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Q9WU42

- NCOR2_MOUSE

UniProt

Q9WU42 - NCOR2_MOUSE

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Protein

Nuclear receptor corepressor 2

Gene

Ncor2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Transcriptional corepressor. Mediates the transcriptional repression activity of some nuclear receptors by promoting chromatin condensation, thus preventing access of the basal transcription. Isoform 1 and isoform 5 have different affinities for different nuclear receptors. Involved in the regulation BCL6-dependent of the germinal center (GC) reactions, mainly through the control of the GC B-cells proliferation and survival.1 Publication

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. DNA binding Source: MGI
  3. sequence-specific DNA binding Source: MGI
  4. transcription corepressor activity Source: UniProtKB

GO - Biological processi

  1. cell proliferation in forebrain Source: MGI
  2. forebrain development Source: MGI
  3. glucose homeostasis Source: MGI
  4. heart morphogenesis Source: MGI
  5. in utero embryonic development Source: MGI
  6. negative regulation of fat cell differentiation Source: MGI
  7. negative regulation of transcription, DNA-templated Source: MGI
  8. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  9. telencephalon development Source: MGI
  10. transcription, DNA-templated Source: UniProtKB-KW
  11. Type I pneumocyte differentiation Source: MGI
  12. white fat cell differentiation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_252217. Transcriptional regulation of white adipocyte differentiation.
REACT_257106. HDACs deacetylate histones.
REACT_257219. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor corepressor 2
Short name:
N-CoR2
Alternative name(s):
Silencing mediator of retinoic acid and thyroid hormone receptor
Short name:
SMRT
Short name:
SMRTe
T3 receptor-associating factor
Short name:
TRAC
Thyroid-, retinoic-acid-receptor-associated corepressor
Gene namesi
Name:Ncor2
Synonyms:Smrt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1337080. Ncor2.

Subcellular locationi

GO - Cellular componenti

  1. histone deacetylase complex Source: MGI
  2. nuclear body Source: MGI
  3. nuclear matrix Source: UniProtKB
  4. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24722472Nuclear receptor corepressor 2PRO_0000055623Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541PhosphoserineBy similarity
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei149 – 1491PhosphoserineBy similarity
Modified residuei152 – 1521PhosphoserineBy similarity
Modified residuei215 – 2151PhosphoserineBy similarity
Modified residuei549 – 5491PhosphothreonineBy similarity
Modified residuei550 – 5501Phosphoserine1 Publication
Modified residuei747 – 7471PhosphoserineBy similarity
Modified residuei750 – 7501PhosphoserineBy similarity
Modified residuei878 – 8781N6-acetyllysineBy similarity
Modified residuei938 – 9381PhosphoserineBy similarity
Modified residuei955 – 9551PhosphoserineBy similarity
Modified residuei958 – 9581N6-acetyllysineBy similarity
Modified residuei1181 – 11811N6-acetyllysineBy similarity
Modified residuei1209 – 12091N6-acetyllysineBy similarity
Modified residuei1220 – 12201PhosphoserineBy similarity
Modified residuei1350 – 13501PhosphothreonineBy similarity
Modified residuei1449 – 14491PhosphoserineBy similarity
Modified residuei1749 – 17491PhosphoserineBy similarity
Modified residuei1819 – 18191PhosphoserineBy similarity
Modified residuei1920 – 19201N6-acetyllysineBy similarity
Modified residuei1963 – 19631PhosphoserineBy similarity
Modified residuei1983 – 19831N6-acetyllysine1 Publication
Modified residuei2004 – 20041PhosphoserineBy similarity
Modified residuei2012 – 20121PhosphoserineBy similarity
Modified residuei2015 – 20151PhosphoserineBy similarity
Modified residuei2016 – 20161PhosphoserineBy similarity
Modified residuei2020 – 20201PhosphothreonineBy similarity
Modified residuei2161 – 21611PhosphoserineBy similarity
Modified residuei2181 – 21811Phosphoserine1 Publication
Modified residuei2215 – 22151Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9WU42.
PaxDbiQ9WU42.
PRIDEiQ9WU42.

