Small ubiquitin related modifier proteins. Medical search. Frequent questions

Protein inhibitor of activated STAT (PIAS), also known as E3 SUMO-protein ligase PIAS, is a protein that regulates transcription in mammals. (wikipedia.org)
These functions include acting as E3 SUMO-protein ligases during SUMOylation, which is an important process in transcriptional regulation. (wikipedia.org)
When it was discovered that PIAS proteins did far more than simply inhibit STATs, it was proposed that the PIAS acronym should stand for Pleiotropic Interactors Associated with SUMO based on their association with SUMO proteins. (wikipedia.org)
Additionally, E3 SUMO-protein ligase PIAS is an alternative name for PIAS proteins. (wikipedia.org)
While PIAS proteins interact with at least 60 different proteins involved in transcription, they are known to act as E3 SUMO-protein ligases. (wikipedia.org)
In essence, the RING-finger-like zinc-binding domain of the PIAS protein assists in the attachment of a SUMO protein to the target transcription factor. (wikipedia.org)
Attachment of a SUMO protein to the target allows for protein-protein interaction between PIAS and the transcription factor. (wikipedia.org)
This gene encodes a member of a family of E3 small ubiquitin-related modifier (SUMO) ligases that mediates the attachment of a SUMO protein to proteins involved in nuclear transport, transcription, chromosome segregation and DNA repair. (nih.gov)
Effects of Nephrolithiasis on Serum DNase (Deoxyribonuclease I and II) Activity and E3 SUMO-Protein Ligase NSE2 (NSMCE2) in Malaysian Individuals. (nih.gov)
Here, we analyzed the impact of the ubiquitin-like protein SUMO on the RPL11-mouse double-minute 2 homolog-p53 signaling. (sdu.dk)
We show that small ubiquitin-related modifier (SUMO)1 and SUMO2 covalently modify RPL11. (sdu.dk)
We find that SUMO negatively modulates the conjugation of the ubiquitin-like protein neural precursor cell-expressed developmentally downregulated 8 (NEDD8) to RPL11 and promotes the translocation of the RP outside of the nucleoli. (sdu.dk)
Collectively, our data identify SUMO protein conjugation to RPL11 as a new regulator of the p53-mediated cellular response to different types of stress and reveal a previously unknown SUMO-NEDD8 interplay. (sdu.dk)
Your body, from protein chief, Drug and activity of chicken ovalbumin upstream promoter transcription factor I (COUP-TF1), which itself is coactivated by the small ubiquitin-related modifier-1 (SUMO-1) conjugase and ligase Ubc9 and PIAS1 (79). (sideload.com)
SUMO (small ubiquitin-related modifier), a member of the ubiquitin-like protein family, regulates diverse cellular functions of a variety of target proteins including transcription, DNA repair, nucleocytoplasmic trafficking and chromosome segregation. (thermofisher.com)
SUMO precursor proteins undergo cleavage of the residues after the "GG" region by SUMO-specific proteases in maturation. (thermofisher.com)
The sentrin-specific (or SUMO-specific) protease (SENP) proteins belong to the peptidase C48 family and include SENP1-3 and SENP5-8. (thermofisher.com)
A protein modification that effectively crosslinks the N6-amino of a peptidyl lysine with the carboxyl-terminal glycine of a sumo (Small Ubiquitin-related MOdifier) protein. (reactome.org)
One major area of interest focuses on how cells attach small proteins - like ubiquitin and the related molecule SUMO - to other proteins to modify their function or fate. (mskcc.org)
