NOC2L_BOVIN
ID NOC2L_BOVIN Reviewed; 746 AA.
AC Q3SYU1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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.
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 -!- SIMILARITY: Belongs to the NOC2 family. {ECO:0000305}.
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DR EMBL; BC103386; AAI03387.1; -; mRNA.
DR RefSeq; NP_001029498.1; NM_001034326.1.
DR AlphaFoldDB; Q3SYU1; -.
DR STRING; 9913.ENSBTAP00000021980; -.
DR PaxDb; Q3SYU1; -.
DR PRIDE; Q3SYU1; -.
DR Ensembl; ENSBTAT00000021980; ENSBTAP00000021980; ENSBTAG00000016528.
DR GeneID; 508638; -.
DR KEGG; bta:508638; -.
DR CTD; 26155; -.
DR VEuPathDB; HostDB:ENSBTAG00000016528; -.
DR VGNC; VGNC:32146; NOC2L.
DR eggNOG; KOG2256; Eukaryota.
DR GeneTree; ENSGT00390000010057; -.
DR HOGENOM; CLU_011272_1_2_1; -.
DR InParanoid; Q3SYU1; -.
DR OMA; FPLRFHC; -.
DR OrthoDB; 1194328at2759; -.
DR Reactome; R-BTA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000016528; Expressed in retina and 104 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0031491; F:nucleosome binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
DR GO; GO:0031497; P:chromatin assembly; IEA:Ensembl.
DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; IEA:Ensembl.
DR GO; GO:0035067; P:negative regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Apoptosis; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..746
FT /note="Nucleolar complex protein 2 homolog"
FT /id="PRO_0000247488"
FT REGION 19..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3T9"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3T9"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3T9"
FT MOD_RES 743
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3T9"
SQ SEQUENCE 746 AA; 84744 MW; 4EE59DE1113F0D76 CRC64;
MAAALSRKRR LEELTVDEFL ASGFDSESES EPEGAPEAET QAVRAAAREP DGPGGSPLAS
RRKGGASEHK DQLSRLKDKD PEFYKFLQEN DQSLLNFSDS DSSEDEEEQL HSLPNMLEEA
SEEEEEEDGV PRGPEGKRRD SVPVTLAMVE KWKQAAKQHL TPKLFHEVVQ AFRAAVATTQ
GDEEGAETSK FQVTDSAVFN ALVTFCIRDL FGCLQKLLFG KAPKDSSRVL QPSSSPLWAK
LRLDVKAYLS SVIQLVACVA EATVAAAILQ HVGSSVPYYL TFPKQCRMLL KRMVVLWSTG
EETLRVLAFV VLIKVCRHKK DVFLSPVLKQ MYITYVRNCK FTSPSTLPLI NFMQRTLTEL
LALDTGVAYQ HAFLYIRQLA IHLRNAMTTR RKETYQSVYN WQFVHCLYLW CRALSTICPS
EALQPLIYPL SQVVIGCIKL VPTARFYPLR MHCVRALTLL SESTGTFIPV LPFILEIFQQ
VDFNRRPGRI SSRPINFAVI LKLSKVNLQE KAYRDGLVEQ LYDLTLEYLH SQAHSIAFPE
LVLPAVLQLK SFLRECKVAN YCRQVRQLLE KVQENAEHIR SVRQKVSFGV SDQRAVDAWE
KRTREEGTPL TKYYSQWRKL RDREIQLEIS GKERLEDLNF PEVKRRKVGD RKDEDRAEFK
DLFDLESDDE DDAPDFTKRG MPGSPGAWQK VEEEDDDSSS SSGEEEVSKS EDGSPDTEAG
LDPQELWQLA QGPEDELQDL QLSEED
