NOL3_HUMAN
ID NOL3_HUMAN Reviewed; 208 AA.
AC O60936; B4DFL0; O60937;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Nucleolar protein 3 {ECO:0000312|HGNC:HGNC:7869};
DE AltName: Full=Apoptosis repressor with CARD {ECO:0000305|PubMed:9560245};
DE AltName: Full=Muscle-enriched cytoplasmic protein {ECO:0000305|PubMed:10196175};
DE Short=Myp {ECO:0000303|PubMed:10196175};
DE AltName: Full=Nucleolar protein of 30 kDa {ECO:0000303|PubMed:10196175};
DE Short=Nop30 {ECO:0000303|PubMed:10196175};
GN Name=NOL3 {ECO:0000312|HGNC:HGNC:7869};
GN Synonyms=ARC {ECO:0000303|PubMed:9560245},
GN NOP {ECO:0000303|PubMed:10196175};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH CASP2 AND
RP CASP8.
RX PubMed=9560245; DOI=10.1073/pnas.95.9.5156;
RA Koseki T., Inohara N., Chen S., Nunez G.;
RT "ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that
RT interacts selectively with caspases.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:5156-5160(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR
RP LOCATION, SUBUNIT, INTERACTION WITH SFRS9, AND FUNCTION (ISOFORM 1).
RC TISSUE=Cervix carcinoma;
RX PubMed=10196175; DOI=10.1074/jbc.274.16.10951;
RA Stoss O., Schwaiger F.-W., Cooper T.A., Stamm S.;
RT "Alternative splicing determines the intracellular localization of the
RT novel nuclear protein Nop30 and its interaction with the splicing factor
RT SRp30c.";
RL J. Biol. Chem. 274:10951-10962(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain cortex;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION (ISOFORM 2), INTERACTION WITH BAX, AND DOMAIN.
RX PubMed=15004034; DOI=10.1074/jbc.m400695200;
RA Gustafsson A.B., Tsai J.G., Logue S.E., Crow M.T., Gottlieb R.A.;
RT "Apoptosis repressor with caspase recruitment domain protects against cell
RT death by interfering with Bax activation.";
RL J. Biol. Chem. 279:21233-21238(2004).
RN [8]
RP FUNCTION (ISOFORM 2), DOMAIN, AND INTERACTION WITH CASP8.
RX PubMed=15509781; DOI=10.1128/mcb.24.22.9763-9770.2004;
RA Jo D.G., Jun J.I., Chang J.W., Hong Y.M., Song S., Cho D.H., Shim S.M.,
RA Lee H.J., Cho C., Kim D.H., Jung Y.K.;
RT "Calcium binding of ARC mediates regulation of caspase 8 and cell death.";
RL Mol. Cell. Biol. 24:9763-9770(2004).
RN [9]
RP INDUCTION.
RX PubMed=16505176; DOI=10.1161/circulationaha.105.576785;
RA Donath S., Li P., Willenbockel C., Al-Saadi N., Gross V., Willnow T.,
RA Bader M., Martin U., Bauersachs J., Wollert K.C., Dietz R.,
RA von Harsdorf R.;
RT "Apoptosis repressor with caspase recruitment domain is required for
RT cardioprotection in response to biomechanical and ischemic stress.";
RL Circulation 113:1203-1212(2006).
RN [10]
RP INDUCTION, UBIQUITINATION, AND MUTAGENESIS OF LYS-17; LYS-68 AND LYS-163.
RX PubMed=17142452; DOI=10.1074/jbc.m609186200;
RA Nam Y.J., Mani K., Wu L., Peng C.F., Calvert J.W., Foo R.S.,
RA Krishnamurthy B., Miao W., Ashton A.W., Lefer D.J., Kitsis R.N.;
RT "The apoptosis inhibitor ARC undergoes ubiquitin-proteasomal-mediated
RT degradation in response to death stimuli: identification of a degradation-
RT resistant mutant.";
RL J. Biol. Chem. 282:5522-5528(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [13]
RP VARIANT MYOCL1 GLN-21, AND CHARACTERIZATION OF VARIANT MYOCL1 GLN-21.
