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SIAH2 (seven in absentia homolog 2 (Drosophila))

Written2011-01Jianfei Qi, Ze'ev Ronai
Signal Transduction Program, Sanford-Burnham Medical Research Institute, La Jolla, CA, 92037, USA

(Note : for Links provided by Atlas : click)

Identity

Alias_namesseven in absentia (Drosophila) homolog 2
seven in absentia homolog 2 (Drosophila)
Other aliashSiah2
HGNC (Hugo) SIAH2
LocusID (NCBI) 6478
Atlas_Id 46199
Location 3q25.1  [Link to chromosome band 3q25]
Location_base_pair Starts at 150741123 and ends at 150763476 bp from pter ( according to hg19-Feb_2009)  [Mapping SIAH2.png]
Fusion genes
(updated 2016)
RPLP1 (15q23) / SIAH2 (3q25.1)SIAH2 (3q25.1) / CFAP97 (4q35.1)SIAH2 (3q25.1) / SIAH2 (3q25.1)

DNA/RNA

 
  Genomic organization of human Siah2. The line indicates intron and boxes indicate coding regions (exon 1-2) of the gene. Exon and intron lengths, the ATG transcription start site and the TGA stop codon are indicated.
Description The human Siah2 gene is composed of 2 exons spanning a genomic region of about 22.4 Kb.
Transcription The transcript length of human Siah2 is 2632 bp. The open reading frame of the coding region is 975 bp.
Pseudogene No pseudogene of Siah2 has been reported.

Protein

 
  Domains of human Siah2 protein.
Description Human Siah2 protein consists of 324 amino acids, with a molecular weight of 36 KDa. Siah protein consists of an N-terminal ring domain, followed by two zinc finger motifs, and a C-terminal substrate binding domain (SBD). The ring domain is the catalytic domain that recruits E2 ubiquitin-conjugating enzymes, while the SBD mediates the binding of adaptor proteins or some Siah substrate proteins. The structure of murine Siah1a SBD has been solved. The structure reveals that Siah is a dimeric protein, and the SBD adopts an eight-stranded beta-sandwich fold (Polekhina et al., 2001). The substrate binding groove is formed by the beta-sandwich fold and the beta-strand that connects to the second zinc finger domain (House et al., 2005).
Expression Siah2 mRNA is widely expressed in the embryonic and adult mouse tissues. It is expressed at a higher level in the olfactory epithelium, retina, forebrain and proliferating cartilage of developing bone (Della et al., 1993). Siah2 mRNA is also expressed in most human tissues (Hu et al., 1997).
Localisation Siah protein can be localized in both cytoplasm and nucleus.
Function Siah2 is the mammalian homolog of Drosophila SINA (seven in absentia), which interacts with transcriptional repressor Tramtrack via adaptor protein PHYL (Phyllopod) and induces the proteasomal degradation of Tramtrack, thereby determining R7 cell fate (Li et al., 1997; Tang et al., 1997). As a ring-finger E3 ubiquitin ligase, Siah targets the degradation of diverse substrates via ubiquitin-proteasome pathway, and affects multiple signaling pathways such as HIF (Nakayama et al., 2004), Ras (Nadeau et al., 2007; Schmidt et al., 2007), NF-kB (Polekhina et al., 2002; Habelhah et al., 2002), and beta-catenin (Liu et al., 2001; Matsuzawa and Reed, 2001). Siah2 transcription is upregulated by hypoxia (Nakayama et al., 2004); p38-mediated phosphorylation of mouse Siah2 on Thr24 and Ser29 alters its subcellular localization (Khurana et al., 2006); HIPK2-mediated phosphorylation of human Siah2 on Thr 26, Ser 28 and Ser 68 decreases the stability of Siah2 and impairs its interaction with HIPK2 (Calzado et al., 2009).
Over 20 Siah substrates have been reported (Nakayama et al., 2009) and some of them can be degradated by Siah2, Siah1 or both of them. In contrast to Siah1a knockout mice which exibit growth retardation and spermatogenesis defect, Siah2 knockout mice display no apparent phenotype, whereas Siah2 and Siah1a double knockout mice are embryonic or neonatal lethal, suggesting that the two Siah homologs have both overlapping and distinct functions in vivo (Frew et al., 2003). Despite the diverse substrates of Siah identified in vitro, loss of Siah2 (or both Siah2 and Siah1a) in vivo largely has no effect on the levels of many Siah substrates and the physiological processes associated with these substrates (Frew et al., 2002; Frew et al., 2003).
Siah2 is implicated in the regulation of hypoxia response through its effect on HIF prolyl hydroxylases or HIPK2 (Nakayama et al., 2004; Calzado et al., 2009). Siah2 knockout mice subject to hypoxia showed impaired respiratory response and defect to adjust levels of red blood cells (Nakayama et al., 2004). Siah2 has been shown to be required for development and progression of several types of cancers via its regulation of HIF or Ras pathways (House et al., 2009). Siah2-dependent degradation of Pard3A is found to control germinal zone exit of neuronal progenitors or immature neurons in mice (Famulski et al., 2010).
Homology Homologs: Human has two Siah genes (Siah1 and Siah2) (Hu et al., 1997), while mouse has three Siah genes (Siah2, Siah1a, Siah1b) (Della et al., 1993). Human Siah2 shares 77% identity with human Siah1 (Hu et al., 1997).
Orthologs: Highly conserved Siah2 orthologs have been identified in all multicellular organisms examined (Nakayama et al., 2009).