The proteins ubiquitin and SUMO (small ubiquitin-like protein modifier) tag other proteins in the cell to redirect them to certain parts of the cell or to influence their interactions with other molecules. (mskcc.org)
Acetylation of K33 in Small ubiquitin-related modifier 2 (SUMO2) inhibits binding to E3 SUMO-protein ligase PIAS2 (PIAS2) . (eu.org)
Small ubiquitin-related modifier (SUMO) can help with folding and stabilization, as can maltose-binding protein (MBP). (addgene.org)
Of these newly discovered ubiquitin-like proteins, the SUMO family has gained prominence as a major regulatory component that impacts numerous aspects of cell growth and differentiation. (tamu.edu)
This chapter will introduce the basic properties of SUMO proteins and the general tenets of sumoylation. (tamu.edu)
SUMO (small ubiquitin related modifier) proteins are 100 amino acid residue proteins which bind to the target protein in the same way as ubiquitin. (microbenotes.com)
Cuerpos esféricos intranucleares sin membrana nucleados por la PROTEÍNA DE LA LEUCEMIA PROMIELOCÍTICA y diversas otras proteínas que contienen un motivo de interacción de modificador pequeño relacionado con la ubiquitina (SUMO, por sus siglas en inglés), o SIM (por sus siglas en inglés), y/o proteínas sumoiladas (por ejemplo, proteína Sp100). (bvsalud.org)
Spherical intranuclear membraneless bodies nucleated by PROMYELOCYTIC LEUKEMIA PROTEIN and various other proteins containing small ubiquitin-related modifier (SUMO) interaction motif (SIM) and/or sumoylated proteins (e.g. (bvsalud.org)
Invertebrates and Fungus exhibit one SUMO proteins, while vertebrates exhibit several useful paralogues, including SUMO-1, SUMO-2, and SUMO-3. (conferencedequebec.org)
Mammalian SUMO-2 and SUMO-3 are 95% similar and regarded as functionally related. (conferencedequebec.org)
The system of SUMO conjugation relates to ubiquitin closely. (conferencedequebec.org)
We also discovered a distinctive subset of membrane-associated protein that connect to SENP2, providing additional insights in to the potential jobs SUMO can play in regulating membrane-associated features. (conferencedequebec.org)
Small ubiquitin-like modifier (SUMO) conjugation (SUMOylation) plays key roles in neurologic function in health and disease. (duke.edu)
The small ubiquitin-related modifier SUMO-1 is a Ub/Ubl family member, and although SUMO-1 shares structural similarity to Ub, SUMO's cellular functions remain distinct insomuch as SUMO modification alters protein function through changes in activity, cellular localisation, or by protecting substrates from ubiquitination. (umbc.edu)
Aberrations in post-translational modifications by ubiquitin or ubiquitin-like proteins (Ubl), such as the small ubiquitin-like modifiers (SUMO) relate to the pathogenesis of lifethreatening diseases, such as cancer, neurodegenerative disorders, and viral infection. (cancer-research-network.com)
who come from the Beckman Research Institute, have identified a allosteric inhibitor of ubiquitin -like 1-activating enzyme (SUMO-activating enzyme), COH000. (cancer-research-network.com)
COH000 is an allosteric, covalent and irreversible inhibitor of Ubiquitin-like 1-activating enzyme (SUMO-activating enzyme), with an IC 50 of 0.2 μM for SUMOylation in vitro. (cancer-research-network.com)
The two NE proteins PML and SP100 are covalently modified by the ubiquitin-related SUMO-1 modifier, and recent work indicates that this modification is critical for the regulation of NE dynamics. (st-andrews.ac.uk)
SUMO (small ubiquitin-like modifier) is attached as a monomer or polymer through a process akin to that of ubiquitination. (horizondiscovery.com)

