NOP53_HUMAN
ID NOP53_HUMAN Reviewed; 478 AA.
AC Q9NZM5; Q9BTC6; Q9HAX6; Q9NPP1; Q9NPR4; Q9UFI2;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Ribosome biogenesis protein NOP53 {ECO:0000305};
DE AltName: Full=Glioma tumor suppressor candidate region gene 2 protein {ECO:0000312|HGNC:HGNC:4333};
DE AltName: Full=Protein interacting with carboxyl terminus 1 {ECO:0000303|PubMed:15355975};
DE Short=PICT-1 {ECO:0000303|PubMed:15355975};
DE AltName: Full=p60 {ECO:0000303|PubMed:10196275};
GN Name=NOP53 {ECO:0000312|HGNC:HGNC:4333};
GN Synonyms=GLT {ECO:0000303|PubMed:21741933},
GN GLTSCR2 {ECO:0000303|PubMed:10708517}, PICT1 {ECO:0000303|PubMed:24556985};
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], VARIANT ARG-389, AND TISSUE SPECIFICITY.
RX PubMed=10708517; DOI=10.1006/geno.1999.6101;
RA Smith J.S., Tachibana I., Pohl U., Lee H.K., Thanarajasingam U.,
RA Portier B.P., Ueki K., Billings S., Ramaswamy S., Mohrenweiser H.W.,
RA Scheithauer B.W., Louis D.N., Jenkins R.B.;
RT "A transcript map of the chromosome 19q-Arm glioma tumor suppressor
RT region.";
RL Genomics 64:44-50(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-389.
RC TISSUE=Muscle;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-478, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH HERPES SIMPLEX VIRUS 1 PROTEINS ICP22 AND ICP0 (MICROBIAL INFECTION).
RX PubMed=10196275; DOI=10.1128/jvi.73.5.3810-3817.1999;
RA Bruni R., Fineschi B., Ogle W.O., Roizman B.;
RT "A novel cellular protein, p60, interacting with both herpes simplex virus
RT 1 regulatory proteins ICP22 and ICP0 is modified in a cell-type-specific
RT manner and is recruited to the nucleus after infection.";
RL J. Virol. 73:3810-3817(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-478, AND VARIANT ARG-389.
RG The European IMAGE consortium;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 218-477, AND VARIANT ARG-389.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH PTEN.
RX PubMed=15355975; DOI=10.1074/jbc.c400377200;
RA Okahara F., Ikawa H., Kanaho Y., Maehama T.;
RT "Regulation of PTEN phosphorylation and stability by a tumor suppressor
RT candidate protein.";
RL J. Biol. Chem. 279:45300-45303(2004).
RN [8]
RP FUNCTION.
RX PubMed=16971513; DOI=10.1091/mbc.e06-04-0301;
RA Okahara F., Itoh K., Nakagawara A., Murakami M., Kanaho Y., Maehama T.;
RT "Critical role of PICT-1, a tumor suppressor candidate, in
RT phosphatidylinositol 3,4,5-trisphosphate signals and tumorigenic
RT transformation.";
RL Mol. Biol. Cell 17:4888-4895(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP INTERACTION WITH HUMAN HERPESVIRUS 8 PROTEIN ORF16 (MICROBIAL INFECTION),
RP SUBCELLULAR LOCATION, AND REGION.
RX PubMed=20042497; DOI=10.1128/jvi.00757-09;
RA Kalt I., Borodianskiy-Shteinberg T., Schachor A., Sarid R.;
RT "GLTSCR2/PICT-1, a putative tumor suppressor gene product, induces the
RT nucleolar targeting of the Kaposi's sarcoma-associated herpesvirus KS-Bcl-2
RT protein.";
RL J. Virol. 84:2935-2945(2010).
RN [11]
RP FUNCTION, AND INDUCTION.
