NOL3

Nucleolar protein 3 is a protein that in humans is encoded by the NOL3 gene.

NOL3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4UZ0
Identifiers
Aliases	NOL3, ARC, FCM, MYP, NOP, NOP30, nucleolar protein 3, MYOCL1
External IDs	OMIM: 605235 MGI: 1925938 HomoloGene: 31208 GeneCards: NOL3
Gene location (Human) Chr. Chromosome 16 (human) Band 16q22.1 Start 67,170,154 bp End 67,175,735 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8 D3|8 53.04 cM Start 106,002,772 bp End 106,008,571 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gastrocnemius muscle skin of abdomen right adrenal gland left adrenal gland body of pancreas right uterine tube anterior pituitary minor salivary glands right coronary artery gastric mucosa Top expressed in extraocular muscle triceps brachii muscle sternocleidomastoid muscle temporal muscle digastric muscle ankle thoracic diaphragm right ventricle interventricular septum soleus muscle More reference expression data BioGPS n/a
Gene ontology Molecular function death effector domain binding calcium ion binding death receptor binding metal ion binding cysteine-type endopeptidase inhibitor activity involved in apoptotic process protein binding RNA binding identical protein binding signaling receptor binding caspase binding Cellular component cytosol membrane sarcoplasmic reticulum sarcoplasm nucleus mitochondrion nucleolus cytoplasm Biological process regulation of apoptotic process release of sequestered calcium ion into cytosol by sarcoplasmic reticulum response to hypoxia negative regulation of striated muscle cell apoptotic process inhibition of cysteine-type endopeptidase activity involved in apoptotic process negative regulation of tumor necrosis factor-mediated signaling pathway negative regulation of muscle atrophy negative regulation of release of cytochrome c from mitochondria response to injury involved in regulation of muscle adaptation negative regulation of extrinsic apoptotic signaling pathway mRNA processing negative regulation of apoptotic process cardiac muscle cell apoptotic process intrinsic apoptotic signaling pathway negative regulation of cardiac muscle cell apoptotic process blood vessel remodeling response to ischemia mRNA splice site selection protein complex oligomerization negative regulation of mitochondrial membrane permeability involved in apoptotic process regulation of gene expression negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway negative regulation of necrotic cell death apoptotic process RNA splicing negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway regulation of NIK/NF-kappaB signaling Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8996 78688 Ensembl ENSG00000140939 ENSMUSG00000014776 UniProt O60936 Q9D1X0 RefSeq (mRNA) NM_001185057 NM_001185058 NM_001276307 NM_001276309 NM_001276311 NM_001276312 NM_001276319 NM_003946 NM_030152 RefSeq (protein) NP_001171986 NP_001263236 NP_001263238 NP_001263240 NP_001263241 NP_001263248 NP_003937 NP_084428 Location (UCSC) Chr 16: 67.17 – 67.18 Mb Chr 8: 106 – 106.01 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Nol3 has been shown to be induced in multiple cancer types and acts as a repressor of apoptosis leading to resistance and proliferation. Paradoxically, loss of Nol3 also leads to hematological disruption in mice resulting in a myeloproliferative neoplasm resembling primary myelofibrosis (PMF), and its deletion has also been detected in patient samples of PMF.

Interactions

NOL3 has been shown to interact with SFRS9 and Caspase 8.

Further reading

• Stoss O, Schwaiger FW, Cooper TA, Stamm S (1999). "Alternative splicing determines the intracellular localization of the novel nuclear protein Nop30 and its interaction with the splicing factor SRp30c". J. Biol. Chem. 274 (16): 10951–62. doi:10.1074/jbc.274.16.10951. PMID 10196175.
• Irie Y, Yamagata K, Gan Y, Miyamoto K, Do E, Kuo CH, Taira E, Miki N (2000). "Molecular cloning and characterization of Amida, a novel protein which interacts with a neuron-specific immediate early gene product arc, contains novel nuclear localization signals, and causes cell death in cultured cells". J. Biol. Chem. 275 (4): 2647–53. doi:10.1074/jbc.275.4.2647. PMID 10644725.
• Li PF, Li J, Müller EC, Otto A, Dietz R, von Harsdorf R (2002). "Phosphorylation by protein kinase CK2: a signaling switch for the caspase-inhibiting protein ARC". Mol. Cell. 10 (2): 247–58. doi:10.1016/S1097-2765(02)00600-7. PMID 12191471.
• Ekhterae D, Platoshyn O, Zhang S, Remillard CV, Yuan JX (2003). "Apoptosis repressor with caspase domain inhibits cardiomyocyte apoptosis by reducing K+ currents". Am. J. Physiol., Cell Physiol. 284 (6): C1405-10. doi:10.1152/ajpcell.00279.2002. PMID 12734105.
• Nam YJ, Mani K, Ashton AW, Peng CF, Krishnamurthy B, Hayakawa Y, Lee P, Korsmeyer SJ, Kitsis RN (2004). "Inhibition of both the extrinsic and intrinsic death pathways through nonhomotypic death-fold interactions". Mol. Cell. 15 (6): 901–12. doi:10.1016/j.molcel.2004.08.020. PMID 15383280.
• Jo DG, Jun JI, Chang JW, Hong YM, Song S, Cho DH, Shim SM, Lee HJ, Cho C, Kim DH, Jung YK (2004). "Calcium binding of ARC mediates regulation of caspase 8 and cell death". Mol. Cell. Biol. 24 (22): 9763–70. doi:10.1128/MCB.24.22.9763-9770.2004. PMC 525473. PMID 15509781.
• Wang M, Qanungo S, Crow MT, Watanabe M, Nieminen AL (2005). "Apoptosis repressor with caspase recruitment domain (ARC) is expressed in cancer cells and localizes to nuclei". FEBS Lett. 579 (11): 2411–5. doi:10.1016/j.febslet.2005.03.040. PMID 15848180. S2CID 28842286.
• Mercier I, Vuolo M, Madan R, Xue X, Levalley AJ, Ashton AW, Jasmin JF, Czaja MT, Lin EY, Armstrong RC, Pollard JW, Kitsis RN (2005). "ARC, an apoptosis suppressor limited to terminally differentiated cells, is induced in human breast cancer and confers chemo- and radiation-resistance". Cell Death Differ. 12 (6): 682–6. doi:10.1038/sj.cdd.4401631. PMID 15861191.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• 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 (2006). "Apoptosis repressor with caspase recruitment domain is required for cardioprotection in response to biomechanical and ischemic stress". Circulation. 113 (9): 1203–12. doi:10.1161/CIRCULATIONAHA.105.576785. PMID 16505176.
• Nam YJ, Mani K, Wu L, Peng CF, Calvert JW, Foo RS, Krishnamurthy B, Miao W, Ashton AW, Lefer DJ, Kitsis RN (2007). "The apoptosis inhibitor ARC undergoes ubiquitin-proteasomal-mediated degradation in response to death stimuli: identification of a degradation-resistant mutant". J. Biol. Chem. 282 (8): 5522–8. doi:10.1074/jbc.M609186200. PMID 17142452.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Stanley RF, Piszczatowski RT, Bartholdy B, Mitchell K, McKimpson WM, Narayanagari S, Walter D, Todorova TI, Hirsch C, Makashima H, Will B, McMahon C, Gritsman K, Maciejewski JP, Kitsis RN, Steidl U (2017). "A myeloid tumor suppressor role for NOL3". J. Exp. Med. 214 (3): 753–771. doi:10.1084/jem.20162089. PMC 5339683. PMID 28232469.