RX PubMed=22926851; DOI=10.1002/ana.23666;
RA Russell J.F., Steckley J.L., Coppola G., Hahn A.F., Howard M.A.,
RA Kornberg Z., Huang A., Mirsattari S.M., Merriman B., Klein E., Choi M.,
RA Lee H.Y., Kirk A., Nelson-Williams C., Gibson G., Baraban S.C.,
RA Lifton R.P., Geschwind D.H., Fu Y.H., Ptacek L.J.;
RT "Familial cortical myoclonus with a mutation in NOL3.";
RL Ann. Neurol. 72:175-183(2012).
RN [14]
RP VARIANT MYOCL1 THR-80.
RX PubMed=25138476; DOI=10.1007/s00415-014-7463-z;
RA Macerollo A., Mencacci N.E., Erro R., Cordivari C., Edwards M.J.,
RA Wood N.W., Bhatia K.P.;
RT "Screening of mutations in NOL3 in a myoclonic syndromes series.";
RL J. Neurol. 261:1830-1831(2014).
CC -!- FUNCTION: [Isoform 1]: May be involved in RNA splicing.
CC {ECO:0000269|PubMed:10196175}.
CC -!- FUNCTION: [Isoform 2]: Functions as an apoptosis repressor that blocks
CC multiple modes of cell death. Inhibits extrinsic apoptotic pathways
CC through two different ways. Firstly by interacting with FAS and FADD
CC upon FAS activation blocking death-inducing signaling complex (DISC)
CC assembly (By similarity). Secondly by interacting with CASP8 in a
CC mitochondria localization- and phosphorylation-dependent manner,
CC limiting the amount of soluble CASP8 available for DISC-mediated
CC activation (By similarity). Inhibits intrinsic apoptotic pathway in
CC response to a wide range of stresses, through its interaction with BAX
CC resulting in BAX inactivation, preventing mitochondrial dysfunction and
CC release of pro-apoptotic factors (PubMed:15004034). Inhibits calcium-
CC mediated cell death by functioning as a cytosolic calcium buffer,
CC dissociating its interaction with CASP8 and maintaining calcium
CC homeostasis (PubMed:15509781). Negatively regulates oxidative stress-
CC induced apoptosis by phosphorylation-dependent suppression of the
CC mitochondria-mediated intrinsic pathway, by blocking CASP2 activation
CC and BAX translocation (By similarity). Negatively regulates hypoxia-
CC induced apoptosis in part by inhibiting the release of cytochrome c
CC from mitochondria in a caspase-independent manner (By similarity). Also
CC inhibits TNF-induced necrosis by preventing TNF-signaling pathway
CC through TNFRSF1A interaction abrogating the recruitment of RIPK1 to
CC complex I (By similarity). Finally through its role as apoptosis
CC repressor, promotes vascular remodeling through inhibition of apoptosis
CC and stimulation of proliferation, in response to hypoxia (By
CC similarity). Inhibits too myoblast differentiation through caspase
CC inhibition (By similarity). {ECO:0000250|UniProtKB:Q62881,
CC ECO:0000250|UniProtKB:Q9D1X0, ECO:0000269|PubMed:15004034,
CC ECO:0000269|PubMed:15509781}.
CC -!- SUBUNIT: Oligomerizes (via CARD doamin). Interacts (via CARD domain)
CC with CASP2; inhibits CASP2 activity in a phosphorylation-dependent
CC manner. Interacts with CASP8; decreases CASP8 activity in a
CC mitochondria localization- and phosphorylation-dependent manner and
CC this interaction is dissociated by calcium. Interacts with TFPT;
CC translocates NOL3 into the nucleus and negatively regulated TFPT-
CC induced cell death (By similarity). Interacts directly (via CARD
CC domain) with FAS and FADD (via DED domain); inhibits death-inducing
CC signaling complex death-inducing signaling complex (DISC) assembly by
CC inhibiting the increase in FAS-FADD binding induced by FAS activation
CC (By similarity). Interacts (via CARD domain) with BAX (via a C-terminal
CC 33 residues); inhibits BAX activation and translocation and
CC consequently cytochrome c release from mitochondria. Interacts with
CC PPM1G; may dephosphorylate NOL3 (By similarity). Interacts (via CARD
CC domain) with BBC3 (via BH3 domain); preventing the association of BBC3
CC with BCL2 and resulting in activation of CASP8 (By similarity).
CC Interacts (via CARD domain) with BAD(via BH3 domain); preventing the
CC association of BAD with BCL2 (By similarity). Interacts directly (via
CC CARD domain) with TNFRSF1A; inhibits TNF-signaling pathway (By
CC similarity). Isoform 1 binds to SFRS9/SRp30C.