Mutations

Note No SIAH2 mutations have been reported.

Implicated in

Note
  
Entity Lung cancer
Note Ahmed et al. showed that Siah2 knockdown in human lung cancer cell lines (BZR, A549, H727, and UMC11) inhibited MAPK-ERK signaling, reduced cell proliferation and increased apoptosis; Siah2 knockdown also reduced anchorage-independent growth of A549 cells in soft agar, and blocked the growth of A549 xenograft tumors in nude mice (Ahmed et al., 2007).
  
  
Entity Melanoma
Note Qi et al. showed that inhibition of Siah2 activity using different inhibitory proteins blocked tumor formation or metastasis of SW1 melanoma cells in a syngeneic mouse model due to the inhibition of Ras and HIF pathways, respectively (Qi et al., 2008). Similary, Shah et al. showed that a putative chemical inhibitor of Siah2, menadione, decreased the levels of HIF-1alpha and phospho-ERK in human melanoma cell line UACC903 and abolished the growth of xenograft tumor in nude mice (Shah et al., 2009).
  
  
Entity Breast cancer
Note Möller et al. showed that inhibition of Siah in a mouse breast cancer cell line reduced the xenograft tumor growth and prolonged the survival of mice due to inhibition of HIF pathway (Möller et al., 2009). Behling et al. examined the SIAH staining in 65 patients of ductal carcinoma in situ (DCIS). Higher level of Siah staining was observed in tumors compared with the normal adjacent tissues, and in tumors with more aggressive features. There was also higher Siah staining in specimens from patients with recurrence as compared to patients without recurrence. This study stuggests that Siah may serve as a prognostic biomarker that predicts DCIS progression to invasive breast cancer (Behling et al., 2010).
  
  
Entity Pancreatic cancer
Note Schmidt et al. showed that inhibition of Siah activity attenuated MAPK-ERK signaling, blocked RAS-induced focus formation in fibroblasts, abolished anchorage-independent growth of human pancreatic cancer cells in soft agar and xenograft tumor growth in nude mice (Schmidt et al., 2008).
  
  
Entity Prostate cancer
Note Qi et al. showed that knockout of Siah2 in the TRAMP model abolished the formation of prostate neuroendocrine tumor, inhibition of Siah2 activity blocked hypoxia-induced neuroendocrine differentiation (NED) in prostate cancer cells or in the xenogaft tumors, and Siah2 protein levels were higher in high-grade PCa that expresss NE markers. This study suggests that Siah2 plays a key role in development of prostate NE tumor and NED of human PCa by controling a cooperation between HIF and NE-specific transcription factor FoxA2 (Qi et al., 2010).
  

Breakpoints

Note There is no breakpoint reported.

Bibliography

Effect of disrupting seven-in-absentia homolog 2 function on lung cancer cell growth.
Ahmed AU, Schmidt RL, Park CH, Reed NR, Hesse SE, Thomas CF, Molina JR, Deschamps C, Yang P, Aubry MC, Tang AH.
J Natl Cancer Inst. 2008 Nov 19;100(22):1606-29. Epub 2008 Nov 11.
PMID 19001609
 
Increased SIAH expression predicts ductal carcinoma in situ (DCIS) progression to invasive carcinoma.
Behling KC, Tang A, Freydin B, Chervoneva I, Kadakia S, Schwartz GF, Rui H, Witkiewicz AK.
Breast Cancer Res Treat. 2010 Nov 19. [Epub ahead of print]
PMID 21088888
 
An inducible autoregulatory loop between HIPK2 and Siah2 at the apex of the hypoxic response.
Calzado MA, de la Vega L, Moller A, Bowtell DD, Schmitz ML.
Nat Cell Biol. 2009 Jan;11(1):85-91. Epub 2008 Nov 30.
PMID 19043406
 
