USP11 antigen
- Known as:
- USP11 antigenic
- Catalog number:
- 'H00008237-Q01-10
- Product Quantity:
- 10
- Category:
- -
- Supplier:
- ACR
- Gene target:
- USP11 antigen
Related genes to: USP11 antigen
- Gene:
- USP11 NIH gene
- Name:
- ubiquitin specific peptidase 11
- Previous symbol:
- -
- Synonyms:
- UHX1
- Chromosome:
- Xp11.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-02-01
- Date modifiied:
- 2016-10-05
Related products to: USP11 antigen
'F 4_80 Antigen (mouse) Host Rat'F 4_80 Antigen (mouse) Host Rat(Anti_Tg)Thyroglobulin Antigen(Des-Asp187)-Melanocyte Protein PMEL 17 (185-193) (human, bovine, mouse)
(Des-Asp187)-ME20M_ME20S (185-193) (human, bovine, mouse), (Des-Asp187)-Melanocyte Lineage-Specific Antigen GP100 (185-193) (hu(Des-Asp187,Met186)-Melanocyte Protein PMEL 17 (185-193) (human, bovine, mouse)
(Des-Asp187,Met186)-Melanoma-Associated ME20 Antigen (185-193) (human, bovine, mouse), (Des-Asp187,Met186)-95 kDa Melano(Des_Asp187,Met186)_Melanocyte Protein PMEL 17 (185_193) (human, bovine, mouse) Salt Trifluoroacetate Binding _ Synonym (Des_Asp187,Met186)_Melanoma_Associated ME20 Antigen (185_193) (human, bovine(Des_Asp187,Met186)_Melanocyte Protein PMEL 17 (185_193) (human, bovine, mouse) Salt Trifluoroacetate Binding _ Synonym (Des_Asp187,Met186)_Melanoma_Associated ME20 Antigen (185_193) (human, bovine(Des_Asp187,Met186)_Melanocyte Protein PMEL 17 (185_193) (human, bovine, mouse) Salt Trifluoroacetate Binding _ Synonym (Des_Asp187,Met186)_Melanoma_Associated ME20 Antigen (185_193) (human, bovine(Des_Asp187,Met186)_Melanocyte Protein PMEL 17 (185_193) (human, bovine, mouse) Salt Trifluoroacetate Binding _ Synonym (Des_Asp187,Met186)_Melanoma_Associated ME20 Antigen (185_193) (human, bovine(Draxin) C1ORf187, Antigen blocking peptide(Val438)-Tyrosinase (432-444) (human)
(Val438)-LB24-AB (432-444) (human), (Val438)-Monophenol Monooxygenase (432-444) (human), (Val438)-SK29-AB (432-444) (human), (Val438)-Tumor Rejection Antigen AB (0x19 Antigen0x2 Antigen1,25-dihydroxyvitamin D3 Competitive ELISA, Coated with Antigen105 kDa islet cell antigen,BEM-3,Brain-enriched membrane-associated protein tyrosine phosphatase,ICA105,PTP IA-2,PTPLP,Ptprn,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase-like N,R-P Related articles to: USP11 antigen
- Pathological cardiac hypertrophy is a key precursor to heart failure. Protein ubiquitination and deubiquitination are crucial mechanisms controlling cardiomyocyte signaling homeostasis. USP11, a ubiquitin-specific protease, has been implicated in multiple cellular regulatory processes, but its cardiac function remains unknown. Here, we investigated whether USP11 modulates cardiac hypertrophy and explored its downstream molecular mechanisms. - Source: PubMed
Publication date: 2026/06/18
Wang XijiaZong WenzheZhou DiJi XiaoyangAn XiaogeLiu ZiheKong LingyaoWang YihuanFang YudongGao LuLi YueZheng ZheLiu GangqiongFan Siyuan - To explore the role and mechanism of X-linked USP11 in mitochondrial dysfunction associated with depression. - Source: PubMed
Feng YuqiLi NingyuanZhang LingfengWang WeiDuan HaoSun SiqiLi RuilingZhang YuhuiSong XinhuaZhang YingyueZhang HonghanNie ZhaowenYan HanchunWang ChaoLiu Zhongchun - To explore the regulatory role of SENP1 in ferroptosis of differentiated thyroid cancer cells and its molecular mechanism. - Source: PubMed
