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NOL3 (nucleolar protein 3 (apoptosis repressor with CARD domain))

Written2009-05Gloria Kung, Wendy McKimpson, Richard N Kitsis
Department of Medicine, Department of Cell Biology, Montefiore-Einstein Center for Cardiovascular Research, Albert Einstein Cancer Center, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461 USA

(Note : for Links provided by Atlas : click)

Identity

Alias_namesnucleolar protein 3 (apoptosis repressor with CARD domain)
Alias_symbol (synonym)ARC
NOP30
MYP
CARD2
Other aliasARC (Apoptosis Repressor with CARD)
NOP
HGNC (Hugo) NOL3
LocusID (NCBI) 8996
Atlas_Id 41552
Location 16q22.1  [Link to chromosome band 16q22]
Location_base_pair Starts at 67173853 and ends at 67175737 bp from pter ( according to hg19-Feb_2009)  [Mapping NOL3.png]
Fusion genes
(updated 2017)		Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
NOL3 (16q22.1) / MICAL2 (11p15.3)NOL3 (16q22.1) / NOL3 (16q22.1)NOL3 (16q22.1) / PLEKHA2 (8p11.22)
NOL3 (16q22.1) / TG (8q24.22)RPRD1B (20q11.23) / NOL3 (16q22.1)
Note The correct name for the locus is NOL3. Sometimes, however, the gene is referred to by names of the putative encoded proteins:
  • ARC (Apoptosis Repressor with CARD) CARD denotes a Caspase Recruitment Domain. The ARC protein resides in the cytoplasm and nucleoplasm, not nucleolus.
  • MYP is an older name for ARC that is currently not used. References to this locus as MYC are incorrect and probably represent typographical errors of MYP. NOL3 is distinct from any of the myc loci.
  • NOP30. In some species, alternative splicing gives rise to a transcript encoding a putative protein NOP30, rather than ARC. When the cDNA for NOP30 is expressed exogenously, the resulting protein is predominantly nucleolar - hence the origin of the gene name: nucleolar protein 3. Importantly, however, endogenous NOP30 protein has not been demonstrated in any cells of any species.

    • DNA/RNA

     
      The NOL3 gene is located on the long arm of human chromosome 16. The gene consists of 4 small exons (exons denoted above as thick boxes) and 3 small introns. The translational start site is in exon 2. Alternative splicing occurs between exons 2 and 3. This involves two splice donors separated by 10 nucleotides in exon 2 connecting to a single splice acceptor in exon 3 (Stoss et al., 1999). Because the separation between the splice donors, 10 nucleotides, is not an exact multiple of 3, alternative splicing results in two open reading frames distal to the splice acceptor. Because of this frame shift, the C-terminus of the two encoded proteins differ as do their stop codons, each of which is in exon 4. One transcript is translated into ARC (Apoptosis Repressor with CARD (Caspase Recruitment Domain)) (Koseki et al., 1998). MYP is an earlier name for ARC that is no longer in use (Geertman et al., 1996). The other transcript encodes a putative protein called NOP30 (Nucleolar Protein of 30 kD). ARC and putative NOP30 proteins share a common N-terminus containing the CARD. Their C-termini differ, however, with ARC containing multiple P/E repeats (acidic) and putative NOP30 containing R/S repeats (basic). While ARC transcripts are present in a variety of human and mouse cell types, NOP30 transcripts are present in human, but not mouse (L. Wu and R. Kitsis, unpublished). Endogenous ARC protein resides in the cytoplasm and nucleoplasm of certain human and mouse cell types (discussed below). In contrast, the existence of endogenous NOP30 protein has not been demonstrated in any cell type of any species. When the cDNA encoding NOP30 is exogenously expressed, the encoded protein is in the nucleolus and nucleoplasm (Stoss et al., 1999).
    Description The NOL3 gene is located on human chromosome 16q21-23. The gene contains 4 exons and 3 introns spanning 1757 bp.
    Transcription The coordinate of the first nucleotide of exon 1 is 65,765,371 bp from pter, and that of the last nucleotide of exon 4 is 65,767,127 bp. Alternative splicing takes place between exons 2 and 3. In exon 2, the splice donor of the NOP30 transcript is 10 bp upstream of the splice donor of the ARC transcript. Both transcripts use a common splice acceptor in exon 3.

