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Validated All-in-One™ qPCR Primer for SUMO1(NM_003352.4) Search again
Product ID:
HQP053990
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
DAP1, GMP1, OFC10, PIC1, SENP2, SMT3, SMT3C, SMT3H3, UBL1
Gene Description:
small ubiquitin like modifier 1
Target Gene Accession:
NM_003352.4(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.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
This gene encodes a protein that is a member of the SUMO (small ubiquitin-like modifier) protein family. It functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. However, unlike ubiquitin which targets proteins for degradation, this protein is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. It is not active until the last four amino acids of the carboxy-terminus have been cleaved off. Several pseudogenes have been reported for this gene. Alternate transcriptional splice variants encoding different isoforms have been characterized.
Gene References into function
- role in modulating nuclear receptor interaction domain of GRIP1
- post-translationally modifies glucocorticoid receptor in a ligand-enhanced fashion
- binding of proteins SALL1, UBE2I and SUMO-1
- p14ARF promotes accumulation of (H)Mdm2 conjugated to the small ubiquitin-like protein SUMO-1.
- role in modifying aryl hydrocarbon receptor nuclear transporter at Lys245
- SUMO1 has a role in PIASy-enhanced modification of C-EPB alpha
- Overexpression of SUMO-1 enhanced PR-mediated gene transcription even in the presence of non-sumoylated mutants of SRC-1.
- SUMO-1 has a role in modifying cAMP-response element-binding protein (CREB) in prolonged hypoxia
- examination of the role of the phosphorylation event in regulating SUMO-1 modification of HSF1
- HSF1 is modified by SUMO-1 and SUMO-2 in a stress-inducible manner.
- SRF is modified by SUMO-1 chiefly at lysine(147) within the DNA-binding domain.
- PIAS1 was found to strongly stimulate sumoylation of STAT1 at Lys703 by SUMO-1 conjugation to STAT1; results suggest a negative regulatory function for sumoylation.
- PIAS1 conjugates SUMO-1 to human mineralocorticoid receptor.
- Smad4 is covalently modified by SUMO-1 and facilitates Smad-dependent transcriptional activation
- PLZF colocalizes with SUMO-1 in the nucleus; lysine 242 in the RD2 domain of human PLZF was identified as the sumoylation site
- SENP1 localization is influenced by expression and localization of SUMO-1-conjugated target proteins within the cell.
- recruitment of SUMO-1 modified proteins into insoluble nuclear inclusions and proteasomal dysfunction may be involved in the pathogenesis neuronal intranuclear inclusion disease
- Dnmt3a interacts with multiple components of the sumoylation machinery, all of which are involved in conjugating the small ubiquitin-like modifier polypeptide, SUMO-1, to its target proteins
- SUMO-1 promotes histone deacetylase-mediated transcriptional repression.
- Regulates protein function by binding to diverse proteins within the cell.
- In interphase, a significant fraction of vertebrate SUMO1-modified RanGAP1 forms a stable complex with the nucleoporin RanBP2/Nup358 at nuclear pore complexes.
- These results suggest that the PPARgamma-dependent transactivation pathway seems to be modulated by SUMO-1 modification and may serve as a novel target for apoptosis-induction therapy in cancer cells.
- SUMO modification of Human Cytomegalovirus (HCMV) IE1-72 kDa contributes to efficient HCMV replication by promoting the accumulation of IE2-86 kDa.
- SUMO-1 conjugation at the Lys-19 residue is crucial for enhancing the transactivation activity of EBV Rta
- CENPC target sites that can be sumoylated by SUMO-2 were shown to be equally susceptible to SUMO-1 attachments which include specific sites on SUMO-2 itself, Ubc9, and the recombinant CENP-C fragments.