CC {ECO:0000250|UniProtKB:Q62881, ECO:0000250|UniProtKB:Q9D1X0,
CC ECO:0000269|PubMed:10196175, ECO:0000269|PubMed:15004034,
CC ECO:0000269|PubMed:15509781, ECO:0000269|PubMed:9560245}.
CC -!- INTERACTION:
CC O60936; Q14790: CASP8; NbExp=3; IntAct=EBI-740992, EBI-78060;
CC O60936; O60936: NOL3; NbExp=2; IntAct=EBI-740992, EBI-740992;
CC O60936; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-740992, EBI-5235340;
CC O60936; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-740992, EBI-717399;
CC O60936; P04637: TP53; NbExp=3; IntAct=EBI-740992, EBI-366083;
CC O60936; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-740992, EBI-947187;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleolus
CC {ECO:0000269|PubMed:10196175}. Note=The SR-rich C-terminus mediates
CC nuclear localization. {ECO:0000269|PubMed:10196175}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:10196175}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q62881}. Sarcoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q62881}. Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Note=Phosphorylation at Thr-149 results in translocation
CC to mitochondria. Colocalized with mitochondria in response to oxidative
CC stress. {ECO:0000250|UniProtKB:Q62881}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2 {ECO:0000305}; Synonyms=Myp {ECO:0000303|PubMed:10196175};
CC IsoId=O60936-2; Sequence=Displayed;
CC Name=1 {ECO:0000305}; Synonyms=Nop30 {ECO:0000303|PubMed:10196175};
CC IsoId=O60936-1; Sequence=VSP_057515;
CC Name=3 {ECO:0000305};
CC IsoId=O60936-3; Sequence=VSP_054607;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle.
CC Detected at low levels in placenta, liver, kidney and pancreas.
CC -!- INDUCTION: Protein expression decreases in hearts failure patients
CC (PubMed:16505176) and in response to oxidative stress
CC (PubMed:17142452). {ECO:0000269|PubMed:16505176,
CC ECO:0000269|PubMed:17142452}.
CC -!- DOMAIN: CARD is critical for both extrinsic and intrinsic apoptotic
CC pathways (By similarity). CARD domain mediates a protective effect
CC against myocardial ischemia/reperfusion, oxidative stress and TNF-
CC induced necrosis (PubMed:15004034). The C-terminal domain (amino acids
CC 99 to 208) is involved in calcium binding and plays a protective role
CC in calcium-mediated cell death (PubMed:15509781).
CC {ECO:0000250|UniProtKB:Q62881, ECO:0000269|PubMed:15004034,
CC ECO:0000269|PubMed:15509781}.
CC -!- PTM: Phosphorylation at Thr-149 is required for its antiapoptotic
CC effect by blocking death-inducing signaling complex death-inducing
CC signaling complex (DISC) activity through the control of interaction
CC with CASP8. Phosphorylation at Thr-149 results in translocation to
CC mitochondria and this translocation enables the binding to CASP8.
CC Dephosphorylated at Thr-149 by calcineurin; doesn't inhibit the
CC association between FADD and CASP8 and the consequent apoptosis.
CC {ECO:0000250|UniProtKB:Q62881}.
CC -!- PTM: Polyubiquitinated by MDM2; promoting proteasomal-dependent
CC degradation in response to apoptotic stimuli.
CC {ECO:0000250|UniProtKB:Q62881, ECO:0000269|PubMed:17142452}.
CC -!- DISEASE: Myoclonus, familial, 1 (MYOCL1) [MIM:614937]: An autosomal
CC dominant neurologic condition characterized by adult onset of cortical
CC myoclonus manifest as involuntary jerks or movements affecting the face
CC and limbs. Affected individuals can also experience falls without
CC seizure activity or loss of consciousness.
CC {ECO:0000269|PubMed:22926851, ECO:0000269|PubMed:25138476}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NOL3ID41552ch16q22.html";
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DR EMBL; AF043244; AAC34993.1; -; mRNA.
DR EMBL; AF064598; AAC18590.1; -; Genomic_DNA.
DR EMBL; AF064598; AAC18591.1; -; Genomic_DNA.
DR EMBL; AF064599; AAC18593.1; -; mRNA.
DR EMBL; AF064600; AAC18594.1; -; mRNA.
DR EMBL; AK294145; BAG57471.1; -; mRNA.
