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Ribosome biogenesis protein NOP53 (Glioma tumor suppressor candidate region gene 2 protein) (Protein interacting with carboxyl terminus 1) (PICT-1) (p60)

 NOP53_HUMAN             Reviewed;         478 AA.
Q9NZM5; Q9BTC6; Q9HAX6; Q9NPP1; Q9NPR4; Q9UFI2;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
18-APR-2006, sequence version 2.
25-OCT-2017, entry version 149.
RecName: Full=Ribosome biogenesis protein NOP53 {ECO:0000305};
AltName: Full=Glioma tumor suppressor candidate region gene 2 protein {ECO:0000312|HGNC:HGNC:4333};
AltName: Full=Protein interacting with carboxyl terminus 1 {ECO:0000303|PubMed:15355975};
Short=PICT-1 {ECO:0000303|PubMed:15355975};
AltName: Full=p60 {ECO:0000303|PubMed:10196275};
Name=NOP53 {ECO:0000312|HGNC:HGNC:4333};
Synonyms=GLT {ECO:0000303|PubMed:21741933},
GLTSCR2 {ECO:0000303|PubMed:10708517},
PICT1 {ECO:0000303|PubMed:24556985};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-389, AND TISSUE SPECIFICITY.
PubMed=10708517; DOI=10.1006/geno.1999.6101;
Smith J.S., Tachibana I., Pohl U., Lee H.K., Thanarajasingam U.,
Portier B.P., Ueki K., Billings S., Ramaswamy S., Mohrenweiser H.W.,
Scheithauer B.W., Louis D.N., Jenkins R.B.;
"A transcript map of the chromosome 19q-Arm glioma tumor suppressor
region.";
Genomics 64:44-50(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-389.
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 9-478, SUBCELLULAR LOCATION, AND
INTERACTION WITH HERPES SIMPLEX VIRUS 1 PROTEINS ICP22 AND ICP0
(MICROBIAL INFECTION).
PubMed=10196275;
Bruni R., Fineschi B., Ogle W.O., Roizman B.;
"A novel cellular protein, p60, interacting with both herpes simplex
virus 1 regulatory proteins ICP22 and ICP0 is modified in a cell-type-
specific manner and is recruited to the nucleus after infection.";
J. Virol. 73:3810-3817(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-478, AND VARIANT ARG-389.
The European IMAGE consortium;
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 218-477, AND VARIANT
ARG-389.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
Greco A., Hochstrasser D.F., Diaz J.-J.;
"Functional proteomic analysis of human nucleolus.";
Mol. Biol. Cell 13:4100-4109(2002).
[7]
FUNCTION, AND INTERACTION WITH PTEN.
PubMed=15355975; DOI=10.1074/jbc.C400377200;
Okahara F., Ikawa H., Kanaho Y., Maehama T.;
"Regulation of PTEN phosphorylation and stability by a tumor
suppressor candidate protein.";
J. Biol. Chem. 279:45300-45303(2004).
[8]
FUNCTION.
PubMed=16971513; DOI=10.1091/mbc.E06-04-0301;
Okahara F., Itoh K., Nakagawara A., Murakami M., Kanaho Y.,
Maehama T.;
"Critical role of PICT-1, a tumor suppressor candidate, in
phosphatidylinositol 3,4,5-trisphosphate signals and tumorigenic
transformation.";
Mol. Biol. Cell 17:4888-4895(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
INTERACTION WITH HUMAN HERPESVIRUS 8 PROTEIN ORF16 (MICROBIAL
INFECTION), SUBCELLULAR LOCATION, AND REGION.
PubMed=20042497; DOI=10.1128/JVI.00757-09;
Kalt I., Borodianskiy-Shteinberg T., Schachor A., Sarid R.;
"GLTSCR2/PICT-1, a putative tumor suppressor gene product, induces the
nucleolar targeting of the Kaposi's sarcoma-associated herpesvirus KS-
Bcl-2 protein.";
J. Virol. 84:2935-2945(2010).
[11]
FUNCTION, AND INDUCTION.
