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Q9Y618 (NCOR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:NCOR2
Synonyms:CTG26
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2525 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.21 Ref.30

Subunit structure

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. Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.21 Ref.26 Ref.30 Ref.31

Subcellular location

Nucleus.

Tissue specificity

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

Induction

Regulated during cell cycle progression.

Domain

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 similarities

Belongs to the N-CoR nuclear receptor corepressors family.

Contains 2 SANT domains.

Sequence caution

The sequence AAB91452.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

The sequence AAC50236.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

The sequence AAD20946.1 differs from that shown. Reason: Frameshift at positions 787 and 794.

The sequence BAD92326.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
   LigandDNA-binding
   Molecular functionRepressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.3. Source: MGI

regulation of cellular ketone metabolic process by negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19955185. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentnuclear body

Inferred from direct assay PubMed 16030140. Source: MGI

nuclear matrix

Inferred from direct assay PubMed 21328542. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.3. Source: MGI

transcriptional repressor complex

Inferred from direct assay PubMed 11804585. Source: BHF-UCL

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Notch binding

Inferred from physical interaction PubMed 10713164. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: InterPro

histone deacetylase binding

Inferred from physical interaction PubMed 16924111. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 16893456. Source: UniProtKB

transcription corepressor activity

Inferred from mutant phenotype PubMed 12628926. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y618-1)

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.
Isoform 2 (identifier: Q9Y618-2)

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.
Isoform 3 (identifier: Q9Y618-3)

Also known as: h-SMRT;

The sequence of this isoform differs from the canonical sequence as follows:
     1034-1041: Missing.
Isoform 4 (identifier: Q9Y618-4)

Also known as: SMRTe;

The sequence of this isoform differs from the canonical sequence as follows:
     724-740: Missing.
Isoform 5 (identifier: Q9Y618-5)

Also known as: SMRT-tau;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25252525Nuclear receptor corepressor 2
PRO_0000055622

Regions

Domain427 – 47852SANT 1
Domain610 – 66152SANT 2
Region254 – 31259Interaction with SIN3A/B By similarity
Region2139 – 21424Required for interaction with RARA in the absence of its ligand
Coiled coil174 – 21542 Potential
Coiled coil522 – 56140 Potential
Motif2147 – 21515CORNR box of ID1
Motif2350 – 23545CORNR box of ID2
Compositional bias494 – 51017Poly-Gln
Compositional bias682 – 6854Poly-Lys
Compositional bias778 – 82043Pro-rich
Compositional bias995 – 10039Poly-Pro
Compositional bias1392 – 13976Poly-Pro
Compositional bias1850 – 18545Poly-Gly
Compositional bias2487 – 24904Poly-Pro

Amino acid modifications

Modified residue541Phosphoserine Ref.20
Modified residue671Phosphoserine Ref.24
Modified residue1491Phosphoserine Ref.19 Ref.22 Ref.24 Ref.27 Ref.29
Modified residue1521Phosphoserine Ref.22 Ref.24 Ref.27 Ref.29
Modified residue1561Phosphothreonine Ref.22
Modified residue2151Phosphoserine Ref.19
Modified residue5531Phosphothreonine Ref.24
Modified residue5541Phosphoserine Ref.24 Ref.27
Modified residue7501Phosphoserine Ref.22
Modified residue7531Phosphoserine Ref.22
Modified residue8781N6-acetyllysine Ref.25
Modified residue9391Phosphoserine Ref.24
Modified residue9561Phosphoserine Ref.27 Ref.29
Modified residue9591N6-acetyllysine Ref.25
Modified residue12181N6-acetyllysine Ref.25
Modified residue12481N6-acetyllysine Ref.25
Modified residue12591Phosphoserine Ref.22
Modified residue13311Phosphoserine Ref.24
Modified residue13911Phosphothreonine Ref.19 Ref.22
Modified residue14871Phosphoserine Ref.22
Modified residue17861Phosphoserine Ref.29
Modified residue18721Phosphoserine Ref.27
Modified residue19701N6-acetyllysine Ref.25
Modified residue20161Phosphoserine Ref.19
Modified residue20371N6-acetyllysine Ref.25
Modified residue20571Phosphoserine Ref.24
Modified residue20651Phosphoserine Ref.22 Ref.24
Modified residue20681Phosphoserine Ref.24
Modified residue20691Phosphoserine Ref.24
Modified residue20731Phosphothreonine Ref.22
Modified residue22141Phosphoserine Ref.27
Modified residue22341Phosphoserine Ref.22 Ref.24 Ref.27
Modified residue22691Phosphoserine Ref.19 Ref.22 Ref.24 Ref.27 Ref.29