    Protein

    Note The start of translation is in exon 2 (prior to the alternative splice donors). Alternative splicing causes a frame shift resulting in transcripts encoding proteins with different C-termini and separate stop codons in exon 4. The stop codon for ARC is 43 bp upstream of that of NOP30.
     
      Alternatively spliced transcripts of NOL3 lead to two different proteins, ARC (blue) and NOP30 (red). These proteins each contain an N-terminal CARD (first 95 amino acids identical), but have different C-termini. The C-terminus of ARC is rich in prolines and glutamic acids, whereas the C-terminus of NOP30 is rich in serines and arginines.
    Description Human ARC protein contains 208 amino acids with Mr 22,629 Da. The protein usually runs at a slower mobility on SDS-PAGE most likely due to the enrichment of proline residues in the C-terminal domain. NOP30 contains 219 amino acids with Mr 24,327 Da.
    Expression Under normal conditions, ARC mRNA and protein is present predominantly in cardiac myocytes, skeletal myocytes, and neurons (Koseki et al., 1998; Abmayr et al., 2004; Geertman et al., 1996; Engidawork et al., 2001). ARC protein is also markedly increased in primary human epithelial cancers of the breast, colon, ovary, and cervix (Mercier et al., 2005; Mercier et al., 2008). NOP30 transcripts are present in some human cell types but have not been detected in mouse cells. Endogenous NOP30 protein has not been demonstrated in cells of any species.
    Localisation Endogenous ARC protein is present in the cytoplasm and nucleoplasm (Mercier et al., 2005). As above, the localization of endogenous NOP30 protein has not been investigated. Exogenously expressed NOP30 protein localizes in the nucleolus and nucleoplasm.
    Function The function of endogenous NOP30 is not known. Exogenous NOP30 interacts with SFRS9/SRp30C and NPM1 and may influence splicing (Stoss et al., 1999).
    ARC is an endogenous inhibitor of apoptosis that is unique in its ability to antagonize both the extrinsic (death receptor) and the intrinsic (mitochondria/ER) death pathways (Nam et al., 2004; Gustafsson et al., 2004; Koseki et al., 1998). ARC inhibits the extrinsic pathway by interfering with DISC (Death Inducing Signaling Complex) formation. This is accomplished by the direct interaction of the ARC CARD with the death domains (DD) of Fas and FADD, and with the death effector domain (DED) of procaspase-8. These death-fold interactions are novel in that they are heterotypic in contrast to the usual homotypic death-fold interactions. ARC inhibits the intrinsic pathway through at least two mechanisms. First, the direct interaction between the ARC CARD and the C-terminus of Bax inhibits death stimulus-induced Bax conformational activation and translocation to the mitochondria. Second, direct interaction between the ARC C-terminal domain with the p53 tetramerization domain inhibits p53 tetramerization (Foo et al., PNAS, 2007). This, in turn, disables p53 transcriptional function and exposes a p53 nuclear export signal that relocates p53 to the cytoplasm.

    Nothing is known about the regulation of NOP30.
    The regulation of ARC is complex. ARC protein abundance decreases rapidly and dramatically in response to hypoxia and oxidative stress (e.g. ischemia-reperfusion) (Ekhterae et al., 1999; Neuss et al., 2001; Nam et al., 2007). These decreases result from increased degradation of ARC protein via the ubiquitin-proteasomal pathway (Nam et al., 2007). The E3 ligase MDM2 may play a role in ARC degradation in this scenario (Foo et al., JBC, 2007), but this role is probably indirect (L. Wu and R. Kitsis, unpublished data). Decreases in ARC protein abundance in response to hypoxia appear to be regulated by p53 repression of nol3 transcription (Li et al., 2008). Apart from ARC protein abundance, the activity of ARC is also regulated post-translationally: dephosphorylation of threonine 149 decreases the anti-apoptotic activity of ARC (Tan et al., 2008).

