• SUMOylation is a post-translational modification of proteins that has been found to play a major role in the Wnt/β-catenin signaling pathway. (frontiersin.org)
  • Post-translational modifications (PTMs) of proteins, including phosphorylation, acetylation, ubiquitination, and SUMOylation, can regulate the function of proteins, determine the active state and subcellular location of proteins, and dynamically interact with other proteins related to carcinogenesis and progression ( 17 - 20 ). (frontiersin.org)
  • SUMOylation of proteins is an important mechanism in cellular responses to environmental stress ( 21 , 22 ). (frontiersin.org)
  • Proteins associated with the Wnt/β-catenin pathway have been identified as SUMOylated substrates, and evidences suggested that the initiation and progression of cancers depended on the function of the SUMOylation ( 23 ). (frontiersin.org)
  • IAS proteins were originally identified in studies that were aimed to decipher the Janus Kinase (JAK)/STAT signaling pathway. (wikipedia.org)
  • An LXXLL signature motif is present within the SAP domain of all PIAS proteins. (wikipedia.org)
  • It was previously described that the LXXLL motif is also responsible for the retention of PIAS3 in the nucleus. (wikipedia.org)
  • The Pro-Ile-Asn-Ile-Thr (PINIT) motif represents a highly conserved region of PIAS proteins, which was shown to be involved in the nuclear retention of PIAS3. (wikipedia.org)
  • INTRODUCTION: Cyclin Dependent Kinase Inhibitor 2A (CDKN2A) is involved in glioma progression, but the specific molecular mechanism of CDKN2A in glioma cell migration and invasion needs to be further explored. (bvsalud.org)
  • Originally, PIAS3 was found to interact specifically with phosphorylated STAT3 in Interleukin -6 (IL-6) activated murine myeloblast M1 cells. (wikipedia.org)
  • These elements are frequently found near gene enhancers and interact with nuclear matrix proteins to provide a unique nuclear microenvironment for transcriptional regulation. (wikipedia.org)
  • The haemagglutinin-neuraminidase (HN) protein plays a crucial role in the infectivity and virulence of Newcastle disease virus (NDV). (bvsalud.org)
  • Herein, we elucidate the crucial role of vimentin, an intermediate filament protein, in regulating NDV infectivity through targeting of the HN protein. (bvsalud.org)
  • The RING-finger-like zinc-binding domain (RLD) is one of the most conserved domains of the PIAS family and has been shown to be important for PIAS3 activity as a SUMO-E3 ligase. (wikipedia.org)
  • PIAS3 protein also functions as a SUMO (small ubiquitin-like modifier)-E3 ligase which catalyzes the covalent attachment of a SUMO protein to specific target substrates. (wikipedia.org)
  • Subsequently, PIAS3 was also found to be a regulator protein of other key transcription factors, including MITF, NFκB, SMAD and estrogen receptor. (wikipedia.org)
  • This evolutionarily conserved domain is found in proteins ranging from yeast to human and is shared by other chromatin-binding proteins, such as scaffold attachment factor A and B. The SAP domain can recognize and bind to AT-rich DNA sequences present in scaffold-attachment regions/matrix-attachment regions. (wikipedia.org)
  • In a previous study, the mutant HN protein was identified as a crucial virulence factor for the velogenic variant NDV strain JS/7/05/Ch, which evolved from the prototypic vaccine strain Mukteswar. (bvsalud.org)
  • E3 SUMO-protein ligase PIAS3 is an enzyme that in humans is encoded by the PIAS3 gene. (wikipedia.org)
  • PIAS3 protein also functions as a SUMO (small ubiquitin-like modifier)-E3 ligase which catalyzes the covalent attachment of a SUMO protein to specific target substrates. (wikipedia.org)
  • The RING-finger-like zinc-binding domain (RLD) is one of the most conserved domains of the PIAS family and has been shown to be important for PIAS3 activity as a SUMO-E3 ligase. (wikipedia.org)
  • The search for calpain 3 substrates using cleavage site recognition have lead to a number of potential targets, one being Protein Inhibitor of Activated Stats 3 (PIAS3), an ubiquitously expressed E3 SUMO ligase implicated in many signaling pathways by modifying the localization and role in transcriptional regulation of transcription factors. (medscape.com)
  • Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. (nih.gov)
  • We have examined single nucleotide polymorphisms (or SNPs) within three genes from the ubiquitin protein system: the ubiquitin conjugating enzyme E2D1 (UBE2D1) gene, the E3 SUMO-protein ligase protein inhibitor of activated STAT 2 (PIAS2) gene, and the E3 ubiquitin ligase F-box and leucine-rich repeat protein 21 (FBXL21) gene, in a Caucasian case-control population for schizophrenia. (nih.gov)
  • 3. RING protein Trim32 associated with skin carcinogenesis has anti-apoptotic and E3-ubiquitin ligase properties. (nih.gov)
  • 5. The E3 SUMO ligase PIASy is a regulator of cellular senescence and apoptosis. (nih.gov)