PubMed=21741933; DOI=10.1016/j.ajpath.2011.05.041;
Kim J.Y., Seok K.O., Kim Y.J., Bae W.K., Lee S., Park J.H.;
"Involvement of GLTSCR2 in the DNA Damage Response.";
Am. J. Pathol. 179:1257-1264(2011).
[12]
FUNCTION, INTERACTION WITH NF2, AND REGION.
PubMed=21167305; DOI=10.1016/j.biocel.2010.12.011;
Chen H., Mei L., Zhou L., Zhang X., Guo C., Li J., Wang H., Zhu Y.,
Zheng Y., Huang L.;
"Moesin-ezrin-radixin-like protein (merlin) mediates protein
interacting with the carboxyl terminus-1 (PICT-1)-induced growth
inhibition of glioblastoma cells in the nucleus.";
Int. J. Biochem. Cell Biol. 43:545-555(2011).
[13]
FUNCTION, INTERACTION WITH TP53, AND SUBCELLULAR LOCATION.
PubMed=22522597; DOI=10.1038/cdd.2012.40;
Lee S., Kim J.Y., Kim Y.J., Seok K.O., Kim J.H., Chang Y.J.,
Kang H.Y., Park J.H.;
"Nucleolar protein GLTSCR2 stabilizes p53 in response to ribosomal
stresses.";
Cell Death Differ. 19:1613-1622(2012).
[14]
SUBCELLULAR LOCATION, AND REGION.
PubMed=22292050; DOI=10.1371/journal.pone.0030825;
Kalt I., Levy A., Borodianskiy-Shteinberg T., Sarid R.;
"Nucleolar localization of GLTSCR2/PICT-1 is mediated by multiple
unique nucleolar localization sequences.";
PLoS ONE 7:E30825-E30825(2012).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[16]
FUNCTION.
PubMed=24120868; DOI=10.1016/j.celrep.2013.08.049;
Sloan K.E., Bohnsack M.T., Watkins N.J.;
"The 5S RNP couples p53 homeostasis to ribosome biogenesis and
nucleolar stress.";
Cell Rep. 5:237-247(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-93, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=24923447; DOI=10.1074/jbc.M114.571893;
Maehama T., Kawahara K., Nishio M., Suzuki A., Hanada K.;
"Nucleolar stress induces ubiquitination-independent proteasomal
degradation of PICT1 protein.";
J. Biol. Chem. 289:20802-20812(2014).
[19]
SUBUNIT.
PubMed=24735870; DOI=10.1016/j.jmb.2014.04.006;
Borodianskiy-Shteinberg T., Kalt I., Kipper S., Nachum N., Katz S.,
Pauker M.H., Barda-Saad M., Gerber D., Sarid R.;
"The nucleolar PICT-1/GLTSCR2 protein forms homo-oligomers.";
J. Mol. Biol. 426:2363-2378(2014).
[20]
FUNCTION, INTERACTION WITH RPL11, AND INDUCTION.
PubMed=24556985; DOI=10.1073/pnas.1400705111;
Yoon J.C., Ling A.J., Isik M., Lee D.Y., Steinbaugh M.J., Sack L.M.,
Boduch A.N., Blackwell T.K., Sinclair D.A., Elledge S.J.;
"GLTSCR2/PICT1 links mitochondrial stress and Myc signaling.";
Proc. Natl. Acad. Sci. U.S.A. 111:3781-3786(2014).
[21]
FUNCTION, INTERACTION WITH NPM1, AND SUBCELLULAR LOCATION.
PubMed=25956029; DOI=10.1016/j.ajpath.2015.03.016;
Kim J.Y., Cho Y.E., Park J.H.;
"The nucleolar protein GLTSCR2 is an upstream negative regulator of
the oncogenic Nucleophosmin-MYC axis.";
Am. J. Pathol. 185:2061-2068(2015).
[22]
FUNCTION.
PubMed=25818168; DOI=10.1111/jcmm.12474;
Kim J.Y., Cho Y.E., An Y.M., Kim S.H., Lee Y.G., Park J.H., Lee S.;
"GLTSCR2 is an upstream negative regulator of nucleophosmin in
cervical cancer.";
J. Cell. Mol. Med. 19:1245-1252(2015).
[23]
SUBUNIT, SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=26903295; DOI=10.1016/j.bbrc.2016.02.070;
Lee S., Cho Y.E., Kim Y.J., Park J.H.;
"c-Jun N-terminal kinase regulates the nucleoplasmic translocation and
stability of nucleolar GLTSCR2 protein.";
Biochem. Biophys. Res. Commun. 472:95-100(2016).