- GATA4 is a SUMO-1-targeted transcription factor and together with PIAS1 is a potent regulator of cardiac gene activity
- the RanGAP1 consensus sumoylation site and SUMO-1 C terminus are both conformationally flexible
- SUMO-1 shows patterns of utilization that are clearly discrete from the patterns of SUMO-2 and -3 throughout the cell cycle
- sumoylation is involved in negative regulation of the transactivating function of PPARgamma2
- reversible SUMO modification at hsTAF5 contributes to the dynamic regulation of TFIID promoter-binding activity in human cells
- structures of heterodimeric Sae1/Sae2-Mg.ATP and Sae1/Sae2-SUMO-1-Mg.ATP complexes
- SUMO1 represses transcriptional activity of SOX3.
- SUMO1 conjugation to the C-terminal K330 of thymine DNA glycosylase modulates the DNA binding function of the N terminus to induce dissociation of the glycosylase from the AP site while it leaves the catalytic properties of the enzyme unaffected.
- ERM is subject to SUMO modification and this post-translational modification causes inhibition of transcription-enhancing activity
- OZF interacts with UBC9, the E2 enzyme involved in the covalent conjugation of the small ubiquitin-like modifier 1 (SUMO-1). Conjugation of SUMO-1 to a Kruppel zinc finger motif.
- In cell culture experiments, we found that the nuclear and perinuclear accumulation of SUMO-1 aggregates could be induced in glioma cells by chemical inhibition of proteasomal protein degradation.
- sumoylation-deficient MDMX mutant undergoes normal ubiquitination and degradation by MDM2, normal nuclear translocation and degradation after DNA damage, and inhibits p53 with wild type efficiency
- Data show that sumoylated LRH-1 is exclusively localized in promyelocytic leukemia protein nuclear bodies, and that this association is a dynamic process regulated in part by 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
- HIPK2 effector function on JNK is modulated through dynamic SUMO-1 modification
- c-Fos/c-Jun AP-1 dimer activity is downregulated by SUMO-1, SUMO-2, and SUMO-3
- SUMO-1 modification of proteins appears to have an important role in EBV lytic replication
- The interaction of SUMO1 and ubiquitin pathways of post-translational protein modification are reported, including their localization and conjugation status during proteasome inhibition.
- these data suggest a novel role for sumoylation in regulating RNA-editing activity.
- Data show that Topors enhances the conjugation of the small ubiquitin-like modifier 1 (SUMO-1) to p53 in vivo and in a reconstituted in vitro system.
- presence of SUMO1 in non-pathological conditions, in a large promyelocytic leukemia-nuclear inclusion bodies in human supraoptic neurons
- our findings place SUMOylation target on the centrosome structure protein, hNinein, which results in the switch localization from centrosome to nucleus
- the SUMO binding motif forms an extended structure that binds between the alpha-helix and a beta-strand of SUMO-1
- Data suggest that testicular SUMO-1 has specific functions in heterochromatin organization, meiotic centromere function, and gene expression.
- NMR characterization of the urea-denatured state of SUMO-1
- SUMO-1 controls the protein stability and the biological function of phosducin.
- SUMO-1 controls the protein stability and the biological function of phosducin.
- SUMO1 polymeric chain assembles on human topoisomerase I in vitro
- findings show that Epstein-Barr virus Rta interacts and colocalizes with PIASxalpha and PIASxbeta in the nucleus; these interactions seem to enhance Rta sumoylation
- SUMO1 is involved in a modification of tau and alpha-synuclein that may also have implications for their pathogenic roles in neurodegenerative diseases
- SUMO has a biological role in enhancing the cytoplasmonuclear transport of its target protein Daxx
- association of SUMO modification of XRCC4 with the control of the repair and recombination associated with DNA breaks
- PML stimulated hSUMO-1 modification in yeast, in a manner that was dependent upon PML's RING-finger domain. PML:RARalpha also stimulated hSUMO-1 conjugation in yeast.
- Using yeast two-hybrid system, bioinformatics, and NMR spectroscopy we define a common SUMO-interacting motif (SIM) and map its binding surfaces on SUMO1 and SUMO2
- MEF2A undergoes sumoylation primarily at a single lysine residue (K395) both in vitro and in vivo.Our results suggest that protein sumoylation could play a pivotal role in controlling MEF2 transcriptional activity.