RX PubMed=21741933; DOI=10.1016/j.ajpath.2011.05.041;
RA Kim J.Y., Seok K.O., Kim Y.J., Bae W.K., Lee S., Park J.H.;
RT "Involvement of GLTSCR2 in the DNA Damage Response.";
RL Am. J. Pathol. 179:1257-1264(2011).
RN [12]
RP FUNCTION, INTERACTION WITH NF2, AND REGION.
RX PubMed=21167305; DOI=10.1016/j.biocel.2010.12.011;
RA Chen H., Mei L., Zhou L., Zhang X., Guo C., Li J., Wang H., Zhu Y.,
RA Zheng Y., Huang L.;
RT "Moesin-ezrin-radixin-like protein (merlin) mediates protein interacting
RT with the carboxyl terminus-1 (PICT-1)-induced growth inhibition of
RT glioblastoma cells in the nucleus.";
RL Int. J. Biochem. Cell Biol. 43:545-555(2011).
RN [13]
RP FUNCTION, INTERACTION WITH TP53, AND SUBCELLULAR LOCATION.
RX PubMed=22522597; DOI=10.1038/cdd.2012.40;
RA Lee S., Kim J.Y., Kim Y.J., Seok K.O., Kim J.H., Chang Y.J., Kang H.Y.,
RA Park J.H.;
RT "Nucleolar protein GLTSCR2 stabilizes p53 in response to ribosomal
RT stresses.";
RL Cell Death Differ. 19:1613-1622(2012).
RN [14]
RP SUBCELLULAR LOCATION, AND REGION.
RX PubMed=22292050; DOI=10.1371/journal.pone.0030825;
RA Kalt I., Levy A., Borodianskiy-Shteinberg T., Sarid R.;
RT "Nucleolar localization of GLTSCR2/PICT-1 is mediated by multiple unique
RT nucleolar localization sequences.";
RL PLoS ONE 7:E30825-E30825(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP FUNCTION.
RX PubMed=24120868; DOI=10.1016/j.celrep.2013.08.049;
RA Sloan K.E., Bohnsack M.T., Watkins N.J.;
RT "The 5S RNP couples p53 homeostasis to ribosome biogenesis and nucleolar
RT stress.";
RL Cell Rep. 5:237-247(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-93, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=24923447; DOI=10.1074/jbc.m114.571893;
RA Maehama T., Kawahara K., Nishio M., Suzuki A., Hanada K.;
RT "Nucleolar stress induces ubiquitination-independent proteasomal
RT degradation of PICT1 protein.";
RL J. Biol. Chem. 289:20802-20812(2014).
RN [19]
RP SUBUNIT.
RX PubMed=24735870; DOI=10.1016/j.jmb.2014.04.006;
RA Borodianskiy-Shteinberg T., Kalt I., Kipper S., Nachum N., Katz S.,
RA Pauker M.H., Barda-Saad M., Gerber D., Sarid R.;
RT "The nucleolar PICT-1/GLTSCR2 protein forms homo-oligomers.";
RL J. Mol. Biol. 426:2363-2378(2014).
RN [20]
RP FUNCTION, INTERACTION WITH RPL11, AND INDUCTION.
RX PubMed=24556985; DOI=10.1073/pnas.1400705111;
RA Yoon J.C., Ling A.J., Isik M., Lee D.Y., Steinbaugh M.J., Sack L.M.,
RA Boduch A.N., Blackwell T.K., Sinclair D.A., Elledge S.J.;
RT "GLTSCR2/PICT1 links mitochondrial stress and Myc signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:3781-3786(2014).
RN [21]
RP FUNCTION, INTERACTION WITH NPM1, AND SUBCELLULAR LOCATION.
RX PubMed=25956029; DOI=10.1016/j.ajpath.2015.03.016;
RA Kim J.Y., Cho Y.E., Park J.H.;
RT "The nucleolar protein GLTSCR2 is an upstream negative regulator of the
RT oncogenic Nucleophosmin-MYC axis.";
RL Am. J. Pathol. 185:2061-2068(2015).
RN [22]
RP FUNCTION.
