> [[PEG3]]<ref name=pmid10681424>{{cite journal | vauthors = Relaix F, Wei XJ, Li W, Pan J, Lin Y, Bowtell DD, Sassoon DA, Wu X | title = Pw1/Peg3 is a potential cell death mediator and cooperates with Siah1a in p53-mediated apoptosis | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 5 | pages = 2105–10 | date = February 2000 | pmid = 10681424 | pmc = 15761 | doi = 10.1073/pnas.040378897 }}</ref> and [[VAV1]].<ref name=pmid10207103>{{cite journal | vauthors = Germani A, Romero F, Houlard M, Camonis J, Gisselbrecht S, Fischer S, Varin-Blank N | title = hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling pathways | journal = Molecular and Cellular Biology | volume = 19 | issue = 5 | pages = 3798–807 | date = May 1999 | pmid = 10207103 | pmc = 84217 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = 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 | date = January 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
| citations =
* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Research | volume = 6 | issue = 9 | pages = 791–806 | date = September 1996 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
*{{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 | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | 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 | date = October 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{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 | vauthors = Hu G, Chung YL, Glover T, Valentine V, Look AT, Fearon ER | title = Characterization of human homologs of the Drosophila seven in absentia (sina) gene | journal = Genomics | volume = 46 | issue = 1 | pages = 103–11 | date = November 1997 | pmid = 9403064 | doi = 10.1006/geno.1997.4997 }}
*{{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 | vauthors = 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 = Molecular and Cellular Biology | volume = 19 | issue = 1 | pages = 724–32 | date = January 1999 | pmid = 9858595 | pmc = 83929 | 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 | vauthors = Germani A, Romero F, Houlard M, Camonis J, Gisselbrecht S, Fischer S, Varin-Blank N | title = hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling pathways | journal = Molecular and Cellular Biology | volume = 19 | issue = 5 | pages = 3798–807 | date = May 1999 | pmid = 10207103 | pmc = 84217 | 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 | vauthors = Relaix F, Wei XJ, Li W, Pan J, Lin Y, Bowtell DD, Sassoon DA, Wu X | title = Pw1/Peg3 is a potential cell death mediator and cooperates with Siah1a in p53-mediated apoptosis | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 5 | pages = 2105–10 | date = February 2000 | pmid = 10681424 | pmc = 15761 | doi = 10.1073/pnas.040378897 }}
*{{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 | vauthors = Joensuu T, Hämäläinen R, Lehesjoki AE, de la Chapelle A, Sankila EM | 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 | date = February 2000 | pmid = 10704288 | doi = 10.1006/geno.1999.6096 }}
*{{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 | vauthors = Matsuzawa SI, Reed JC | title = Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses | journal = Molecular Cell | volume = 7 | issue = 5 | pages = 915–26 | date = May 2001 | pmid = 11389839 | doi = 10.1016/S1097-2765(01)00242-8 }}
*{{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 | vauthors = Boehm J, He Y, Greiner A, Staudt L, Wirth T | title = Regulation of BOB.1/OBF.1 stability by SIAH | journal = The EMBO Journal | volume = 20 | issue = 15 | pages = 4153–62 | date = August 2001 | pmid = 11483518 | pmc = 149152 | doi = 10.1093/emboj/20.15.4153 }}
*{{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 | vauthors = Wheeler TC, Chin LS, Li Y, Roudabush FL, Li L | title = Regulation of synaptophysin degradation by mammalian homologues of seven in absentia | journal = The Journal of Biological Chemistry | volume = 277 | issue = 12 | pages = 10273–82 | date = March 2002 | pmid = 11786535 | doi = 10.1074/jbc.M107857200 }}
*{{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 | vauthors = 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 | title = NotI flanking sequences: a tool for gene discovery and verification of the human genome | journal = Nucleic Acids Research | volume = 30 | issue = 14 | pages = 3163–70 | date = July 2002 | pmid = 12136098 | pmc = 135748 | doi = 10.1093/nar/gkf428 }}
*{{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 | vauthors = Habelhah H, Frew IJ, Laine A, Janes PW, Relaix F, Sassoon D, Bowtell DD, Ronai Z | title = Stress-induced decrease in TRAF2 stability is mediated by Siah2 | journal = The EMBO Journal | volume = 21 | issue = 21 | pages = 5756–65 | date = November 2002 | pmid = 12411493 | pmc = 131073 | doi = 10.1093/emboj/cdf576 }}
*{{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 | vauthors = Okabe H, Satoh S, Furukawa Y, Kato T, Hasegawa S, Nakajima Y, Yamaoka Y, Nakamura Y | title = Involvement of PEG10 in human hepatocellular carcinogenesis through interaction with SIAH1 | journal = Cancer Research | volume = 63 | issue = 12 | pages = 3043–8 | date = June 2003 | pmid = 12810624 | doi =  }}
*{{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 | vauthors = Fanelli M, Fantozzi A, De Luca P, Caprodossi S, Matsuzawa S, Lazar MA, Pelicci PG, Minucci S | 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 = The Journal of Biological Chemistry | volume = 279 | issue = 7 | pages = 5374–9 | date = February 2004 | pmid = 14645235 | doi = 10.1074/jbc.M306407200 }}
*{{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 | vauthors = Germani A, Prabel A, Mourah S, Podgorniak MP, Di Carlo A, Ehrlich R, Gisselbrecht S, Varin-Blank N, Calvo F, Bruzzoni-Giovanelli H | title = SIAH-1 interacts with CtIP and promotes its degradation by the proteasome pathway | journal = Oncogene | volume = 22 | issue = 55 | pages = 8845–51 | date = December 2003 | pmid = 14654780 | doi = 10.1038/sj.onc.1206994 }}
*{{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 | vauthors = 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 | 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 | date = June 2004 | pmid = 15210114 | doi = 10.1016/j.cell.2004.06.001 }}
*{{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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Latest revision as of 06:20, 11 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

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.[2]

Interactions

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

References

  1. ↑ 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.
  2. ↑ 2.0 2.1 "Entrez Gene: SIAH2 seven in absentia homolog 2 (Drosophila)".
  3. ↑ 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.
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ 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. PMC 84217. PMID 10207103.

Further reading

Retrieved from "https://www.wikidoc.org/index.php?title=SIAH2&oldid=1413061"