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)
SUMOylation of RPL11 is triggered by ribosomal stress, as well as by alternate reading frame protein upregulation. (sdu.dk)
Unlike ubiquitinylation which often leads to protein turn over, sumoylation performs a variety of functions such as altering protein stability, protein trafficking, protein-protein interaction, and protein activity. (tamu.edu)
protein sumoylation in different cellular compartments. (huji.ac.il)
Collectively, our results indicate that SENP2 binds to intracellular membranes where it interacts with membrane-associated protein and gets the potential to modify their sumoylation and membrane-associated features. (conferencedequebec.org)
To various other ubiquitin-like protein Likewise, sumoylation provides another Zolpidem known degree Zolpidem of legislation to proteins activity, balance, and localization. (conferencedequebec.org)
Small ubiquitin-like modifier (SUMO1-3) conjugation (SUMOylation), a posttranslational modification, modulates almost all major cellular processes. (duke.edu)
KEPE--a motif frequently superimposed on sumoylation sites in metazoan chromatin proteins and transcription factors. (ox.ac.uk)

Over the last 10 years, the ubiquitin family has expanded to include a variety of ubiquitin-related small modifier proteins that are all covalently attached to a lysine residue on target proteins via series of enzymatic reactions. (tamu.edu)
This family of genes encode small ubiquitin-related modifiers that are attached to proteins and control the target proteins' subcellular localization, stability, or activity. (wn.com)
The ubiquitin/proteasome pathway that degrades ubiquitin-tagged cell target proteins through the proteasome is a common regulatory modification system involved in the regulation of cell cycle, signal transduction, DNA damage response, apoptosis, and immune response. (amerigoscientific.com)

ubiquitin-conjugating (E2) enzymes, and ubiquitin ligases (E3), respectively. (123dok.net)
E1 enzymes (ubiquitin-activating enzymes), E2 enzymes (ubiquitin-conjugating enzymes), and E3 enzymes (ubiquitin ligases). (amerigoscientific.com)

Results were correlated with immunoreactivity for USP7 (herpes virus-associated ubiquitin-specific protease 7) and SUMO2/3 (small ubiquitin-related modifier protein 2/3) as well as PTEN and p53 FISH gene status. (biomedcentral.com)
Small ubiquitin-like modifier 2 (SUMO2) is critical for memory processes in mice. (duke.edu)

Protein degradation helps maintain the proper balance of protein production and breakdown (protein homeostasis). (medlineplus.gov)
A second major area of interest focuses on how proteins contribute to RNA stability and degradation. (mskcc.org)
The patriarch of the protein modifiers is ubiquitin which plays a central role in protein degradation and protein targeting. (tamu.edu)
Ubiquitin functions as a reversible post-translational modifier of proteins to regulate many different cellular processes such as DNA repair, chromatin dynamics, cell cycle regulation, membrane and protein trafficking, endocytosis, autophagy, but most notably proteasome-dependent protein degradation [2-4]. (123dok.net)
The level of protein within cells is determined by both the rate of synthesis and the rate of degradation. (amerigoscientific.com)
The difference in protein degradation rates is an important aspect of cell regulation. (amerigoscientific.com)
In eukaryotic cells, the ubiquitin/proteasome pathway and lysosomal proteolysis are the two main pathways of protein degradation. (amerigoscientific.com)

Signaling is initiated when the Wnt ligand binds to the Frizzled receptor on the cell membrane and the LDL receptor-associated protein 5/6 (LRP5/6) co-receptor. (frontiersin.org)
MURF-1 also binds to ubiquitin-conjugating enzyme-9 and isopeptidase T-3, enzymes involved in small ubiquitin-related modifier-mediated nuclear import, and with glucocorticoid modulatory element binding protein-1 (GMEB-1), a transcriptional regulator. (rupress.org)
Aids in proper protein folding - few lectin molecules called calnexin binds to glycosylated proteins and assist in its folding. (microbenotes.com)
Ubiquitin binds reversibly to the target protein via an enzyme cascade including ubiquitin-activating enzyme E1, ubiquitin-conjugation enzyme E2, and ubiquitin-protein ligase E3. (amerigoscientific.com)

Furthermore, Ach decreases ISGylation of STAT1 (protein conjugation of a small ubiquitin-like modifier, ISG15, Western blot), which preserves STAT1 activation. (nebraska.edu)
Normally, the conjugation of ubiquitin to other proteins involves the formation of an isopeptide bond between the α-carboxyl group of the C-terminal glycine of a ubiquitin molecule with an ε-amino group of a specific lysine residue within the target protein [2,3]. (123dok.net)

The ribosomal protein L11 (RPL11) integrates different types of stress into a p53-mediated response. (sdu.dk)

Prokaryotes can also have a hard time folding eukaryotic proteins. (addgene.org)
Ubiquitin is a highly conserved small eukaryotic protein. (123dok.net)
Ubiquitin is a small eukaryotic protein of 76 amino acids whose name (i.e., it occurs ubiquitously) results from its remarkable evolutionary conservation [1]. (123dok.net)
Ubiquitin is an 8.5-kDa polypeptide that exists in all eukaryotic cells and acts as a tag in post-translational modification of proteins. (amerigoscientific.com)

