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*  The N-end rule pathway is a proteolytic system where its recognition - Role of adrenergic receptors in human coronary vasomotion
The N-end rule pathway is a proteolytic system where its recognition components (N-recognins) recognize destabilizing N-terminal residues of short-lived proteins as an important part of specific degrons called N-degrons. like a scaffold E3 that promotes HR6B/UbcH2-reliant ubiquitylation of H2A and H2B however not H3 and H4 via a system distinct from normal polyubiquitylation. The E3 activity of UBR2 in histone ubiquitylation is activated by dipeptides bearing destabilizing N-terminal residues allosterically. Insufficient monoubiquitylation and polyubiquitylation on UBR2-lacking meiotic chromosomes correlate to problems in dual strand break (DSB) restoration along with other meiotic procedures leading to pachytene arrest at stage IV and apoptosis. A few of these features of UBR2 are found in somatic cells where UBR2 is really a chromatin-binding proteins involved in chromatin-associated ubiquitylation upon DNA damage. UBR2-deficient somatic cells show an array of chromosomal ...
http://researchreportone.com/?p=2433
*  SIAH E3 Ubiquitin Protein Ligase Family, Member 1 - CAGS
The SIAH1 gene encodes a RING-type E3 ubiquitin ligase belonging to the Seven in Absentia Homolog (SIAH) family. The enzyme carries out the ubiquitination of a wide variety of targets, either by direct binding or by acting as the essential RING domain subunit for larger E3 ubiquitin ligase complexes. By carrying out its function, the protein marks its targets for proteasomal degradation. Target substrates of SIAH1 include transcription regulators such as ELL2, MYB, POU2AF1, PML and RBBP8, the signal transduction molecules TIEG1 and NUMB, the cell surface receptor DCC and the anti-aopoptotic protein BAG1. It also ubiquitinates SYP, a protein involved in synaptic vesicle function in neurons. The protein is thus involved in the regulation of several key biological processes such as apoptosis, axon guidance, cell cycle, spermatogenesis and nervous system development. ...
http://cags.org.ae/ctga/details.aspx?id=2441
*  UBR4 (ubiquitin protein ligase E3 component n-recognin 4)
... , Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.
http://atlasgeneticsoncology.org/Genes/GC_UBR4.html
*  UBR5 (ubiquitin protein ligase E3 component n-recognin 5)
... , Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.
http://atlasgeneticsoncology.org/Genes/GC_UBR5.html
*  Anti-Human Parkin Antibody | Human Parkin Antibody | Parkin Antibody
Parkin is encoded by the PARK2 gene in humans; its precise function is unknown. However, it is known to be part of a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. The ubiquitin-tagged proteins are then degraded by ubiquitin-proteasome complexes. Mutations in the PARK2 gene are associated with familial and autosomal recessive juvenile forms of Parkinson disease. It has been suggested that loss of function of the parkin protein leads to dopaminergic cell death, but the mechanism is not clear. Parkin is also known as Parkinson protein 2, E3 ubiquitin protein ligase; Parkinson disease (autosomal recessive, juvenile) 2, parkin; E3 ubiquitin-protein ligase parkin, Parkinson disease protein 2, PDJ, PRKN, ...
http://www.clontech.com/US/Products/Cell_Biology_and_Epigenetics/Brain_and_CNS/Parkin?sitex=10020:22372:US&PEBCL1=VLEPFh7Mdl7opBauxkgsoB8I96&PEBCL1_pses=ZGBA2BF6594C3443A4EF078C272CF6E69E776C772C42F00223804777CEFEA668F9BE415A1C01503FFC42B93B65C373766D48F61CA7A67670D2
*  Anti-Human Parkin Antibody | Human Parkin Antibody | Parkin Antibody
Parkin is encoded by the PARK2 gene in humans; its precise function is unknown. However, it is known to be part of a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. The ubiquitin-tagged proteins are then degraded by ubiquitin-proteasome complexes. Mutations in the PARK2 gene are associated with familial and autosomal recessive juvenile forms of Parkinson disease. It has been suggested that loss of function of the parkin protein leads to dopaminergic cell death, but the mechanism is not clear. Parkin is also known as Parkinson protein 2, E3 ubiquitin protein ligase; Parkinson disease (autosomal recessive, juvenile) 2, parkin; E3 ubiquitin-protein ligase parkin, Parkinson disease protein 2, PDJ, PRKN, ...