RX PubMed=25818168; DOI=10.1111/jcmm.12474;
RA Kim J.Y., Cho Y.E., An Y.M., Kim S.H., Lee Y.G., Park J.H., Lee S.;
RT "GLTSCR2 is an upstream negative regulator of nucleophosmin in cervical
RT cancer.";
RL J. Cell. Mol. Med. 19:1245-1252(2015).
RN [23]
RP SUBUNIT, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=26903295; DOI=10.1016/j.bbrc.2016.02.070;
RA Lee S., Cho Y.E., Kim Y.J., Park J.H.;
RT "c-Jun N-terminal kinase regulates the nucleoplasmic translocation and
RT stability of nucleolar GLTSCR2 protein.";
RL Biochem. Biophys. Res. Commun. 472:95-100(2016).
RN [24]
RP FUNCTION, INTERACTION WITH UBTF, AND SUBCELLULAR LOCATION.
RX PubMed=27729611; DOI=10.18632/oncotarget.12288;
RA Chen H., Duo Y., Hu B., Wang Z., Zhang F., Tsai H., Zhang J., Zhou L.,
RA Wang L., Wang X., Huang L.;
RT "PICT-1 triggers a pro-death autophagy through inhibiting rRNA
RT transcription and AKT/mTOR/p70S6K signaling pathway.";
RL Oncotarget 7:78747-78763(2016).
RN [25]
RP FUNCTION, INTERACTION WITH RPL11, SUBCELLULAR LOCATION, INDUCTION,
RP PHOSPHORYLATION, AND MUTAGENESIS OF SER-233 AND THR-289.
RX PubMed=27829214; DOI=10.18632/oncotarget.13082;
RA Chen H., Han L., Tsai H., Wang Z., Wu Y., Duo Y., Cao W., Chen L., Tan Z.,
RA Xu N., Huang X., Zhuang J., Huang L.;
RT "PICT-1 is a key nucleolar sensor in DNA damage response signaling that
RT regulates apoptosis through the RPL11-MDM2-p53 pathway.";
RL Oncotarget 7:83241-83257(2016).
RN [26]
RP FUNCTION, INTERACTION WITH DDX58, AND SUBCELLULAR LOCATION.
RX PubMed=27824081; DOI=10.1038/srep36226;
RA Wang P., Meng W., Han S.C., Li C.C., Wang X.J., Wang X.J.;
RT "The nucleolar protein GLTSCR2 is required for efficient viral
RT replication.";
RL Sci. Rep. 6:36226-36226(2016).
RN [27]
RP INTERACTION WITH CDKN2A/ISOFORM TUMOR SUPPRESSOR ARF, SUBCELLULAR LOCATION,
RP AND REGION.
RX PubMed=27323397; DOI=10.18632/oncotarget.9957;
RA Lee S., Cho Y.E., Kim S.H., Kim Y.J., Park J.H.;
RT "GLTSCR2 promotes the nucleoplasmic translocation and subsequent
RT degradation of nucleolar ARF.";
RL Oncotarget 8:16293-16302(2017).