PTM databases

PhosphoSiteiQ9WU42.

Expressioni

Tissue specificityi

Ubiquitous. Also widely expressed in early embryos.

Gene expression databases

BgeeiQ9WU42.
CleanExiMM_NCOR2.
ExpressionAtlasiQ9WU42. baseline and differential.
GenevestigatoriQ9WU42.

Interactioni

Subunit structurei

Forms a large corepressor complex that contains SIN3A/B and histone deacetylases HDAC1 and HDAC2. This complex associates with the thyroid (TR) and the retinoid acid receptors (RAR) in the absence of ligand, and may stabilize their interaction with TFIIB. Interacts directly with RARA in the absence of ligand; the interaction represses RARA activity. Interacts (isoform SMRT) with HDAC10. Interacts with MINT. Component of the N-Cor repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1R, CORO2A and GPS2. Interacts with CBFA2T3 and ATXN1L. Interacts with RARB; the interaction is weak and does not repress RARB transactivational activity. Interacts with HDAC7 and C1D. Interacts with NR4A2; this interaction increases in the absence of PITX3. Interacts with BCL6 (via the BTB domain), required for BCL6 transcriptional repressor activity on a subset of target genes. Forms ternary complexes with BCOR and BCL6 on target gene promoters but, on enhancer elements, interacts with BCL6 and HDAC3 to repress proximal gene expression. May interact with DEAF1. Interacts with RXRA.5 Publications

Protein-protein interaction databases

BioGridi203350. 8 interactions.
IntActiQ9WU42. 3 interactions.
MINTiMINT-3154743.
STRINGi10090.ENSMUSP00000107033.

Structurei

3D structure databases

ProteinModelPortaliQ9WU42.
SMRiQ9WU42. Positions 167-207, 408-476, 611-681.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini427 – 47852SANT 1PROSITE-ProRule annotationAdd
BLAST
Domaini606 – 65752SANT 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni254 – 31259Interaction with SIN3A/BBy similarityAdd
BLAST
Regioni2086 – 20905Required for interaction with RARA in the absence of its ligandBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili165 – 20743Sequence AnalysisAdd
BLAST
Coiled coili492 – 56069Sequence AnalysisAdd
BLAST
Coiled coili658 – 68225Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2094 – 20985CORNR box of ID1
Motifi2296 – 23005CORNR box of ID2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi494 – 50714Poly-GlnAdd
BLAST
Compositional biasi775 – 80430Pro-richAdd
BLAST
Compositional biasi989 – 99911Pro-richAdd
BLAST
Compositional biasi1351 – 13577Pro-rich
Compositional biasi1615 – 16195Poly-Ala
Compositional biasi2434 – 24374Poly-Pro

Domaini

The N-terminal region contains repression functions that are divided into three independent repression domains (RD1, RD2 and RD3). The C-terminal region contains the nuclear receptor-interacting domains that are divided in two separate interaction domains (ID1 and ID2).
The two interaction domains (ID) contain a conserved sequence referred to as the CORNR box. This motif is required and sufficient to permit binding to unligated TR and RARS. Sequences flanking the CORNR box determine nuclear hormone receptor specificity.

