RCHY1 Recombinant Monoclonal Antibody

1. High Pirh2 expression was positively correlated with high tumor grade in brain glioma specimens. PMID: 28258514
2. Data indicate cellular E3 ubiquitin ligase ring-finger and CHY zinc-finger domain-containing 1 (RCHY1) as an interacting partner of the viral SARS-unique domain (SUD) and papain-like protease (PL(pro)), and, as a consequence, the involvement of cellular p53 as antagonist of coronaviral replication. PMID: 27519799
3. p27 and its cognate ubiquitin ligases, Skp2/KPC/Pirh2, are specifically involved in determining the clinical profiles of lung carcinomas. PMID: 28601655
4. Decrease of PIRH2 expression in the breast cancer cell line MDA-MB-231 resulted in reduced tumor cell growth via the inhibition of cell proliferation and the interruption of cell cycle transition. PMID: 27393961
5. The Hoxa2-mediated decay of RCHY1 involves both the 19S and 20S proteasome complexes PMID: 26496426
6. Tumor suppressor p63 regulates expression of ubiquitin ligase PIRH2. PMID: 26995965
7. Overexpression of Pirh2 decreased the replication of prototype foamy virus, whereas knockdown of Pirh2 with specific siRNA increased PFV replication. PMID: 25848801
8. Pirh2 has a physiologically relevant role in keratinocyte differentiation through the posttranslational modification of p63 protein. PMID: 23235527
9. suggested that the interaction of SCYL1BP1/Pirh2 could accelerate Pirh2 degradation through an ubiquitin-dependent pathway. SCYL1BP1 may function as an important tumor suppressor gene in HCC development PMID: 22570270
10. Compared to full-length PIRH2A, PIRH2E lacks amino acids 235-261, while PIRH2F is missing C-terminal amino acids 227-261 and both isoforms harbor the RING domain. PMID: 22766706
11. low expression of human PIRH2 in lung, ovarian, and breast cancers correlates with decreased patients' survival PMID: 22125490
12. Data show that Pirh2 monoubiquitinates PolH at one of multiple lysine residues, and that monoubiquitination of PolH inhibits its ability to interact with PCNA and bypass UV-induced lesions, leading to decreased viability. PMID: 21791603
13. Pirh2 promotes the proteasomal turnover of TAp73, and thus targeting Pirh2 to restore TAp73-mediated growth suppression in p53-deficient tumors may be developed as a novel anti-cancer strategy. PMID: 21852228
14. identified a novel Pirh2-interacting protein, AIG1, by yeast two-hybrid screening and confirmed its interaction with p53 both in vitro and in vivo PMID: 21622095
15. Our results suggest that Pirh2 mediates the degradation of p27(Kip1) and participates in cell proliferation in human hepatocellular carcinoma PMID: 21236467
16. This comprehensive analysis of the Pirh2 and Mdm2 RING domains provides structural and mechanistic insight into p53 regulation by its E3 ligases. PMID: 21084285
17. MDM2, MDMX, Pirh2 and COP1 might inhibit p53 activity synergistically in vivo. PMID: 20333547
18. SCYL1-BP1 can be ubiquitinated and degraded by Pirh2 but not by MDM2, which suggests that SCYL1-BP1 can be regulated by Pirh2. PMID: 20598683
19. low level of expression of hPirh2 was found both at transcriptional and translational level in human hepatocellular carcinoma (HCC) when compared to non-cancerous tissue. The protein shows no ubiquitin protein ligase activity. PMID: 20452352
20. found that DNA polymerase eta is recruited by Pirh2 and degraded by 20S proteasome in a ubiquitin-independent manner. PMID: 20008555
21. increased expression of PIRH2 was correlated with poor survival in patients with hepatocellular carcinoma; PIRH2 is a novel prognostic marker for hepatocellular carcinoma PMID: 19551892
22. expression of measles virus antigens in non-small cell lung carcinoma is associated with expression of Pirh2. The presence of Pirh2 itself was associated with improved survival. PMID: 19895323
23. cloning and characterization of an androgen receptor N-terminal-interacting protein with ubiquitin-protein ligase activity [androgen-receptor N-terminal-interacting protein; hARNIP] PMID: 12200228
24. This protein is a p53-induced ubiquitin-protein ligase which promotes p53 degradation. PMID: 12654245
25. These results are consistent with the hypothesis that increased Pirh2 expression affects lung tumorigenesis by reducing p53 activity. PMID: 15547185
26. Human PIRH2 as a key modulator of AR function, opening a new direction for targeted therapy in aggressive human prostate cancer. PMID: 16914734
27. Study evaluated Pirh2, MDM2, p53 and p21 expression after DNA damage using cancer cell lines with wildtype, mutant and null p53 and found that unlike MDM2, Pirh2 expression was not affected by wildtype p53 in the cancer cells. PMID: 16934800
28. phosphorylation of Pirh2 may act as a fine-tuning to maintain the balance of p53-Pirh2 autoregulatory feedback loop, which facilitates the tight regulation of p53 stability and tumor suppression PMID: 17568776
29. PIRH2 functions as a regulator for COP I complex. PMID: 17721809
30. Given the importance of Pirh2 in regulating p53 stability, its interaction with PLAGL2 may provide valuable therapeutic targets in treating Pirh2-overexpression malignancies. PMID: 17950244
31. Pirh2 acts as a negative regulator of p27(Kip1) function by promoting ubiquitin-dependent proteasomal degradation PMID: 18006823
32. The authors show that Pirh2-p53 interaction is dependent on the C-terminal zinc binding module of Pirh2, which binds to the tetramerization domain of p53. PMID: 19043414
33. The RCHY1 protein was displayed an unexpected role in regulating the organization of the network of K8/18 keratin filaments. PMID: 19282868
34. Pirh2 overexpression may have an important role in the development and maintenance of head and neck squamous cell carcinoma at least partially through p27 degradation PMID: 19445020
35. Pirh2 ubiquitin ligase has two novel isoforms that negatively regulate p53 independent of RING finger domains PMID: 19483087
36. Pirh2 (ZNF363), a gene regulated by p53, encodes a RING-H2 domain-containing protein with intrinsic ubiquitin-protein ligase activity. Pirh2 protein physically interacts with p53 and promotes ubiquitination and degradation of p53 independently of Mdm2. PMID: 12654245

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HGNC: 17479

OMIM: 607680

KEGG: hsa:25898

STRING: 9606.ENSP00000321239

UniGene: Hs.48297