  • 11. TRIM32 protein sensitizes cells to tumor necrosis factor (TNFα)-induced apoptosis via its RING domain-dependent E3 ligase activity against X-linked inhibitor of apoptosis (XIAP). (nih.gov)
  • 12. SYT-SSX1 (synovial sarcoma translocated) regulates PIASy ligase activity to cause overexpression of NCOA3 protein. (nih.gov)
  • 17. SUMO-1 modification of PIASy, an E3 ligase, is necessary for PIASy-dependent activation of Tcf-4. (nih.gov)
  • Regulates E3 ubiquitin-protein ligase activity of RNF19A (By similarity). (nih.gov)
  • The modification of proteins by s mall u biquitin-related mo difier (SUMO) molecules, SUMOylation, is a key post-translational modification involved in a variety of biological processes, such as chromosome organization, DNA replication and repair, transcription, nuclear transport, and cell signaling transduction. (mdpi.com)
  • 20. Nitric oxide destabilizes Pias3 and regulates sumoylation. (nih.gov)
  • IAS proteins were originally identified in studies that were aimed to decipher the Janus Kinase (JAK)/STAT signaling pathway. (wikipedia.org)
  • This gene encodes a member of the PIAS [protein inhibitor of activated STAT (signal transducer and activator of transcription)] family of transcriptional modulators. (nih.gov)
  • Originally, PIAS3 was found to interact specifically with phosphorylated STAT3 in Interleukin -6 (IL-6) activated murine myeloblast M1 cells. (wikipedia.org)
  • This interaction is mediated via PIAS3 binding to the STAT3 DNA binding domain. (wikipedia.org)
  • Subsequent yeast two-hybrid screening identified PIAS3 (protein inhibitor of activated STAT3) as an ATF1-binding protein. (nih.gov)
  • and 4) ATF1 knockdown with siRNA increased ferritin H expression, whereas PIAS3 knockdown decreased basal expression and oxidative stress-mediated induction of ferritin H. These results suggest that PIAS3 antagonizes the repressor function of ATF1, at least in part by blocking its DNA binding, and ultimately activates the ARE. (nih.gov)
  • The mammalian PIAS family consists of four members: PIAS1, PIAS2, PIAS3 and PIAS4. (wikipedia.org)
  • Probe Set ID Ref Seq Protein ID Signal Strength Name Gene Symbol Species Function Swiss-Prot ID Amino Acid Sequence 1367452_at NP_598278 7.9 small ubiquitin-related modifier 2 precursor Sumo2 Rattus norvegicus " Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. (nih.gov)
  • This gene encodes an elastase-specific inhibitor that functions as an antimicrobial peptide against Gram-positive and Gram-negative bacteria. (anticorps-enligne.fr)
  • PIAS3 interacts with ATF1 and regulates the human ferritin H gene through an antioxidant-responsive element. (nih.gov)
  • Collectively our results suggest that PIAS3 is a new regulator of ATF1 that regulates the ARE-mediated transcription of the ferritin H gene. (nih.gov)
  • This evolutionarily conserved domain is found in proteins ranging from yeast to human and is shared by other chromatin-binding proteins, such as scaffold attachment factor A and B. The SAP domain can recognize and bind to AT-rich DNA sequences present in scaffold-attachment regions/matrix-attachment regions. (wikipedia.org)
  • Calpain 3 is anchored to the giant structural/scaffold protein titin in a stable and inactive manner, to keep it from degrading itself autolytically. (medscape.com)
  • These elements are frequently found near gene enhancers and interact with nuclear matrix proteins to provide a unique nuclear microenvironment for transcriptional regulation. (wikipedia.org)
  • [ 5 ] This group proposed that the protease activity of calpain 3 is required to protect muscle from degeneration under exercise-induced stress, and that loss of protease activity affected the dynamic distribution of calpain 3 during physical activity and its interaction with MARP2, a stress-response transcriptional regulator protein, in close proximity to calpain 3 on the N2A region of titin. (medscape.com)
  • Description of the protein which includes the UniProt Function and the NCBI Gene Summary. (nih.gov)
  • Gene-expression profiling and recent protein studies have shown a decrease in the expression of ubiquitin pathway proteins in the prefrontal cortex of schizophrenia patients. (nih.gov)
  • The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. (nih.gov)
  • This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. (nih.gov)
  • The Pro-Ile-Asn-Ile-Thr (PINIT) motif represents a highly conserved region of PIAS proteins, which was shown to be involved in the nuclear retention of PIAS3. (wikipedia.org)
  • Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (By similarity). (nih.gov)
  • The protein contains a WAP-type four-disulfide core (WFDC) domain, and is thus a member of the WFDC domain family. (anticorps-enligne.fr)
  • The SAF-A/B, Acinus and PIAS (SAP) domain is located at the N-terminal of PIAS proteins. (wikipedia.org)
  • An LXXLL signature motif is present within the SAP domain of all PIAS proteins. (wikipedia.org)
  • The RLD domain is also involved in the positive regulation of SMAD3 by PIAS3. (wikipedia.org)