NOP53_MOUSE
ID NOP53_MOUSE Reviewed; 484 AA.
AC Q8BK35; Q8VD18;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Ribosome biogenesis protein NOP53 {ECO:0000305};
DE AltName: Full=Glioma tumor suppressor candidate region gene 2 protein {ECO:0000312|MGI:MGI:2154441};
DE AltName: Full=PreS1-binding protein {ECO:0000312|EMBL:AAS46029.1};
GN Name=Nop53 {ECO:0000312|MGI:MGI:2154441};
GN Synonyms=Gltscr2 {ECO:0000312|MGI:MGI:2154441},
GN Pict1 {ECO:0000303|PubMed:21804542};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cheng J., Dong J., Liu Y.;
RT "Cloning of murine gene of hepatitis B virus PreS1 binding protein.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Heart, Kidney, and Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, INTERACTION WITH RPL11, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21804542; DOI=10.1038/nm.2392;
RA Sasaki M., Kawahara K., Nishio M., Mimori K., Kogo R., Hamada K., Itoh B.,
RA Wang J., Komatsu Y., Yang Y.R., Hikasa H., Horie Y., Yamashita T.,
RA Kamijo T., Zhang Y., Zhu Y., Prives C., Nakano T., Mak T.W., Sasaki T.,
RA Maehama T., Mori M., Suzuki A.;
RT "Regulation of the MDM2-P53 pathway and tumor growth by PICT1 via nucleolar
RT RPL11.";
RL Nat. Med. 17:944-951(2011).
CC -!- FUNCTION: Nucleolar protein which is involved in the integration of the
CC 5S RNP into the ribosomal large subunit during ribosome biogenesis. In
CC ribosome biogenesis, may also play a role in rRNA transcription (By
CC similarity). Also functions as a nucleolar sensor that regulates the
CC activation of p53/TP53 in response to ribosome biogenesis perturbation,
CC DNA damage and other stress conditions. DNA damage or perturbation of
CC ribosome biogenesis disrupt the interaction between NOP53 and RPL11
CC allowing RPL11 transport to the nucleoplasm where it can inhibit MDM2
CC and allow p53/TP53 activation (PubMed:21804542). It may also positively
CC regulate the function of p53/TP53 in cell cycle arrest and apoptosis
CC through direct interaction, preventing its MDM2-dependent ubiquitin-
CC mediated proteasomal degradation. 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. May also inhibit cell proliferation
CC and increase apoptosis through its interaction with NF2. May negatively
CC regulate NPM1 by regulating its nucleoplasmic localization,
CC oligomerization and ubiquitin-mediated proteasomal degradation.
CC Thereby, may prevent NPM1 interaction with MYC and negatively regulate
CC transcription mediated by the MYC-NPM1 complex. May also regulate
CC cellular aerobic respiration. In the cellular response to viral
CC infection, may play a role in the attenuation of interferon-beta
CC through the inhibition of DDX58/RIG-1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9NZM5, ECO:0000269|PubMed:21804542}.
CC -!- SUBUNIT: Homooligomer. Interacts with PTEN; regulates PTEN
CC phosphorylation and increases its stability (By similarity). Interacts
CC with RPL11; retains RPL11 into the nucleolus (PubMed:21804542).
CC Interacts with CDKN2A/isoform tumor suppressor ARF; the interaction is
CC direct and promotes ARF nucleoplasmic relocalization and ubiquitin-
CC mediated proteasomal degradation. Interacts with NPM1; the interaction
CC is direct and competitive with MYC. Interacts with NF2 (via FERM
CC domain); the interaction is direct. Interacts with p53/TP53 (via the
CC oligomerization region); the interaction is direct and may prevent the
CC MDM2-mediated proteasomal degradation of p53/TP53. Interacts with
CC DDX58; may regulate DDX58 through USP15-mediated 'Lys-63'-linked
CC deubiquitination. Interacts with UBTF (By similarity).
CC {ECO:0000250|UniProtKB:Q9NZM5, ECO:0000269|PubMed:21804542}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:21804542}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9NZM5}. Note=In the
CC nucleolus may be more specifically localized to the fibrillar center.
CC Mainly nucleolar it relocalizes to the nucleoplasm under specific
CC conditions including ribosomal stress enabling it to interact and
CC regulate nucleoplasmic proteins like p53/TP53. Also detected in the
CC cytosol. {ECO:0000250|UniProtKB:Q9NZM5}.
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:0000250|UniProtKB:Q9NZM5}.
CC -!- PTM: Phosphorylated upon DNA damage probably by ATM and DNA-PK; may
CC regulate NOP53 degradation. {ECO:0000250|UniProtKB:Q9NZM5}.
CC -!- DISRUPTION PHENOTYPE: Knockout embryos are not able to form viable
CC blastocysts. Transgenic mice lacking the expression of Nop53 in the
CC thymus display a dramatic reduction of the number of thymic cells and
CC of the size of the thymus. {ECO:0000269|PubMed:21804542}.
CC -!- SIMILARITY: Belongs to the NOP53 family. {ECO:0000305}.