CC -!- FUNCTION: Nucleolar protein which is involved in the integration of the
CC 5S RNP into the ribosomal large subunit during ribosome biogenesis
CC (PubMed:24120868). In ribosome biogenesis, may also play a role in rRNA
CC transcription (PubMed:27729611). Also functions as a nucleolar sensor
CC that regulates the activation of p53/TP53 in response to ribosome
CC biogenesis perturbation, DNA damage and other stress conditions
CC (PubMed:21741933, PubMed:24120868, PubMed:27829214). DNA damage or
CC perturbation of ribosome biogenesis disrupt the interaction between
CC NOP53 and RPL11 allowing RPL11 transport to the nucleoplasm where it
CC can inhibit MDM2 and allow p53/TP53 activation (PubMed:24120868,
CC PubMed:27829214). It may also positively regulate the function of
CC p53/TP53 in cell cycle arrest and apoptosis through direct interaction,
CC preventing its MDM2-dependent ubiquitin-mediated proteasomal
CC degradation (PubMed:22522597). Originally identified as a tumor
CC suppressor, it may also play a role in cell proliferation and apoptosis
CC by positively regulating the stability of PTEN, thereby antagonizing
CC the PI3K-AKT/PKB signaling pathway (PubMed:15355975, PubMed:16971513,
CC PubMed:27729611). May also inhibit cell proliferation and increase
CC apoptosis through its interaction with NF2 (PubMed:21167305). May
CC negatively regulate NPM1 by regulating its nucleoplasmic localization,
CC oligomerization and ubiquitin-mediated proteasomal degradation
CC (PubMed:25818168). Thereby, may prevent NPM1 interaction with MYC and
CC negatively regulate transcription mediated by the MYC-NPM1 complex
CC (PubMed:25956029). May also regulate cellular aerobic respiration
CC (PubMed:24556985). In the cellular response to viral infection, may
CC play a role in the attenuation of interferon-beta through the
CC inhibition of DDX58/RIG-1 (PubMed:27824081).
CC {ECO:0000269|PubMed:15355975, ECO:0000269|PubMed:16971513,
CC ECO:0000269|PubMed:21167305, ECO:0000269|PubMed:21741933,
CC ECO:0000269|PubMed:22522597, ECO:0000269|PubMed:24120868,
CC ECO:0000269|PubMed:24556985, ECO:0000269|PubMed:25818168,
CC ECO:0000269|PubMed:25956029, ECO:0000269|PubMed:27729611,
CC ECO:0000269|PubMed:27824081, ECO:0000269|PubMed:27829214}.
CC -!- SUBUNIT: Homooligomer (PubMed:24735870, PubMed:26903295). Interacts
CC with PTEN; regulates PTEN phosphorylation and increases its stability
CC (PubMed:15355975). Interacts with RPL11; retains RPL11 into the
CC nucleolus (PubMed:24556985, PubMed:27829214). Interacts with
CC CDKN2A/isoform tumor suppressor ARF; the interaction is direct and
CC promotes ARF nucleoplasmic relocalization and ubiquitin-mediated
CC proteasomal degradation (PubMed:27323397). Interacts with NPM1; the
CC interaction is direct and competitive with MYC (PubMed:25956029).
CC Interacts with NF2 (via FERM domain); the interaction is direct
CC (PubMed:21167305). Interacts with p53/TP53 (via the oligomerization
CC region); the interaction is direct and may prevent the MDM2-mediated
CC proteasomal degradation of p53/TP53 (PubMed:22522597). Interacts with
CC DDX58; may regulate DDX58 through USP15-mediated 'Lys-63'-linked
CC deubiquitination (PubMed:27824081). Interacts with UBTF
CC (PubMed:27729611). {ECO:0000269|PubMed:15355975,
CC ECO:0000269|PubMed:21167305, ECO:0000269|PubMed:22522597,
CC ECO:0000269|PubMed:24556985, ECO:0000269|PubMed:24735870,
CC ECO:0000269|PubMed:25956029, ECO:0000269|PubMed:26903295,
CC ECO:0000269|PubMed:27323397, ECO:0000269|PubMed:27729611,
CC ECO:0000269|PubMed:27824081, ECO:0000269|PubMed:27829214}.
CC -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus 1
CC early proteins ICP22 and ICP0. {ECO:0000269|PubMed:10196275}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Human herpesvirus 8
CC protein ORF16; may sequester ORF16 in host nucleolus and reduce its
CC antiapoptotic activity. {ECO:0000269|PubMed:20042497}.