Isolation and characterisation of murine homologues of the Drosophila seven in absentia gene (sina).
Della NG, Senior PV, Bowtell DD.
Oncotarget. 2010 Sep 24;1(5):379-385.
PMID 8404535
 
Siah regulation of Pard3A controls neuronal cell adhesion during germinal zone exit.
Famulski JK, Trivedi N, Howell D, Yang Y, Tong Y, Gilbertson R, Solecki DJ.
Science. 2010 Dec 24;330(6012):1834-8. Epub 2010 Nov 25.
PMID 21109632
 
Normal p53 function in primary cells deficient for Siah genes.
Frew IJ, Dickins RA, Cuddihy AR, Del Rosario M, Reinhard C, O'Connell MJ, Bowtell DD.
Mol Cell Biol. 2002 Dec;22(23):8155-64.
PMID 12417719
 
Generation and analysis of Siah2 mutant mice.
Frew IJ, Hammond VE, Dickins RA, Quinn JM, Walkley CR, Sims NA, Schnall R, Della NG, Holloway AJ, Digby MR, Janes PW, Tarlinton DM, Purton LE, Gillespie MT, Bowtell DD.
Mol Cell Biol. 2003 Dec;23(24):9150-61.
PMID 14645526
 
Stress-induced decrease in TRAF2 stability is mediated by Siah2.
Habelhah H, Frew IJ, Laine A, Janes PW, Relaix F, Sassoon D, Bowtell DD, Ronai Z.
EMBO J. 2002 Nov 1;21(21):5756-65.
PMID 12411493
 
Elucidation of the substrate binding site of Siah ubiquitin ligase.
House CM, Hancock NC, Moller A, Cromer BA, Fedorov V, Bowtell DD, Parker MW, Polekhina G.
Structure. 2006 Apr;14(4):695-701.
PMID 16615911
 
Siah proteins: novel drug targets in the Ras and hypoxia pathways.
House CM, Moller A, Bowtell DD.
Cancer Res. 2009 Dec 1;69(23):8835-8. Epub 2009 Nov 17. (REVIEW)
PMID 19920190
 
Characterization of human homologs of the Drosophila seven in absentia (sina) gene.
Hu G, Chung YL, Glover T, Valentine V, Look AT, Fearon ER.
Genomics. 1997 Nov 15;46(1):103-11.
PMID 9403064
 
Regulation of the ring finger E3 ligase Siah2 by p38 MAPK.
Khurana A, Nakayama K, Williams S, Davis RJ, Mustelin T, Ronai Z.
J Biol Chem. 2006 Nov 17;281(46):35316-26. Epub 2006 Sep 25.
PMID 17003045
 
Photoreceptor cell differentiation requires regulated proteolysis of the transcriptional repressor Tramtrack.
Li S, Li Y, Carthew RW, Lai ZC.
Cell. 1997 Aug 8;90(3):469-78.
PMID 9267027
 
Siah-1 mediates a novel beta-catenin degradation pathway linking p53 to the adenomatous polyposis coli protein.
Liu J, Stevens J, Rote CA, Yost HJ, Hu Y, Neufeld KL, White RL, Matsunami N.
Mol Cell. 2001 May;7(5):927-36.
PMID 11389840
 
Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses.
Matsuzawa SI, Reed JC.
Mol Cell. 2001 May;7(5):915-26.
PMID 11389839
 
Inhibition of Siah ubiquitin ligase function.
Moller A, House CM, Wong CS, Scanlon DB, Liu MC, Ronai Z, Bowtell DD.
Oncogene. 2009 Jan 15;28(2):289-96. Epub 2008 Oct 13.
PMID 18850011
 
Regulation of Sprouty2 stability by mammalian Seven-in-Absentia homolog 2.
Nadeau RJ, Toher JL, Yang X, Kovalenko D, Friesel R.
J Cell Biochem. 2007 Jan 1;100(1):151-60.
PMID 16888801
 
The ubiquitin ligase Siah2 and the hypoxia response.
Nakayama K, Qi J, Ronai Z.
Mol Cancer Res. 2009 Apr;7(4):443-51. (REVIEW)
PMID 19372575
 
Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-alpha signaling.
Polekhina G, House CM, Traficante N, Mackay JP, Relaix F, Sassoon DA, Parker MW, Bowtell DD.
Nat Struct Biol. 2002 Jan;9(1):68-75.
PMID 11742346
 