Sequence similaritiesi

Contains 2 SANT domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00730000110846.
HOGENOMiHOG000113746.
HOVERGENiHBG052587.
InParanoidiQ9WU42.
KOiK06065.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]
PfamiPF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51293. SANT. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Alpha (identifier: Q9WU42-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSGSTQPVAQ TWRAAEPRYP PHGISYPVQI ARSHTDVGLL EYQHHPRDYT
60 70 80 90 100
SHLSPGSIIQ PQRRRPSLLS EFQPGSERSQ ELHLRPESRT FLPELGKPDI
110 120 130 140 150
EFTESKRPRL ELLPDTLLRP SPLLATGQPS GSEDLTKDRS LAGKLEPVSP
160 170 180 190 200
PSPPHADPEL ELAPSRLSKE ELIQNMDRVD REITMVEQQI SKLKKKQQQL
210 220 230 240 250
EEEAAKPPEP EKPVSPPPIE SKHRSLVQII YDENRKKAEA AHRILEGLGP
260 270 280 290 300
QVELPLYNQP SDTRQYHENI KINQAMRKKL ILYFKRRNHA RKQWEQRFCQ
310 320 330 340 350
RYDQLMEAWE KKVERIENNP RRRAKESKVR EYYEKQFPEI RKQRELQERM
360 370 380 390 400
QSRVGQRGSG LSMSAARSEH EVSEIIDGLS EQENLEKQMR QLAVIPPMLY
410 420 430 440 450
DADQQRIKFI NMNGLMDDPM KVYKDRQVTN MWSEQERDTF REKFMQHPKN
460 470 480 490 500
FGLIASFLER KTVAECVLYY YLTKKNENYK SLVRRSYRRR GKSQQQQQQQ
510 520 530 540 550
QQQQQQQMAR SSQEEKEEKE KEKEADKEEE KQDAENEKEE LSKEKTDDTS
560 570 580 590 600
GEDNDEKEAV ASKGRKTANS QGRRKGRITR SMANEANHEE TATPQQSSEL
610 620 630 640 650
ASMEMNESSR WTEEEMETAK KGLLEHGRNW SAIARMVGSK TVSQCKNFYF
660 670 680 690 700
NYKKRQNLDE ILQQHKLKME KERNARRKKK KTPAAASEET AFPPAAEDEE
710 720 730 740 750
MEASGASANE EELAEEAEAS QASGNEVPRV GECSGPAAVN NSSDTESVPS
760 770 780 790 800
PRSEATKDTG PKPTGTEALP AATQPPVPPP EEPAVAPAEP SPVPDASGPP
810 820 830 840 850
SPEPSPSPAA PPATVDKDEQ EAPAAPAPQT EDAKEQKSEA EEIDVGKPEE
860 870 880 890 900
PEASEEPPES VKSDHKEETE EEPEDKAKGT EAIETVSEAP LKVEEAGSKA
910 920 930 940 950
AVTKGSSSGA TQDSDSSATC SADEVDEPEG GDKGRLLSPR PSLLTPAGDP
960 970 980 990 1000
RASTSPQKPL DLKQLKQRAA AIPPIVTKVH EPPREDTVPP KPVPPVPPPT
1010 1020 1030 1040 1050
QHLQPEGDVS QQSGGSPRGK SRSPVPPAEK EAEKPAFFPA FPTEGPKLPT
1060 1070 1080 1090 1100
EPPRWSSGLP FPIPPREVIK TSPHAADPSA FSYTPPGHPL PLGLHDSARP
1110 1120 1130 1140 1150
VLPRPPISNP PPLISSAKHP GVLERQLGAI SQQGMSVQLR VPHSEHAKAP
1160 1170 1180 1190 1200
MGPLTMGLPL AVDPKKLGTA LGSATSGSIT KGLPSTRAAD GPSYRGSITH
