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Nuclear receptor corepressor 1 (N-CoR) (N-CoR1) (Fragment)

 NCOR1_RAT               Reviewed;         533 AA.
Q9WUB5; O70463;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
20-JUN-2018, entry version 124.
RecName: Full=Nuclear receptor corepressor 1;
Short=N-CoR;
Short=N-CoR1;
Flags: Fragment;
Name=Ncor1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=10441327; DOI=10.1093/hmg/8.9.1647;
Boutell J.M., Thomas P., Neal J.W., Weston V.J., Duce J., Harper P.S.,
Jones A.L.;
"Aberrant interactions of transcriptional repressor proteins with the
Huntington's disease gene product, huntingtin.";
Hum. Mol. Genet. 8:1647-1655(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 476-528.
TISSUE=Skeletal muscle;
PubMed=10491148; DOI=10.1046/j.1432-1327.1999.00706.x;
Schuler M.J., Buehler S., Pette D.;
"Effects of contractile activity and hypothyroidism on nuclear hormone
receptor mRNA isoforms in rat skeletal muscle.";
Eur. J. Biochem. 264:982-988(1999).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-196; SER-214;
SER-230; SER-245; SER-529 AND SER-531, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Mediates transcriptional repression by certain nuclear
receptors. Part of a complex which promotes histone deacetylation
and the formation of repressive chromatin structures which may
impede the access of basal transcription factors. Participates in
the transcriptional repressor activity produced by BCL6 (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Forms a large corepressor complex that contains SIN3A/B
and histone deacetylases HDAC1 and HDAC2. This complex associates
with the thyroid receptor (TR) and the retinoid acid receptor
(RAR) in the absence of ligand. Interacts directly with RARA; the
interaction is facilitated with RARA trimethylation. Component of
the N-Cor repressor complex, at least composed of CBFA2T3, HEXIM1,
NCOR1, NCOR2, HDAC3, TBL1X, TBL1XR1, CORO2A and GPS2. Interacts
with ZBTB33; the interaction serves to recruit the N-CoR complex
to promoter regions containing methylated CpG dinucleotides.
Interacts with TRIM28 and KDM3A. Interacts (via the RD1 domain)
with BAZ1A (via its N-terminal); the interaction corepresses a
number of NCOR1-regulated genes. Interacts with BCL6, C1D, DACH1,
HEXIM1, HDAC7, RORA, RORC, SAP30, SIAH2, SIN3A and SIN3B. May
interact with DEAF1. Interacts with RXRA. Interacts with SETD5.
Interacts with VDR. {ECO:0000250|UniProtKB:O75376,
ECO:0000250|UniProtKB:Q60974}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- DOMAIN: The N-terminal region contains three independent domains
that are capable of mediating transcriptional repression (RD1, RD2
and RD3). {ECO:0000250}.
-!- DOMAIN: The C-terminal region contains two separate nuclear
receptor-interacting domains (ID1 and ID2), each of which contains
a conserved sequence referred to as the CORNR box. This motif is
necessary and sufficient for binding to unligated nuclear hormone
receptors, while sequences flanking the CORNR box determine the
precise nuclear hormone receptor specificity (By similarity).
{ECO:0000250}.
-!- PTM: Ubiquitinated; mediated by SIAH2 and leading to its
subsequent proteasomal degradation. {ECO:0000250}.
-!- SIMILARITY: Belongs to the N-CoR nuclear receptor corepressors
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF124821; AAD32566.1; -; mRNA.
EMBL; AF059311; AAC14567.1; -; mRNA.
UniGene; Rn.24948; -.
iPTMnet; Q9WUB5; -.
PeptideAtlas; Q9WUB5; -.
PRIDE; Q9WUB5; -.
UCSC; RGD:3612; rat.
RGD; 3612; Ncor1.
HOGENOM; HOG000113746; -.
HOVERGEN; HBG052587; -.
InParanoid; Q9WUB5; -.
PhylomeDB; Q9WUB5; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0003682; F:chromatin binding; IDA:RGD.
GO; GO:0030331; F:estrogen receptor binding; IPI:RGD.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:RGD.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0042974; F:retinoic acid receptor binding; IPI:RGD.
GO; GO:0046965; F:retinoid X receptor binding; IPI:RGD.
GO; GO:0001012; F:RNA polymerase II regulatory region DNA binding; IDA:RGD.
GO; GO:0021549; P:cerebellum development; IEP:RGD.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0007595; P:lactation; IEP:RGD.
GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
1: Evidence at protein level;
Chromatin regulator; Complete proteome; DNA-binding; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN <1 533 Nuclear receptor corepressor 1.
/FTId=PRO_0000055619.
REGION 130 209 ID1. {ECO:0000250}.
REGION 145 148 Required for interaction with RARA in the
absence of its ligand. {ECO:0000250}.
REGION 306 367 ID2. {ECO:0000250}.
MOTIF 29 33 CORNR box 1.
MOTIF 153 157 CORNR box 2.
MOTIF 357 361 CORNR box 3.
COMPBIAS 48 59 Poly-Ser.
MOD_RES 73 73 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 196 196 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 230 230 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 278 278 Phosphoserine.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 492 492 Phosphothreonine.
{ECO:0000250|UniProtKB:O75376}.
MOD_RES 529 529 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 531 531 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CONFLICT 484 484 R -> W (in Ref. 2; AAC14567).
{ECO:0000305}.
CONFLICT 497 497 A -> V (in Ref. 2; AAC14567).
{ECO:0000305}.
NON_TER 1 1
SEQUENCE 533 AA; 57795 MW; 7DF60F8228227EC2 CRC64;
KDKGPPPKSR YEEELRTRGK TTITAANFID VIITRQIASD KDARERGSQS SDSSSSLSSH
RYEAPSDAIE VISPASSPAP PQEKPQTYQP EMVKANQAEN ESPQQYEGPL THYRSQQGSP
SPQQQPPLPP SSQAEGMGQV PRTHRLITLA DHICQIITQD FARNQVPSQP STSTFQTSPS
ALSSTPVRTK PSSRYSPESQ SQTVLHPRPG PRVSPENLVD KSRGSRPGKS PERSHIPSEP
YEPISPPQGP AVHEKQDSML LLSQRGMDPA EQRSDSRSPG SISYLPYFFT KLESTSPMVK
SKKQEIFRKL NSSGGGDSDM AAAQPGTEIF NLPAVTTSGA VSSRSHSFAD PASNLGLEDI
IRKALMGSFD DKVEDHGVVM PHPVGVVPGS ASTSVVTSSE TRRDEGDPSP HSGVCKPKLI
NKSNSRKSKS PIPGQNYLGT ERPSSVSSVH SEGDYHRQTP GWAWEDRPSS TGSTQFPYNP
LTIRMLSSTP PTPIACAPSA ITQAAPHQQS RIWEREPAPL LSAQYETLSD SDD


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