Proteins SUMO1 , Human
- Known as:
- Proteins SUMO1 , Human
- Catalog number:
- C175
- Product Quantity:
- 10μg
- Category:
- -
- Supplier:
- Novoprotein
- Gene target:
- Proteins SUMO1 Human
Related genes to: Proteins SUMO1 , Human
- Gene:
- SUMO1 NIH gene
- Name:
- small ubiquitin like modifier 1
- Previous symbol:
- UBL1
- Synonyms:
- PIC1, GMP1, SMT3C, SUMO-1, SMT3H3, OFC10
- Chromosome:
- 2q33.1
- Locus Type:
- gene with protein product
- Date approved:
- 1996-06-04
- Date modifiied:
- 2019-02-18
Related products to: Proteins SUMO1 , Human
Related articles to: Proteins SUMO1 , Human
- Following the publication of the above paper, it was drawn to the Editor's attention by a concerned reader that certain of the western blot data shown in Fig. 1B on p. 1692 had already been submitted for publication to the journal in an article written by different authors at different research institutes. A subsequent analysis of the data in this paper undertaken by the Editorial Office revealed that, within the paper itself, some of the western blot data featured in Fig. 6C on p. 1695 were strikingly similar to those that were featured in Fig. 1B. Owing to the fact that the contentious data in the above article had already been submitted for publication prior to its submission to , the Editor has decided that this paper should be retracted from the Journal. The authors were asked for an explanation to account for these concerns, but the Editorial Office did not receive a reply. The Editor apologizes to the readership for any inconvenience caused. [Molecular Medicine Reports 17: 1690‑1698, 2018; DOI: 10.3892/mmr.2017.8037]. - Source: PubMed
Publication date: 2026/04/17
Hu JiaoliXue PengchengMao XinbangXie LinLi GuodongYou Zhipeng - The receptor tyrosine kinase EphB4 is frequently overexpressed in epithelial cancers, including prostate cancer (PCa). SUMOylation is a post-translational modification that influences protein interactions, localisation and stability. This study investigated how SUMOylation regulates EphB4 localisation, stability and function in PCa. - Source: PubMed
Publication date: 2026/04/15
Maharaj Mohanan Sada NandMertens-Walker IngaLisle Jessica EHerington AdrianStephens CarsonChai MelissaMeutermans WimStephenson Sally-Anne - Small ubiquitin-related modifiers (SUMOs) are covalently conjugated onto the proteome and serve as signaling molecules in many aspects of eukaryotic cell biology, from and to . The conjugatable SUMO variants, SUMO1 and the almost identical SUMO2 and SUMO3 (designated SUMO2/3), are processed by an E1(SAE1:SAE2)-E2(UBC9)-E3 enzyme cascade to produce SUMO-modified proteins. The prerogative of the SUMO biology field is to identify and study the specific proteins undergoing SUMOylation, which grants us insights into the biological pathway of interest. This protocol was developed using the human osteosarcoma cell line U2OS to enable the investigation of SUMO conjugates in mitosis, the cell division phase of the cell cycle. We enrich the cell population for mitotic cells, which are isolated and subjected to stringent lysis conditions involving a high concentration of SDS and DTT in RIPA buffer, to promote complete protein denaturation. The lysates in high SDS RIPA buffer are diluted to reduce the overall SDS concentration and undergo conventional immunoprecipitation using SUMO1- or SUMO2/3-specific antibodies bound to protein A/G agarose beads. The samples are then compatible with downstream readouts such as western blots and mass spectrometry. This protocol detects endogenous SUMOylated proteins and avoids exogenous SUMO overexpression, which can alter SUMO conjugate formation. Furthermore, this denaturing protocol ensures only SUMOylated proteins are immunoprecipitated, and not their interactors. Key features • Purifies endogenous SUMO-modified proteins by building on Becker et al. [1]. • Enriches and isolates cells in mitosis using nocodazole and mitotic shake-off. • 1% SDS RIPA lysis promotes robust denaturation ahead of SUMO-specific immunoprecipitation. • Compatible with downstream readouts such as western blots and mass spectrometry. - Source: PubMed
Publication date: 2026/04/05
Walker Alexandra KLanz Alexander JMorris Joanna R - Meiotic prophase-I chromosomes are organized into linear arrays of chromatin loops anchored to proteinaceous axes that define the interaction interfaces for the pairing and synapsis of homologous chromosomes. Chromatin loop size and axial chromosome length are inversely correlated and vary widely both between and within species, including between the sexes. The molecular basis of this variation remains unclear. Here, we provide evidence that the small ubiquitin-like modifier, SUMO, regulates loop-axis organization in mouse meiosis. Our analysis shows that the longer axes of oocyte chromosomes contain more SUMO per unit length than the shorter axes of spermatocyte chromosomes. In mouse models, the loss of SUMO1 results in shorter axes and longer chromatin loops. Conversely, increased SUMO1 conjugation, caused by mutation of the SENP1 isopeptidase, produces longer axes with shorter loops. Axis length positively correlates with meiotic recombination. Accordingly, and mutations respectively decrease and increase crossover frequency. These findings identify SUMO as a key regulator of meiotic chromosome architecture and suggest a molecular basis for the physiological variation in chromosome length and recombination rates seen among species, sexes, individuals, and individual meiocytes. - Source: PubMed
Publication date: 2026/03/11
Yun YanQiao HuanyuWhite MartinSandhu SumitQiu WendyBourne SarahDeshpande AnushaBhatt ShubhangSharma AjayBailey LoganTran HungVan BenRao H B D PrasadaHunter Neil - Protein post-translational modifications are crucial in driving cancer development and progression. The SUMO E3 ligase PIAS4 regulates various cellular processes, thereby promoting tumour advancement. However, the role of PIAS4 in breast cancer remains unclear. This study aimed to examine the protein levels of PIAS4 in clinical specimens, explore PIAS4 regulates cell cycle mechanism and investigate the synergistic inhibitory effects of PIAS4 and CDK6 inhibition on breast cancer progression. Our findings revealed that PIAS4 was highly expressed in breast cancer and negatively correlated with prognosis. Abrogation of PIAS4 inhibited breast cancer cell proliferation and induced G1 phase cell cycle delay. The primary mechanism involved PIAS4-mediated SUMOylation of CDK6, which enhanced retinoblastoma 1 (RB1) phosphorylation and the transcription of downstream cell cycle genes, facilitating cell cycle G1 phase progression. We found that CDK6 underwent SUMO1 and SUMO2/3 modifications and identified the main SUMO2/3 modification sites. Mutations at these sites inhibit CDK6-mediated RB1 phosphorylation, consequently blocking cell cycle progression in the G1 phase. CDK6 kinase activity is reduced following PIAS4 knockdown, which may be associated with decreased binding of Cyclin D1 to CDK6. Moreover, in mouse xenograft models, combining PIAS4 and CDK6 inhibition enhanced therapeutic efficacy against breast cancer. Therefore, targeting PIAS4 to impede cell cycle progression may be a novel strategy for breast cancer treatment. - Source: PubMed
Publication date: 2026/04/07
Chen HuiHu XinyangFeng LifengCheng XiaoqingZhu LiyuanXu FeiZhu TaoGao YongmeiWang JinJin HongchuanJiang Zhinong