Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Smt3, a homolog of small ubiquitin-like modifier (sumo), is a non-canonical RIDD target in Drosophila S2 cells. Unlike other RIDD targets, the sumo transcript does not stably associate with the ER membrane
SUMO conjugation is required for the assembly of Su(Hw) and Mod(mdg4) into insulator bodies that facilitate insulator complex formation.
although knockdown of the homeodomain-interacting protein kinase (show CDK7 Proteins) (Hipk) suppresses Smt3 depletion-induced activation of JNK (show MAPK8 Proteins), Hipk overexpression synergistically enhances this type of JNK (show MAPK8 Proteins) activation
modification of septins by the Smt3 conjugation system
Ulp1 may prevent proteins from leaving the nucleus with SUMO still attached.
Sumoylation by SUMO stimulates Vestigial protein function during wing morphogenesis.
Smt3 is required for the ecdysteroid synthesis pathway at the time of puparium formation.
A genome-wide RNA interference screen in Drosophila melanogaster cells for components regulating and mediating SUMO-dependent transcriptional repression.
Drosophila p53 modification by SUMO modulates its transactivation and pro-apoptotic functions
SUMO coordinates multiple regulatory processes during oogenesis and early embryogenesis
Study found expression of several mutated forms of SOD1 (show SOD1 Proteins) in the NSC-34 motor neuronal cells induces the formation of cytosolic and sometimes nuclear aggregates containing the SUMO-1 protein and showed that the formation of these aggregates can be modulated by action on the K75 (show KRT75 Proteins) SUMOylation site
The LKB1 (show STK11 Proteins) K178R SUMO mutant had defective AMPK (show PRKAA1 Proteins) signaling and mitochondrial function, inducing death in energy-deprived cells.
These findings point to a significant contribution of SUMO1 modification on neuronal function which may have implications for mechanisms involved in mental retardation and neurodegeneration.
PML (show PML Proteins) IV/ARF interaction enhances p53 (show TP53 Proteins) SUMO-1 conjugation, activation, and senescence.
SUMO1 accelerates the accumulation of autophagic vacuoles and promotes Abeta (show APP Proteins) production.
The present study used immunohistochemical and immunoblot analysis with the different developmental stages of mice and demonstrated the developmentally regulated distribution of SUMO1.
The results of this study indicate that post-translational modifications of SERCA2a (show ATP2A2 Proteins) caused by the toxic environment of the hypertrophied and failing myocardium can be prevented by SUMO-1.
SUMO-1 plays crucial roles for spindle organization, chromosome congression, and chromosome segregation during mouse oocyte meiotic maturation.
Results indicate that a functional SUMO1-3 expression is essential for emotionality and cognition
Adult mice showed proportionately greater increases in SUMO-1 than the aged group.
SUMO and p21Cip1 (show CDKN1A Proteins) regulate the transit of proteins through the nucleolus; disruption of nucleolar export by DNA damage induces SUMO and p21Cip1 (show CDKN1A Proteins) to act as hub proteins to form a multiprotein complex in the nucleolus.
This study reveals an essential role of SUMOylated FADD (show FADD Proteins) in Drp1 (show CRMP1 Proteins)- and caspase-10 (show CASP10 Proteins)-dependent necrosis.
SUMO-1 gene silencing inhibits proliferation and promotes apoptosis of human gastric cancer cells.
the critical role of Cys52 in maintaining SUMO-1 conformation and function
Findings suggest SUMO-1 protein and PGE2 receptor subtype 4 (EP4 (show PTGER4 Proteins)) as two potential targets for new therapeutic or prevention strategies for endometrial cancers.
This study demonstrated that the rs12472035 polymorphism of SUMO1 was significantly associated with an increased risk of AD in male group.
FOXP2 (show FOXP2 Proteins) can be modified with all three human SUMO proteins and that PIAS1 (show PIAS1 Proteins) promotes this process.
Ang II (show AGT Proteins)-induced upregulation of ATF3 (show ATF3 Proteins) and SUMO1 in vitro and in vivo was blocked by Ang II (show AGT Proteins) type I receptor antagonist olmesartan. Moreover, Ang II (show AGT Proteins) induced ATF3 (show ATF3 Proteins) SUMOylation at lysine 42, which is SUMO1 dependent.
Data show that mutation of key residues in the binding site abolishes binding and that small ubiquitin-like modifier 1 (SUMO1) can simultaneously and non-cooperatively bind both the ZZ domain and a canonical SIM (show SIM2 Proteins) motif of CREB-binding protein (CBP/p300 (show CREBBP Proteins)).
Roles for SUMO in pre-mRNA processing (show PRPF39 Proteins)
we provide evidence for the existence of a preferential conjugation of AtSUMO1/2 compared with AtSUMO3/5, which is determined by a role of the E1-activating enzyme in SUMO paralogue discrimination.
SUMO1 becomes conjugated with ubiquitin during heat stress, showing posttranslational modifications.
SUM3 (show SUMO3 Proteins) promotes plant defense downstream of salicylic acid, while SUM1 and SUM2 (show SUMO2 Proteins) together prevent salicylic acid accumulation in noninfected plants.
SIZ1-mediated conjugation of SUMO1 and SUMO2 (show SUMO2 Proteins) to other intracellular proteins is essential in Arabidopsis, possibly through stress-induced modification of a potentially diverse pool of nuclear proteins.
results support the critical role of SUMO-1 in SERCA2a (show ATP2A2 Proteins) function and underline the therapeutic potential of SUMO-1 for HF patients
Analysis of protein interactions showed that K179A, K180A, and K221A substitutions of classical swine fever virus core protein disrupt core-SUMO-1 binding, while K220A substitution precludes core-UBC9 (show UBE2I Proteins) binding.
The gene knockout technique is important in xenotransplantation research; here we have described the molecular cloning of SUMO-1 gene that may be a candidates to overcome the poor rate of homologous recombination.
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.
, lethal (2) SH0182
, small Ubiquitin-like modifier
, SMT3 suppressor of mif two 3 homolog 1 (S. cerevisiae)
, small ubiquitin-related modifier 1
, SMT3 suppressor of mif two 3-like 1
, small ubiquitin-related protein 1
, smt3 suppressor of mif two 3 homolog 1
, death-associated protein 1
, PSD-95/SAP90-binding protein 1
, SAP90/PSD-95-associated protein 1
, disks large-associated protein 1
, guanylate kinase associated protein
, guanylate kinase-associated protein
, GAP modifying protein 1
, SMT3 homolog 3
, SMT3 suppressor of mif two 3 homolog 1
, ubiquitin-homology domain protein PIC1
, ubiquitin-like protein SMT3C
, ubiquitin-like protein UBL1
, small ubiquitin-related modifier-1
, ubiquitin-like 1 (sentrin)
, small ubiquitin-like modifier 1
, SUMO-1 related peptidase
, ubiquitin-like 1
, Small ubiquitin-related modifier 1