     
      Regulation of the extrinsic (death receptor) and intrinsic (mitochondria/ER) apoptosis pathways by ARC. Not shown are ARC interactions with and regulation of p53.
    Homology ARC is highly conserved among mammals. There is approximately 85% identity both at the amino acid and the nucleotide level among human, rat, mouse, dog, and bovine ARC. Interestingly, an ARC homolog has yet to be identified in Danio rerio, Drosophila melanogaster, or Caenorhabditis elegans.

    Implicated in

    Note
      
    Entity Epithelial cancers
    Disease Increased levels of ARC protein have been observed in the epithelium of primary human breast, colon, ovarian, and cervical cancers (Mercier et al., 2005; Mercier et al., 2008). Increased levels of both ARC RNA and protein have been observed in renal cell carcinoma (Heikaus et al., 2008).
    Prognosis ARC overexpression in a breast cancer cell line increases resistance to chemotherapy and radiation (Mercier et al., 2005; Wang et al., 2009). In a melanoma cell line, ARC overexpression causes increased resistance to endoplasmic reticulum stress-induced caspase-8 activation (Chen et al., 2008).
      
      
    Entity Myocardial infarction, myocardial ischemia-reperfusion
    Prognosis ARC plays an important role in regulating heart muscle damage during myocardial infarction. Endogenous ARC protein undergoes rapid proteasomal degradation during myocardial ischemia-reperfusion (Nam et al., 2007). This decrease in ARC abundance is causally linked with the subsequent cell death (Nam et al., 2004). Accordingly, transgenic overexpression of ARC in vivo decreases the size of myocardial infarctions (Gustafsson et al., 2002; Pyo et al., 2008; S. Jha and R. Kitsis, unpublished data). As would be predicted, knockout of ARC has been reported to result in larger infarcts (Donath et al., 2006). However, the aforementioned knockout studies were performed on only small numbers of mice on a mixed genetic background. Subsequent knockout studies involving large numbers of mice on several pure genetic backgrounds have not demonstrated larger infarcts in ARC-/- mice subjected to ischemia-reperfusion (J. Saurabh, S. Y. Ji, and R. Kitsis, unpublished data). This is probably due to the dramatic rapid degradation of ARC protein during reperfusion even in wild type mice (see above).
      
      
    Entity Heart failure
    Prognosis ARC protein levels decrease during heart failure. Moreover, knockout of ARC exacerbates pathological cardiac remodeling in response to hemodynamic overload, a model of heart failure (Donath et al., 2006).
      
      
    Entity Neuropathology (several individual entities)
    Prognosis The protein level of ARC is increased in the frontal cortex of patients with Alzheimer's disease (Engidawork et al., 2001). During ischemic injury of the brain, there is a decrease in ARC protein in hippocampal neurons (Hong et al., 2003). Other studies have also shown that caloric restriction increases expression of ARC in the brain (Shelke et al., 2003).
      

    Breakpoints

    Note Not known.

    Bibliography

    Characterization of ARC, apoptosis repressor interacting with CARD, in normal and dystrophin-deficient skeletal muscle.
    Abmayr S, Crawford RW, Chamberlain JS.
    Hum Mol Genet. 2004 Jan 15;13(2):213-21. Epub 2003 Nov 25.
    PMID 14645204
     
    Inhibition of endoplasmic reticulum stress-induced apoptosis of melanoma cells by the ARC protein.
    Chen LH, Jiang CC, Watts R, Thorne RF, Kiejda KA, Zhang XD, Hersey P.
    Cancer Res. 2008 Feb 1;68(3):834-42.
    PMID 18245485
     
    Apoptosis repressor with caspase recruitment domain is required for cardioprotection in response to biomechanical and ischemic stress.
    Donath S, Li P, Willenbockel C, Al-Saadi N, Gross V, Willnow T, Bader M, Martin U, Bauersachs J, Wollert KC, Dietz R, von Harsdorf R; German Heart Failure Network.
    Circulation. 2006 Mar 7;113(9):1203-12. Epub 2006 Feb 27.
    PMID 16505176
     
    ARC inhibits cytochrome c release from mitochondria and protects against hypoxia-induced apoptosis in heart-derived H9c2 cells.
    Ekhterae D, Lin Z, Lundberg MS, Crow MT, Brosius FC 3rd, Nunez G.
    Circ Res. 1999 Dec 9;85(12):e70-7.
    PMID 10590251
     
