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Nuclear receptor coactivator 6 (Activating signal cointegrator 2) (ASC-2) (Amplified in breast cancer protein 3) (Cancer-amplified transcriptional coactivator ASC-2) (Nuclear receptor coactivator RAP250) (NRC) (Nuclear receptor-activating protein, 250 kDa) (Peroxisome proliferator-activated receptor-interacting protein) (PPAR-interacting protein) (Thyroid hormone receptor-binding protein)

 NCOA6_MOUSE             Reviewed;        2067 AA.
Q9JL19; Q9JLT9;
12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
27-SEP-2017, entry version 126.
RecName: Full=Nuclear receptor coactivator 6;
AltName: Full=Activating signal cointegrator 2;
Short=ASC-2;
AltName: Full=Amplified in breast cancer protein 3;
AltName: Full=Cancer-amplified transcriptional coactivator ASC-2;
AltName: Full=Nuclear receptor coactivator RAP250;
Short=NRC;
AltName: Full=Nuclear receptor-activating protein, 250 kDa;
AltName: Full=Peroxisome proliferator-activated receptor-interacting protein;
Short=PPAR-interacting protein;
AltName: Full=Thyroid hormone receptor-binding protein;
Name=Ncoa6; Synonyms=Aib3, Prip, Rap250, Trbp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND INTERACTION WITH
PPARA; PPARG; RARA; RXRA; ESR1; ESR2 AND THRB.
TISSUE=Liver;
PubMed=10788465; DOI=10.1074/jbc.275.18.13510;
Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S.,
Reddy J.K.;
"Isolation and characterization of peroxisome proliferator-activated
receptor (PPAR) interacting protein (PRIP) as a coactivator for
PPAR.";
J. Biol. Chem. 275:13510-13516(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=FVB/N; TISSUE=Mammary tumor;
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 786-1142 (ISOFORM 1), INTERACTION WITH
PPARA; PPARG; ESR1; ESR2; THRA AND THRB, AND MUTAGENESIS OF
891-LEU--LEU-894.
TISSUE=Embryo;
PubMed=10681503; DOI=10.1074/jbc.275.8.5308;
Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.;
"Cloning and characterization of RAP250, a nuclear receptor
coactivator.";
J. Biol. Chem. 275:5308-5317(2000).
[4]
INTERACTION WITH RBM39.
PubMed=11704680; DOI=10.1074/jbc.M110417200;
Jung D.-J., Na S.-Y., Na D.S., Lee J.W.;
"Molecular cloning and characterization of CAPER, a novel coactivator
of activating protein-1 and estrogen receptors.";
J. Biol. Chem. 277:1229-1234(2002).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2022, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1822 AND LYS-1825, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[7]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-95; ARG-1050; ARG-1061 AND
ARG-1099, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Nuclear receptor coactivator that directly binds nuclear
receptors and stimulates the transcriptional activities in a
hormone-dependent fashion. Coactivates expression in an
agonist- and AF2-dependent manner. Involved in the coactivation of
different nuclear receptors, such as for steroids (GR and ERs),
retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR)
and prostanoids (PPARs). Probably functions as a general
coactivator, rather than just a nuclear receptor coactivator. May
also be involved in the coactivation of the NF-kappa-B pathway.
May coactivate expression via a remodeling of chromatin and its
interaction with histone acetyltransferase proteins. Involved in
placental, cardiac, hepatic and embryonic development.
-!- SUBUNIT: Monomer and homodimer. Interacts in vitro with the basal
transcription factors GTF2A and TBP, suggesting an autonomous
transactivation function. Interacts with NCOA1, CRSP3, RBM14, the
histone acetyltransferase proteins EP300 and CREBBP, and with
methyltransferase proteins NCOA6IP and PRMT2 (By similarity).
Interacts with RBM39. Component of the MLL2/3 complex (also named
ASCOM complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3,
ASH2L, RBBP5, WDR5, NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and
alpha- and beta-tubulin (By similarity). Interacts with ZNF335;
may enhance ligand-dependent transcriptional activation by nuclear
hormone receptors (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9JL19-1; Sequence=Displayed;
Name=2;
IsoId=Q9JL19-2; Sequence=VSP_003410;
Note=Acts as a dominant negative repressor.;
-!- TISSUE SPECIFICITY: Widely expressed. High expression in testis
and weak expression in small intestine.
-!- DEVELOPMENTAL STAGE: Expressed at E9 in placenta and at weaker
level in uterus. High expression in neural tube and in CNS
throughout development. High expression in sensory ganglia and
retina from E11. In the alimentary tract and olfactory epithelium
expression was seen from E13. Strong expression present in liver
and kidney, from E11 and E13 respectively, and then expression
decreased at later stages of development. Moderate expression in
lung from E13, while it decreases during postnatal life. Strong
expression in thymus from E15 onwards, and in spleen from E17 and
during early postnatal life, then, the expression decreases.
