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Protein

Nuclear receptor corepressor 2

Gene

NCOR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.2 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • histone deacetylase binding Source: UniProtKB
  • ligand-dependent nuclear receptor binding Source: GO_Central
  • Notch binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • transcription corepressor activity Source: UniProtKB
  • transcription factor binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:G66-33796-MONOMER.
ReactomeiR-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-3214815. HDACs deacetylate histones.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
SignaLinkiQ9Y618.
SIGNORiQ9Y618.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor corepressor 2
Short name:
N-CoR2
Alternative name(s):
CTG repeat protein 26
SMAP270
Silencing mediator of retinoic acid and thyroid hormone receptor
Short name:
SMRT
T3 receptor-associating factor
Short name:
TRAC
Thyroid-, retinoic-acid-receptor-associated corepressor
Gene namesi
Name:NCOR2
Synonyms:CTG26
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:7673. NCOR2.

Subcellular locationi

GO - Cellular componenti

  • histone deacetylase complex Source: GO_Central
  • membrane Source: UniProtKB
  • nuclear body Source: MGI
  • nuclear chromatin Source: BHF-UCL
  • nuclear matrix Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: MGI
  • transcriptional repressor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2139R → A: Abolishes interaction with the apo LBD of RARA. Restores some interaction on the addition of inverse agonist BMS493. 1 Publication1
Mutagenesisi2141V → P: Abolishes interaction with the apo LBD of RARA. No change on interaction on the addition of inverse agonist BMS493. 1 Publication1
Mutagenesisi2142T → G: Abolishes interaction with the apo LBD of RARA. Restores some interaction on the addition of inverse agonist BMS493. 1 Publication1

Organism-specific databases

DisGeNETi9612.
PharmGKBiPA31478.

Chemistry databases

ChEMBLiCHEMBL2111363.

Polymorphism and mutation databases

BioMutaiNCOR2.
DMDMi226713806.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000556221 – 2525Nuclear receptor corepressor 2Add BLAST2525

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei18Asymmetric dimethylarginineBy similarity1
Modified residuei54PhosphoserineCombined sources1
Modified residuei67PhosphoserineCombined sources1
Modified residuei149PhosphoserineCombined sources1
Modified residuei152PhosphoserineCombined sources1
Modified residuei156PhosphothreonineCombined sources1
Modified residuei215PhosphoserineCombined sources1
Modified residuei493PhosphoserineCombined sources1
Modified residuei553PhosphothreonineCombined sources1
Modified residuei554PhosphoserineCombined sources1
Modified residuei750PhosphoserineCombined sources1
Modified residuei753PhosphoserineCombined sources1
Modified residuei878N6-acetyllysineCombined sources1
Modified residuei939PhosphoserineCombined sources1
Modified residuei946PhosphothreonineCombined sources1
Modified residuei956PhosphoserineCombined sources1
Modified residuei959N6-acetyllysineCombined sources1
Modified residuei1181PhosphoserineCombined sources1
Modified residuei1218N6-acetyllysineCombined sources1
Modified residuei1248N6-acetyllysineCombined sources1
Modified residuei1259PhosphoserineCombined sources1
Modified residuei1331PhosphoserineCombined sources1
Modified residuei1391PhosphothreonineCombined sources1
Modified residuei1487PhosphoserineCombined sources1
Modified residuei1547PhosphoserineCombined sources1
Modified residuei1603PhosphoserineBy similarity1
Modified residuei1627PhosphoserineCombined sources1
Modified residuei1661Asymmetric dimethylarginineCombined sources1
Modified residuei1783PhosphoserineCombined sources1
Modified residuei1786PhosphoserineCombined sources1
Modified residuei1872PhosphoserineCombined sources1
Modified residuei1970N6-acetyllysineCombined sources1
Modified residuei2016PhosphoserineCombined sources1
Modified residuei2037N6-acetyllysineCombined sources1
Modified residuei2057PhosphoserineCombined sources1
Modified residuei2065PhosphoserineCombined sources1
Modified residuei2068PhosphoserineCombined sources1
Modified residuei2069PhosphoserineCombined sources1
Modified residuei2071PhosphoserineBy similarity1
Modified residuei2073PhosphothreonineCombined sources1
Modified residuei2088PhosphoserineCombined sources1
Modified residuei2214PhosphoserineCombined sources1
Modified residuei2234PhosphoserineCombined sources1
Modified residuei2269PhosphoserineCombined sources1
Modified residuei2424PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ9Y618.
PaxDbiQ9Y618.
PeptideAtlasiQ9Y618.
PRIDEiQ9Y618.