http://www.clontech.com/US/Products/Cell_Biology_and_Epigenetics/Brain_and_CNS/Parkin?sitex=10020:22372:US&PEBCL1=lCwf69edpZwYmj2bnPlIqspoiK&PEBCL1_pses=ZG2ED0338CB8FB9AD2E4FFA1B47BFA0877762259441549A3B17291289F0E0A4FDC04EA318A1591AC68A59CCAA0EC3A875FBC966282464175FD
*  Anti-Human Parkin Antibody | Human Parkin Antibody | Parkin Antibody
Parkin is encoded by the PARK2 gene in humans; its precise function is unknown. However, it is known to be part of a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. The ubiquitin-tagged proteins are then degraded by ubiquitin-proteasome complexes. Mutations in the PARK2 gene are associated with familial and autosomal recessive juvenile forms of Parkinson disease. It has been suggested that loss of function of the parkin protein leads to dopaminergic cell death, but the mechanism is not clear. Parkin is also known as Parkinson protein 2, E3 ubiquitin protein ligase; Parkinson disease (autosomal recessive, juvenile) 2, parkin; E3 ubiquitin-protein ligase parkin, Parkinson disease protein 2, PDJ, PRKN, ...
http://www.clontech.com/US/Products/Cell_Biology_and_Epigenetics/Brain_and_CNS/Parkin?sitex=10020:22372:US&PEBCL1=rX5QrxTuaDDNuwzpI232mi18nV&PEBCL1_pses=ZG5543D5900D5479633E8127EEF0673DDBD5539FC2F35D30F6BB0502DFFE0DB35BE24B22B5E0F05B91C81162DA56B87946D02E890C6F5D4E8F
*  Anti-Human Parkin Antibody | Human Parkin Antibody | Parkin Antibody
Parkin is encoded by the PARK2 gene in humans; its precise function is unknown. However, it is known to be part of a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. The ubiquitin-tagged proteins are then degraded by ubiquitin-proteasome complexes. Mutations in the PARK2 gene are associated with familial and autosomal recessive juvenile forms of Parkinson disease. It has been suggested that loss of function of the parkin protein leads to dopaminergic cell death, but the mechanism is not clear. Parkin is also known as Parkinson protein 2, E3 ubiquitin protein ligase; Parkinson disease (autosomal recessive, juvenile) 2, parkin; E3 ubiquitin-protein ligase parkin, Parkinson disease protein 2, PDJ, PRKN, ...
http://www.clontech.com/US/Products/Cell_Biology_and_Epigenetics/Brain_and_CNS/Parkin?sitex=10020:22372:US&PEBCL1=uJjJljFAWUmSNl6BtwIXXb5TkO&PEBCL1_pses=ZG41C1DEB1A751C5526702B7BF06D1178F208D945EB6B11C1F09BD2E5FA419514957022FB205C38736B4DFD2F32C2BABFBD7EFA09A25CE45B7
*  Plus it
Attempts to target mutant KRAS have been unsuccessful. Most of the current therapeutic approaches are indirect, mainly via inhibiting KRAS down-stream signaling, which have been marginally successful. Here we report the identification of Smad ubiquitination regulatory factor 2 (SMURF2), a HECT-type ubiquitin ligase (E3) as a critical regulator of mutant KRAS protein stability. We show that the loss of SMURF2 either by si-/sh-RNA mediated gene silencing or by overexpression of a catalytically inactive SMURF2 Cys716Ala (CA) mutant, can cause lysosome-mediated KRAS degradation; whereas, overexpression of wild type SMURF2 enhances KRAS protein stability. Most importantly, we found that mutant KRAS protein is more susceptible to SMURF2 alterations in that mutant protein half-life decreased from ,12h in control siRNA-treated cells to ,3h with Smurf2 siRNA treatment, whereas only marginal differences were noted for ...