DR EMBL; AC074143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471092; EAW83087.1; -; Genomic_DNA.
DR EMBL; BC012798; AAH12798.1; -; mRNA.
DR CCDS; CCDS42176.1; -. [O60936-2]
DR CCDS; CCDS58473.1; -. [O60936-1]
DR CCDS; CCDS61960.1; -. [O60936-3]
DR RefSeq; NP_001171986.1; NM_001185057.2. [O60936-1]
DR RefSeq; NP_001263236.1; NM_001276307.1. [O60936-2]
DR RefSeq; NP_001263238.1; NM_001276309.1. [O60936-2]
DR RefSeq; NP_001263240.1; NM_001276311.1.
DR RefSeq; NP_001263241.1; NM_001276312.1. [O60936-2]
DR RefSeq; NP_001263248.1; NM_001276319.1. [O60936-3]
DR RefSeq; NP_003937.1; NM_003946.6. [O60936-2]
DR RefSeq; XP_016879332.1; XM_017023843.1.
DR PDB; 4UZ0; X-ray; 2.40 A; A/B=1-95.
DR PDBsum; 4UZ0; -.
DR AlphaFoldDB; O60936; -.
DR SMR; O60936; -.
DR BioGRID; 114477; 43.
DR DIP; DIP-29940N; -.
DR IntAct; O60936; 12.
DR STRING; 9606.ENSP00000457243; -.
DR iPTMnet; O60936; -.
DR PhosphoSitePlus; O60936; -.
DR BioMuta; NOL3; -.
DR EPD; O60936; -.
DR jPOST; O60936; -.
DR MassIVE; O60936; -.
DR MaxQB; O60936; -.
DR PaxDb; O60936; -.
DR PeptideAtlas; O60936; -.
DR PRIDE; O60936; -.
DR ProteomicsDB; 4053; -.
DR ProteomicsDB; 49679; -. [O60936-1]
DR ProteomicsDB; 49680; -. [O60936-2]
DR Antibodypedia; 3976; 383 antibodies from 39 providers.
DR DNASU; 8996; -.
DR Ensembl; ENST00000268605.11; ENSP00000268605.7; ENSG00000140939.14. [O60936-2]
DR Ensembl; ENST00000564053.5; ENSP00000457243.1; ENSG00000140939.14. [O60936-3]
DR Ensembl; ENST00000568146.1; ENSP00000454598.1; ENSG00000140939.14. [O60936-1]
DR GeneID; 8996; -.
DR KEGG; hsa:8996; -.
DR UCSC; uc010vjd.4; human. [O60936-2]
DR CTD; 8996; -.
DR DisGeNET; 8996; -.
DR GeneCards; NOL3; -.
DR HGNC; HGNC:7869; NOL3.
DR HPA; ENSG00000140939; Low tissue specificity.
DR MalaCards; NOL3; -.
DR MIM; 605235; gene.
DR MIM; 614937; phenotype.
DR neXtProt; NX_O60936; -.
DR OpenTargets; ENSG00000140939; -.
DR Orphanet; 319189; Familial cortical myoclonus.
DR PharmGKB; PA31673; -.
DR VEuPathDB; HostDB:ENSG00000140939; -.
DR eggNOG; ENOG502SR4M; Eukaryota.
DR GeneTree; ENSGT00510000049353; -.
DR HOGENOM; CLU_1261120_0_0_1; -.
DR InParanoid; O60936; -.
DR OMA; RCAQQTV; -.
DR OrthoDB; 1497464at2759; -.
DR PhylomeDB; O60936; -.
DR TreeFam; TF336957; -.
DR PathwayCommons; O60936; -.
DR SignaLink; O60936; -.
DR SIGNOR; O60936; -.
DR BioGRID-ORCS; 8996; 13 hits in 1082 CRISPR screens.
DR ChiTaRS; NOL3; human.
DR GeneWiki; NOL3; -.
DR GenomeRNAi; 8996; -.
DR Pharos; O60936; Tbio.
DR PRO; PR:O60936; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O60936; protein.
DR Bgee; ENSG00000140939; Expressed in apex of heart and 199 other tissues.
DR ExpressionAtlas; O60936; baseline and differential.
DR Genevisible; O60936; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IMP:UniProtKB.
DR GO; GO:0089720; F:caspase binding; IPI:UniProtKB.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0035877; F:death effector domain binding; IBA:GO_Central.