    Alteration of caspases and apoptosis-related proteins in brains of patients with Alzheimer's disease.
    Engidawork E, Gulesserian T, Yoo BC, Cairns N, Lubec G.
    Biochem Biophys Res Commun. 2001 Feb 16;281(1):84-93.
    PMID 11178964
     
    Ubiquitination and degradation of the anti-apoptotic protein ARC by MDM2.
    Foo RS, Chan LK, Kitsis RN, Bennett MR.
    J Biol Chem. 2007 Feb 23;282(8):5529-35. Epub 2006 Dec 2.
    PMID 17142834
     
    Regulation of p53 tetramerization and nuclear export by ARC.
    Foo RS, Nam YJ, Ostreicher MJ, Metzl MD, Whelan RS, Peng CF, Ashton AW, Fu W, Mani K, Chin SF, Provenzano E, Ellis I, Figg N, Pinder S, Bennett MR, Caldas C, Kitsis RN.
    Proc Natl Acad Sci U S A. 2007 Dec 26;104(52):20826-31. Epub 2007 Dec 17.
    PMID 18087040
     
    Cloning and characterization of cDNAs for novel proteins with glutamic acid-proline dipeptide tandem repeats.
    Geertman R, McMahon A, Sabban EL.
    Biochim Biophys Acta. 1996 May 2;1306(2-3):147-52.
    PMID 8634331
     
    Apoptosis repressor with caspase recruitment domain protects against cell death by interfering with Bax activation.
    Gustafsson AB, Tsai JG, Logue SE, Crow MT, Gottlieb RA.
    J Biol Chem. 2004 May 14;279(20):21233-8. Epub 2004 Mar 5.
    PMID 15004034
     
    Caspase-8 and its inhibitors in RCCs in vivo: the prominent role of ARC.
    Heikaus S, Kempf T, Mahotka C, Gabbert HE, Ramp U.
    Apoptosis. 2008 Jul;13(7):938-49.
    PMID 18516683
     
    Down-regulation of ARC contributes to vulnerability of hippocampal neurons to ischemia/hypoxia.
    Hong YM, Jo DG, Lee JY, Chang JW, Nam JH, Noh JY, Koh JY, Jung YK.
    FEBS Lett. 2003 May 22;543(1-3):170-3.
    PMID 12753927
     
    ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that interacts selectively with caspases.
    Koseki T, Inohara N, Chen S, Nunez G.
    Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):5156-60.
    PMID 9560245
     
    p53 initiates apoptosis by transcriptionally targeting the antiapoptotic protein ARC.
    Li YZ, Lu DY, Tan WQ, Wang JX, Li PF.
    Mol Cell Biol. 2008 Jan;28(2):564-74. Epub 2007 Nov 12.
    PMID 17998337
     
    ARC (apoptosis repressor with caspase recruitment domain) is a novel marker of human colon cancer.
    Mercier I, Vuolo M, Jasmin JF, Medina CM, Williams M, Mariadason JM, Qian H, Xue X, Pestell RG, Lisanti MP, Kitsis RN.
    Cell Cycle. 2008 Jun 1;7(11):1640-7. Epub 2008 Mar 19.
    PMID 18469522
     
    The apoptosis inhibitor ARC undergoes ubiquitin-proteasomal-mediated degradation in response to death stimuli: identification of a degradation-resistant mutant.
    Nam YJ, Mani K, Wu L, Peng CF, Calvert JW, Foo RS, Krishnamurthy B, Miao W, Ashton AW, Lefer DJ, Kitsis RN.
    J Biol Chem. 2007 Feb 23;282(8):5522-8. Epub 2006 Dec 1.
    PMID 17142452
     
    The apoptotic regulatory protein ARC (apoptosis repressor with caspase recruitment domain) prevents oxidant stress-mediated cell death by preserving mitochondrial function.
    Neuss M, Monticone R, Lundberg MS, Chesley AT, Fleck E, Crow MT.
    J Biol Chem. 2001 Sep 7;276(36):33915-22. Epub 2001 Jul 3.
    PMID 11438535
     