CC -!- INTERACTION:
CC Q9NZM5; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-720156, EBI-739624;
CC Q9NZM5; O95786: DDX58; NbExp=2; IntAct=EBI-720156, EBI-995350;
CC Q9NZM5; P26583: HMGB2; NbExp=4; IntAct=EBI-720156, EBI-1057009;
CC Q9NZM5; Q9H2G4: TSPYL2; NbExp=4; IntAct=EBI-720156, EBI-947459;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10196275,
CC ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:20042497,
CC ECO:0000269|PubMed:22292050, ECO:0000269|PubMed:22522597,
CC ECO:0000269|PubMed:24923447, ECO:0000269|PubMed:25956029,
CC ECO:0000269|PubMed:27729611, ECO:0000269|PubMed:27829214}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:22522597, ECO:0000269|PubMed:24923447,
CC ECO:0000269|PubMed:26903295, ECO:0000269|PubMed:27323397}. Note=In the
CC nucleolus may be more specifically localized to the fibrillar center
CC (PubMed:27729611). Mainly nucleolar it relocalizes to the nucleoplasm
CC under specific conditions including ribosomal stress enabling it to
CC interact and regulate nucleoplasmic proteins like p53/TP53
CC (PubMed:22522597, PubMed:24923447, PubMed:27323397, PubMed:26903295).
CC Also detected in the cytosol (PubMed:24923447, PubMed:27824081).
CC {ECO:0000269|PubMed:22522597, ECO:0000269|PubMed:24923447,
CC ECO:0000269|PubMed:26903295, ECO:0000269|PubMed:27323397,
CC ECO:0000269|PubMed:27729611, ECO:0000269|PubMed:27824081}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in heart and pancreas,
CC moderate levels in placenta, liver, skeletal muscle, and kidney, and
CC low levels in brain and lung. {ECO:0000269|PubMed:10708517}.
CC -!- INDUCTION: Down-regulated by nucleolar stress through ubiquitin-
CC independent proteasomal degradation (at protein level)
CC (PubMed:24923447). Up-regulated upon mitochondrial stress (at protein
CC level) (PubMed:24556985). Expression of the protein might be regulated
CC by DNA damage but results are not consistent (PubMed:21741933,
CC PubMed:27829214). {ECO:0000269|PubMed:21741933,
CC ECO:0000269|PubMed:24556985, ECO:0000269|PubMed:24923447,
CC ECO:0000269|PubMed:27829214}.
CC -!- PTM: Ubiquitin-mediated proteasomal degradation is regulated by c-JUN.
CC It is associated with relocalization to the nucleoplasm and decreased
CC homooligomerization. {ECO:0000269|PubMed:26903295}.
CC -!- PTM: Phosphorylated upon DNA damage probably by ATM and DNA-PK; may
CC regulate NOP53 degradation. {ECO:0000269|PubMed:27829214}.
CC -!- SIMILARITY: Belongs to the NOP53 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GLTSCR2ID40723ch19q13.html";
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DR EMBL; AF182076; AAF62873.1; -; mRNA.
DR EMBL; BC004229; AAH04229.2; -; mRNA.
DR EMBL; BC006311; AAH06311.1; -; mRNA.
DR EMBL; BC010095; AAH10095.1; -; mRNA.
DR EMBL; AF296124; AAG30413.1; -; mRNA.
DR EMBL; AL359335; CAB94786.1; -; mRNA.
DR EMBL; AL359336; CAB94787.1; -; mRNA.
DR EMBL; AL122063; CAB59242.1; -; mRNA.
DR CCDS; CCDS12705.1; -.
DR RefSeq; NP_056525.2; NM_015710.4.
DR AlphaFoldDB; Q9NZM5; -.
DR BioGRID; 119021; 288.
DR IntAct; Q9NZM5; 140.
DR MINT; Q9NZM5; -.
DR STRING; 9606.ENSP00000246802; -.
DR iPTMnet; Q9NZM5; -.
DR PhosphoSitePlus; Q9NZM5; -.
DR BioMuta; NOP53; -.
DR DMDM; 93141272; -.
DR SWISS-2DPAGE; Q9NZM5; -.
DR EPD; Q9NZM5; -.
DR jPOST; Q9NZM5; -.
DR MassIVE; Q9NZM5; -.
DR MaxQB; Q9NZM5; -.