By identifying many sGAG-specific interacting proteins, our data provide a resource for upcoming studies aimed at molecular mechanisms and understanding of sGAG cellular effects. (degruyter.com)
Our results suggest that cold temperature significantly affects genes related to protein translation and cellular metabolism in this chilling sensitive species. (biomedcentral.com)
In 2010, Dr. Lima - in collaboration with chemist Derek S. Tan and a multidisciplinary team of researchers at Memorial Sloan Kettering - determined the mechanism for how a family of enzymes called E1 activates ubiquitin, shedding light on a complex reaction that plays a key role in regulating cellular behavior. (mskcc.org)
Post-translational modifications of proteins, which are not gene- template based, can regulate the protein functions, by causing changes in protein activity, their cellular locations and dynamic interactions with other proteins. (microbenotes.com)
However, identifying innate cellular pathologies, particularly for age-related neurodegenerative diseases, has been challenging. (scienceopen.com)
We have analyzed the phenotypic effects of a genomic ubi1∆ub-HA ubi2∆ mutant, which expresses a ubiquitin-free HA-tagged eL40A protein as the sole source of cellular eL40. (123dok.net)

The UBA1 gene provides instructions for making the ubiquitin-activating enzyme E1. (medlineplus.gov)
This enzyme is necessary for the ubiquitin-proteasome system, which targets damaged or unneeded proteins to be broken down (degraded) within cells. (medlineplus.gov)
Most cases of VEXAS syndrome are caused by genetic variants that change the protein building block (amino acid) methione at position 41 in the ubiquitin-activating enzyme E1 to another amino acid. (medlineplus.gov)
This shortage of functional enzyme allows damaged or unneeded proteins to build up inside cells instead of being broken down, which may damage cells and contribute to cell death. (medlineplus.gov)

PIAS proteins act as transcriptional co-regulators with at least 60 different proteins in order to either activate or repress transcription. (wikipedia.org)
The transcription factors STAT, NF-κB, p73, and p53 are among the many proteins that PIAS interacts with. (wikipedia.org)
The protein described in this record is located in the cytoplasm and specifically modifies IKBA, leading to negative regulation of NF-kappa-B-dependent transcription of the IL12B gene. (wn.com)
Protein hydroxylation is one type of PTM that involves the conversion of -CH group into -COH group and these hydroxylated amino acids are involved in the regulation of some important factors called transcription factors. (microbenotes.com)
They also confer the transcription regulatory activity of the protein and help in the transport of the target protein from cytosol to the nucleus. (microbenotes.com)

PIAS proteins contain each conserved domain and motif of the PIAS protein family, with a few exceptions. (wikipedia.org)
Therefore, we investigated whether this pattern might define a more general protein motif. (ox.ac.uk)
When considering requirements for the motif to be functional (evolutionary conservation, structural accessibility of the motif and proper cell localization of the protein), more than 130 human proteins were retrieved from the UniProt/Swiss-Prot database. (ox.ac.uk)
Here we report the isolation of a further cDNA, encoding the SP100C protein, that contains the PHD-bromodomain motif characteristic of chromatin proteins. (st-andrews.ac.uk)

Sulfate modidication takes place by the addition of sulphate molecules and these modifications of proteins occurs at tyrosine residues. (microbenotes.com)
Any one of the seven lysine residues or N-terminal Met1 residues is likely to be involved in ubiquitin chain formation. (amerigoscientific.com)
Ubiquitin chains occur when ubiquitin proteins are linked by the carboxy terminus of one ubiquitin to one of lysine residues (K6, K11, K27, K29, K33, K48, and K63) or the N-terminal methionine residue (M1) on the other ubiquitin. (amerigoscientific.com)

What are some of the hurdles to overcome in order to overexpress a recombinant protein? (addgene.org)
His-Ubiquitin recombinant protein probed with Mouse anti Histidine Tag ( MCA1396 ). (bio-rad-antibodies.com)

Reversible post-translational modification is a rapid and efficient system to control the activity of pre-existing proteins. (tamu.edu)

Due to alternative splicing, some PIAS protein-encoding genes encode multiple protein products called isoforms. (wikipedia.org)