-!- DOMAIN: Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Only
motif 1 is essential for the association with nuclear receptors.
-!- PTM: Phosphorylated. {ECO:0000250}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AF216186; AAF35860.1; -; mRNA.
EMBL; BC031113; AAH31113.1; -; mRNA.
EMBL; AF135169; AAF35973.1; -; mRNA.
UniGene; Mm.27592; -.
ProteinModelPortal; Q9JL19; -.
SMR; Q9JL19; -.
DIP; DIP-61283N; -.
ELM; Q9JL19; -.
IntAct; Q9JL19; 2.
MINT; MINT-5200950; -.
STRING; 10090.ENSMUSP00000045386; -.
iPTMnet; Q9JL19; -.
PhosphoSitePlus; Q9JL19; -.
EPD; Q9JL19; -.
PaxDb; Q9JL19; -.
PeptideAtlas; Q9JL19; -.
PRIDE; Q9JL19; -.
MGI; MGI:1929915; Ncoa6.
eggNOG; ENOG410IK20; Eukaryota.
eggNOG; ENOG410XW4F; LUCA.
HOVERGEN; HBG052586; -.
InParanoid; Q9JL19; -.
Reactome; R-MMU-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
ChiTaRS; Ncoa6; mouse.
PRO; PR:Q9JL19; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_NCOA6; -.
GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:CACAO.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0051427; F:hormone receptor binding; IBA:GO_Central.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IBA:GO_Central.
GO; GO:0046966; F:thyroid hormone receptor binding; ISS:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
GO; GO:0007420; P:brain development; IMP:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:MGI.
GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
GO; GO:0030099; P:myeloid cell differentiation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0009725; P:response to hormone; IBA:GO_Central.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR026638; NCOA6.
InterPro; IPR032715; NCOA6_nucleic_acid-bd.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
PANTHER; PTHR15690:SF1; PTHR15690:SF1; 1.
Pfam; PF13820; Nucleic_acid_bd; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Complete proteome;
Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Transcription; Transcription regulation.
CHAIN 1 2067 Nuclear receptor coactivator 6.
/FTId=PRO_0000094414.
REGION 1 1314 NCOA1-binding region. {ECO:0000250}.
REGION 1 1060 CREBBP-binding region. {ECO:0000250}.
REGION 1 932 TBP/GTF2A-binding region. {ECO:0000250}.
REGION 777 931 NCOA6IP-binding region. {ECO:0000250}.
REGION 1644 2067 EP300/CRSP3-binding region.
{ECO:0000250}.
MOTIF 891 895 LXXLL motif 1.
MOTIF 1495 1499 LXXLL motif 2.
COMPBIAS 227 1044 Gln-rich.
COMPBIAS 376 381 Poly-Pro.
COMPBIAS 917 922 Poly-Lys.
COMPBIAS 1543 1592 Ser-rich.
MOD_RES 95 95 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 888 888 Phosphoserine.
{ECO:0000250|UniProtKB:Q14686}.
MOD_RES 1050 1050 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1061 1061 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1099 1099 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1325 1325 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14686}.
MOD_RES 1822 1822 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1825 1825 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 2022 2022 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 458 2067 Missing (in isoform 2).
{ECO:0000303|PubMed:10788465,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_003410.
MUTAGEN 891 894 LVNL->AVNA: Abolishes interaction with
nuclear receptors.
{ECO:0000269|PubMed:10681503}.
CONFLICT 39 39 G -> S (in Ref. 2; AAH31113).
{ECO:0000305}.
CONFLICT 109 109 W -> R (in Ref. 2; AAH31113).
{ECO:0000305}.
CONFLICT 194 194 M -> I (in Ref. 2; AAH31113).
{ECO:0000305}.
CONFLICT 290 290 Q -> QQ (in Ref. 2; AAH31113).
{ECO:0000305}.
CONFLICT 1014 1014 P -> L (in Ref. 3; AAF35973).
{ECO:0000305}.
CONFLICT 1141 1142 SE -> RS (in Ref. 3; AAF35973).
{ECO:0000305}.