[24]
FUNCTION, INTERACTION WITH UBTF, AND SUBCELLULAR LOCATION.
PubMed=27729611; DOI=10.18632/oncotarget.12288;
Chen H., Duo Y., Hu B., Wang Z., Zhang F., Tsai H., Zhang J., Zhou L.,
Wang L., Wang X., Huang L.;
"PICT-1 triggers a pro-death autophagy through inhibiting rRNA
transcription and AKT/mTOR/p70S6K signaling pathway.";
Oncotarget 7:78747-78763(2016).
[25]
FUNCTION, INTERACTION WITH RPL11, SUBCELLULAR LOCATION, INDUCTION,
PHOSPHORYLATION, AND MUTAGENESIS OF SER-233 AND THR-289.
PubMed=27829214; DOI=10.18632/oncotarget.13082;
Chen H., Han L., Tsai H., Wang Z., Wu Y., Duo Y., Cao W., Chen L.,
Tan Z., Xu N., Huang X., Zhuang J., Huang L.;
"PICT-1 is a key nucleolar sensor in DNA damage response signaling
that regulates apoptosis through the RPL11-MDM2-p53 pathway.";
Oncotarget 7:83241-83257(2016).
[26]
FUNCTION, INTERACTION WITH DDX58, AND SUBCELLULAR LOCATION.
PubMed=27824081; DOI=10.1038/srep36226;
Wang P., Meng W., Han S.C., Li C.C., Wang X.J., Wang X.J.;
"The nucleolar protein GLTSCR2 is required for efficient viral
replication.";
Sci. Rep. 6:36226-36226(2016).
[27]
INTERACTION WITH CDKN2A/ISOFORM TUMOR SUPPRESSOR ARF, SUBCELLULAR
LOCATION, AND REGION.
PubMed=27323397; DOI=10.18632/oncotarget.9957;
Lee S., Cho Y.E., Kim S.H., Kim Y.J., Park J.H.;
"GLTSCR2 promotes the nucleoplasmic translocation and subsequent
degradation of nucleolar ARF.";
Oncotarget 8:16293-16302(2017).
-!- FUNCTION: Nucleolar protein which is involved in the integration
of the 5S RNP into the ribosomal large subunit during ribosome
biogenesis (PubMed:24120868). In ribosome biogenesis, may also
play a role in rRNA transcription (PubMed:27729611). Also
functions as a nucleolar sensor that regulates the activation of
p53/TP53 in response to ribosome biogenesis perturbation, DNA
damage and other stress conditions (PubMed:21741933,
PubMed:24120868, PubMed:27829214). DNA damage or perturbation of
ribosome biogenesis disrupt the interaction between NOP53 and
RPL11 allowing RPL11 transport to the nucleoplasm where it can
inhibit MDM2 and allow p53/TP53 activation (PubMed:24120868,
PubMed:27829214). It may also positively regulate the function of
p53/TP53 in cell cycle arrest and apoptosis through direct
interaction, preventing its MDM2-dependent ubiquitin-mediated
proteasomal degradation (PubMed:22522597). Originally identified
as a tumor suppressor, it may also play a role in cell
proliferation and apoptosis by positively regulating the stability
of PTEN, thereby antagonizing the PI3K-AKT/PKB signaling pathway
(PubMed:15355975, PubMed:16971513, PubMed:27729611). May also
inhibit cell proliferation and increase apoptosis through its
interaction with NF2 (PubMed:21167305). May negatively regulate
NPM1 by regulating its nucleoplasmic localization, oligomerization
and ubiquitin-mediated proteasomal degradation (PubMed:25818168).
Thereby, may prevent NPM1 interaction with MYC and negatively
regulate transcription mediated by the MYC-NPM1 complex
(PubMed:25956029). May also regulate cellular aerobic respiration
(PubMed:24556985). In the cellular response to viral infection,
may play a role in the attenuation of interferon-beta through the
inhibition of DDX58/RIG-1 (PubMed:27824081).