Siah2-dependent concerted activity of HIF and FoxA2 regulates formation of neuroendocrine phenotype and neuroendocrine prostate tumors.
Qi J, Nakayama K, Cardiff RD, Borowsky AD, Kaul K, Williams R, Krajewski S, Mercola D, Carpenter PM, Bowtell D, Ronai ZA.
Cancer Cell. 2010 Jul 13;18(1):23-38.
PMID 20609350
 
Inhibition of RAS-mediated transformation and tumorigenesis by targeting the downstream E3 ubiquitin ligase seven in absentia homologue.
Schmidt RL, Park CH, Ahmed AU, Gundelach JH, Reed NR, Cheng S, Knudsen BE, Tang AH.
Cancer Res. 2007 Dec 15;67(24):11798-810.
PMID 18089810
 
Inhibition of Siah2 ubiquitin ligase by vitamin K3 (menadione) attenuates hypoxia and MAPK signaling and blocks melanoma tumorigenesis.
Shah M, Stebbins JL, Dewing A, Qi J, Pellecchia M, Ronai ZA.
Pigment Cell Melanoma Res. 2009 Dec;22(6):799-808. Epub 2009 Aug 27.
PMID 19712206
 
PHYL acts to down-regulate TTK88, a transcriptional repressor of neuronal cell fates, by a SINA-dependent mechanism.
Tang AH, Neufeld TP, Kwan E, Rubin GM.
Cell. 1997 Aug 8;90(3):459-67.
PMID 9267026
 

Citation

This paper should be referenced as such :
Qi, J ; Ronai, Z
SIAH2 (seven in absentia homolog 2 (Drosophila))
Atlas Genet Cytogenet Oncol Haematol. 2011;15(8):677-680.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/SIAH2ID46199ch3q25.html