    Protection of cardiomyocytes from ischemic/hypoxic cell death via Drbp1 and pMe2GlyDH in cardio-specific ARC transgenic mice.
    Pyo JO, Nah J, Kim HJ, Chang JW, Song YW, Yang DK, Jo DG, Kim HR, Chae HJ, Chae SW, Hwang SY, Kim SJ, Kim HJ, Cho C, Oh CG, Park WJ, Jung YK.
    J Biol Chem. 2008 Nov 7;283(45):30707-14. Epub 2008 Sep 9.
    PMID 18782777
     
    Lifelong caloric restriction increases expression of apoptosis repressor with a caspase recruitment domain (ARC) in the brain.
    Shelke RR, Leeuwenburgh C.
    FASEB J. 2003 Mar;17(3):494-6. Epub 2003 Jan 2.
    PMID 12514107
     
    Alternative splicing determines the intracellular localization of the novel nuclear protein Nop30 and its interaction with the splicing factor SRp30c.
    Stoss O, Schwaiger FW, Cooper TA, Stamm S.
    J Biol Chem. 1999 Apr 16;274(16):10951-62.
    PMID 10196175
     
    Novel cardiac apoptotic pathway: the dephosphorylation of apoptosis repressor with caspase recruitment domain by calcineurin.
    Tan WQ, Wang JX, Lin ZQ, Li YR, Lin Y, Li PF.
    Circulation. 2008 Nov 25;118(22):2268-76. Epub 2008 Nov 10.
    PMID 19001025
     
    Apoptosis repressor with caspase recruitment domain contributes to chemotherapy resistance by abolishing mitochondrial fission mediated by dynamin-related protein-1.
    Wang JX, Li Q, Li PF.
    Cancer Res. 2009 Jan 15;69(2):492-500.
    PMID 19147562
     

    Citation

    This paper should be referenced as such :
    Kung, G ; McKimpson, W ; Kitsis, RN
    NOL3 (nucleolar protein 3 (apoptosis repressor with CARD domain))
    Atlas Genet Cytogenet Oncol Haematol. 2010;14(4):400-403.
    Free journal version : [ pdf ]   [ DOI ]
    On line version : http://AtlasGeneticsOncology.org/Genes/NOL3ID41552ch16q22.html

