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Q9Y618

- NCOR2_HUMAN

UniProt

Q9Y618 - NCOR2_HUMAN

Protein

Nuclear receptor corepressor 2

Gene

NCOR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 2 (24 Mar 2009)
      Previous versions | rss
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    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

    1. chromatin binding Source: InterPro
    2. DNA binding Source: UniProtKB-KW
    3. histone deacetylase binding Source: UniProtKB
    4. Notch binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein N-terminus binding Source: UniProtKB
    7. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. cellular lipid metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    4. Notch signaling pathway Source: Reactome
    5. regulation of cellular ketone metabolic process by negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    6. small molecule metabolic process Source: Reactome
    7. transcription, DNA-templated Source: Reactome
    8. transcription initiation from RNA polymerase II promoter Source: Reactome
    9. transforming growth factor beta receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinkiQ9Y618.

    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
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:7673. NCOR2.

    Subcellular locationi

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. nuclear body Source: MGI
    3. nuclear matrix Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: MGI
    6. transcriptional repressor complex Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2139 – 21391R → A: Abolishes interaction with the apo LBD of RARA. Restores some interaction on the addition of inverse agonist BMS493. 1 Publication
    Mutagenesisi2141 – 21411V → P: Abolishes interaction with the apo LBD of RARA. No change on interaction on the addition of inverse agonist BMS493. 1 Publication
    Mutagenesisi2142 – 21421T → G: Abolishes interaction with the apo LBD of RARA. Restores some interaction on the addition of inverse agonist BMS493. 1 Publication

    Organism-specific databases

    PharmGKBiPA31478.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25252525Nuclear receptor corepressor 2PRO_0000055622Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei54 – 541Phosphoserine1 Publication
    Modified residuei67 – 671Phosphoserine1 Publication
    Modified residuei149 – 1491Phosphoserine5 Publications
    Modified residuei152 – 1521Phosphoserine4 Publications
    Modified residuei156 – 1561Phosphothreonine1 Publication
    Modified residuei215 – 2151Phosphoserine1 Publication
    Modified residuei553 – 5531Phosphothreonine1 Publication
    Modified residuei554 – 5541Phosphoserine2 Publications
    Modified residuei750 – 7501Phosphoserine1 Publication
    Modified residuei753 – 7531Phosphoserine1 Publication
    Modified residuei878 – 8781N6-acetyllysine1 Publication
    Modified residuei939 – 9391Phosphoserine1 Publication
    Modified residuei956 – 9561Phosphoserine2 Publications
    Modified residuei959 – 9591N6-acetyllysine1 Publication
    Modified residuei1218 – 12181N6-acetyllysine1 Publication
    Modified residuei1248 – 12481N6-acetyllysine1 Publication
    Modified residuei1259 – 12591Phosphoserine1 Publication
    Modified residuei1331 – 13311Phosphoserine1 Publication
    Modified residuei1391 – 13911Phosphothreonine2 Publications
    Modified residuei1487 – 14871Phosphoserine1 Publication
    Modified residuei1786 – 17861Phosphoserine1 Publication
    Modified residuei1872 – 18721Phosphoserine1 Publication
    Modified residuei1970 – 19701N6-acetyllysine1 Publication
    Modified residuei2016 – 20161Phosphoserine1 Publication
    Modified residuei2037 – 20371N6-acetyllysine1 Publication
    Modified residuei2057 – 20571Phosphoserine1 Publication
    Modified residuei2065 – 20651Phosphoserine2 Publications
    Modified residuei2068 – 20681Phosphoserine1 Publication
    Modified residuei2069 – 20691Phosphoserine1 Publication
    Modified residuei2073 – 20731Phosphothreonine1 Publication
    Modified residuei2214 – 22141Phosphoserine1 Publication
    Modified residuei2234 – 22341Phosphoserine3 Publications
    Modified residuei2269 – 22691Phosphoserine5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y618.
    PaxDbiQ9Y618.
    PRIDEiQ9Y618.

    PTM databases

    PhosphoSiteiQ9Y618.

    Expressioni

    Tissue specificityi

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

    Inductioni

    Regulated during cell cycle progression.

    Gene expression databases

    ArrayExpressiQ9Y618.
    BgeeiQ9Y618.
    CleanExiHS_NCOR2.
    GenevestigatoriQ9Y618.

    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.12 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

    Protein-protein interaction databases

    BioGridi114974. 104 interactions.
    DIPiDIP-951N.
    IntActiQ9Y618. 32 interactions.
    MINTiMINT-129997.
    STRINGi9606.ENSP00000348551.