http://mcr.aacrjournals.org/content/12/12_Supplement/B48
*  Ubiquitin Ligase RNF5 | Ronai Lab
RNF5 (RING finger domain E3 ligase), also known as RMA1, is an membrane anchored (ER and/or mitochondria) E3 ubiquitin ligase. Anchored to the ER membrane via a single transmembrane-spanning domain located within the C-terminal region, RNF5 also consists of a RING domain, and a formin-like homology domain.. RNF5 emerges as a regulator of ER Associated Degradation (ERAD), and as part of the greater ER stress response that specializes in the degradation of misfolded proteins. RNF5 contributes to control of autophagy, glutamine metabolism as well as in cytoskeletal organization. The following summarizes key observations for RNF5. By mediating ubiquitination of paxillin, RNF5 affects cell motility.. RNF5 is deregulated in Inclusion Body Myocytis (IBM) - a muscle disorder. Transgenic RNF5 mice exhibit phenotypes that resemble IBM and samples from IBM patients exhibit deregulation of RNF5 expression.. RNF5 regulates a 7 transmembrane protein, ...
http://ronailab.net/research-projects/the-ubiquitin-ligase-rnf5.html
*  June 2016 - Page 2 - Polo-Like Kinases and Aurora Kinases in Cancer Therapy
E3 ubiquitin ligases have a significant role in carcinogenesis and include a large family of proteins that catalyze the ubiquitination of many protein substrates for targeted degradation by the 26S proteasome. ubiquitin ligases for GC are discussed IPI-493 in the review. (a very interesting new gene) fingers IPI-493 and U-box domains[21]. There are about 30 proteins containing the HECT domain. The fingers and U-box quitin ligases contain the new gene (finger domain but only a small part functions as an E3 ubiquitin ligase. Unlike RING proteins most HECT proteins if not all are believed to function as E3 ubiquitin ligases. RING and HECT E3 ubiquitin ligases use different catalytic mechanisms to promote the transfer of ...
http://technumber.com/2016/06/page/2/
*  Antibody Development for Modified Parkin Proteins Identified in the Human Brain | Parkinson's Disease
The PARK2 gene encodes the Parkin protein. It is one of three genes that protect from young-onset Parkinson disease (PD); in Parkin's absence, symptoms and signs usually begin before the age of forty. Despite the gene's discovery in 1998 by Kitada et al., few Parkin-specific antibodies exist. The antibodies available do not readily detect specific, modified forms of Parkin and higher-order variants that are found in the human brain. The lack of variant-specific tools has limited progress and understanding of Parkin's functions in the human brain in both healthy and diseased states.. Hypothesis: ...
https://www.michaeljfox.org/foundation/grant-detail.php?grant_id=1568
*  Difference between revisions of "CH391L/S2013 Alesha Stewart Feb 13 2013" - OpenWetWare
The parkin gene, PARK2, contains 12 exons and 1.5 Mb [2]. PARK2 is located on a region of chromosome 6 that is known to be fragile and unstable; making it prone to mutations and deletions [1]. Genetically acquiring a mutation in PARK2 can lead to developing early onset autosomal recessive Parkinson's Disease (PD). The protein is an E3 ubiquitin ligase, which functions as a component of the ubiquitin proteasome degradation system. It consists of 465 amino acids, an ubiquitin-like domain, and two RING finger domains [1]. Ubiquitination (and polyubiquitination) marks proteins to be degraded by the proteasome. Mutations of parkin can result in the loss of this function and endanger the cell. Studies have shown that improper protein degradation can cause a build-up of parkin substrates and neuronal death of the cells producing dopamine. Mitochondrion function and integrity is ...
https://openwetware.org/wiki/?title=CH391L/S2013_Alesha_Stewart_Feb_13_2013&curid=130341&diff=0&oldid=677558
*  HERC4 - Probable E3 ubiquitin-protein ligase HERC4 - Homo sapiens (Human) - HERC4 gene & protein
Probable E3 ubiquitin-protein ligase involved in either protein trafficking or in the distribution of cellular structures. Required for spermatozoon maturation and fertility, and for the removal of the cytoplasmic droplet of the spermatozoon. E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer it to targeted substrates.