PIAS protein's interaction with STAT signaling requires tyrosine phosphorylation of STAT proteins. (wikipedia.org)
Both own phosphorylation status and direct protein-protein interactions are increasingly investigated [ 5 ]. (biomedcentral.com)
After synthesis is completed, proteins can be modified by various methods such as phosphorylation, glycosylation, ADP ribosylation, hydroxylation, and addition of other groups. (microbenotes.com)
Post Translational Phosphorylation is one of the most common protein modifications that occur in animal cells. (microbenotes.com)
Majority of phosphorylation occurs as a mechanism to regulate the biological activity of a protein. (microbenotes.com)
Government of LY294004 didn't more affect the Akt and PI3K phosphorylation that has been maximally suppressed by iPSCs at 5 107 cells/kg or even the equivalent level of iPSC CM. Meanwhile, such medicinal treatment also showed no effect on the details related to lung injury and neutrophil infiltration that have been maximally inhibited by iPSCs or iPSC CM in wild type recipients but not in Akt heterozygous knockout recipients. (pimpathway.com)

This mutant shows a severe slow-growth phenotype, which could be fully suppressed by increased dosage of the ubi1∆ub-HA allele, or partially by the replacement of ubiquitin by the ubiquitin-like Smt3 protein. (123dok.net)

it turns on (activates) a small protein called ubiquitin. (medlineplus.gov)

The C terminus of ubiquitin must be activated before it can form isopeptide bonds with other proteins. (amerigoscientific.com)

The interaction of sGAG with α2-macroglobulin receptor-associated protein (LRPAP1), exportin-1 (XPO1), and serine protease HTRA1 (HTRA1) was confirmed in reverse assays. (degruyter.com)
The current study validated the cleavage activity of 3C protease in Escherichia coli and silkworm-BEVS systems by mixing the cell or fat body lysates of 3C protein and 3C site containing target protein in vitro . (silverchair.com)

The transcriptional coactivator Yes-associated protein (YAP) has been demonstrated to interact with and to enhance p73-dependent apoptosis in response to DNA damage. (ox.ac.uk)

These knockouts enable study of pathway redundancy, identification of subcellular function and characterization of the proteins themselves by providing a clean background in which mutants can be expressed. (horizondiscovery.com)

It is generated by proteolytic cleavage of precursor proteins in which it is fused either to itself, constituting a polyubiquitin precursor of head-to-tail monomers, or as a single N-terminal moiety to ribosomal proteins. (123dok.net)

Promyelocytic leukemia nuclear bodies regulate posttranslational modifications of partner proteins (e.g. (bvsalud.org)
In keeping with membrane association, biotin id (BioID) revealed connections between SENP2 and endoplasmic reticulum, Golgi, and internal nuclear membrane-associated protein. (conferencedequebec.org)
The SP100 protein, together with PML, represents a major constituent of the PML-SP100 nuclear bodies (NBs). (st-andrews.ac.uk)

An affinity tag, generally a relatively small sequence of amino acids, is basically a molecular leash for your protein. (addgene.org)

The activated ubiquitin is then transferred via a transesterification reaction to a cysteine residue in the active site of the E2 enzymes, which finally transfers the activated ubiquitin moiety to an amino group of the target protein. (amerigoscientific.com)

Utility of these systems broadly correlates with evolutionary complexity: small animal models such as rodents and the fruit fly are appropriate for pharmacological modeling and cognitive/behavioral assessment, the roundworm Caenorhabditis elegans allows analysis of tissue-specific disease features, and unicellular organisms such as the yeast Saccharomyces cerevisiae and the bacterium Escherichia coli are ideal for molecular studies. (scienceopen.com)
Herein, we used the amenable yeast Saccharomyces cerevisiae to study whether ubiquitin facilitates the expression of the fused eL40 (Ubi1 and Ubi2 precursors) and eS31 (Ubi3 precursor) ribosomal proteins. (123dok.net)

The mechanism by which Ach down-regulates pSTAT1 is related to an enhanced interaction between IFNαR2 and USP18 that finally dysregulates the cross talk between the IFN receptor on the cell surface and STAT1. (nebraska.edu)

Dr. Lima's laboratory uses structural, biochemical, and functional analyses of molecules involved in RNA processing and protein modification with a focus on understanding how these pathways contribute to cell growth and disease. (mskcc.org)
A protein modification that effectively results from forming an adduct with ADP-ribose through formation of a glycosidic bond. (reactome.org)
A protein modification that effectively converts an L-serine residue to O-phospho-L-serine. (reactome.org)
O-linked β-N-acetylglucosamine modification of proteins is activated in post-ischemic brains of young but not aged mice: Implications for impaired functional recovery from ischemic stress. (duke.edu)