DR PaxDb; Q9NZM5; -.
DR PeptideAtlas; Q9NZM5; -.
DR PRIDE; Q9NZM5; -.
DR ProteomicsDB; 83451; -.
DR Antibodypedia; 18226; 200 antibodies from 25 providers.
DR DNASU; 29997; -.
DR Ensembl; ENST00000246802.10; ENSP00000246802.4; ENSG00000105373.19.
DR GeneID; 29997; -.
DR KEGG; hsa:29997; -.
DR MANE-Select; ENST00000246802.10; ENSP00000246802.4; NM_015710.5; NP_056525.2.
DR UCSC; uc002phm.3; human.
DR CTD; 29997; -.
DR DisGeNET; 29997; -.
DR GeneCards; NOP53; -.
DR HGNC; HGNC:4333; NOP53.
DR HPA; ENSG00000105373; Low tissue specificity.
DR MIM; 605691; gene.
DR neXtProt; NX_Q9NZM5; -.
DR OpenTargets; ENSG00000105373; -.
DR PharmGKB; PA28736; -.
DR VEuPathDB; HostDB:ENSG00000105373; -.
DR eggNOG; KOG2823; Eukaryota.
DR GeneTree; ENSGT00390000017267; -.
DR HOGENOM; CLU_035888_0_0_1; -.
DR InParanoid; Q9NZM5; -.
DR OMA; WRKTDIQ; -.
DR OrthoDB; 1025498at2759; -.
DR PhylomeDB; Q9NZM5; -.
DR TreeFam; TF313004; -.
DR PathwayCommons; Q9NZM5; -.
DR SignaLink; Q9NZM5; -.
DR BioGRID-ORCS; 29997; 500 hits in 1089 CRISPR screens.
DR ChiTaRS; GLTSCR2; human.
DR GeneWiki; GLTSCR2; -.
DR GenomeRNAi; 29997; -.
DR Pharos; Q9NZM5; Tbio.
DR PRO; PR:Q9NZM5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NZM5; protein.
DR Bgee; ENSG00000105373; Expressed in left ovary and 182 other tissues.
DR ExpressionAtlas; Q9NZM5; baseline and differential.
DR Genevisible; Q9NZM5; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0008097; F:5S rRNA binding; IDA:HGNC.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IMP:UniProtKB.
DR GO; GO:1901797; P:negative regulation of signal transduction by p53 class mediator; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:1901837; P:negative regulation of transcription of nucleolar large rRNA by RNA polymerase I; IMP:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:1903006; P:positive regulation of protein K63-linked deubiquitination; IMP:UniProtKB.
DR GO; GO:1902570; P:protein localization to nucleolus; IEA:Ensembl.
DR GO; GO:1990173; P:protein localization to nucleoplasm; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:1903715; P:regulation of aerobic respiration; IMP:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0039535; P:regulation of RIG-I signaling pathway; IMP:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:HGNC.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR InterPro; IPR011687; Nop53/GLTSCR2.
DR PANTHER; PTHR14211; PTHR14211; 1.
DR Pfam; PF07767; Nop53; 1.
DR PIRSF; PIRSF017302; Gltscr2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Host-virus interaction; Nucleus; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..478
FT /note="Ribosome biogenesis protein NOP53"
FT /id="PRO_0000218960"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..431
FT /note="Mediates interaction with CDKN2A/isoform tumor
FT suppressor ARF"
FT /evidence="ECO:0000269|PubMed:27323397"
FT REGION 181..478
FT /note="Mediates interaction with NF2"
FT /evidence="ECO:0000269|PubMed:21167305"
FT REGION 303..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..386
FT /note="Mediates interaction with human herpesvirus 8
FT protein ORF16"
FT /evidence="ECO:0000269|PubMed:20042497"
FT REGION 347..395
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000269|PubMed:22292050"
FT REGION 396..478
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000269|PubMed:22292050"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BK35"
FT VARIANT 16
FT /note="S -> R (in dbSNP:rs1042401)"
FT /id="VAR_024456"
FT VARIANT 389
FT /note="Q -> R (in dbSNP:rs1804994)"
FT /evidence="ECO:0000269|PubMed:10708517,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.4"
FT /id="VAR_011486"
FT MUTAGEN 233
FT /note="S->A: Decreased phosphorylation, degradation and
FT increased interaction with RPL11 in response to DNA damage;
FT when associated with A-289."