1210 1220 1230 1240 1250
GTPADVLYKG TISRIVGEDS PSRLDRARED TLPKGHVIYE GKKGHVLSYE
1260 1270 1280 1290 1300
GGMSVSQCSK EDGRSSSGPP HETAAPKRTY DMMEGRVGRT VTSASIEGLM
1310 1320 1330 1340 1350
GRAIPEQHSP HLKEQHHIRG SITQGIPRSY VEAQEDYLRR EAKLLKREGT
1360 1370 1380 1390 1400
PPPPPPPRDL TETYKPRPLD PLGPLKLKPT HEGVVATVKE AGRSIHEIPR
1410 1420 1430 1440 1450
EELRRTPELP LAPRPLKEGS ITQGTPLKYD SGAPSTGTKK HDVRSIIGSP
1460 1470 1480 1490 1500
GRPFPALHPL DIMADARALE RACYEESLKS RSGTSSGAGG SITRGAPVVV
1510 1520 1530 1540 1550
PELGKPRQSP LTYEDHGAPF TSHLPRGSPV TTREPTPRLQ EGSLLSSKAS
1560 1570 1580 1590 1600
QDRKLTSTPR EIAKSPHSTV PEHHPHPISP YEHLLRGVTG VDLYRGHIPL
1610 1620 1630 1640 1650
AFDPTSIPRG IPLEAAAAAY YLPRHLAPSP TYPHLYPPYL IRGYPDTAAL
1660 1670 1680 1690 1700
ENRQTIINDY ITSQQMHHNA ASAMAQRADM LRGLSPRESS LALNYAAGPR
1710 1720 1730 1740 1750
GIIDLSQVPH LPVLVPPTPG TPATAIDRLA YLPTAPPPFS SRHSSSPLSP
1760 1770 1780 1790 1800
GGPTHLAKPT ATSSSERERE RERERDKSIL TSTTTVEHAP IWRPGTEQSS
1810 1820 1830 1840 1850
GAGGSSRPAS HTHQHSPISP RTQDALQQRP SVLHNTSMKG VVTSVEPGTP
1860 1870 1880 1890 1900
TVLRWARSTS TSSPVRPAAT FPPATHCPLG GTLEGVYPTL MEPVLLPKET
1910 1920 1930 1940 1950
SRVARPERPR VDAGHAFLTK PPAREPASSP SKSSEPRSLA PPSSSHTAIA
1960 1970 1980 1990 2000
RTPAKNLAPH HASPDPPAPT SASDLHREKT QSKPFSIQEL ELRSLGYHSG
2010 2020 2030 2040 2050
AGYSPDGVEP ISPVSSPSLT HDKGLSKPLE ELEKSHLEGE LRHKQPGPMK
2060 2070 2080 2090 2100
LSAEAAHLPH LRPLPESQPS SSPLLQTAPG IKGHQRVVTL AQHISEVITQ
2110 2120 2130 2140 2150
DYTRHHPQQL SGPLPAPLYS FPGASCPVLD LRRPPSDLYL PPPDHGTPAR
2160 2170 2180 2190 2200
GSPHSEGGKR SPEPSKTSVL GSSEDAIEPV SPPEGMTEPG HARSTAYPLL
2210 2220 2230 2240 2250
YRDGEQGEPR MGSKSPGNTS QPPAFFSKLT ESNSAMVKSK KQEINKKLNT
2260 2270 2280 2290 2300
HNRNEPEYNI GQPGTEIFNM PAITGAGLMT CRSQAVQEHA STNMGLEAII
2310 2320 2330 2340 2350
RKALMGKYDQ WEEPPPLGAN AFNPLNASAS LPAAAMPITT ADGRSDHALT
2360 2370 2380 2390 2400
SPGGGGKAKV SGRPSSRKAK SPAPGLASGD RPPSVSSVHS EGDCNRRTPL
2410 2420 2430 2440 2450
TNRVWEDRPS SAGSTPFPYN PLIMRLQAGV MASPPPPGLA AGSGPLAGPH
2460 2470
HAWDEEPKPL LCSQYETLSD SE
Length:2,472
Mass (Da):269,807
Last modified:July 27, 2011 - v3
Checksum:i8068020DF0AAB9B7
GO
Isoform Beta (identifier: Q9WU42-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     36-254: Missing.