PTM databases

iPTMnetiQ9Y618.
PhosphoSitePlusiQ9Y618.

Expressioni

Tissue specificityi

Ubiquitous. High levels of expression are detected in lung, spleen and brain.

Inductioni

Regulated during cell cycle progression.

Gene expression databases

BgeeiENSG00000196498.
CleanExiHS_NCOR2.
ExpressionAtlasiQ9Y618. baseline and differential.
GenevisibleiQ9Y618. HS.

Organism-specific databases

HPAiHPA001928.

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. Interacts with MECP2 (By similarity).By similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AHRP358692EBI-80830,EBI-80780
ARNTP275402EBI-80830,EBI-80809
E2F1Q010942EBI-80830,EBI-448924
HDAC1Q135472EBI-80830,EBI-301834
PML-RARQ151562EBI-80830,EBI-867256
RBPJQ063303EBI-80830,EBI-632552
SNW1Q135734EBI-80830,EBI-632715
TP53P046377EBI-80830,EBI-366083

GO - Molecular functioni

  • histone deacetylase binding Source: UniProtKB
  • ligand-dependent nuclear receptor binding Source: GO_Central
  • Notch binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • transcription factor binding Source: GO_Central

Protein-protein interaction databases

BioGridi114974. 117 interactors.
DIPiDIP-951N.
IntActiQ9Y618. 39 interactors.
MINTiMINT-129997.
STRINGi9606.ENSP00000384018.

Chemistry databases

BindingDBiQ9Y618.

Structurei

Secondary structure

12525
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi168 – 170Combined sources3
Helixi171 – 205Combined sources35
Beta strandi414 – 417Combined sources4
Helixi419 – 428Combined sources10
Helixi434 – 446Combined sources13
Helixi451 – 456Combined sources6
Turni458 – 460Combined sources3
Helixi463 – 473Combined sources11
Turni474 – 476Combined sources3
Helixi617 – 629Combined sources13
Turni630 – 632Combined sources3
Helixi634 – 640Combined sources7
Beta strandi642 – 644Combined sources3
Helixi646 – 655Combined sources10
Helixi661 – 679Combined sources19
Beta strandi1116 – 1118Combined sources3
Beta strandi1424 – 1428Combined sources5
Helixi2350 – 2358Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KKQX-ray3.00E/F/G/H2347-2365[»]
1R2BX-ray2.20C/D1422-1438[»]
1XC5NMR-A412-480[»]
2GPVX-ray2.85G/H/I2346-2367[»]
2L5GNMR-B167-207[»]
2LTPNMR-A615-685[»]
2ODDNMR-B1109-1121[»]
2RT5NMR-B2518-2525[»]
3R29X-ray2.90C/D2346-2361[»]
3R2AX-ray3.00E/F2346-2361[»]
4A69X-ray2.06C/D389-480[»]
4OARX-ray2.41B2346-2362[»]
ProteinModelPortaliQ9Y618.
SMRiQ9Y618.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y618.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini427 – 478SANT 1PROSITE-ProRule annotationAdd BLAST52
Domaini610 – 661SANT 2PROSITE-ProRule annotationAdd BLAST52

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni254 – 312Interaction with SIN3A/BBy similarityAdd BLAST59
Regioni2139 – 2142Required for interaction with RARA in the absence of its ligand4

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili174 – 215Sequence analysisAdd BLAST42
Coiled coili522 – 561Sequence analysisAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2147 – 2151CORNR box of ID15
Motifi2350 – 2354CORNR box of ID25

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi494 – 510Poly-GlnAdd BLAST17
Compositional biasi682 – 685Poly-Lys4
Compositional biasi778 – 820Pro-richAdd BLAST43
Compositional biasi995 – 1003Poly-Pro9
Compositional biasi1392 – 1397Poly-Pro6
Compositional biasi1850 – 1854Poly-Gly5
Compositional biasi2487 – 2490Poly-Pro4

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

eggNOGiKOG1878. Eukaryota.
ENOG410YDXP. LUCA.
HOVERGENiHBG052587.
InParanoidiQ9Y618.
KOiK06065.
PhylomeDBiQ9Y618.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR031557. N-CoR_GPS2_interact.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]
PfamiPF15784. GPS2_interact. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51293. SANT. 2 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y618-1) [UniParc]FASTAAdd to basket
Also known as: SMRT-alpha, TRAC-2