Natural variations

Alternative sequence1 – 17101710Missing in isoform 2.
VSP_003412
Alternative sequence724 – 74017Missing in isoform 4 and isoform 5.
VSP_036595
Alternative sequence1034 – 10418Missing in isoform 3.
VSP_036596
Alternative sequence2361 – 240646Missing in isoform 2 and isoform 5.
VSP_003413
Natural variant7811G → E. Ref.6
Corresponds to variant rs7978237 [ dbSNP | Ensembl ].
VAR_060073
Natural variant17071A → T. Ref.2 Ref.3 Ref.4 Ref.8
Corresponds to variant rs2229840 [ dbSNP | Ensembl ].
VAR_054751
Natural variant20121P → S.
Corresponds to variant rs2230944 [ dbSNP | Ensembl ].
VAR_060074

Experimental info

Mutagenesis21391R → A: Abolishes interaction with the apo LBD of RARA. Restores some interaction on the addition of inverse agonist BMS493. Ref.26
Mutagenesis21411V → P: Abolishes interaction with the apo LBD of RARA. No change on interaction on the addition of inverse agonist BMS493. Ref.26
Mutagenesis21421T → G: Abolishes interaction with the apo LBD of RARA. Restores some interaction on the addition of inverse agonist BMS493. Ref.26
Sequence conflict71P → L in AAD20946. Ref.2
Sequence conflict2951E → K in AAD20946. Ref.2
Sequence conflict3091W → L in AAD20946. Ref.2
Sequence conflict3521Missing in AAD22973. Ref.3
Sequence conflict3521Missing in AAX77219. Ref.4
Sequence conflict3651A → P in AAD22973. Ref.3
Sequence conflict3651A → P in AAX77219. Ref.4
Sequence conflict612 – 6132SS → EF in AAB91446. Ref.7
Sequence conflict7111S → T in AAD22973. Ref.3
Sequence conflict7111S → T in AAX77219. Ref.4
Sequence conflict7961P → S in AAD22973. Ref.3
Sequence conflict7961P → S in AAX77219. Ref.4
Sequence conflict8041G → L in AAD22973. Ref.3
Sequence conflict8041G → L in AAX77219. Ref.4
Sequence conflict8141S → F in AAD22973. Ref.3
Sequence conflict8141S → F in AAX77219. Ref.4
Sequence conflict8171A → S in AAD22973. Ref.3
Sequence conflict8171A → S in AAX77219. Ref.4
Sequence conflict8891G → R in AAD22973. Ref.3
Sequence conflict8891G → R in AAX77219. Ref.4
Sequence conflict15701T → M in AAD20946. Ref.2
Sequence conflict15701T → M in AAD22973. Ref.3
Sequence conflict15701T → M in AAX77219. Ref.4
Sequence conflict15701T → M in AAC50236. Ref.8
Sequence conflict19021T → K in AAD20946. Ref.2
Sequence conflict19021T → K in AAD22973. Ref.3
Sequence conflict19021T → K in AAX77219. Ref.4
Sequence conflict19021T → K in AAC50236. Ref.8
Sequence conflict25021P → A in AAB50847. Ref.1

Secondary structure

.................................. 2525
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SMRT-alpha) (TRAC-2) [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 9B8689CA013C4513

FASTA2,525274,804
        10         20         30         40         50         60 
MSGSTQPVAQ TWRATEPRYP PHSLSYPVQI ARTHTDVGLL EYQHHSRDYA SHLSPGSIIQ 

        70         80         90        100        110        120 
PQRRRPSLLS EFQPGNERSQ ELHLRPESHS YLPELGKSEM EFIESKRPRL ELLPDPLLRP 

       130        140        150        160        170        180 
SPLLATGQPA GSEDLTKDRS LTGKLEPVSP PSPPHTDPEL ELVPPRLSKE ELIQNMDRVD 