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DR EMBL; AY535001; AAS46029.1; -; mRNA.
DR EMBL; AK077341; BAC36760.1; -; mRNA.
DR EMBL; AK146916; BAE27528.1; -; mRNA.
DR EMBL; AK151836; BAE30729.1; -; mRNA.
DR EMBL; AK160070; BAE35605.1; -; mRNA.
DR EMBL; AK169290; BAE41047.1; -; mRNA.
DR EMBL; AC148990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466654; EDL42118.1; -; Genomic_DNA.
DR EMBL; BC017637; AAH17637.1; -; mRNA.
DR CCDS; CCDS39779.1; -.
DR RefSeq; NP_598592.2; NM_133831.3.
DR AlphaFoldDB; Q8BK35; -.
DR STRING; 10090.ENSMUSP00000043981; -.
DR iPTMnet; Q8BK35; -.
DR PhosphoSitePlus; Q8BK35; -.
DR EPD; Q8BK35; -.
DR jPOST; Q8BK35; -.
DR MaxQB; Q8BK35; -.
DR PaxDb; Q8BK35; -.
DR PeptideAtlas; Q8BK35; -.
DR PRIDE; Q8BK35; -.
DR ProteomicsDB; 253095; -.
DR Antibodypedia; 18226; 200 antibodies from 25 providers.
DR DNASU; 68077; -.
DR Ensembl; ENSMUST00000044158; ENSMUSP00000043981; ENSMUSG00000041560.
DR GeneID; 68077; -.
DR KEGG; mmu:68077; -.
DR UCSC; uc009fgr.2; mouse.
DR CTD; 29997; -.
DR MGI; MGI:2154441; Nop53.
DR VEuPathDB; HostDB:ENSMUSG00000041560; -.
DR eggNOG; KOG2823; Eukaryota.
DR GeneTree; ENSGT00390000017267; -.
DR HOGENOM; CLU_035888_0_0_1; -.
DR InParanoid; Q8BK35; -.
DR OMA; WRKTDIQ; -.
DR OrthoDB; 1025498at2759; -.
DR PhylomeDB; Q8BK35; -.
DR TreeFam; TF313004; -.
DR BioGRID-ORCS; 68077; 19 hits in 70 CRISPR screens.
DR PRO; PR:Q8BK35; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BK35; protein.
DR Bgee; ENSMUSG00000041560; Expressed in embryonic brain and 246 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0033553; C:rDNA heterochromatin; ISO:MGI.
DR GO; GO:0008097; F:5S rRNA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:1901797; P:negative regulation of signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:1901837; P:negative regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISS: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; ISS:UniProtKB.
DR GO; GO:1902570; P:protein localization to nucleolus; IMP:UniProtKB.
DR GO; GO:1990173; P:protein localization to nucleoplasm; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:1903715; P:regulation of aerobic respiration; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0039535; P:regulation of RIG-I signaling pathway; ISO:MGI.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; ISO:MGI.
DR GO; GO:0000027; P:ribosomal large subunit assembly; ISS:UniProtKB.
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; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NZM5"
FT CHAIN 2..484
FT /note="Ribosome biogenesis protein NOP53"
FT /id="PRO_0000440968"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..437
FT /note="Mediates interaction with CDKN2A/isoform tumor
FT suppressor ARF"
FT /evidence="ECO:0000250|UniProtKB:Q9NZM5"
FT REGION 304..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..392
FT /note="Mediates interaction with human herpesvirus 8
FT protein ORF16"
FT /evidence="ECO:0000250|UniProtKB:Q9NZM5"
FT REGION 353..401
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9NZM5"
FT REGION 402..484
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q9NZM5"
FT COMPBIAS 336..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZM5"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZM5"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 317
FT /note="G -> A (in Ref. 5; AAH17637)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="A -> V (in Ref. 5; AAH17637)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 55793 MW; EB67949BCBE92D44 CRC64;
MAAGGNRDGE KRGSRSQADS GFLGLRPTSV DPALRRRRRG PRNKKRGWRR LAEEPLGLEV
DQFLEDVRLQ ERTTGGLLAE APNEKLFFVD TGFKRKEPRK KRTLVQKKSQ RLQKPLRVDL
ALENHSKIPA PKDILAHQVP NAKKLRRKEE LWEKLAKQGE LPRDVRKAQA RLLSPPTPKA
KPGPQDIIER PFYDLWNPDN PLDTPLIGQD AFFLEQTKKK GVRRPQRLHI KPSQVPAVEV
IPAGASYNPT FEDHQALLRE AHEVELQREK EAEKLERQLA LPTSEQAATQ ESVFREMCEG
LLEESDGEDE HEAGRAGQPE AGDGTTEISP TGAAGPEKRM EKKTEQQRRR EKAARKLRVQ
QAALRAARLQ HQELFRLRGI KAQVARRLAE LARRREQRRI RRLAEADKPR RLGRLKYQAP
DIDVQLSSEL SGSLRTLKPE GHILRDRFKS FQKRNMIEPR ERAKFKRKYK VKLVEKRAYR
EIQL