Homologues of PIAS proteins have been found in other eukaryotes, and several are listed below: Zimp/dPIAS in Drosophila melanogaster zfPIAS4a in zebrafish SIZ1 and SIZ2 in yeast PIAS proteins contribute to the control of gene expression, and may be considered transcriptional co-regulators. (wikipedia.org)
One function of PIAS proteins is to relocate transcriptional regulators to different compartments within the nucleus of the cell. (wikipedia.org)
Additionally, PIAS proteins are important transcriptional co-regulators of the JAK/STAT signaling pathway. (wikipedia.org)

RNA, or ribonucleic acid, has numerous functions in the cell including the ability to convey genetic information in a form called messenger RNA, which is read by ribosomes to make proteins. (mskcc.org)
Proteins are synthesized by ribosomes translating mRNA into polypeptide chains, which may then undergo modifications to form the mature protein product. (microbenotes.com)

In yeast cells and in neurons alphaSyn accumulation is cytotoxic, but little is known about its normal function or pathobiology. (scienceopen.com)
Here, we exploited mutation correction of iPS cells and conserved proteotoxic mechanisms from yeast to humans to discover and reverse phenotypic responses to α-synuclein (αsyn), a key protein involved in Parkinson's disease (PD). (scienceopen.com)

Enrichment analysis for protein localization showed that mainly intracellular and cell-associated interacting proteins were identified. (degruyter.com)

Previous studies have demonstrated that glycolysis inhibitors reduce the proliferation of non‑small cell lung cancer (NSCLC) cells by interfering with the aerobic glycolytic pathway. (spandidos-publications.com)

Modifiers range from small chemical moieties, such as phosphate groups, to proteins themselves as the modifier. (tamu.edu)
Phosphoryalation is the addition of one or more phosphate groups to the protein. (microbenotes.com)

To investigate the functional significance of this interaction, we expressed green fluorescent protein fusion constructs encoding defined fragments of titin's M-line region and MURF-1 in cardiac myocytes. (rupress.org)

In response to low temperature, many biochemical and physiological processes change in plants through regulation of cold responsive (COR) gene expression as well as through posttranslational protein modifications. (biomedcentral.com)

In exploring the functional relationships between NBs and chromatin, we have shown previously that SP100 interacts with members of the HP1 family of nonhistone chromosomal proteins and that a variant SP100 cDNA encodes a high-mobility group (HMG1/2) protein. (st-andrews.ac.uk)

Protein tags are usually smallish peptides incorporated into a translated protein. (addgene.org)
Subsequently, the ubiquitin-labeled target protein is recognized by the proteasome and eventually degraded into small peptides. (amerigoscientific.com)

The RNA exosome is composed of many protein subunits that assemble into a unique arrangement capable of binding and degrading targeted RNA molecules. (mskcc.org)

E1 enzymes activate ubiquitin (Ub) and ubiquitin-like (Ubl) proteins in two steps by carboxy-terminal adenylation and thioester bond formation to a conserved catalytic cysteine in the E1 Cys domain. (rcsb.org)
Initially, ubiquitin is conjugated in an ATP-requiring reaction to E1 enzymes via a thioester bond. (amerigoscientific.com)

Here we used an affinity-purification mass spectrometry-based (AP-MS) approach to identify novel and particularly intracellular sGAG-interacting proteins in human bone marrow stromal cells (hBMSC). (degruyter.com)
Various fusion tags facilitate protein purification, leaving the potential risk to influence the target protein's biological activity negatively. (silverchair.com)
We also achieved the glutathione-S-transferase (GST) tag-cleaved product of the VP15 protein from the White spot syndrome virus after purification, suggesting that we successfully established a coinfection-based recognition-and-reaction BEVS platform for the tag-free protein engineering. (silverchair.com)
Protein expression and purification have become an essential technology to uncover the protein-involved mechanisms and to produce pharmaceutically relevant products, such as vaccines and drugs [ 1-3 ]. (silverchair.com)
After several decades of trying to address these challenges, researchers have amassed a considerable molecular tool box of tags and fusion proteins to aid in the expression and purification of recombinant proteins. (addgene.org)
Though there are a number of chemical and peptide-based proteosome inhibitors, glutathione S-transferase (GST), which can be fused to recombinant proteins for one-step purification with glutathione, can also protect against proteolysis. (addgene.org)