       190        200        210        220        230        240 
REITMVEQQI SKLKKKQQQL EEEAAKPPEP EKPVSPPPIE SKHRSLVQII YDENRKKAEA 

       250        260        270        280        290        300 
AHRILEGLGP QVELPLYNQP SDTRQYHENI KINQAMRKKL ILYFKRRNHA RKQWEQKFCQ 

       310        320        330        340        350        360 
RYDQLMEAWE KKVERIENNP RRRAKESKVR EYYEKQFPEI RKQRELQERM QSRVGQRGSG 

       370        380        390        400        410        420 
LSMSAARSEH EVSEIIDGLS EQENLEKQMR QLAVIPPMLY DADQQRIKFI NMNGLMADPM 

       430        440        450        460        470        480 
KVYKDRQVMN MWSEQEKETF REKFMQHPKN FGLIASFLER KTVAECVLYY YLTKKNENYK 

       490        500        510        520        530        540 
SLVRRSYRRR GKSQQQQQQQ QQQQQQQQQQ PMPRSSQEEK DEKEKEKEAE KEEEKPEVEN 

       550        560        570        580        590        600 
DKEDLLKEKT DDTSGEDNDE KEAVASKGRK TANSQGRRKG RITRSMANEA NSEEAITPQQ 

       610        620        630        640        650        660 
SAELASMELN ESSRWTEEEM ETAKKGLLEH GRNWSAIARM VGSKTVSQCK NFYFNYKKRQ 

       670        680        690        700        710        720 
NLDEILQQHK LKMEKERNAR RKKKKAPAAA SEEAAFPPVV EDEEMEASGV SGNEEEMVEE 

       730        740        750        760        770        780 
AEALHASGNE VPRGECSGPA TVNNSSDTES IPSPHTEAAK DTGQNGPKPP ATLGADGPPP 

       790        800        810        820        830        840 
GPPTPPPEDI PAPTEPTPAS EATGAPTPPP APPSPSAPPP VVPKEEKEEE TAAAPPVEEG 

       850        860        870        880        890        900 
EEQKPPAAEE LAVDTGKAEE PVKSECTEEA EEGPAKGKDA EAAEATAEGA LKAEKKEGGS 

       910        920        930        940        950        960 
GRATTAKSSG APQDSDSSAT CSADEVDEAE GGDKNRLLSP RPSLLTPTGD PRANASPQKP 

       970        980        990       1000       1010       1020 
LDLKQLKQRA AAIPPIQVTK VHEPPREDAA PTKPAPPAPP PPQNLQPESD APQQPGSSPR 

      1030       1040       1050       1060       1070       1080 
GKSRSPAPPA DKEAEKPVFF PAFAAEAQKL PGDPPCWTSG LPFPVPPREV IKASPHAPDP 

      1090       1100       1110       1120       1130       1140 
SAFSYAPPGH PLPLGLHDTA RPVLPRPPTI SNPPPLISSA KHPSVLERQI GAISQGMSVQ 

      1150       1160       1170       1180       1190       1200 
LHVPYSEHAK APVGPVTMGL PLPMDPKKLA PFSGVKQEQL SPRGQAGPPE SLGVPTAQEA 

      1210       1220       1230       1240       1250       1260 
SVLRGTALGS VPGGSITKGI PSTRVPSDSA ITYRGSITHG TPADVLYKGT ITRIIGEDSP 

      1270       1280       1290       1300       1310       1320 
SRLDRGREDS LPKGHVIYEG KKGHVLSYEG GMSVTQCSKE DGRSSSGPPH ETAAPKRTYD 

      1330       1340       1350       1360       1370       1380 
MMEGRVGRAI SSASIEGLMG RAIPPERHSP HHLKEQHHIR GSITQGIPRS YVEAQEDYLR 

      1390       1400       1410       1420       1430       1440 
REAKLLKREG TPPPPPPSRD LTEAYKTQAL GPLKLKPAHE GLVATVKEAG RSIHEIPREE 

      1450       1460       1470       1480       1490       1500 
LRHTPELPLA PRPLKEGSIT QGTPLKYDTG ASTTGSKKHD VRSLIGSPGR TFPPVHPLDV 