Zhu FeifeiYan NaYang JiwenChen XiaoleiWang Yingying - Rta and Zta are transcription factors expressed by Epstein-Barr virus (EBV) during the immediate-early stage of the lytic cycle. While these two proteins do not interact directly, they bind to a scaffold protein, RanBPM, to synergistically activate the transcription of EBV lytic genes. Earlier studies have shown that both Rta and Zta are destabilized through ubiquitination, which plays a crucial role in influencing EBV's lytic development. It is also known that Rta's ubiquitination is facilitated by the ubiquitin E3 ligase, RNF4. In this study, we show that RNF4 also promotes the ubiquitination of Zta. Meanwhile, a deubiquitinase, ubiquitin-specific protease (USP11), is known to interact with RanBPM. When tethered to RanBPM, Rta and Zta are deubiquitinated and stabilized by USP11. While host cells may utilize ubiquitination as a defense mechanism to destabilize Rta and Zta, thereby restricting EBV proliferation, EBV exploits RanBPM and the deubiquitination of Rta and Zta as a counter-defense strategy that favors EBV lytic replication. This study uncovers the interplay between the host and the viral mechanisms involving RNF4 and USP11 in modulating EBV lytic progression.IMPORTANCEEpstein-Barr virus (EBV) is known to express two crucial transcription factors, Rta and Zta, which are essential for activating the transcription of viral lytic genes. These two proteins are indispensable for viral lytic proliferation. While Rta and Zta can function independently to promote transcription, they also cooperate synergistically, leading to robust expression of EBV lytic proteins. In an earlier study, we showed that this synergy requires the formation of a complex involving Rta, Zta, and RanBPM at the Zta response elements in EBV lytic promoters. Recent studies showed that, despite their importance, these transcription factors are destabilized by ubiquitination, potentially serving as a mechanism through which the host restricts EBV proliferation. This study shows that EBV exploits USP11, which interacts with RanBPM, to deubiquitinate and stabilize Rta and Zta. The stabilization by USP11 is critical for EBV to overcome host-imposed restrictions and maximize its lytic proliferation. - Source: PubMed
Publication date: 2026/05/21
Chen Chi-YuanChen Po-ChunLu Yi-ShanLin Xin-RuYang Ya-ChunLee Yi-KaiCheng Zi-YunChang Shu-YinChiu Ya-FangChang Li-Kwan - The ubiquitin-specific proteases (USPs) family is the largest family of human deubiquitinating enzymes (DUBs). While most USPs are agnostic to polyubiquitin linkage-type, their substrate specificity is thought to be mediated by the recognition of the ubiquitnated protein itself. In addition to their catalytic domain, USPs have one or more auxiliary domains (ADs) with key functions in regulating DUB activity and localization. We hypothesize that some ADs bind short linear motifs (SLiMs) typically found in intrinsically disordered regions of proteins to achieve targeting to substrates and multiprotein complexes. To test this, we systematically assess the potential of 29 USP-ADs and two full-length USPs for SLiM binding using a combination of proteomic-peptide phage display, peptide SPOT arrays and affinity measurements. We discover SLiM-based interactions for 14 ADs from 9 USP-DUBs, including CYLD, USP11, USP19, USP20, USP22 and USP33, and define the consensus motif and properties of the SLiM-AD binding. Interestingly, we establish that the zf-UBP and DUSP2 domains of USP20 and USP33 are SLiM binding ADs with similar binding profiles, explaining the functional redundancy between the two DUBs. Our work reveals unique motifs recognized by the auxiliary domains CAP-Gly, UBL, zf-UBP and DUSP, with potential functional implications for substrate recognition and complex assemblies. - Source: PubMed
Publication date: 2026/05/18
Konstantinou AimilianiCórdova-Pérez AliciaVarga Julia KMadhu PriyankaSimonetti LeandroVieler MaximilianIshimura RyosukeLamoliatte FredericSchueler-Furman OraDavey Norman EKulathu YogeshIvarsson Ylva