Small ubiquitin-related modifier 4 is a protein that in humans is encoded by the SUMO4 gene . (wn.com)

Sp100 protein). (bvsalud.org)

Apart from PIAS1, each gene encodes two protein isoforms. (wikipedia.org)

Post-translational modifications refer to any alteration in the amino acid sequence of the protein after its synthesis. (microbenotes.com)
We conclude that ubiquitin might serve as a cis-acting molecular chaperone that assists in the folding and synthesis of the fused eL40 and eS31 ribosomal proteins. (123dok.net)
Faulty or damaged proteins are recognized and rapidly degraded within the cells, thereby eliminating the consequences of errors in protein synthesis. (amerigoscientific.com)

PTEN is a protean protein with a dual-specificity cytosolic lipid and tyrosine phosphatase activity. (biomedcentral.com)

The encoded protein is part of the structural maintenance of chromosomes (SMC) 5/6 complex which plays a key role genome maintenance, facilitating chromosome segregation and suppressing mitotic recombination. (nih.gov)

Homologues of PIAS proteins have been found in other eukaryotes, including Zimp/dPIAS in Drosophila melanogaster and zfPIAS4a in zebrafish. (wikipedia.org)
Eukaryotes and some bacteria deploy proteosomes to degrade what the cell might consider junk protein. (addgene.org)
Understanding the role of the ubiquitin fused to ribosomal proteins becomes relevant, as these proteins are practically invariably eS31 and eL40 in the different eukaryotes. (123dok.net)
In most eukaryotes studied, ubiquitin is encoded by two classes of genes: (i) The first comprises genes coding for a single copy of ubiquitin fused to ribosomal proteins (r-proteins), most commonly eL40 and eS31. (123dok.net)

It may involve modifying the amino acid side chain, terminal amino or carboxyl group using covalent or enzymatic means following protein biosynthesis. (microbenotes.com)

When a chain of ubiquitin proteins is attached to a protein, the protein is recognized and destroyed by a complex of enzymes called a proteasome. (medlineplus.gov)

In addition to ubiquitin, there are several ubiquitin-like proteins (UBLs) that can also be conjugated to and alter the function of substrate proteins. (amerigoscientific.com)

The COOH-terminal A168-170 region of the giant sarcomeric protein titin interacts with muscle-specific RING finger-1 (MURF-1). (rupress.org)

Apart from signal peptide, some polypeptide sequence of the protein is also cleaved resulting in the final sequence. (microbenotes.com)

The known functions of these domains and motifs are similar among all PIAS protein family members. (wikipedia.org)

Three types of enzymes are required to ubiquitination process of proteins. (amerigoscientific.com)

The seven proteins that belong to the mammalian PIAS family are encoded by four genes: PIAS1, PIAS2 (PIASx), PIAS3, and PIAS4 (PIASy). (wikipedia.org)
The table below lists the seven known proteins that belong to the mammalian PIAS protein family. (wikipedia.org)
UBLs are a family of proteins that have similar three-dimensional structures and related sequences to ubiquitin. (amerigoscientific.com)

Anatomy3

Organisms2

Chemicals and Drugs40

Analytical, Diagnostic and Therapeutic Techniques and Equipment4

Phenomena and Processes17

Information Science2

Health Care1

SUMO38

SUMOylation11

Target proteins3

Ligases2

SUMO22

Degradation7

Binds4

Conjugation2

Ribosomal protein1

Eukaryotic4

Cellular6

Enzyme4

Transcription5

Motif4

Residues3

Recombinant protein2

Post-translationa1

Genes encode1

Phosphorylation6

SMT31

Activates1

Isopeptide1

Protease2

Apoptosis1

Subcellular1

Precursor proteins1

Nuclear3

Amino acids1

Moiety1

Saccharomyces2

Regulates1

Modification4

Transcriptional3

Ribosomes2

Yeast2

Localization1

Pathway1

Phosphate groups2

Interaction1

Posttranslational1

Chromatin1

Peptides2

Molecules1

Thioester2

Purification6

Humans1

Sp1001

Gene encodes1

Synthesis3

Tyrosine1

Chromosome segregation1

Eukaryotes4

Enzymatic1

Enzymes called1

Substrate1

Interacts1

Polypeptide1

Motifs1

Ubiquitination1

Family3