DR GO; GO:0005123; F:death receptor binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0006376; P:mRNA splice site selection; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:1902109; P:negative regulation of mitochondrial membrane permeability involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0014736; P:negative regulation of muscle atrophy; IEA:Ensembl.
DR GO; GO:0060547; P:negative regulation of necrotic cell death; IEA:Ensembl.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
DR GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0014876; P:response to injury involved in regulation of muscle adaptation; IEA:Ensembl.
DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR Pfam; PF00619; CARD; 1.
DR SMART; SM00114; CARD; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50209; CARD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Calcium; Cytoplasm;
KW Disease variant; Lipoprotein; Membrane; Metal-binding; Mitochondrion;
KW mRNA processing; mRNA splicing; Myristate; Nucleus; Phosphoprotein;
KW Reference proteome; Sarcoplasmic reticulum; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CHAIN 2..208
FT /note="Nucleolar protein 3"
FT /id="PRO_0000144099"
FT DOMAIN 4..95
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT REGION 107..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..208
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 149
FT /note="Phosphothreonine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q62881"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:25255805"
FT VAR_SEQ 1
FT /note="M -> MPVLGKAGEERRATADAWGQKEEPEEETGQSVWRGRRTPSSPCWPPG
FT PVLAEPSGGWDRAPTM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054607"
FT VAR_SEQ 96..208
FT /note="VGPGYRDRSYDPPCPGHWTPEAPGSGTTCPGLPRASDPDEAGGPEGSEAVQS
FT GTPEEPEPELEAEASKEAEPEPEPEPELEPEAEAEPEPELEPEPDPEPEPDFEERDESE
FT DS -> ATGTAAMTLHAQATGRRRHPARGPHAPGCPELQTLTRPGALRAPRRCNPGPRR
FT SQSQSWKLRPLKRLNRSRSQSQSWNPRLKQNQSRNWSQNRTQSPSPTSRKGTSPKIPEG
FT QSSDRRCPAHAG (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10196175"
FT /id="VSP_057515"
FT VARIANT 21
FT /note="E -> Q (in MYOCL1; the mutation may alter post-
FT translational modification of the protein;
FT dbSNP:rs397514600)"
FT /evidence="ECO:0000269|PubMed:22926851"
FT /id="VAR_069731"
FT VARIANT 80
FT /note="A -> T (in MYOCL1; dbSNP:rs780601409)"
FT /evidence="ECO:0000269|PubMed:25138476"
FT /id="VAR_072644"
FT MUTAGEN 17
FT /note="K->R: Abolished ubiquitination in response to an
FT apoptotic stimulus; when associated with R-68 and R-163."
FT /evidence="ECO:0000269|PubMed:17142452"
FT MUTAGEN 31
FT /note="L->F: Did not reduce creatine kinase release or
FT infarct size after myocardial ischemia/reperfusion. Causes
FT loss of mitochondrial membrane potential and nuclear
FT condensation. Failes to prevent the increase in Bax.
FT Interacts with BAX."
FT /evidence="ECO:0000269|PubMed:15004034"
FT MUTAGEN 68
FT /note="K->R: Abolished ubiquitination in response to an
FT apoptotic stimulus; when associated with R-17 and R-163."
FT /evidence="ECO:0000269|PubMed:17142452"
FT MUTAGEN 163
FT /note="K->R: Abolished ubiquitination in response to an
FT apoptotic stimulus; when associated with R-17 and R-68."
FT /evidence="ECO:0000269|PubMed:17142452"
FT HELIX 8..23
FT /evidence="ECO:0007829|PDB:4UZ0"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:4UZ0"
FT HELIX 42..50
FT /evidence="ECO:0007829|PDB:4UZ0"
FT HELIX 54..68
FT /evidence="ECO:0007829|PDB:4UZ0"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:4UZ0"
SQ SEQUENCE 208 AA; 22629 MW; 239EF1A143EF6168 CRC64;
MGNAQERPSE TIDRERKRLV ETLQADSGLL LDALLARGVL TGPEYEALDA LPDAERRVRR
LLLLVQGKGE AACQELLRCA QRTAGAPDPA WDWQHVGPGY RDRSYDPPCP GHWTPEAPGS
GTTCPGLPRA SDPDEAGGPE GSEAVQSGTP EEPEPELEAE ASKEAEPEPE PEPELEPEAE
AEPEPELEPE PDPEPEPDFE ERDESEDS
