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We show that PRP31, a component of U4 snRNP, is modified with K63-linked ubiquitin chains by the PRP19 complex and deubiquitinated by USP15 and its substrate targeting factor SART3. USP15SART3 makes a complex with USP4 and this ternary complex serves as a platform to deubiquitinate PRP31 and PRP3
The complex structure of SART3 nuclear localization signal (NLS (show ALDH1A2 Proteins)) and importin-alpha reveals bipartite binding, and removal of SART3 NLS (show ALDH1A2 Proteins) prevents the entry of USP4 (show USP4 Proteins) (and USP15 (show USP15 Proteins)) into the nucleus and abrogates the subsequent deubiquitinase activity of USP4 (show USP4 Proteins).
crystal structures of SART3 in the apo (show C9orf3 Proteins)-form and in complex with the DUSP (show DUSP5 Proteins)-UBL domain of USP15 (show USP15 Proteins) at 2.0 and 3.0 A, respectively. Structural analysis reveals SART3 contains 12 half-a-tetratricopeptide (HAT (show MGEA5 Proteins)) repeats, organized into two subdomains, HAT (show MGEA5 Proteins)-N and HAT (show MGEA5 Proteins)-C. SART3 dimerizes through the concave surface of HAT (show MGEA5 Proteins)-C, whereas the HAT (show MGEA5 Proteins)-C convex surface binds USP15 (show USP15 Proteins) in a novel bipartite mode.
miR (show MLXIP Proteins)-124 regulates Tip110 expression and differentiation of human cord blood CD34 (show CD34 Proteins)(+) cells
Hypoxia led to Tip110 protein degradation through the ubiquitin-proteasome system. Under hypoxia, Tip110 stabilized p53 (show TP53 Proteins), which in return destabilized Tip110.
SART3 recruits ubH2B, which may be evicted from DNA during transcription, for deubiquitination by Usp15 (show USP15 Proteins)
YB-1 (show YBX1 Proteins) potentiates the Tip110/Tat (show TAT Proteins)-mediated transactivation of the HIV-1 LTR promoter.
findings show C-MYC (show MYC Proteins) upregulates transcription of TIP110 through interaction with the TIP110 E-box in the TIP110 promoter, ensuring high-level Tip110 expression in proliferating embryonic stem cells (hESCs); further show TIP110 regulates OCT4 (show POU5F1 Proteins) alternative splicing in hESCs
TIP110 is also expressed in human embryonic stem cells (hESCs) and expression was decreased with differentiation of these ESCs (show NR2E3 Proteins).
Results suggest that U4 and U6 small nuclear ribonucleoproteins (snRNPs) accumulate in Cajal bodies for the purpose of assembly into U4/U6 snRNPs by SART3/p110.
The protein encoded by this gene is an RNA-binding nuclear protein that is a tumor-rejection antigen. This antigen possesses tumor epitopes capable of inducing HLA-A24-restricted and tumor-specific cytotoxic T lymphocytes in cancer patients and may be useful for specific immunotherapy. This gene product is found to be an important cellular factor for HIV-1 gene expression and viral replication. It also associates transiently with U6 and U4/U6 snRNPs during the recycling phase of the spliceosome cycle. This encoded protein is thought to be involved in the regulation of mRNA splicing.
squamous cell carcinoma antigen recognized by T cells 3
, Squamous cell carcinoma antigen recognized by T-cells 3
, squamous cell carcinoma antigen recognized by T-cells 3-like
, earl grey
, squamous cell carcinoma antigen recognized by T-cells 3
, tat-interacting protein of 110 kDa
, tumor-rejection antigen SART3