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 TWRATEPRYP PHSLSYPVQI ARTHTDVGLL EYQHHSRDYA
60 70 80 90 100
SHLSPGSIIQ PQRRRPSLLS EFQPGNERSQ ELHLRPESHS YLPELGKSEM
110 120 130 140 150
EFIESKRPRL ELLPDPLLRP SPLLATGQPA GSEDLTKDRS LTGKLEPVSP
160 170 180 190 200
PSPPHTDPEL ELVPPRLSKE ELIQNMDRVD REITMVEQQI SKLKKKQQQL
210 220 230 240 250
EEEAAKPPEP EKPVSPPPIE SKHRSLVQII YDENRKKAEA AHRILEGLGP
260 270 280 290 300
QVELPLYNQP SDTRQYHENI KINQAMRKKL ILYFKRRNHA RKQWEQKFCQ
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 NMNGLMADPM KVYKDRQVMN MWSEQEKETF REKFMQHPKN
460 470 480 490 500
FGLIASFLER KTVAECVLYY YLTKKNENYK SLVRRSYRRR GKSQQQQQQQ
510 520 530 540 550
QQQQQQQQQQ PMPRSSQEEK DEKEKEKEAE KEEEKPEVEN DKEDLLKEKT
560 570 580 590 600
DDTSGEDNDE KEAVASKGRK TANSQGRRKG RITRSMANEA NSEEAITPQQ
610 620 630 640 650
SAELASMELN ESSRWTEEEM ETAKKGLLEH GRNWSAIARM VGSKTVSQCK
660 670 680 690 700
NFYFNYKKRQ NLDEILQQHK LKMEKERNAR RKKKKAPAAA SEEAAFPPVV
710 720 730 740 750
EDEEMEASGV SGNEEEMVEE AEALHASGNE VPRGECSGPA TVNNSSDTES
760 770 780 790 800
IPSPHTEAAK DTGQNGPKPP ATLGADGPPP GPPTPPPEDI PAPTEPTPAS
810 820 830 840 850
EATGAPTPPP APPSPSAPPP VVPKEEKEEE TAAAPPVEEG EEQKPPAAEE
860 870 880 890 900
LAVDTGKAEE PVKSECTEEA EEGPAKGKDA EAAEATAEGA LKAEKKEGGS
910 920 930 940 950
GRATTAKSSG APQDSDSSAT CSADEVDEAE GGDKNRLLSP RPSLLTPTGD
960 970 980 990 1000
PRANASPQKP LDLKQLKQRA AAIPPIQVTK VHEPPREDAA PTKPAPPAPP
1010 1020 1030 1040 1050
PPQNLQPESD APQQPGSSPR GKSRSPAPPA DKEAEKPVFF PAFAAEAQKL
1060 1070 1080 1090 1100
PGDPPCWTSG LPFPVPPREV IKASPHAPDP SAFSYAPPGH PLPLGLHDTA
1110 1120 1130 1140 1150
RPVLPRPPTI SNPPPLISSA KHPSVLERQI GAISQGMSVQ LHVPYSEHAK
1160 1170 1180 1190 1200
APVGPVTMGL PLPMDPKKLA PFSGVKQEQL SPRGQAGPPE SLGVPTAQEA
1210 1220 1230 1240 1250
SVLRGTALGS VPGGSITKGI PSTRVPSDSA ITYRGSITHG TPADVLYKGT
1260 1270 1280 1290 1300
ITRIIGEDSP SRLDRGREDS LPKGHVIYEG KKGHVLSYEG GMSVTQCSKE
1310 1320 1330 1340 1350
DGRSSSGPPH ETAAPKRTYD MMEGRVGRAI SSASIEGLMG RAIPPERHSP
1360 1370 1380 1390 1400