{ECO:0000269|PubMed:15355975, ECO:0000269|PubMed:16971513,
ECO:0000269|PubMed:21167305, ECO:0000269|PubMed:21741933,
ECO:0000269|PubMed:22522597, ECO:0000269|PubMed:24120868,
ECO:0000269|PubMed:24556985, ECO:0000269|PubMed:25818168,
ECO:0000269|PubMed:25956029, ECO:0000269|PubMed:27729611,
ECO:0000269|PubMed:27824081, ECO:0000269|PubMed:27829214}.
-!- SUBUNIT: Homooligomer (PubMed:24735870, PubMed:26903295).
Interacts with PTEN; regulates PTEN phosphorylation and increases
its stability (PubMed:15355975). Interacts with RPL11; retains
RPL11 into the nucleolus (PubMed:24556985, PubMed:27829214).
Interacts with CDKN2A/isoform tumor suppressor ARF; the
interaction is direct and promotes ARF nucleoplasmic
relocalization and ubiquitin-mediated proteasomal degradation
(PubMed:27323397). Interacts with NPM1; the interaction is direct
and competitive with MYC (PubMed:25956029). Interacts with NF2
(via FERM domain); the interaction is direct (PubMed:21167305).
Interacts with p53/TP53 (via the oligomerization region); the
interaction is direct and may prevent the MDM2-mediated
proteasomal degradation of p53/TP53 (PubMed:22522597). Interacts
with DDX58; may regulate DDX58 through USP15-mediated 'Lys-63'-
linked deubiquitination (PubMed:27824081). Interacts with UBTF
(PubMed:27729611). {ECO:0000269|PubMed:15355975,
ECO:0000269|PubMed:21167305, ECO:0000269|PubMed:22522597,
ECO:0000269|PubMed:24556985, ECO:0000269|PubMed:24735870,
ECO:0000269|PubMed:25956029, ECO:0000269|PubMed:26903295,
ECO:0000269|PubMed:27323397, ECO:0000269|PubMed:27729611,
ECO:0000269|PubMed:27824081, ECO:0000269|PubMed:27829214}.
-!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus
1 early proteins ICP22 and ICP0 (PubMed:10196275). Interacts with
human herpesvirus 8 protein ORF16; may sequester ORF16 in host
nucleolus and reduce its antiapoptotic activity (PubMed:20042497).
{ECO:0000269|PubMed:10196275, ECO:0000269|PubMed:20042497}.
-!- INTERACTION:
O95786:DDX58; NbExp=2; IntAct=EBI-720156, EBI-995350;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:10196275, ECO:0000269|PubMed:12429849,
ECO:0000269|PubMed:20042497, ECO:0000269|PubMed:22292050,
ECO:0000269|PubMed:22522597, ECO:0000269|PubMed:24923447,
ECO:0000269|PubMed:25956029, ECO:0000269|PubMed:27729611,
ECO:0000269|PubMed:27829214}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:22522597, ECO:0000269|PubMed:24923447,
ECO:0000269|PubMed:26903295, ECO:0000269|PubMed:27323397}. Note=In
the nucleolus may be more specifically localized to the fibrillar
center (PubMed:27729611). Mainly nucleolar it relocalizes to the
nucleoplasm under specific conditions including ribosomal stress
enabling it to interact and regulate nucleoplasmic proteins like
p53/TP53 (PubMed:22522597, PubMed:24923447, PubMed:27323397,
PubMed:26903295). Also detected in the cytosol (PubMed:24923447,
PubMed:27824081). {ECO:0000269|PubMed:22522597,
ECO:0000269|PubMed:24923447, ECO:0000269|PubMed:26903295,
ECO:0000269|PubMed:27323397, ECO:0000269|PubMed:27729611,
ECO:0000269|PubMed:27824081}.
-!- TISSUE SPECIFICITY: Expressed at high levels in heart and
pancreas, moderate levels in placenta, liver, skeletal muscle, and
kidney, and low levels in brain and lung.
{ECO:0000269|PubMed:10708517}.