http://www.uniprot.org/uniprot/Q5GLZ8
*  Trim56 - E3 ubiquitin-protein ligase TRIM56 - Mus musculus (Mouse) - Trim56 gene & protein
E3 ubiquitin-protein ligase that plays a key role in innate antiviral immunity. In response to pathogen- and host-derived double-stranded DNA (dsDNA), targets TMEM173/STING to 'Lys-63'-linked ubiquitination, thereby promoting its homodimerization, a step required for the production of type I interferon IFN-beta. Independently of its E3 ubiquitin ligase activity, positive regulator of TLR3 signaling. Potentiates extracellular double stranded RNA (dsRNA)-induced expression of IFNB1 and interferon-stimulated genes ISG15, IFIT1/ISG56, CXCL10, OASL and CCL5/RANTES (By similarity).
http://www.uniprot.org/uniprot/Q80VI1
*  Mitochondrial Contagion Induced by Parkin Deficiency in Drosophila Hearts and Its Containment by Suppressing MitofusinNovelty...
Here, we show that cardiomyocyte Parkin is essential to mitochondrial and cardiac hemostasis in Drosophila. This warrants re-evaluation of the notion, derived from absence of a basal cardiac phenotype in parkin null mice,16 that Parkin is dispensable to normal heart function. By interrogating genetic epistasis between Drosophila Parkin and mitofusin (MARF), we uncover a completely new mechanism for end-organ dysfunction produced by Parkin insufficiency: ongoing mitochondrial fusion contributes to mitochondrial contagion when Parkin signaling (and presumably Parkin-dependent mitophagic elimination of abnormal organelles) is impaired. These findings suggest that general mitochondrial health and end-organ function could be preserved in mitophagically impaired tissues through chronic suppression of fusion-induced mitochondrial contamination.. The PINK1-Parkin interaction is central to mitophagic quality control in most tissues, but published studies provide an inconsistent picture of the role of ...
http://circres.ahajournals.org/content/114/2/257
*  In absentia health care - Wikipedia
The most common mode of healthcare delivery is through personal, face-to-face contact between a healthcare provider and a beneficiary (patient). There is, however, an increasing trend towards the provision of healthcare in the absence of personal contact. This limit of contact during patient care is known as 'in absentia health care'. In Absentia healthcare, or distance medicine, occurs when the patient and care giver are at different locations, but still communicate by audio and video, or sometimes without any personal contact. A face-to-face contact is often a necessary prelude to rendering health care. This, however, may not be necessary for care; in fact current technologies permit with no prior or concurrent contact.[1][2] Some people argue that this type of in absentia medical care may derail the traditional sequences of examination, diagnosis and treatment, and that such a detour may challenge existing values of modern medicine. In absentia care assumes heightened relevance today because ...
https://en.wikipedia.org/wiki/In_absentia_health_care
*  Characterization of the novel role of parkin in Gliomagenesis | ScholarBank@NUS
Mutations in the parkin gene, which encodes a ubiquitin ligase, has been implicated as one of causative factor for genetic parkinsonism. Interestingly, parkin role has also been implicated in cancer as a putative tumor suppressor with the gene been frequently targeted by deletion and inactivation in several human malignant tumors. Here, we demonstrated a potential tumor suppressor role for parkin in gliomas. We found that parkin expression was dramatically reduced in glioma cells and that the restoration of parkin expression promoted G1 phase cell-cycle arrest and mitigated the proliferation rate of glioma cells in vitro and in vivo. Furthermore, parkin-expressing glioma cells showed a reduction in levels of cyclin D1, but not cyclin E, and a selective downregulation of Akt serine-473 phosphorylation and VEGF receptor levels. In accordance, cells derived from a parkin-null mouse model exhibited increased levels of cyclin D1, VEGF receptor, and Akt phosphorylation, and divided significantly ...