    External links

    Nomenclature
    HGNC (Hugo)NOL3   7869
    Cards
    AtlasNOL3ID41552ch16q22
    Entrez_Gene (NCBI)NOL3  8996  nucleolar protein 3
    AliasesARC; FCM; MYOCL1; MYP; 
    NOP; NOP30
    GeneCards (Weizmann)NOL3
    Ensembl hg19 (Hinxton)ENSG00000140939 [Gene_View]
    Ensembl hg38 (Hinxton)ENSG00000140939 [Gene_View]  ENSG00000140939 [Sequence]  chr16:67173853-67175737 [Contig_View]  NOL3 [Vega]
    ICGC DataPortalENSG00000140939
    TCGA cBioPortalNOL3
    AceView (NCBI)NOL3
    Genatlas (Paris)NOL3
    WikiGenes8996
    SOURCE (Princeton)NOL3
    Genetics Home Reference (NIH)NOL3
    Genomic and cartography
    GoldenPath hg38 (UCSC)NOL3  -     chr16:67173853-67175737 +  16q22.1   [Description]    (hg38-Dec_2013)
    GoldenPath hg19 (UCSC)NOL3  -     16q22.1   [Description]    (hg19-Feb_2009)
    GoldenPathNOL3 - 16q22.1 [CytoView hg19]  NOL3 - 16q22.1 [CytoView hg38]
    ImmunoBaseENSG00000140939
    Mapping of homologs : NCBINOL3 [Mapview hg19]  NOL3 [Mapview hg38]
    OMIM605235   614937   
    Gene and transcription
    Genbank (Entrez)AF043244 AF064599 AF064600 AK092623 AK294145
    RefSeq transcript (Entrez)NM_001185057 NM_001185058 NM_001276307 NM_001276309 NM_001276311 NM_001276312 NM_001276319 NM_003946
    RefSeq genomic (Entrez)
    Consensus coding sequences : CCDS (NCBI)NOL3
    Cluster EST : UnigeneHs.513667 [ NCBI ]
    CGAP (NCI)Hs.513667
    Alternative Splicing GalleryENSG00000140939
    Gene ExpressionNOL3 [ NCBI-GEO ]   NOL3 [ EBI - ARRAY_EXPRESS ]   NOL3 [ SEEK ]   NOL3 [ MEM ]
    Gene Expression Viewer (FireBrowse)NOL3 [ Firebrowse - Broad ]
    SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
    GenevestigatorExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
    BioGPS (Tissue expression)8996
    GTEX Portal (Tissue expression)NOL3
    Human Protein AtlasENSG00000140939-NOL3 [pathology]   [cell]   [tissue]
    Protein : pattern, domain, 3D structure
    UniProt/SwissProtO60936   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
    NextProtO60936  [Sequence]  [Exons]  [Medical]  [Publications]
    With graphics : InterProO60936
    Splice isoforms : SwissVarO60936
    PhosPhoSitePlusO60936
    Domaine pattern : Prosite (Expaxy)CARD (PS50209)   
    Domains : Interpro (EBI)CARD    DEATH-like_dom_sf   
    Domain families : Pfam (Sanger)CARD (PF00619)   
    Domain families : Pfam (NCBI)pfam00619   
    Domain families : Smart (EMBL)CARD (SM00114)  
    Conserved Domain (NCBI)NOL3
    DMDM Disease mutations8996
    Blocks (Seattle)NOL3
    PDB (RSDB)4UZ0   
    PDB Europe4UZ0   
    PDB (PDBSum)4UZ0   
    PDB (IMB)4UZ0   
    Structural Biology KnowledgeBase4UZ0   
    SCOP (Structural Classification of Proteins)4UZ0   
    CATH (Classification of proteins structures)4UZ0   
    SuperfamilyO60936
    Human Protein Atlas [tissue]ENSG00000140939-NOL3 [tissue]
    Peptide AtlasO60936
    HPRD05572
    IPIIPI00105916   IPI00216346   IPI00977318   
    Protein Interaction databases
    DIP (DOE-UCLA)O60936
    IntAct (EBI)O60936
    FunCoupENSG00000140939
    BioGRIDNOL3
    STRING (EMBL)NOL3
    ZODIACNOL3
    Ontologies - Pathways
    QuickGOO60936
    Ontology : AmiGOresponse to hypoxia  blood vessel remodeling  response to ischemia  RNA binding  death receptor binding  calcium ion binding  protein binding  nucleolus  mitochondrion  cytosol  mRNA splice site selection  RNA splicing  cardiac muscle cell apoptotic process  negative regulation of cardiac muscle cell apoptotic process  negative regulation of tumor necrosis factor-mediated signaling pathway  negative regulation of muscle atrophy  release of sequestered calcium ion into cytosol by sarcoplasmic reticulum  response to injury involved in regulation of muscle adaptation  membrane  sarcoplasmic reticulum  death effector domain binding  identical protein binding  cysteine-type endopeptidase inhibitor activity involved in apoptotic process  negative regulation of apoptotic process  protein complex oligomerization  negative regulation of necrotic cell death  caspase binding  negative regulation of release of cytochrome c from mitochondria  intrinsic apoptotic signaling pathway  regulation of NIK/NF-kappaB signaling  negative regulation of mitochondrial membrane permeability involved in apoptotic process  negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway  negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway  inhibition of cysteine-type endopeptidase activity involved in apoptotic process  negative regulation of extrinsic apoptotic signaling pathway  