SEQUENCE 2067 AA; 219663 MW; C855F8777167AD48 CRC64;
MVLDDLPNFE DIYTSLCSST MGDSEVEFDS GLEDDDTKGD SILEDSTIFV AFKGNIDDKD
FKWKLDAILK NVPNLLHMES SKLKVQKVEP WNSVRVTFNI PREAAERLWI LAQSNNQQLR
DLGILSVQIE GEGAINLALG QNRSQDVRMN GPVASGNSVR MEAGFPMASG PGLIRMTSPA
AVMTPQGGNM SSSMMAPGPN PELQPRTPRP ASQSDAMDPL LSGLHIQQQS HPSGSLPPAH
HSMQPVPVNR QMNPANFPQL QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ LQTRPLQQHQ
QQPQGIRPQF TAPTQVPVPP GWNQLPSGAL QPPPAQGSLG TMTTNQGWKK APLPSPMQAQ
LQARPSLATV QTPSHPPPPY PFGSQQASQA HTNFPQMSNP GQFTAPQMKG LQGGPSRVPT
PLQQPHLTNK SPASSPSSFQ QGSPASSPTV NQTQQQMGPR PPQNNPLSQG FQQPVSSPGR
NPMVQQGNVP PNFMVMQQQP PNQGPQSLHP GLGGMPKRLP PGFSAGQANP NFMQGQVPST
TAATPGNSGA LQLQANQNVQ HAGGQGAGPP QNQMQVSHGP PNMMQPSLMG IHGNINNQQA
GSSGVPQVTL GNMQGQPQQG PPSQLMGMHQ QIVPSQGQMA QQQGTLNPQN PMILSRAQLM
PQGQMMVNAQ NQNLGPSPQR MTPPKQMLPQ QGPQMMAPHN QMMGPQGQVL LQQNPMIEQI
MTNQMQGNKA QFNSQNQSNV MPGPAQIMRG PTPNMQGNMV QFTGQMSGQM LPQQGPVNNS
PSQVMGIQGQ VLRPPGPSPH MAQQHTDPVT TANNDVNLSQ MMPDVSMQQA SMVPPHVQSM
QGNSASGSHF SGHGVSFNAP FGGAPNGSQM SCGQNPGFPV NKDVTLTSPL LVNLLQSDIS
AGHFGVNNKQ NNTNANKPKK KKPPRKKKNC HQDLNTPDNR PTGLEEVDQQ SLPGEQGINL
DTTGPKLPDF SNRPPGYPTQ PVEQRPLPQM PPQLMQHVAP PPQPPQQQPQ PQLPQQQQPP
PPSQPQSQQQ QQQQQMMMML MMQQDPKSIR LPVSQNVHPP RGPLNPDSQR MPVQQSGNVP
VMVGLQGPAS VPPSPDKQRM PMSVNTPMGS NSRKMVYQEN PQNSSSSPLG EMSSLPEASG
SEVPSVAGGP NNMPSHLVVS QNQLMMTGPK PGPSPLSATQ GATPQQPPVN SLPSSHGHHF
PNVAAPTQTS RPKTPNRASP RPYYPQTPNN RPPSTEPSEI SLSPERLNAS IAGLFPPQIN
IPLPPRPNLN RGFDQQGLNP TTLKAIGQAP SNLTITNPPN FAAPQAHKLD SVVVNSGKQS
NPGTTKRASP SNSRRSSPGS SRKTTPSPGR QNSKAPKLTL ASQTSTTMLQ NMELPRNVLV
GPTPLANPPL PGSFPNNTGL NPQNPTVPVP AMGTVLEDNK ESVNIPQDSD CQNAQGRKEQ
VNTELKVVPT QEAKMAVPED QSKKDGQPLD PNKLPSVEEN KNLMSPAMRE APTSLSQLLD
NSGAPNVTIK PPGLTDLEVT PPVVSGEDLR KASVIPTLQD PPSKEPSTSL SSPHSSEPCS
TLARSELSEV SSNAAPSIPP VMSRPVSSSS ISTPLPPNQI TVFVTSNPIT TSSNTSAALP
THLQSALMST VVTMPNVGNK VMVSEGQSAA QSNARPQFIT PVFINSSSII QVMKGSQPST
IPATPLTTNS GLMPPSVAVV GPLHIPQNIK FSSAPVTPNV PSSSPAPNIQ TGRPLVLSSR
ATPVQLPSPP CTSSPVVAPN PSVQQVKELN PDEASPQTNT SADQSTLPPS QPTTVVSSLL
TNSPGSSANR RSPVSSSKGK GKVDKIGQIL LTKACKKVTG SLEKGEEQYG ADGETEGPGL
EITTPGLMGT EQCSTELDSK TPTPSAPTLL KMTSSPMAPS STSTGPILPG GALPTSVRSI
VTTLVPSELI STAPTTKGNH GGVTSEPLAG GLVEEKVGSH PELLPSIAPS QNLAPKETPA
TALQGSVARP ELEANAAIAS GQSCEPKEIV EKSKTLTSRR NSRTEEPTMA SESVENGHRK
RSSRPASASS STKDITGAVQ SKRRKSK


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