http://scholarbank.nus.edu.sg/handle/10635/33346
*  NEDD4-like E3 ubiquitin-protein ligase elisa and antibody
Shop NEDD4-like E3 ubiquitin-protein ligase ELISA Kit, Recombinant Protein and NEDD4-like E3 ubiquitin-protein ligase Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
https://www.mybiosource.com/protein_family.php?root=nedd4-like-e3-ubiquitin-protein-ligase
*  PLOS ONE: A U-Box E3 Ubiquitin Ligase, PUB20, Interacts with the Arabidopsis G-Protein β Subunit, AGB1
An Arabidopsis U-box E3 ubiquitin ligase Plant U-box 20 (PUB20; alternatively called AtCMPG1) was identified as a possible interactor of the Arabidopsis G-protein β subunit, AGB1, by yeast two-hybrid screening. A bimolecular fluorescence complementation (BiFC) assay showed that PUB20 interacted with AGB1 in the nuclei and the cytosol. The expression levels of PUB20 and its closest homolog, PUB21 were stable under many conditions. GUS driven by the PUB20 promoter was active in anthers, pollen, premature seeds and receptacles and GUS driven by the PUB21 promoter was active in anthers and funiculi. PUB20 was found to have autoubiquitination activity in vitro.
http://journals.plos.org/plosone/article/comments?id=10.1371/journal.pone.0049207
*  Rnf8 - E3 ubiquitin-protein ligase RNF8 - Rattus norvegicus (Rat) - Rnf8 gene & protein
E3 ubiquitin-protein ligase that plays a key role in DNA damage signaling via 2 distinct roles: by mediating the 'Lys-63'-linked ubiquitination of histones H2A and H2AX and promoting the recruitment of DNA repair proteins at double-strand breaks (DSBs) sites, and by catalyzing 'Lys-48'-linked ubiquitination to remove target proteins from DNA damage sites. Following DNA DSBs, it is recruited to the sites of damage by ATM-phosphorylated MDC1 and catalyzes the 'Lys-63'-linked ubiquitination of histones H2A and H2AX, thereby promoting the formation of TP53BP1 and BRCA1 ionizing radiation-induced foci (IRIF). Also controls the recruitment of UIMC1-BRCC3 (RAP80-BRCC36) and PAXIP1/PTIP to DNA damage sites. Also recruited at DNA interstrand cross-links (ICLs) sites and catalyzes 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20 and Fanconi ...
http://www.uniprot.org/uniprot/Q4KLN8
*  JADE2 - E3 ubiquitin-protein ligase Jade-2 - Homo sapiens (Human) - JADE2 gene & protein
Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo (PubMed:16387653). Acts as a E3 ubiquitin-protein ligase mediating the ubiquitination and subsequent proteasomal degradation of target protein histone demethylase KDM1A (PubMed:25018020). Also acts as a ubiquitin ligase E3 toward itself. Positive regulator of neurogenesis (By similarity).
http://www.uniprot.org/uniprot/Q9NQC1
*  E3 ubiquitin-protein ligase RNF4
E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation ...
https://pharos.nih.gov/idg/targets/P78317
*  RNF152 - E3 ubiquitin-protein ligase RNF152 - Homo sapiens (Human) - RNF152 gene & protein
E3 ubiquitin-protein ligase mediating 'Lys-63'-linked polyubiquitination of RRAGA in response to amino acid starvation. Thereby, regulates mTORC1 signaling and plays a role in the cellular response to amino acid availability (PubMed:25936802). Also mediates 'Lys-48'-linked polyubiquitination of target proteins and their subsequent targeting to the proteasome for degradation. Induces apoptosis when overexpressed (PubMed:21203937).
http://www.uniprot.org/uniprot/Q8N8N0
*  Ubiquitin‐Activated Interaction Traps (UBAITs) identify E3 ligase binding partners | EMBO Reports
In vitro and in vivo results presented here validate Ubiquitin‐Activated Interacting Traps (UBAITs) as useful tools for identification of substrates and other interacting proteins for both HECT and RING ubiquitin ligases. While the approach was conceived to be specific for HECT ubiquitin ligases (e.g., Rsp5 and Itch), the lack of dependence on the active‐site cysteine suggested that the same approach could be applied to RING ubiquitin ligases, and this was validated with three different RING E3s (Psh1, RNF126, and RNF168). Furthermore, the RNF168 UBAIT identified histone H2AZ as a new target of this E3.. Thirty percent of the proteins that were isolated with the Rsp5 UBAIT and passed filtering criteria were known Rsp5‐interacting proteins, and these represented approximately 32% of all proteins reported to interact with Rsp5 ...
http://embor.embopress.org/content/16/12/1699