HHLKEQHHIR GSITQGIPRS YVEAQEDYLR REAKLLKREG TPPPPPPSRD
1410 1420 1430 1440 1450
LTEAYKTQAL GPLKLKPAHE GLVATVKEAG RSIHEIPREE LRHTPELPLA
1460 1470 1480 1490 1500
PRPLKEGSIT QGTPLKYDTG ASTTGSKKHD VRSLIGSPGR TFPPVHPLDV
1510 1520 1530 1540 1550
MADARALERA CYEESLKSRP GTASSSGGSI ARGAPVIVPE LGKPRQSPLT
1560 1570 1580 1590 1600
YEDHGAPFAG HLPRGSPVTT REPTPRLQEG SLSSSKASQD RKLTSTPREI
1610 1620 1630 1640 1650
AKSPHSTVPE HHPHPISPYE HLLRGVSGVD LYRSHIPLAF DPTSIPRGIP
1660 1670 1680 1690 1700
LDAAAAYYLP RHLAPNPTYP HLYPPYLIRG YPDTAALENR QTIINDYITS
1710 1720 1730 1740 1750
QQMHHNAATA MAQRADMLRG LSPRESSLAL NYAAGPRGII DLSQVPHLPV
1760 1770 1780 1790 1800
LVPPTPGTPA TAMDRLAYLP TAPQPFSSRH SSSPLSPGGP THLTKPTTTS
1810 1820 1830 1840 1850
SSERERDRDR ERDRDREREK SILTSTTTVE HAPIWRPGTE QSSGSSGSSG
1860 1870 1880 1890 1900
GGGGSSSRPA SHSHAHQHSP ISPRTQDALQ QRPSVLHNTG MKGIITAVEP
1910 1920 1930 1940 1950
STPTVLRSTS TSSPVRPAAT FPPATHCPLG GTLDGVYPTL MEPVLLPKEA
1960 1970 1980 1990 2000
PRVARPERPR ADTGHAFLAK PPARSGLEPA SSPSKGSEPR PLVPPVSGHA
2010 2020 2030 2040 2050
TIARTPAKNL APHHASPDPP APPASASDPH REKTQSKPFS IQELELRSLG
2060 2070 2080 2090 2100
YHGSSYSPEG VEPVSPVSSP SLTHDKGLPK HLEELDKSHL EGELRPKQPG
2110 2120 2130 2140 2150
PVKLGGEAAH LPHLRPLPES QPSSSPLLQT APGVKGHQRV VTLAQHISEV
2160 2170 2180 2190 2200
ITQDYTRHHP QQLSAPLPAP LYSFPGASCP VLDLRRPPSD LYLPPPDHGA
2210 2220 2230 2240 2250
PARGSPHSEG GKRSPEPNKT SVLGGGEDGI EPVSPPEGMT EPGHSRSAVY
2260 2270 2280 2290 2300
PLLYRDGEQT EPSRMGSKSP GNTSQPPAFF SKLTESNSAM VKSKKQEINK
2310 2320 2330 2340 2350
KLNTHNRNEP EYNISQPGTE IFNMPAITGT GLMTYRSQAV QEHASTNMGL
2360 2370 2380 2390 2400
EAIIRKALMG KYDQWEESPP LSANAFNPLN ASASLPAAMP ITAADGRSDH
2410 2420 2430 2440 2450
TLTSPGGGGK AKVSGRPSSR KAKSPAPGLA SGDRPPSVSS VHSEGDCNRR
2460 2470 2480 2490 2500
TPLTNRVWED RPSSAGSTPF PYNPLIMRLQ AGVMASPPPP GLPAGSGPLA
2510 2520
GPHHAWDEEP KPLLCSQYET LSDSE
Length:2,525
Mass (Da):274,804
Last modified:March 24, 2009 - v2
Checksum:i9B8689CA013C4513
GO
Isoform 2 (identifier: Q9Y618-2) [UniParc]FASTAAdd to basket
Also known as: TRAC-1