Show »
Length:2,253
Mass (Da):245,029
Checksum:i7FA45277FC6300A1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761M → RL in AAD22972. (PubMed:10097068)Curated
Sequence conflicti396 – 4027PPMLYDA → RHVVRR in AAD22972. (PubMed:10097068)Curated
Sequence conflicti555 – 5551D → H in AAD20944. (PubMed:10077563)Curated
Sequence conflicti756 – 7561T → M in AAD20944. (PubMed:10077563)Curated
Sequence conflicti785 – 7851V → A in AAD22972. (PubMed:10097068)Curated
Sequence conflicti806 – 84641PSPAA…EIDVG → HHLPHPRLLWTRMNKKPRLL QLPRQRMPRSRSLRPRRSMW E in AAD20944. (PubMed:10077563)CuratedAdd
BLAST
Sequence conflicti806 – 84641PSPAA…EIDVG → HHLPHPRLLWTRMNKKPRLL QLPRQRMPRSRSLRPRRSMW E in AAD20945. (PubMed:10077563)CuratedAdd
BLAST
Sequence conflicti856 – 8561E → K in AAD20945. (PubMed:10077563)Curated
Sequence conflicti859 – 8591E → K in AAD20945. (PubMed:10077563)Curated
Sequence conflicti867 – 8671E → K in AAD20945. (PubMed:10077563)Curated
Sequence conflicti895 – 8951E → K in AAD20945. (PubMed:10077563)Curated
Sequence conflicti916 – 9161S → F in AAD20944. (PubMed:10077563)Curated
Sequence conflicti975 – 9751I → IQ in AAD20944. (PubMed:10077563)Curated
Sequence conflicti1046 – 106318PKLPT…LPFPI → QSYRLSPHAGHRLPSH in AAD22972. (PubMed:10097068)CuratedAdd
BLAST
Sequence conflicti1073 – 10808PHAADPSA → TRADPL in AAD22972. (PubMed:10097068)Curated
Sequence conflicti1133 – 11331Missing in AAD22972. (PubMed:10097068)Curated
Sequence conflicti1149 – 11491Missing in AAD22972. (PubMed:10097068)Curated
Sequence conflicti1157 – 11571G → E in AAD22972. (PubMed:10097068)Curated
Sequence conflicti1172 – 120130GSATS…SITHG → APPPVEASPRASQYPGCRRP QLQRLYHPR in AAD22972. (PubMed:10097068)CuratedAdd
BLAST
Sequence conflicti1696 – 16961A → S in AAD22972. (PubMed:10097068)Curated
Sequence conflicti1855 – 18573Missing in AAD22972. (PubMed:10097068)Curated
Sequence conflicti1909 – 19091P → A in AAD20944. (PubMed:10077563)Curated
Sequence conflicti1909 – 19091P → A in AAD20945. (PubMed:10077563)Curated
Sequence conflicti1913 – 19131A → G in AAD22972. (PubMed:10097068)Curated
Sequence conflicti1923 – 19231A → G in AAD20944. (PubMed:10077563)Curated
Sequence conflicti1923 – 19231A → G in AAD20945. (PubMed:10077563)Curated
Sequence conflicti1956 – 19561N → S in AAD22972. (PubMed:10097068)Curated
Sequence conflicti1968 – 19681A → G in AAD22972. (PubMed:10097068)Curated
Sequence conflicti2195 – 21962TA → AV in AAD22972. (PubMed:10097068)Curated
Sequence conflicti2213 – 22142SK → LE in AAD20944. (PubMed:10077563)Curated
Sequence conflicti2224 – 22241A → T in AAD20944. (PubMed:10077563)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei36 – 254219Missing in isoform Beta. 1 PublicationVSP_003414Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF113001 mRNA. Translation: AAD20944.1.
AF113002 mRNA. Translation: AAD20945.1.
AF125671 mRNA. Translation: AAD22972.1.
AC132118 Genomic DNA. No translation available.
AC139377 Genomic DNA. No translation available.
CCDSiCCDS57382.1. [Q9WU42-2]
RefSeqiNP_001240833.1. NM_001253904.1.
NP_001240834.1. NM_001253905.1. [Q9WU42-2]
UniGeneiMm.278646.

