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The protein encoded by RCHY1 has ubiquitin ligase activity. Additionally we are shipping Ring Finger and CHY Zinc Finger Domain Containing 1, E3 Ubiquitin Protein Ligase Antibodies (49) and many more products for this protein.
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This study showed that ORF3 protein of porcine circovirus type 2 interacted competitively with p53 tumor suppressor protein (show TP53 Proteins) in binding to porcine Pirh2.
Results show that the PCV2 ORF3 protein specifically interacts with pPirh2 and inhibits its stabilization; this may lead to increasing p53 (show TP53 Proteins) expression, resulting in apoptosis.
Findings indicate that PIRH2 has central roles in the ubiquitylation of Chk2 (show CHEK2 Proteins) and its turnover and in the regulation of its function.
This study provides evidence that the ubiquitination of p73 (show ARHGAP24 Proteins) mediated by Pirh2 represents an important pathway for controlling the suppressive function of p73 (show ARHGAP24 Proteins)
these data reveal the in vivo roles of Pirh2 in the regulation of p53 and c-Myc stability and support its role as a tumor suppressor
Data show that Pirh2 monoubiquitinates PolH (show POLH Proteins) at one of multiple lysine residues, and that monoubiquitination of PolH (show POLH Proteins) inhibits its ability to interact with PCNA (show PCNA Proteins) and bypass UV-induced lesions, leading to decreased viability.
cloning and characterization of an androgen receptor N-terminal-interacting protein with ubiquitin-protein ligase (show UBE2K Proteins) activity [androgen-receptor N-terminal-interacting protein; mARNIP]
Pirh2 (Zfp363), a gene regulated by p53 (show TP53 Proteins), encodes a RING-H2 domain-containing protein with intrinsic ubiquitin-protein ligase (show UBE2K Proteins) activity. Pirh2 physically interacts with p53 (show TP53 Proteins) and promotes ubiquitination and degradation of p53 (show TP53 Proteins) independently of Mdm2 (show MDM2 Proteins).
These results are consistent with the hypothesis that increased Pirh2 expression affects lung tumorigenesis by reducing p53 (show TP53 Proteins) activity.
Pirh2 acts as a negative regulator of p27(Kip1 (show CDKN1B Proteins)) function by promoting ubiquitin-dependent proteasomal degradation
The Hoxa2 (show HOXA2 Proteins)-mediated decay of RCHY1 involves both the 19S and 20S proteasome (show PSMA5 Proteins) complexes
Tumor suppressor p63 (show RPE65 Proteins) regulates expression of ubiquitin ligase PIRH2.
Overexpression of Pirh2 decreased the replication of prototype foamy virus, whereas knockdown of Pirh2 with specific siRNA increased PFV replication.
Pirh2 has a physiologically relevant role in keratinocyte differentiation through the posttranslational modification of p63 (show RPE65 Proteins) protein.
suggested that the interaction of SCYL1BP1 (show GORAB Proteins)/Pirh2 could accelerate Pirh2 degradation through an ubiquitin-dependent pathway. SCYL1BP1 (show GORAB Proteins) may function as an important tumor suppressor gene in HCC (show FAM126A Proteins) development
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.
low expression of human PIRH2 in lung, ovarian, and breast cancers correlates with decreased patients' survival
Pirh2 promotes the proteasomal turnover of TAp73 (show TP73 Proteins), and thus targeting Pirh2 to restore TAp73 (show TP73 Proteins)-mediated growth suppression in p53 (show TP53 Proteins)-deficient tumors may be developed as a novel anti-cancer strategy.
The protein encoded by this gene has ubiquitin ligase activity. It mediates E3-dependent ubiquitination and proteasomal degradation of target proteins, including TP53, HDAC1 and CDKN1B, thus regulating their levels and cell cycle progression. Alternatively spliced transcript variants encoding different isoforms have been described for this gene.
CH-rich-interacting match with PLAG1
, E3 ubiquitin-protein ligase Pirh2
, RING finger and CHY zinc finger domain-containing protein 1
, androgen receptor N-terminal-interacting protein
, zinc finger protein 363
, CH-rich interacting match with PLAG1
, RING finger protein 199
, androgen-receptor N-terminal-interacting protein
, p53-induced protein with a RING-H2 domain