- SUMO-1 Sam68 fusion protein, on the other hand, inhibited the ability of Sam68 to induce apoptosis but was a strong repressor of cyclin D1 expression
- It shows that Ubc9 interacts with SOX4 and represses its transcriptional activity independent of its SUMO-1-conjugating activity.
- SUMOylation and activation of ataxia-telangiectasia-mutated protein, PKCdelta, caspase-3, and nuclear factor kappaB signaling pathways modulate salivary adaptive responses to stress in cells exposed to either 1% O(2) or DFO.
- A study evalution the mechanisms of regulation of the sumoylation pathway by the SUMO-specific proteases is presented.
- Myeloid elf-1-like factor (MEF) or Elf4 is modified by conjugation with SUMO-1/-2 (small ubiquitin-related modifier).
- role for SUMO1 in mammalian development; findings suggest that sumoylation regulates a network of genes that converge in palate development
- SUMO-1, PML and ZNF198 colocalize to punctate structures, shown by immunocytochemistry to be PML bodies.
- TDG sumoylation promotes intramolecular interactions with amino- and carboxy-terminal SUMO-1 binding motifs that dramatically alter the biochemical properties and subcellular localization of TDG
- sumoylation has a role in keratinocyte differentiation
- NMR characterization of the energy landscape of SUMO-1.
- The increased expression of SUMO-1 in rheumatoid arthritis (RA) synovial fibroblasts (SFs) contributes to the resistance of these cells against Fas-induced apoptosis through increased SUMOylation of nuclear PML protein.
- analysis of SUMO-Ubc9 interaction
- These results suggest that KyoT2 is a substrate of SUMO modification catalyzed by PIAS1, and that SUMOylation may modulate the transcriptional repression effect of KyoT2 on the Notch/RBP-J signaling pathway [Kyot2].
- overexpression of Mdm2 caused by overexpression of SUMO-1 may be involved in tumor aggressiveness even in patients with early stage oral squamous cell carcinoma
- SUMO-specific protease 1 transcription is induced by the androgen receptor in prostate cancer cells
- Topors enhances the formation of high-molecular weight SUMO-1 conjugates of TOP1 in a reconstituted in vitro system and also in human osteosarcoma cells
- Sumoylation negatively affects estrogen-related receptor-alpha and -gamma transcriptional activity through a synergy control motif.
- TRAF6 is modified by small ubiquitin-related modifier-1, interacts with histone deacetylase 1, and represses c-Myb-mediated transactivation.
- the transcription repressor function of RIP140 is modulated by SUMOylation
- SUMO1 participates in the modulation of ER-mediated CRH mRNA expression which may be important for the regulation of the stress response.
- SATB1 has a role in controlling transcription in immune cells during normal cell functions or in assisting in efficient and rapid clearance of nonfunctional or potentially damaging immune cells through its action with SUMO
- SUMO1 modification serves as a positive regulator for Nkx2.5 transcriptional activity
- We show that, during late pachynema, SUMO-1 appears on the constitutive heterochromatin, but is excluded from the XY body facultative heterochromatin.
- Our data suggest that SUMO-1 may be involved in maintenance and/or protection of the autosomal synaptonemal complex in men.
- unambiguously show that serine 2 of the endogenous SUMO-1 N-terminal protrusion is phosphorylated in vivo using very high mass accuracy mass spectrometry at both the MS and the MS/MS level and complementary fragmentation techniques
- Data show that SUMO-1-associated inclusion body proteins are immunocaptured using an anti-SUMO-1 antibody in the intranuclear inclusion bodies from brain tissue of a case with familial neuronal intranuclear inclusion disease.
- These data are the first to suggest a role for SUMO1 gene variation in human non-syndromic cleft lip with or without cleft palate development.
- CTCF protein can be posttranslationally modified by the small ubiquitin-like protein SUMO.
- RORalpha is SUMOylated by both SUMO-1 and SUMO-2.