The sequence of this isoform differs from the canonical sequence as follows:
     1-1710: Missing.
     2361-2406: Missing.

Note: Contains only the C-terminal receptor-interacting domain and acts as an antirepressor.
Show »
Length:769
Mass (Da):81,608
Checksum:i399E0A5142E83975
GO
Isoform 3 (identifier: Q9Y618-3) [UniParc]FASTAAdd to basket
Also known as: h-SMRT

The sequence of this isoform differs from the canonical sequence as follows:
     1034-1041: Missing.

Show »
Length:2,517
Mass (Da):273,888
Checksum:iD9616717A5C342DB
GO
Isoform 4 (identifier: Q9Y618-4) [UniParc]FASTAAdd to basket
Also known as: SMRTe

The sequence of this isoform differs from the canonical sequence as follows:
     724-740: Missing.

Show »
Length:2,508
Mass (Da):273,141
Checksum:i8738AABD508422AA
GO
Isoform 5 (identifier: Q9Y618-5) [UniParc]FASTAAdd to basket
Also known as: SMRT-tau

The sequence of this isoform differs from the canonical sequence as follows:
     724-740: Missing.
     2361-2406: Missing.

Show »
Length:2,462
Mass (Da):268,361
Checksum:i31DC105B162AFD57
GO

Sequence cautioni

The sequence AAB91452 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated
The sequence AAC50236 differs from that shown. Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence AAD20946 differs from that shown. Reason: Frameshift at positions 787 and 794.Curated
The sequence BAD92326 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti7P → L in AAD20946 (PubMed:10077563).Curated1
Sequence conflicti295E → K in AAD20946 (PubMed:10077563).Curated1
Sequence conflicti309W → L in AAD20946 (PubMed:10077563).Curated1
Sequence conflicti352Missing in AAD22973 (PubMed:10097068).Curated1
Sequence conflicti352Missing in AAX77219 (Ref. 4) Curated1
Sequence conflicti365A → P in AAD22973 (PubMed:10097068).Curated1
Sequence conflicti365A → P in AAX77219 (Ref. 4) Curated1
Sequence conflicti612 – 613SS → EF in AAB91446 (PubMed:9225980).Curated2
Sequence conflicti711S → T in AAD22973 (PubMed:10097068).Curated1
Sequence conflicti711S → T in AAX77219 (Ref. 4) Curated1
Sequence conflicti796P → S in AAD22973 (PubMed:10097068).Curated1
Sequence conflicti796P → S in AAX77219 (Ref. 4) Curated1
Sequence conflicti804G → L in AAD22973 (PubMed:10097068).Curated1
Sequence conflicti804G → L in AAX77219 (Ref. 4) Curated1
Sequence conflicti814S → F in AAD22973 (PubMed:10097068).Curated1
Sequence conflicti814S → F in AAX77219 (Ref. 4) Curated1
Sequence conflicti817A → S in AAD22973 (PubMed:10097068).Curated1
Sequence conflicti817A → S in AAX77219 (Ref. 4) Curated1
Sequence conflicti889G → R in AAD22973 (PubMed:10097068).Curated1
Sequence conflicti889G → R in AAX77219 (Ref. 4) Curated1
Sequence conflicti1570T → M in AAD20946 (PubMed:10077563).Curated1
Sequence conflicti1570T → M in AAD22973 (PubMed:10097068).Curated1
Sequence conflicti1570T → M in AAX77219 (Ref. 4) Curated1
Sequence conflicti1570T → M in AAC50236 (PubMed:7566127).Curated1
Sequence conflicti1902T → K in AAD20946 (PubMed:10077563).Curated1
Sequence conflicti1902T → K in AAD22973 (PubMed:10097068).Curated1
Sequence conflicti1902T → K in AAX77219 (Ref. 4) Curated1
Sequence conflicti1902T → K in AAC50236 (PubMed:7566127).Curated1
Sequence conflicti2502P → A in AAB50847 (PubMed:8813722).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_060073781G → E.1 PublicationCorresponds to variant rs7978237dbSNPEnsembl.1
Natural variantiVAR_0547511707A → T.4 PublicationsCorresponds to variant rs2229840dbSNPEnsembl.1
Natural variantiVAR_0600742012P → S.Corresponds to variant rs2230944dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0034121 – 1710Missing in isoform 2. 1 PublicationAdd BLAST1710
Alternative sequenceiVSP_036595724 – 740Missing in isoform 4 and isoform 5. 2 PublicationsAdd BLAST17
Alternative sequenceiVSP_0365961034 – 1041Missing in isoform 3. 1 Publication8
Alternative sequenceiVSP_0034132361 – 2406Missing in isoform 2 and isoform 5. 2 PublicationsAdd BLAST46

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83390 mRNA. Translation: AAB50847.1.
AF113003 mRNA. Translation: AAD20946.1. Frameshift.
AF125672 mRNA. Translation: AAD22973.1.
AY965853 mRNA. Translation: AAX77219.1.
AC069261 Genomic DNA. No translation available.
AC073916 Genomic DNA. No translation available.
AB209089 mRNA. Translation: BAD92326.1. Different initiation.
U80750 mRNA. Translation: AAB91446.1.
U80761 mRNA. Translation: AAB91452.1. Sequence problems.
U37146 mRNA. Translation: AAC50236.1. Sequence problems.
PIRiS60255.
RefSeqiNP_001070729.2. NM_001077261.3.
NP_001193583.1. NM_001206654.1.
NP_006303.4. NM_006312.5.
UniGeneiHs.137510.

