NOC2L_MOUSE
ID NOC2L_MOUSE Reviewed; 747 AA.
AC Q9WV70; Q8VE16;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Nucleolar complex protein 2 homolog;
DE Short=Protein NOC2 homolog;
DE AltName: Full=NOC2-like protein;
DE AltName: Full=Novel INHAT repressor;
GN Name=Noc2l; Synonyms=Nir;
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 [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 483-747.
RC STRAIN=H129;
RA Han S.J., Lee J.H.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16322561; DOI=10.1101/gad.351205;
RA Hublitz P., Kunowska N., Mayer U.P., Muller J.M., Heyne K., Yin N.,
RA Fritzsche C., Poli C., Miguet L., Schupp I.W., van Grunsven L.A.,
RA Potiers N., van Dorsselaer A., Metzger E., Roemer K., Schule R.;
RT "NIR is a novel INHAT repressor that modulates the transcriptional activity
RT of p53.";
RL Genes Dev. 19:2912-2924(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673 AND SER-674, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673 AND SER-674, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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).
CC -!- FUNCTION: Acts as an inhibitor of histone acetyltransferase activity;
CC prevents acetylation of all core histones by the EP300/p300 histone
CC acetyltransferase at p53/TP53-regulated target promoters in a histone
CC deacetylases (HDAC)-independent manner. Acts as a transcription
CC corepressor of p53/TP53- and TP63-mediated transactivation of the
CC p21/CDKN1A promoter. Involved in the regulation of p53/TP53-dependent
CC apoptosis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with p53/TP53. Interacts (via the N- and C-terminus
CC domains) with AURKB (via the middle kinase domain). Interacts with TP63
CC (via activation domain). Interacts with histone H3 (via N-terminus and
CC non-acetylated form preferentially). Associates with core histones and
CC nucleosomes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus,
CC nucleolus {ECO:0000250}. Note=Translocates from the nucleoli to the
CC nucleoplasm in presence of several stressors like ultraviolet
CC irradiation and actinomycin-D. Predominantly detected in the nucleoli
CC in non-mitotic cells. Predominantly detected in nucleoplasma in cells
CC undergoing mitosis (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16322561}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis between 8.5 and
CC 18.5 dpc. {ECO:0000269|PubMed:16322561}.
CC -!- SIMILARITY: Belongs to the NOC2 family. {ECO:0000305}.
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DR EMBL; BC020013; AAH20013.1; -; mRNA.
DR EMBL; AF155546; AAD38407.1; -; mRNA.
DR AlphaFoldDB; Q9WV70; -.
DR STRING; 10090.ENSMUSP00000137253; -.
DR iPTMnet; Q9WV70; -.
DR PhosphoSitePlus; Q9WV70; -.
DR EPD; Q9WV70; -.
DR jPOST; Q9WV70; -.
DR MaxQB; Q9WV70; -.
DR PaxDb; Q9WV70; -.
DR PeptideAtlas; Q9WV70; -.
DR PRIDE; Q9WV70; -.
DR ProteomicsDB; 295501; -.
DR MGI; MGI:1931051; Noc2l.
DR eggNOG; KOG2256; Eukaryota.
DR InParanoid; Q9WV70; -.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR ChiTaRS; Noc2l; mouse.
DR PRO; PR:Q9WV70; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9WV70; protein.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030690; C:Noc1p-Noc2p complex; IBA:GO_Central.
DR GO; GO:0030691; C:Noc2p-Noc3p complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISA:MGI.
DR GO; GO:0005634; C:nucleus; ISA:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISA:MGI.
DR GO; GO:0031491; F:nucleosome binding; ISO:MGI.
DR GO; GO:0002039; F:p53 binding; ISA:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0034644; P:cellular response to UV; ISO:MGI.
DR GO; GO:0031497; P:chromatin assembly; ISO:MGI.
DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; ISO:MGI.
DR GO; GO:0035067; P:negative regulation of histone acetylation; ISA:MGI.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISA:MGI.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR005343; Noc2.
DR PANTHER; PTHR12687; PTHR12687; 1.
DR Pfam; PF03715; Noc2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..747
FT /note="Nucleolar complex protein 2 homolog"
FT /id="PRO_0000121049"
FT REGION 23..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..721
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3T9"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 744
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3T9"
FT CONFLICT 531
FT /note="I -> T (in Ref. 2; AAD38407)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="E -> Q (in Ref. 2; AAD38407)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="A -> P (in Ref. 2; AAD38407)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 747 AA; 85424 MW; 1BC61817FC586C47 CRC64;
MAASRAPRRR LEDLSVDEFL ASGFESGSES ELEGAAEERR ARGAAWNRER RGARTSPGPA
GRLRKGRASE HKDQLSRLKD RDPEFYKFLQ ENDRSLLDFS DSDSSAEEEE PFHSLPDTLE
EASETEEDGG EDSDALPRGL RSKKNEPVPV TLAMVERWRQ GSRHHLTPRL FHEVVQAFRA
AVATTQGEQE AAETCRFQVA DSAVFNALVT FCIRDLCGCL QKLLFGKTPK DSNRLLLPSS
SPLWGKLRVD VKSYLSAVVQ LAACLAEATV SAAVLQHISS LVPYFLTFPK QCRMLLKRMV
VLWSTGEESL RVLAFLVLIR VCRHKKEAFL GPILKQMYIM YVRNCKFTSP STLPLISFMQ
RTLTEMLALD PSVSYQHAFL YIRQLAVHLR NAMTTGKKET HQSVYNWQYV HCLYLWCRVL
STLGSSEILQ PLLYPLSQII IGCIKLLPTA RFYPLRMHCV RALTLLSQTI GTFIPVLPFI
LEIFQQVDFN RRPGRMSSKP INFSVILKLS STNLQEKAYR DGLLEQLCDL ILEYLHSQAH
SIAFPELVLP TVLQLKSFLR ECKVANYCRQ VRQLLEKVQE NARHIESLRQ SATFSVSDRT
AVDAWEKQVR EEGTPLTRYY GHWKKLRDRE IQLEISGKER LEDLNFPEIK RRKVEDRKDE
DRKELKDLFE LDSSEGEDST DFFERGVPRL PEAHQGLKED QEEEDKEEGD SDSEDGDTDT
GVDLSELWQL AQGAQDELED LQLSEED