      1510       1520       1530       1540       1550       1560 
MADARALERA CYEESLKSRP GTASSSGGSI ARGAPVIVPE LGKPRQSPLT YEDHGAPFAG 

      1570       1580       1590       1600       1610       1620 
HLPRGSPVTT REPTPRLQEG SLSSSKASQD RKLTSTPREI AKSPHSTVPE HHPHPISPYE 

      1630       1640       1650       1660       1670       1680 
HLLRGVSGVD LYRSHIPLAF DPTSIPRGIP LDAAAAYYLP RHLAPNPTYP HLYPPYLIRG 

      1690       1700       1710       1720       1730       1740 
YPDTAALENR QTIINDYITS QQMHHNAATA MAQRADMLRG LSPRESSLAL NYAAGPRGII 

      1750       1760       1770       1780       1790       1800 
DLSQVPHLPV LVPPTPGTPA TAMDRLAYLP TAPQPFSSRH SSSPLSPGGP THLTKPTTTS 

      1810       1820       1830       1840       1850       1860 
SSERERDRDR ERDRDREREK SILTSTTTVE HAPIWRPGTE QSSGSSGSSG GGGGSSSRPA 

      1870       1880       1890       1900       1910       1920 
SHSHAHQHSP ISPRTQDALQ QRPSVLHNTG MKGIITAVEP STPTVLRSTS TSSPVRPAAT 

      1930       1940       1950       1960       1970       1980 
FPPATHCPLG GTLDGVYPTL MEPVLLPKEA PRVARPERPR ADTGHAFLAK PPARSGLEPA 

      1990       2000       2010       2020       2030       2040 
SSPSKGSEPR PLVPPVSGHA TIARTPAKNL APHHASPDPP APPASASDPH REKTQSKPFS 

      2050       2060       2070       2080       2090       2100 
IQELELRSLG YHGSSYSPEG VEPVSPVSSP SLTHDKGLPK HLEELDKSHL EGELRPKQPG 

      2110       2120       2130       2140       2150       2160 
PVKLGGEAAH LPHLRPLPES QPSSSPLLQT APGVKGHQRV VTLAQHISEV ITQDYTRHHP 

      2170       2180       2190       2200       2210       2220 
QQLSAPLPAP LYSFPGASCP VLDLRRPPSD LYLPPPDHGA PARGSPHSEG GKRSPEPNKT 

      2230       2240       2250       2260       2270       2280 
SVLGGGEDGI EPVSPPEGMT EPGHSRSAVY PLLYRDGEQT EPSRMGSKSP GNTSQPPAFF 

      2290       2300       2310       2320       2330       2340 
SKLTESNSAM VKSKKQEINK KLNTHNRNEP EYNISQPGTE IFNMPAITGT GLMTYRSQAV 

      2350       2360       2370       2380       2390       2400 
QEHASTNMGL EAIIRKALMG KYDQWEESPP LSANAFNPLN ASASLPAAMP ITAADGRSDH 

      2410       2420       2430       2440       2450       2460 
TLTSPGGGGK AKVSGRPSSR KAKSPAPGLA SGDRPPSVSS VHSEGDCNRR TPLTNRVWED 

      2470       2480       2490       2500       2510       2520 
RPSSAGSTPF PYNPLIMRLQ AGVMASPPPP GLPAGSGPLA GPHHAWDEEP KPLLCSQYET 


LSDSE 

« Hide

Isoform 2 (TRAC-1) [UniParc].

Checksum: 399E0A5142E83975
Show »

FASTA76981,608
Isoform 3 (h-SMRT) [UniParc].

Checksum: D9616717A5C342DB
Show »

FASTA2,517273,888
Isoform 4 (SMRTe) [UniParc].

Checksum: 8738AABD508422AA
Show »

FASTA2,508273,141
Isoform 5 (SMRT-tau) [UniParc].