-!- INDUCTION: Down-regulated by nucleolar stress through ubiquitin-
independent proteasomal degradation (at protein level)
(PubMed:24923447). Up-regulated upon mitochondrial stress (at
protein level) (PubMed:24556985). Expression of the protein might
be regulated by DNA damage but results are not consistent
(PubMed:21741933, PubMed:27829214). {ECO:0000269|PubMed:21741933,
ECO:0000269|PubMed:24556985, ECO:0000269|PubMed:24923447,
ECO:0000269|PubMed:27829214}.
-!- PTM: Ubiquitin-mediated proteasomal degradation is regulated by c-
JUN. It is associated with relocalization to the nucleoplasm and
decreased homooligomerization. {ECO:0000269|PubMed:26903295}.
-!- PTM: Phosphorylated upon DNA damage probably by ATM and DNA-PK;
may regulate NOP53 degradation. {ECO:0000269|PubMed:27829214}.
-!- SIMILARITY: Belongs to the NOP53 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/GLTSCR2ID40723ch19q13.html";
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EMBL; AF182076; AAF62873.1; -; mRNA.
EMBL; BC004229; AAH04229.2; -; mRNA.
EMBL; BC006311; AAH06311.1; -; mRNA.
EMBL; BC010095; AAH10095.1; -; mRNA.
EMBL; AF296124; AAG30413.1; -; mRNA.
EMBL; AL359335; CAB94786.1; -; mRNA.
EMBL; AL359336; CAB94787.1; -; mRNA.
EMBL; AL122063; CAB59242.1; -; mRNA.
CCDS; CCDS12705.1; -.
RefSeq; NP_056525.2; NM_015710.4.
UniGene; Hs.421907; -.
ProteinModelPortal; Q9NZM5; -.
BioGrid; 119021; 145.
IntAct; Q9NZM5; 25.
MINT; MINT-1410423; -.
STRING; 9606.ENSP00000246802; -.
iPTMnet; Q9NZM5; -.
PhosphoSitePlus; Q9NZM5; -.
BioMuta; GLTSCR2; -.
DMDM; 93141272; -.
SWISS-2DPAGE; Q9NZM5; -.
EPD; Q9NZM5; -.
MaxQB; Q9NZM5; -.
PaxDb; Q9NZM5; -.
PeptideAtlas; Q9NZM5; -.
PRIDE; Q9NZM5; -.
DNASU; 29997; -.
Ensembl; ENST00000246802; ENSP00000246802; ENSG00000105373.
GeneID; 29997; -.
KEGG; hsa:29997; -.
UCSC; uc002phm.3; human.
CTD; 29997; -.
DisGeNET; 29997; -.
EuPathDB; HostDB:ENSG00000105373.18; -.
GeneCards; NOP53; -.
HGNC; HGNC:4333; NOP53.
HPA; HPA018999; -.
HPA; HPA049600; -.
MIM; 605691; gene.
neXtProt; NX_Q9NZM5; -.
OpenTargets; ENSG00000105373; -.
PharmGKB; PA28736; -.
eggNOG; KOG2823; Eukaryota.
eggNOG; ENOG4111GSN; LUCA.
GeneTree; ENSGT00390000017267; -.
HOGENOM; HOG000070127; -.
HOVERGEN; HBG051849; -.
InParanoid; Q9NZM5; -.
KO; K14840; -.
OMA; KSAWRKT; -.
OrthoDB; EOG091G0BKI; -.
PhylomeDB; Q9NZM5; -.
TreeFam; TF313004; -.
ChiTaRS; GLTSCR2; human.
GeneWiki; GLTSCR2; -.
GenomeRNAi; 29997; -.
PRO; PR:Q9NZM5; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105373; -.
CleanEx; HS_GLTSCR2; -.
ExpressionAtlas; Q9NZM5; baseline and differential.
Genevisible; Q9NZM5; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0001650; C:fibrillar center; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; NAS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0008097; F:5S rRNA binding; IDA:HGNC.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
GO; GO:0007095; P:mitotic G2 DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0031333; P:negative regulation of protein complex assembly; IMP:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:1901797; P:negative regulation of signal transduction by p53 class mediator; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:1901837; P:negative regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter; IMP:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:1903006; P:positive regulation of protein K63-linked deubiquitination; IMP:UniProtKB.