Genome annotation databases

EnsembliENST00000356219; ENSP00000348551; ENSG00000196498.
GeneIDi9612.
KEGGihsa:9612.
UCSCiuc058uwu.1. human. [Q9Y618-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83390 mRNA. Translation: AAB50847.1.
AF113003 mRNA. Translation: AAD20946.1. Frameshift.
AF125672 mRNA. Translation: AAD22973.1.
AY965853 mRNA. Translation: AAX77219.1.
AC069261 Genomic DNA. No translation available.
AC073916 Genomic DNA. No translation available.
AB209089 mRNA. Translation: BAD92326.1. Different initiation.
U80750 mRNA. Translation: AAB91446.1.
U80761 mRNA. Translation: AAB91452.1. Sequence problems.
U37146 mRNA. Translation: AAC50236.1. Sequence problems.
PIRiS60255.
RefSeqiNP_001070729.2. NM_001077261.3.
NP_001193583.1. NM_001206654.1.
NP_006303.4. NM_006312.5.
UniGeneiHs.137510.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KKQX-ray3.00E/F/G/H2347-2365[»]
1R2BX-ray2.20C/D1422-1438[»]
1XC5NMR-A412-480[»]
2GPVX-ray2.85G/H/I2346-2367[»]
2L5GNMR-B167-207[»]
2LTPNMR-A615-685[»]
2ODDNMR-B1109-1121[»]
2RT5NMR-B2518-2525[»]
3R29X-ray2.90C/D2346-2361[»]
3R2AX-ray3.00E/F2346-2361[»]
4A69X-ray2.06C/D389-480[»]
4OARX-ray2.41B2346-2362[»]
ProteinModelPortaliQ9Y618.
SMRiQ9Y618.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114974. 117 interactors.
DIPiDIP-951N.
IntActiQ9Y618. 39 interactors.
MINTiMINT-129997.
STRINGi9606.ENSP00000384018.

Chemistry databases

BindingDBiQ9Y618.
ChEMBLiCHEMBL2111363.

PTM databases

iPTMnetiQ9Y618.
PhosphoSitePlusiQ9Y618.

Polymorphism and mutation databases

BioMutaiNCOR2.
DMDMi226713806.

Proteomic databases

EPDiQ9Y618.
PaxDbiQ9Y618.
PeptideAtlasiQ9Y618.
PRIDEiQ9Y618.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356219; ENSP00000348551; ENSG00000196498.
GeneIDi9612.
KEGGihsa:9612.
UCSCiuc058uwu.1. human. [Q9Y618-1]

Organism-specific databases

CTDi9612.
DisGeNETi9612.
GeneCardsiNCOR2.
H-InvDBHIX0026341.
HGNCiHGNC:7673. NCOR2.
HPAiHPA001928.
MIMi600848. gene.
neXtProtiNX_Q9Y618.
PharmGKBiPA31478.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1878. Eukaryota.
ENOG410YDXP. LUCA.
HOVERGENiHBG052587.
InParanoidiQ9Y618.
KOiK06065.
PhylomeDBiQ9Y618.

Enzyme and pathway databases

BioCyciZFISH:G66-33796-MONOMER.
ReactomeiR-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-3214815. HDACs deacetylate histones.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-400206. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
SignaLinkiQ9Y618.
SIGNORiQ9Y618.

Miscellaneous databases

ChiTaRSiNCOR2. human.
EvolutionaryTraceiQ9Y618.
GeneWikiiNuclear_receptor_co-repressor_2.
GenomeRNAii9612.
PROiQ9Y618.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196498.
CleanExiHS_NCOR2.
ExpressionAtlasiQ9Y618. baseline and differential.
GenevisibleiQ9Y618. HS.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR009057. Homeodomain-like.
IPR031557. N-CoR_GPS2_interact.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]
PfamiPF15784. GPS2_interact. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51293. SANT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNCOR2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y618
Secondary accession number(s): O00613
, O15416, O15421, Q13354, Q56D06, Q59GM0, Q9Y5U0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: March 24, 2009
Last modified: November 30, 2016
This is version 187 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.