Checksum: 31DC105B162AFD57
Show »

FASTA2,462268,361

References

« Hide 'large scale' references
[1]"Identification of TRACs (T3 receptor-associating cofactors), a family of cofactors that associate with, and modulate the activity of, nuclear hormone receptors."
Sande S., Privalsky M.L.
Mol. Endocrinol. 10:813-825(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Fetal liver.
[2]"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] (ISOFORM 3), VARIANT THR-1707.
Tissue: Pituitary.
[3]"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 4), VARIANT THR-1707.
Tissue: Cervix adenocarcinoma.
[4]Chen J.D.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), VARIANT THR-1707.
[5]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1451, VARIANT GLU-781.
Tissue: Brain.
[7]"cDNAs with long CAG trinucleotide repeats from human brain."
Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S., Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.
Hum. Genet. 100:114-122(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 428-613.
Tissue: Brain cortex.
[8]"A transcriptional co-repressor that interacts with nuclear hormone receptors."
Chen J.D., Evans R.M.
Nature 377:454-457(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1023-2525, VARIANT THR-1707.
Tissue: Cervix adenocarcinoma.
[9]"A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness."
Guenther M.G., Lane W.S., Fischle W., Verdin E., Lazar M.A., Shiekhattar R.
Genes Dev. 14:1048-1057(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, COMPONENT OF THE N-COR COMPLEX WITH TBL1X AND HDAC3.
[10]"Both corepressor proteins SMRT and N-CoR exist in large protein complexes containing HDAC3."
Li J., Wang J., Wang J., Nawaz Z., Liu J.M., Qin J., Wong J.
EMBO J. 19:4342-4350(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPONENT OF THE N-COR COMPLEX WITH TBL1X AND HDAC3.
[11]"Sharp, an inducible cofactor that integrates nuclear receptor repression and activation."
Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M.
Genes Dev. 15:1140-1151(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MINT.
[12]"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.
[13]"The N-CoR-HDAC3 nuclear receptor corepressor complex inhibits the JNK pathway through the integral subunit GPS2."
Zhang J., Kalkum M., Chait B.T., Roeder R.G.
Mol. Cell 9:611-623(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPONENT OF THE N-COR COMPLEX WITH NCOR1; GPS2; TBL1X; TBL1R AND HDAC3.
[14]"Isolation and characterization of a novel class II histone deacetylase, HDAC10."
Fischer D.D., Cai R., Bhatia U., Asselbergs F.A.M., Song C., Terry R., Trogani N., Widmer R., Atadja P., Cohen D.
J. Biol. Chem. 277:6656-6666(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC10.
[15]"Retinoic acid receptors beta and gamma do not repress, but instead activate target gene transcription in both the absence and presence of hormone ligand."
Hauksdottir H., Farboud B., Privalsky M.L.
Mol. Endocrinol. 17:373-385(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RARB.
[16]"MTA3 and the Mi-2/NuRD complex regulate cell fate during B lymphocyte differentiation."
Fujita N., Jaye D.L., Geigerman C., Akyildiz A., Mooney M.R., Boss J.M., Wade P.A.
Cell 119:75-86(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCL6.
[17]"Boat, an AXH domain protein, suppresses the cytotoxicity of mutant ataxin-1."
Mizutani A., Wang L., Rajan H., Vig P.J.S., Alaynick W.A., Thaler J.P., Tsai C.-C.
EMBO J. 24:3339-3351(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATXN1L.
[18]"Alternative mRNA splicing of SMRT creates functional diversity by generating corepressor isoforms with different affinities for different nuclear receptors."
Goodson M.L., Jonas B.A., Privalsky M.L.
J. Biol. Chem. 280:7493-7503(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 5).
[19]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-215; THR-1391; SER-2016 AND SER-2269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"CtBP is an essential corepressor for BCL6 autoregulation."
Mendez L.M., Polo J.M., Yu J.J., Krupski M., Ding B.B., Melnick A., Ye B.H.
Mol. Cell. Biol. 28:2175-2186(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS BCL6 COREPRESSOR, INTERACTION WITH BCL6.
[22]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-152; THR-156; SER-750; SER-753; SER-1259; THR-1391; SER-1487; SER-2065; THR-2073; SER-2234 AND SER-2269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-149; SER-152; THR-553; SER-554; SER-939; SER-1331; SER-2057; SER-2065; SER-2068; SER-2069; SER-2234 AND SER-2269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[25]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-878; LYS-959; LYS-1218; LYS-1248; LYS-1970 AND LYS-2037, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"A unique secondary-structure switch controls constitutive gene repression by retinoic acid receptor."
le Maire A., Teyssier C., Erb C., Grimaldi M., Alvarez S., de Lera A.R., Balaguer P., Gronemeyer H., Royer C.A., Germain P., Bourguet W.
Nat. Struct. Mol. Biol. 17:801-807(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RARA, MUTAGENESIS OF ARG-2139; VAL-2141 AND THR-2142.
[27]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-152; SER-554; SER-956; SER-1872; SER-2214; SER-2234 AND SER-2269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-152; SER-956; SER-1786 AND SER-2269, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"A hybrid mechanism of action for BCL6 in B cells defined by formation of functionally distinct complexes at enhancers and promoters."
Hatzi K., Jiang Y., Huang C., Garrett-Bakelman F., Gearhart M.D., Giannopoulou E.G., Zumbo P., Kirouac K., Bhaskara S., Polo J.M., Kormaksson M., Mackerell A.D. Jr., Xue F., Mason C.E., Hiebert S.W., Prive G.G., Cerchietti L., Bardwell V.J., Elemento O., Melnick A.
Cell Rep. 4:578-588(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS BCL6 COREPRESSOR, INTERACTION WITH BCL6 AND HDAC3, IDENTIFICATION IN A COMPLEX WITH BCL6 AND BCOR.
[31]"Structural and functional analysis of the DEAF-1 and BS69 MYND domains."
Kateb F., Perrin H., Tripsianes K., Zou P., Spadaccini R., Bottomley M., Franzmann T.M., Buchner J., Ansieau S., Sattler M.
PLoS ONE 8:E54715-E54715(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DEAF1.
[32]"Mechanism of SMRT corepressor recruitment by the BCL6 BTB domain."
Ahmad K.F., Melnick A., Lax S., Bouchard D., Liu J., Kiang C.L., Mayer S., Takahashi S., Licht J.D., Prive G.G.
Mol. Cell 12:1551-1564(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1422-1438 IN COMPLEX WITH BL6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS60255.
RefSeqNP_001070729.2. NM_001077261.3.
NP_001193583.1. NM_001206654.1.
NP_006303.4. NM_006312.5.
UniGeneHs.137510.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ9Y618.
SMRQ9Y618. Positions 167-207, 408-476, 582-685.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114974. 104 interactions.
DIPDIP-951N.
IntActQ9Y618. 32 interactions.
MINTMINT-129997.
STRING9606.ENSP00000348551.