External links

Nomenclature
HGNC (Hugo)SIAH2   10858
Cards
AtlasSIAH2ID46199ch3q25
Entrez_Gene (NCBI)SIAH2  6478  siah E3 ubiquitin protein ligase 2
AliaseshSiah2
GeneCards (Weizmann)SIAH2
Ensembl hg19 (Hinxton)ENSG00000181788 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000181788 [Gene_View]  chr3:150741123-150763476 [Contig_View]  SIAH2 [Vega]
ICGC DataPortalENSG00000181788
TCGA cBioPortalSIAH2
AceView (NCBI)SIAH2
Genatlas (Paris)SIAH2
WikiGenes6478
SOURCE (Princeton)SIAH2
Genetics Home Reference (NIH)SIAH2
Genomic and cartography
GoldenPath hg38 (UCSC)SIAH2  -     chr3:150741123-150763476 -  3q25.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)SIAH2  -     3q25.1   [Description]    (hg19-Feb_2009)
EnsemblSIAH2 - 3q25.1 [CytoView hg19]  SIAH2 - 3q25.1 [CytoView hg38]
Mapping of homologs : NCBISIAH2 [Mapview hg19]  SIAH2 [Mapview hg38]
OMIM602213   
Gene and transcription
Genbank (Entrez)AK055290 AK223565 AW377592 BC013082 BF514387
RefSeq transcript (Entrez)NM_005067
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)SIAH2
Cluster EST : UnigeneHs.692394 [ NCBI ]
CGAP (NCI)Hs.692394
Alternative Splicing GalleryENSG00000181788
Gene ExpressionSIAH2 [ NCBI-GEO ]   SIAH2 [ EBI - ARRAY_EXPRESS ]   SIAH2 [ SEEK ]   SIAH2 [ MEM ]
Gene Expression Viewer (FireBrowse)SIAH2 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)6478
GTEX Portal (Tissue expression)SIAH2
Protein : pattern, domain, 3D structure
UniProt/SwissProtO43255   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtO43255  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProO43255
Splice isoforms : SwissVarO43255
Catalytic activity : Enzyme2.3.2.27 [ Enzyme-Expasy ]   2.3.2.272.3.2.27 [ IntEnz-EBI ]   2.3.2.27 [ BRENDA ]   2.3.2.27 [ KEGG ]   
PhosPhoSitePlusO43255
Domaine pattern : Prosite (Expaxy)ZF_RING_2 (PS50089)    ZF_SIAH (PS51081)   
Domains : Interpro (EBI)7-in-absentia-prot_TRAF-dom    SIAH-type    SINA-like    TRAF-like    Znf_RING    Znf_RING/FYVE/PHD    Znf_SIAH   
Domain families : Pfam (Sanger)Sina (PF03145)   
Domain families : Pfam (NCBI)pfam03145   
Conserved Domain (NCBI)SIAH2
DMDM Disease mutations6478
Blocks (Seattle)SIAH2
PDB (SRS)5H9M   
PDB (PDBSum)5H9M   
PDB (IMB)5H9M   
PDB (RSDB)5H9M   
Structural Biology KnowledgeBase5H9M   
SCOP (Structural Classification of Proteins)5H9M   
CATH (Classification of proteins structures)5H9M   
SuperfamilyO43255
Human Protein AtlasENSG00000181788
Peptide AtlasO43255
HPRD03737
IPIIPI00305283   IPI00981863   IPI00946273   
Protein Interaction databases
DIP (DOE-UCLA)O43255
IntAct (EBI)O43255
FunCoupENSG00000181788
BioGRIDSIAH2
STRING (EMBL)SIAH2
ZODIACSIAH2
Ontologies - Pathways
QuickGOO43255
Ontology : AmiGOprotein polyubiquitination  transcription corepressor activity  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  protein binding  nucleoplasm  cytoplasm  early endosome  cytosol  cytosol  ubiquitin-dependent protein catabolic process  apoptotic process  cell cycle  small GTPase mediated signal transduction  axon guidance  zinc ion binding  protein deubiquitination  regulation of protein ubiquitination  ubiquitin conjugating enzyme binding  neuron projection  neuronal cell body  negative regulation of apoptotic process  negative regulation of cysteine-type endopeptidase activity involved in apoptotic process  intracellular membrane-bounded organelle  cellular protein catabolic process  cellular protein metabolic process  negative regulation of canonical Wnt signaling pathway  negative regulation of nucleic acid-templated transcription  negative regulation of extrinsic apoptotic signaling pathway  
Ontology : EGO-EBIprotein polyubiquitination  transcription corepressor activity  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  protein binding  nucleoplasm  cytoplasm  early endosome  cytosol  cytosol  ubiquitin-dependent protein catabolic process  apoptotic process  cell cycle  small GTPase mediated signal transduction  axon guidance  zinc ion binding  protein deubiquitination  regulation of protein ubiquitination  ubiquitin conjugating enzyme binding  neuron projection  neuronal cell body  negative regulation of apoptotic process  negative regulation of cysteine-type endopeptidase activity involved in apoptotic process  intracellular membrane-bounded organelle  cellular protein catabolic process  cellular protein metabolic process  negative regulation of canonical Wnt signaling pathway  negative regulation of nucleic acid-templated transcription  negative regulation of extrinsic apoptotic signaling pathway  
REACTOMEO43255 [protein]
REACTOME PathwaysR-HSA-983168 [pathway]   
NDEx NetworkSIAH2
Atlas of Cancer Signalling NetworkSIAH2
Wikipedia pathwaysSIAH2
Orthology - Evolution
OrthoDB6478
GeneTree (enSembl)ENSG00000181788
Phylogenetic Trees/Animal Genes : TreeFamSIAH2
HOVERGENO43255
HOGENOMO43255
Homologs : HomoloGeneSIAH2
Homology/Alignments : Family Browser (UCSC)SIAH2
Gene fusions - Rearrangements
Fusion : MitelmanSIAH2/CFAP97 [3q25.1/4q35.1]  
Fusion: TCGASIAH2 3q25.1 KIAA1430 BRCA
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerSIAH2 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)SIAH2
dbVarSIAH2
ClinVarSIAH2
1000_GenomesSIAH2 
Exome Variant ServerSIAH2
ExAC (Exome Aggregation Consortium)SIAH2 (select the gene name)
Genetic variants : HAPMAP6478
Genomic Variants (DGV)SIAH2 [DGVbeta]
DECIPHERSIAH2 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisSIAH2 
Mutations
ICGC Data PortalSIAH2 
TCGA Data PortalSIAH2 
Broad Tumor PortalSIAH2
OASIS PortalSIAH2 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICSIAH2  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDSIAH2
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch SIAH2
DgiDB (Drug Gene Interaction Database)SIAH2
DoCM (Curated mutations)SIAH2 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)SIAH2 (select a term)
intoGenSIAH2
NCG5 (London)SIAH2
Cancer3DSIAH2(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM602213   
Orphanet
MedgenSIAH2
Genetic Testing Registry SIAH2
NextProtO43255 [Medical]
TSGene6478
GENETestsSIAH2
Target ValidationSIAH2
Huge Navigator SIAH2 [HugePedia]
snp3D : Map Gene to Disease6478
BioCentury BCIQSIAH2
ClinGenSIAH2
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD6478
Chemical/Pharm GKB GenePA35760
Clinical trialSIAH2
Miscellaneous
canSAR (ICR)SIAH2 (select the gene name)
Probes
Litterature
PubMed91 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineSIAH2
EVEXSIAH2
GoPubMedSIAH2
iHOPSIAH2
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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