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Validated All-in-One™ qPCR Primer for UBE2I(NM_194259.3) Search again
Product ID:
HQP162536
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
C358B7.1, P18, UBC9
Gene Description:
ubiquitin conjugating enzyme E2 I
Target Gene Accession:
NM_194259.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. Four alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq].
Gene References into function
- Identification of a substrate recognition site on Ubc9.
- structure of the protein surfaces involved in UBC9 interaction with Sumo-1 and Smt3
- binding of proteins SALL1, UBE2I and SUMO-1
- SUMO-1 overexpression enhances and Ubc9 knockdown reduces levels of intranuclear Smad4, growth inhibitory response, as well as transcriptional responses to TGF-beta.
- interacts with Mason-Pfizer monkey virus Gag in cells. This strengthens the hypothesis that Gag proteins transiently associate with the nuclear compartment during viral replication, and suggest that hUbc9 plays a role in this process
- ubiquitin-conjugating enzyme E2I functions as a novel COUP-TFI corepressor, the function of which is distinct from its SUMO-1 conjugating enzyme activity.
- The interaction of Ubc9 with Daxx and subsequent alteration in the subcellular localization of Daxx may contribute to the increased sensitivity to anticancer drugs in the cells expressing Ubc9-DN.
- It is revealed with an in vitro SUMO-1 and Ad4BP/SF-1 that DNA binding activity and interaction with Sox9 are unaffected.
- SUMO conjugation is a novel regulator of Elk-1 function through the control of its nuclear-cytoplasmic shuttling.
- Ubc9 has a role in inhibition of diadenosine triphosphate hydrolase activity of the putative tumor suppressor protein Fhit
- Ubc9- small ubiquitin-like modifier (SUMO-1) thioester could be recruited to RanBP2 via SUMO-1 in the absence of strong binding between Ubc9 and RanBP2
- data support a physiological role of Ubc9 and PIAS1 as transcriptional coactivators in COUP-TFI-mediated CYP11B2 transcription
- specific interactions of SUMO-3 with its modifying enzyme, UBC9.
- these results suggest a role for Ubc9 in tumorigenesis at least partially through regulation of bcl-2 expression.
- p14ARF acts through a common modification of diverse binding partners, including Ubc9
- OZF interacts with UBC9, the E2 enzyme involved in the covalent conjugation of the small ubiquitin-like modifier 1 (SUMO-1).
- Nup358/RanBP2 acts as an E3 by binding both SUMO and Ubc9 to position the SUMO-E2-thioester in an optimal orientation to enhance conjugation
- Findings suggest that the interaction of small ubiquitin-like modifier 1 with N-terminus of ataxin-3 first and the relevant sumoylation probably participate in the post-translation modifying of ataxin-3 and in the pathogenesis of SCA3/MJD.
- Thus, we did not find evidence for uniquely interacting partner proteins using this approach, but did identify four new lamin A/C interactive partners
- SUMO-1 controls the protein stability and the biological function of phosducin.
- In targeting RanGAP1 to nuclear pore complexes, Ubc9 conjugates SUMO to RanGAP1, and is also required to form a stable ternary complex with SUMO-1 modified RanGAP1 and Nup358.
- Results suggest that Ubc9 might regulate bcl-2 expression through the ER signaling pathway, which ultimately contributes to the alterations of drug responsiveness and tumor growth.
- It shows that Ubc9 interacts with SOX4 and represses its transcriptional activity independent of its SUMO-1-conjugating activity.
- This is the first report demonstrating the interaction of hUbc9 with a structural protein of plus-strand RNA viruses, indicating a new drug target for SARS-CoV.
- results indicate that Ubc9 influences herpesvirus 6 immediate-early 2 protein function and provide new information on the complex interactions that occur between herpesviruses and the sumoylation pathway
- the nucleocapsid protein of severe acute respiratory syndrome coronavirus is sumoylated by interaction with Ubc9
- Ubc9 has a role as a transcriptional MR coactivator, beyond the known SUMO E2-conjugating enzyme
- Expressed at high levels in melanoma-positive lymph nodes; plays a crucial role in preventing advanced-stage melanomas from undergoing chemotherapy-induced apoptosis.
- We show here that TRPS1 is SUMOylated at multiple sites, both in vivo and in vitro, through interaction with UBC9. Overexpression of wild-type UBC9 enhances TRPS1-mediated transcriptional repression.
- analysis of SUMO-Ubc9 interaction
- Ubc9 is an important C/EBPalphap30 target through which C/EBPalphap30 enhances the sumoylation of C/EBPalphap42 to inhibit granulocytic differentiation.
- RAP80 interacts with the SUMO-conjugating enzyme UBC9 and is a novel target for sumoylation
- RSUME increases noncovalent binding of SUMO-1 to Ubc9 and enhances Ubc9 thioester formation and SUMO polymerization.
- Both SUMO E2 conjugating enzyme Ubc9 and E3 ligase protein inhibitor of activated STAT3 (Pias3) are targets for S-nitrosation
- MEL-18 bound to HSF2 inhibits its sumoylation by binding to and inhibiting the activity of UBC9 enzymes in the vicinity of HSF2.
- Data show that the nuclear accumulation of Smad1 and Smad4 are inhibited by Ubc9 silencing, and thus Ubc9 plays an important role in the up-regulation of the bone morphogenetic protein signaling pathway.
- These data suggests that Ubc9 can function as a co-factor of PLAGL2, uncoupling from its enzymatic activity, to mediate PLAGL2 interactive SP-C promoter activity.
- The crystal structure of sumoylated Ubc9 demonstrates how the newly created binding interface can provide a gain in affinity otherwise provided by E3 ligases.