FT /evidence="ECO:0000269|PubMed:27829214"
FT MUTAGEN 233
FT /note="S->D: Loss of localization to the nucleolus and in
FT response to DNA damage increased degradation and decreased
FT interaction with RPL11; when associated with D-289."
FT /evidence="ECO:0000269|PubMed:27829214"
FT MUTAGEN 289
FT /note="T->A: Decreased degradation in response to DNA
FT damage. Decreased phosphorylation, degradation and
FT increased interaction with RPL11 in response to DNA damage;
FT when associated with A-233."
FT /evidence="ECO:0000269|PubMed:27829214"
FT MUTAGEN 289
FT /note="T->D: Loss of localization to the nucleolus and in
FT response to DNA damage increased degradation and decreased
FT interaction with RPL11; when associated with D-233."
FT /evidence="ECO:0000269|PubMed:27829214"
FT CONFLICT 9
FT /note="G -> R (in Ref. 3; AAG30413)"
FT /evidence="ECO:0000305"
FT CONFLICT 146..191
FT /note="RRKEQLWEKLAKQGELPREVRRAQARLLNPSATRAKPGPQDTVERP -> SG
FT RSSYGRSWPSRASSPGGAQGPSPVAQPFCNKGPNPAPGHRIAA (in Ref. 3;
FT AAG30413)"
FT /evidence="ECO:0000305"
FT CONFLICT 198..215
FT /note="SDNPLDRPLVGQDEFFLE -> LNNPDKPVVWPGCLFPG (in Ref. 3;
FT AAG30413)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="A -> S (in Ref. 2; AAH04229)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="D -> H (in Ref. 3; AAG30413)"
FT /evidence="ECO:0000305"
FT CONFLICT 433..477
FT /note="PEGNILRDRFKSFQRRNMIEPRERAKFKRKYKVKLVEKRAFREIQ -> VLT
FT VSCRGAPCPVMTPSLLPVPPRGYGRHHGCPWAGPVGPMPRG (in Ref. 5;
FT CAB59242)"
FT /evidence="ECO:0000305"
FT CONFLICT 434..478
FT /note="EGNILRDRFKSFQRRNMIEPRERAKFKRKYKVKLVEKRAFREIQL -> RGQ
FT HSFETGSRAFRGGI (in Ref. 3; AAG30413)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 54389 MW; 7F1BA13D04BFB618 CRC64;
MAAGGSGVGG KRSSKSDADS GFLGLRPTSV DPALRRRRRG PRNKKRGWRR LAQEPLGLEV
DQFLEDVRLQ ERTSGGLLSE APNEKLFFVD TGSKEKGLTK KRTKVQKKSL LLKKPLRVDL
ILENTSKVPA PKDVLAHQVP NAKKLRRKEQ LWEKLAKQGE LPREVRRAQA RLLNPSATRA
KPGPQDTVER PFYDLWASDN PLDRPLVGQD EFFLEQTKKK GVKRPARLHT KPSQAPAVEV
APAGASYNPS FEDHQTLLSA AHEVELQRQK EAEKLERQLA LPATEQAATQ ESTFQELCEG
LLEESDGEGE PGQGEGPEAG DAEVCPTPAR LATTEKKTEQ QRRREKAVHR LRVQQAALRA
ARLRHQELFR LRGIKAQVAL RLAELARRQR RRQARREAEA DKPRRLGRLK YQAPDIDVQL
SSELTDSLRT LKPEGNILRD RFKSFQRRNM IEPRERAKFK RKYKVKLVEK RAFREIQL
