RBCK1 Antibody

1. This study demonstrated that Mutations outside the N-terminal part of RBCK1 may cause polyglucosan body myopathy with immunological dysfunction. PMID: 29260357
2. The binding of SHARPIN or HOIL-1L facilitates the E2 loading of HOIP. PMID: 28978479
3. LUBAC components control TLR3-mediated innate immunity, thereby preventing development of immunodeficiency and autoinflammation. PMID: 27810922
4. results unveil HOIL1 as a negative regulator of lymphocyte activation cleaved by MALT1. PMID: 27006117
5. HOXA1-mediated activation of NF-kappaB is non-transcriptional and the RBCK1 and TRAF2 influences on NF-kappaB are epistatic to HOXA1 PMID: 27382069
6. Late in the NF-kappaB activation cycle HOIL1 cleavage transiently reduces linear ubiquitination, including of NEMO and RIP1, dampening NF-kappaB activation and preventing reactivation. PMID: 26525107
7. human HOIP is essential for the assembly and function of LUBAC, which includes HOIL-1, and for various processes governing inflammation and immunity in both hematopoietic and nonhematopoietic cells PMID: 26008899
8. findings support a role for RBCK1 in the regulation of FKBPL with important implications for estrogen receptor signaling, cell proliferation and response to endocrine therapy. PMID: 23912458
9. RBCK1 deficiency is a frequent cause of polyglucosan storage myopathy associated with progressive muscle weakness and cardiomyopathy. PMID: 23798481
10. Suggest that RBCK1 is important for the ubiquitination of PXR and may play a role in its proteasomal degradation. PMID: 23160820
11. Estrogen receptor-alpha, RBCK1, and protein kinase C beta 1 cooperate to regulate estrogen receptor-alpha gene expression. PMID: 23042805
12. Patients from two kindreds of a new fatal inherited disorder characterized by chronic autoinflammation, invasive bacterial infections and muscular amylopectinosis carried biallelic loss-of-expression and loss-of-function mutations in HOIL1. PMID: 23104095
13. The solution structure of the HOIL1 Ubl domain was solved using NMR spectroscopy to compare it with that of parkin to determine the structural elements responsible for S5a subunit of the 26S proteasome intermolecular interactions. PMID: 22517668
14. analysis of recognition of linear ubiquitin chains by the Npl4 zinc finger (NZF) domain of the HOIL-1L subunit of the linear ubiquitin chain assembly complex PMID: 22139374
15. Data report the identification of the related proteins Sipl1 (Shank-interacting protein-like 1) and Rbck1 (RBCC protein interacting with PKC1) as novel interaction partners of Eya1. PMID: 20956555
16. Findings suggest that RBCK1 regulates cell cycle progression and proliferation of ERalpha-positive breast cancer cells by supporting transcription of ERalpha and cyclin B1. PMID: 20103625
17. RBCK1 (human C20orf18 and rat Pkcbpb15) is involved in transcriptional machinery in the nuclear bodies, and its transcriptional activity is regulated by nucleocytoplasmic shuttling. PMID: 15833741
18. RBCK2 serves as a cytoplasmic tethering protein for RBCK1 PMID: 16083853
19. HOIL-1 expression stabilizes SOCS6 and induces the ubiquitination and degradation of proteins associated with SOCS6 PMID: 16643902
20. findings suggest that RBCK1 is involved in negative regulation of inflammatory signaling triggered by TNF and IL-1 through targeting TAB2/3 for degradation PMID: 17449468
21. These data demonstrate that HOIL-1 is not required for iron-dependent degradation of IRP2 in HEK293 cells, and suggest that a HOIL-1 independent mechanism is used for IRP2 degradation in most cell types. PMID: 17822790
22. the E3 activity of RBCK1 is controlled by two distinct manners, interaction with RBCK2 and phosphorylation by PKCbeta PMID: 18303026
23. Study shows that the E3 ubiquitin ligase RBCC protein interacting with PKC1 (RBCK1) catalyzes the ubiquitination and degradation of IRF3. PMID: 18711448
24. The shRNA barcode screening technique identified RBCK1 as being involved in p53 regulation. PMID: 19277210
25. RBCK2 functions as an adaptor protein for the polyubiquitinated protein and the S5a subunit in 26S proteasome through its novel zinc finger motif and ubiquitin-like domain, respectively. PMID: 19796170

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HGNC: 15864

OMIM: 610924

KEGG: hsa:10616

STRING: 9606.ENSP00000348632

UniGene: Hs.247280