GO; GO:1902570; P:protein localization to nucleolus; IEA:Ensembl.
GO; GO:1990173; P:protein localization to nucleoplasm; IMP:UniProtKB.
GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
GO; GO:1903715; P:regulation of aerobic respiration; IMP:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
GO; GO:0001932; P:regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0039535; P:regulation of RIG-I signaling pathway; IMP:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IMP:UniProtKB.
GO; GO:0000027; P:ribosomal large subunit assembly; IMP:HGNC.
GO; GO:0000055; P:ribosomal large subunit export from nucleus; IBA:GO_Central.
InterPro; IPR011687; Nop53/GLTSCR2.
PANTHER; PTHR14211; PTHR14211; 1.
Pfam; PF07767; Nop53; 1.
PIRSF; PIRSF017302; Gltscr2; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Ribosome biogenesis.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 478 Ribosome biogenesis protein NOP53.
/FTId=PRO_0000218960.
REGION 148 431 Mediates interaction with CDKN2A/isoform
tumor suppressor ARF.
{ECO:0000269|PubMed:27323397}.
REGION 181 478 Mediates interaction with NF2.
{ECO:0000269|PubMed:21167305}.
REGION 342 386 Mediates interaction with human
herpesvirus 8 protein ORF16.
{ECO:0000269|PubMed:20042497}.
REGION 347 395 Nucleolar localization signal.
{ECO:0000269|PubMed:22292050}.
REGION 396 478 Nucleolar localization signal.
{ECO:0000269|PubMed:22292050}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 93 93 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 305 305 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BK35}.
VARIANT 16 16 S -> R (in dbSNP:rs1042401).
/FTId=VAR_024456.
VARIANT 389 389 Q -> R (in dbSNP:rs1804994).
{ECO:0000269|PubMed:10708517,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|Ref.4}.
/FTId=VAR_011486.
MUTAGEN 233 233 S->A: Decreased phosphorylation,
degradation and increased interaction
with RPL11 in response to DNA damage;
when associated with A-289.
{ECO:0000269|PubMed:27829214}.
MUTAGEN 233 233 S->D: Loss of localization to the
nucleolus and in response to DNA damage
increased degradation and decreased
interaction with RPL11; when associated
with D-289.
{ECO:0000269|PubMed:27829214}.
MUTAGEN 289 289 T->A: Decreased degradation in response
to DNA damage. Decreased phosphorylation,
degradation and increased interaction
with RPL11 in response to DNA damage;
when associated with A-233.
{ECO:0000269|PubMed:27829214}.
MUTAGEN 289 289 T->D: Loss of localization to the
nucleolus and in response to DNA damage
increased degradation and decreased
interaction with RPL11; when associated
with D-233.
{ECO:0000269|PubMed:27829214}.
CONFLICT 9 9 G -> R (in Ref. 3; AAG30413).
{ECO:0000305}.
CONFLICT 146 191 RRKEQLWEKLAKQGELPREVRRAQARLLNPSATRAKPGPQD
TVERP -> SGRSSYGRSWPSRASSPGGAQGPSPVAQPFCN
KGPNPAPGHRIAA (in Ref. 3; AAG30413).
{ECO:0000305}.
CONFLICT 198 215 SDNPLDRPLVGQDEFFLE -> LNNPDKPVVWPGCLFPG
(in Ref. 3; AAG30413). {ECO:0000305}.
CONFLICT 235 235 A -> S (in Ref. 2; AAH04229).
{ECO:0000305}.
CONFLICT 417 417 D -> H (in Ref. 3; AAG30413).
{ECO:0000305}.
CONFLICT 433 477 PEGNILRDRFKSFQRRNMIEPRERAKFKRKYKVKLVEKRAF
REIQ -> VLTVSCRGAPCPVMTPSLLPVPPRGYGRHHGCP
WAGPVGPMPRG (in Ref. 5; CAB59242).
{ECO:0000305}.
CONFLICT 434 478 EGNILRDRFKSFQRRNMIEPRERAKFKRKYKVKLVEKRAFR
EIQL -> RGQHSFETGSRAFRGGI (in Ref. 3;
AAG30413). {ECO:0000305}.
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


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