Genome annotation databases

EnsembliENSMUST00000111394; ENSMUSP00000107025; ENSMUSG00000029478. [Q9WU42-2]
ENSMUST00000111398; ENSMUSP00000107029; ENSMUSG00000029478. [Q9WU42-1]
GeneIDi20602.
KEGGimmu:20602.
UCSCiuc008zra.2. mouse. [Q9WU42-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF113001 mRNA. Translation: AAD20944.1 .
AF113002 mRNA. Translation: AAD20945.1 .
AF125671 mRNA. Translation: AAD22972.1 .
AC132118 Genomic DNA. No translation available.
AC139377 Genomic DNA. No translation available.
CCDSi CCDS57382.1. [Q9WU42-2 ]
RefSeqi NP_001240833.1. NM_001253904.1.
NP_001240834.1. NM_001253905.1. [Q9WU42-2 ]
UniGenei Mm.278646.

3D structure databases

ProteinModelPortali Q9WU42.
SMRi Q9WU42. Positions 167-207, 408-476, 611-681.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203350. 8 interactions.
IntActi Q9WU42. 3 interactions.
MINTi MINT-3154743.
STRINGi 10090.ENSMUSP00000107033.

PTM databases

PhosphoSitei Q9WU42.

Proteomic databases

MaxQBi Q9WU42.
PaxDbi Q9WU42.
PRIDEi Q9WU42.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000111394 ; ENSMUSP00000107025 ; ENSMUSG00000029478 . [Q9WU42-2 ]
ENSMUST00000111398 ; ENSMUSP00000107029 ; ENSMUSG00000029478 . [Q9WU42-1 ]
GeneIDi 20602.
KEGGi mmu:20602.
UCSCi uc008zra.2. mouse. [Q9WU42-2 ]

Organism-specific databases

CTDi 9612.
MGIi MGI:1337080. Ncor2.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00730000110846.
HOGENOMi HOG000113746.
HOVERGENi HBG052587.
InParanoidi Q9WU42.
KOi K06065.

Enzyme and pathway databases

Reactomei REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_252217. Transcriptional regulation of white adipocyte differentiation.
REACT_257106. HDACs deacetylate histones.
REACT_257219. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

ChiTaRSi Ncor2. mouse.
NextBioi 298933.
PROi Q9WU42.
SOURCEi Search...

Gene expression databases

Bgeei Q9WU42.
CleanExi MM_NCOR2.
ExpressionAtlasi Q9WU42. baseline and differential.
Genevestigatori Q9WU42.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
InterProi IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view ]
Pfami PF00249. Myb_DNA-binding. 1 hit.
[Graphical view ]
SMARTi SM00717. SANT. 2 hits.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 2 hits.
PROSITEi PS51293. SANT. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Unique forms of human and mouse nuclear receptor corepressor SMRT."
    Ordentlich P., Downes M., Xie W., Genin A., Spinner N.B., Evans R.M.
    Proc. Natl. Acad. Sci. U.S.A. 96:2639-2644(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
    Tissue: Brain and Spleen.
  2. "SMRTe, a silencing mediator for retinoid and thyroid hormone receptors-extended isoform that is more related to the nuclear receptor corepressor."
    Park E.J., Schroen D.J., Yang M., Li H., Li L., Chen J.D.
    Proc. Natl. Acad. Sci. U.S.A. 96:3519-3524(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
    Tissue: Embryo.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "Cloning and characterization of a corepressor and potential component of the nuclear hormone receptor repression complex."
    Zamir I., Dawson J., Lavinsky R.M., Glass C.K., Rosenfeld M.G., Lazar M.A.
    Proc. Natl. Acad. Sci. U.S.A. 94:14400-14405(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C1D.
  5. "Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression."
    Kao H.-Y., Downes M., Ordentlich P., Evans R.M.
    Genes Dev. 14:55-66(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC7.
  6. "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain."
    Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N., Downing J.R., Meyers S., Hiebert S.W.
    Mol. Cell. Biol. 21:6470-6483(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBFA2T3.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550 AND SER-2215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation through release of SMRT-mediated repression."
    Jacobs F.M., van Erp S., van der Linden A.J., von Oerthel L., Burbach J.P., Smidt M.P.
    Development 136:531-540(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NR4A2.
  9. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    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.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1983, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  11. "Lineage-specific functions of Bcl-6 in immunity and inflammation are mediated by distinct biochemical mechanisms."
    Huang C., Hatzi K., Melnick A.
    Nat. Immunol. 14:380-388(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, INTERACTION WITH BCL6.

Entry informationi

Entry nameiNCOR2_MOUSE
AccessioniPrimary (citable) accession number: Q9WU42
Secondary accession number(s): E9Q9V0, Q9WU43, Q9WUC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3