    Ontology : EGO-EBIresponse to hypoxia  blood vessel remodeling  response to ischemia  RNA binding  death receptor binding  calcium ion binding  protein binding  nucleolus  mitochondrion  cytosol  mRNA splice site selection  RNA splicing  cardiac muscle cell apoptotic process  negative regulation of cardiac muscle cell apoptotic process  negative regulation of tumor necrosis factor-mediated signaling pathway  negative regulation of muscle atrophy  release of sequestered calcium ion into cytosol by sarcoplasmic reticulum  response to injury involved in regulation of muscle adaptation  membrane  sarcoplasmic reticulum  death effector domain binding  identical protein binding  cysteine-type endopeptidase inhibitor activity involved in apoptotic process  negative regulation of apoptotic process  protein complex oligomerization  negative regulation of necrotic cell death  caspase binding  negative regulation of release of cytochrome c from mitochondria  intrinsic apoptotic signaling pathway  regulation of NIK/NF-kappaB signaling  negative regulation of mitochondrial membrane permeability involved in apoptotic process  negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway  negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway  inhibition of cysteine-type endopeptidase activity involved in apoptotic process  negative regulation of extrinsic apoptotic signaling pathway  
    NDEx NetworkNOL3
    Atlas of Cancer Signalling NetworkNOL3
    Wikipedia pathwaysNOL3
    Orthology - Evolution
    OrthoDB8996
    GeneTree (enSembl)ENSG00000140939
    Phylogenetic Trees/Animal Genes : TreeFamNOL3
    HOGENOMO60936
    Homologs : HomoloGeneNOL3
    Homology/Alignments : Family Browser (UCSC)NOL3
    Gene fusions - Rearrangements
    Fusion : FusionGDB24551    24552    24553    24554    32032    4219   
    Fusion : Fusion_HubHSF4--NOL3    NCKAP5L--NOL3    NOL3--EIF2AK3    NOL3--FLII    NOL3--MICAL2    NOL3--NDOR1    NOL3--NELFE    NOL3--NOL3    NOL3--PAN2    NOL3--PLEKHA2    NOL3--TG    NOL3--TJAP1    NOL3--UBE2D2    RPRD1B--NOL3   
    Fusion : QuiverNOL3
    Polymorphisms : SNP and Copy number variants
    NCBI Variation ViewerNOL3 [hg38]
    dbSNP Single Nucleotide Polymorphism (NCBI)NOL3
    dbVarNOL3
    ClinVarNOL3
    1000_GenomesNOL3 
    Exome Variant ServerNOL3
    ExAC (Exome Aggregation Consortium)ENSG00000140939
    GNOMAD BrowserENSG00000140939
    Varsome BrowserNOL3
    Genetic variants : HAPMAP8996
    Genomic Variants (DGV)NOL3 [DGVbeta]
    DECIPHERNOL3 [patients]   [syndromes]   [variants]   [genes]  
    CONAN: Copy Number AnalysisNOL3 
    Mutations
    ICGC Data PortalNOL3 
    TCGA Data PortalNOL3 
    Broad Tumor PortalNOL3
    OASIS PortalNOL3 [ Somatic mutations - Copy number]
    Somatic Mutations in Cancer : COSMICNOL3  [overview]  [genome browser]  [tissue]  [distribution]  
    Somatic Mutations in Cancer : COSMIC3DNOL3
    Mutations and Diseases : HGMDNOL3
    LOVD (Leiden Open Variation Database)Whole genome datasets
    LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
    LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
    BioMutasearch NOL3
    DgiDB (Drug Gene Interaction Database)NOL3
    DoCM (Curated mutations)NOL3 (select the gene name)
    CIViC (Clinical Interpretations of Variants in Cancer)NOL3 (select a term)
    intoGenNOL3
    NCG5 (London)NOL3
    Cancer3DNOL3(select the gene name)
    Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
    Diseases
    OMIM605235    614937   
    Orphanet21622   
    DisGeNETNOL3
    MedgenNOL3
    Genetic Testing Registry NOL3
    NextProtO60936 [Medical]
    TSGene8996
    GENETestsNOL3
    Target ValidationNOL3
    Huge Navigator NOL3 [HugePedia]
    snp3D : Map Gene to Disease8996
    BioCentury BCIQNOL3
    ClinGenNOL3
    Clinical trials, drugs, therapy
    Chemical/Protein Interactions : CTD8996
    Chemical/Pharm GKB GenePA31673
    Clinical trialNOL3
    Miscellaneous
    canSAR (ICR)NOL3 (select the gene name)
    DataMed IndexNOL3
    Probes
    Litterature
    PubMed47 Pubmed reference(s) in Entrez
    GeneRIFsGene References Into Functions (Entrez)
    CoreMineNOL3
    EVEXNOL3
    GoPubMedNOL3
    iHOPNOL3
    REVIEW articlesautomatic search in PubMed
    Last year publicationsautomatic search in PubMed

    Search in all EBI   NCBI

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    indexed on : Wed Nov 13 21:43:45 CET 2019
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