Chemistry

BindingDBQ9Y618.
ChEMBLCHEMBL2096976.

PTM databases

PhosphoSiteQ9Y618.

Polymorphism databases

DMDM226713806.

Proteomic databases

PaxDbQ9Y618.
PRIDEQ9Y618.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356219; ENSP00000348551; ENSG00000196498.
GeneID9612.
KEGGhsa:9612.
UCSCuc001ugj.1. human. [Q9Y618-1]
uc010tax.2. human. [Q9Y618-2]

Organism-specific databases

CTD9612.
GeneCardsGC12M124808.
H-InvDBHIX0026341.
HGNCHGNC:7673. NCOR2.
HPAHPA001928.
MIM600848. gene.
neXtProtNX_Q9Y618.
PharmGKBPA31478.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG052587.
KOK06065.
PhylomeDBQ9Y618.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_71. Gene Expression.
SignaLinkQ9Y618.

Gene expression databases

ArrayExpressQ9Y618.
BgeeQ9Y618.
CleanExHS_NCOR2.
GenevestigatorQ9Y618.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
InterProIPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]
PfamPF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTSM00717. SANT. 2 hits.
[Graphical view]
SUPFAMSSF46689. SSF46689. 2 hits.
PROSITEPS51293. SANT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNCOR2. human.
EvolutionaryTraceQ9Y618.
GeneWikiNuclear_receptor_co-repressor_2.
GenomeRNAi9612.
NextBio36061.
PROQ9Y618.
SOURCESearch...

Entry information

Entry nameNCOR2_HUMAN
AccessionPrimary (citable) accession number: Q9Y618
Secondary accession number(s): O00613 expand/collapse secondary AC list , O15416, O15421, Q13354, Q56D06, Q59GM0, Q9Y5U0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: March 24, 2009
Last modified: April 16, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM