Recombinant Human SIAH1 protein
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Recombinant Human SIAH1 protein is a Human Fragment protein, in the 90 to 282 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
HUMSIAH, SIAH1, E3 ubiquitin-protein ligase SIAH1, RING-type E3 ubiquitin transferase SIAH1, Seven in absentia homolog 1, Siah-1a, Siah-1
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human SIAH1 protein (AB131709)
15% SDS-PAGE showing ab131709 at approximately 24.1 kDa (3µg).
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human SIAH1 protein (AB131709)
ab131709 at 3 μg analysed by SDS PAGE.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
SIAH1 influences cell cycle control and apoptosis by interacting with components of protein complexes. It associates with the ubiquitin-proteasome pathway to mediate degradation of key regulatory proteins. SIAH1 helps in reducing cellular proliferation and enhances apoptotic signaling which are vital processes for maintaining balance between cell survival and death. As part of these processes studies have connected SIAH1 to modulating the fate of proteins involved in cell cycle arrest.
Pathways
Several interactions of SIAH1 contribute to signal transduction and apoptosis. One significant pathway involving SIAH1 is the p53 signaling pathway. SIAH1 regulates the degradation of proteins within this pathway including p21 and cyclin D1 which influence cellular responses to DNA damage. Additionally SIAH1 interacts with β-catenin linking it to the Wnt signaling pathway. This interaction affects the regulation of cell growth and differentiation.
Specifications
Form
Liquid
Additional notes
ab131709 is purified using conventional chromatography techniques
General info
Function
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed : 14506261, PubMed : 14645235, PubMed : 14654780, PubMed : 15064394, PubMed : 16085652, PubMed : 19224863, PubMed : 20508617, PubMed : 22483617, PubMed : 28546513, PubMed : 32430360, PubMed : 33591310, PubMed : 9334332, PubMed : 9858595). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed : 14506261, PubMed : 14645235, PubMed : 14654780, PubMed : 15064394, PubMed : 16085652, PubMed : 19224863, PubMed : 20508617, PubMed : 22483617, PubMed : 9334332, PubMed : 9858595). Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes (PubMed : 14506261, PubMed : 14645235, PubMed : 14654780, PubMed : 15064394, PubMed : 16085652, PubMed : 19224863, PubMed : 20508617, PubMed : 22483617, PubMed : 9334332, PubMed : 9858595). Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (ELL2, MYB, POU2AF1, PML and RBBP8), a cell surface receptor (DCC), the cell-surface receptor-type tyrosine kinase FLT3, the cytoplasmic signal transduction molecules (KLF10/TIEG1 and NUMB), an antiapoptotic protein (BAG1), a microtubule motor protein (KIF22), a protein involved in synaptic vesicle function in neurons (SYP), a structural protein (CTNNB1) and SNCAIP (PubMed : 10747903, PubMed : 11146551, PubMed : 11389839, PubMed : 11389840, PubMed : 11483517, PubMed : 11483518, PubMed : 11752454, PubMed : 12072443). Confers constitutive instability to HIPK2 through proteasomal degradation (PubMed : 18536714, PubMed : 33591310). It is thereby involved in many cellular processes such as apoptosis, tumor suppression, cell cycle, axon guidance, transcription regulation, spermatogenesis and TNF-alpha signaling (PubMed : 14506261, PubMed : 14645235, PubMed : 14654780, PubMed : 15064394, PubMed : 16085652, PubMed : 19224863, PubMed : 20508617, PubMed : 22483617, PubMed : 9334332, PubMed : 9858595). Has some overlapping function with SIAH2 (PubMed : 14506261, PubMed : 14645235, PubMed : 14654780, PubMed : 15064394, PubMed : 16085652, PubMed : 19224863, PubMed : 20508617, PubMed : 22483617, PubMed : 9334332, PubMed : 9858595). Induces apoptosis in cooperation with PEG3 (By similarity). Upon nitric oxid (NO) generation that follows apoptotic stimulation, interacts with S-nitrosylated GAPDH, mediating the translocation of GAPDH to the nucleus (By similarity). GAPDH acts as a stabilizer of SIAH1, facilitating the degradation of nuclear proteins (By similarity). Mediates ubiquitination and degradation of EGLN2 and EGLN3 in response to the unfolded protein response (UPR), leading to their degradation and subsequent stabilization of ATF4 (By similarity). Also part of the Wnt signaling pathway in which it mediates the Wnt-induced ubiquitin-mediated proteasomal degradation of AXIN1 (PubMed : 28546513, PubMed : 32430360).
Sequence similarities
Belongs to the SINA (Seven in absentia) family.
Post-translational modifications
Phosphorylated on Ser-19 by ATM and ATR. This phosphorylation disrupts SIAH1 interaction with HIPK2, and subsequent proteasomal degradation of HIPK2.
Subcellular localisation
Nucleus
Product protocols
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Target data
Product promise
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