    Structurei

    Secondary structure

    1
    2525
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi168 – 1703
    Helixi171 – 20535
    Beta strandi414 – 4174
    Helixi419 – 42810
    Helixi434 – 44613
    Helixi451 – 4566
    Turni458 – 4603
    Helixi463 – 47311
    Turni474 – 4763
    Helixi617 – 62913
    Turni630 – 6323
    Helixi634 – 6407
    Beta strandi642 – 6443
    Helixi646 – 65510
    Helixi661 – 67919
    Beta strandi1116 – 11183
    Beta strandi1424 – 14285
    Helixi2351 – 23577

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ9Y618.
    SMRiQ9Y618. Positions 167-207, 408-476, 582-685.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y618.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini427 – 47852SANT 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini610 – 66152SANT 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni254 – 31259Interaction with SIN3A/BBy similarityAdd
    BLAST
    Regioni2139 – 21424Required for interaction with RARA in the absence of its ligand

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili174 – 21542Sequence AnalysisAdd
    BLAST
    Coiled coili522 – 56140Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2147 – 21515CORNR box of ID1
    Motifi2350 – 23545CORNR box of ID2

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi494 – 51017Poly-GlnAdd
    BLAST
    Compositional biasi682 – 6854Poly-Lys
    Compositional biasi778 – 82043Pro-richAdd
    BLAST
    Compositional biasi995 – 10039Poly-Pro
    Compositional biasi1392 – 13976Poly-Pro
    Compositional biasi1850 – 18545Poly-Gly
    Compositional biasi2487 – 24904Poly-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.
    HOVERGENiHBG052587.
    KOiK06065.
    PhylomeDBiQ9Y618.

    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    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

    MSGSTQPVAQ TWRATEPRYP PHSLSYPVQI ARTHTDVGLL EYQHHSRDYA     50
    SHLSPGSIIQ PQRRRPSLLS EFQPGNERSQ ELHLRPESHS YLPELGKSEM 100
    EFIESKRPRL ELLPDPLLRP SPLLATGQPA GSEDLTKDRS LTGKLEPVSP 150
    PSPPHTDPEL ELVPPRLSKE ELIQNMDRVD REITMVEQQI SKLKKKQQQL 200
    EEEAAKPPEP EKPVSPPPIE SKHRSLVQII YDENRKKAEA AHRILEGLGP 250
    QVELPLYNQP SDTRQYHENI KINQAMRKKL ILYFKRRNHA RKQWEQKFCQ 300
    RYDQLMEAWE KKVERIENNP RRRAKESKVR EYYEKQFPEI RKQRELQERM 350
    QSRVGQRGSG LSMSAARSEH EVSEIIDGLS EQENLEKQMR QLAVIPPMLY 400
    DADQQRIKFI NMNGLMADPM KVYKDRQVMN MWSEQEKETF REKFMQHPKN 450
    FGLIASFLER KTVAECVLYY YLTKKNENYK SLVRRSYRRR GKSQQQQQQQ 500
    QQQQQQQQQQ PMPRSSQEEK DEKEKEKEAE KEEEKPEVEN DKEDLLKEKT 550
    DDTSGEDNDE KEAVASKGRK TANSQGRRKG RITRSMANEA NSEEAITPQQ 600
    SAELASMELN ESSRWTEEEM ETAKKGLLEH GRNWSAIARM VGSKTVSQCK 650
    NFYFNYKKRQ NLDEILQQHK LKMEKERNAR RKKKKAPAAA SEEAAFPPVV 700
    EDEEMEASGV SGNEEEMVEE AEALHASGNE VPRGECSGPA TVNNSSDTES 750
    IPSPHTEAAK DTGQNGPKPP ATLGADGPPP GPPTPPPEDI PAPTEPTPAS 800
    EATGAPTPPP APPSPSAPPP VVPKEEKEEE TAAAPPVEEG EEQKPPAAEE 850
    LAVDTGKAEE PVKSECTEEA EEGPAKGKDA EAAEATAEGA LKAEKKEGGS 900
    GRATTAKSSG APQDSDSSAT CSADEVDEAE GGDKNRLLSP RPSLLTPTGD 950
    PRANASPQKP LDLKQLKQRA AAIPPIQVTK VHEPPREDAA PTKPAPPAPP 1000
    PPQNLQPESD APQQPGSSPR GKSRSPAPPA DKEAEKPVFF PAFAAEAQKL 1050
    PGDPPCWTSG LPFPVPPREV IKASPHAPDP SAFSYAPPGH PLPLGLHDTA 1100
    RPVLPRPPTI SNPPPLISSA KHPSVLERQI GAISQGMSVQ LHVPYSEHAK 1150
    APVGPVTMGL PLPMDPKKLA PFSGVKQEQL SPRGQAGPPE SLGVPTAQEA 1200
    SVLRGTALGS VPGGSITKGI PSTRVPSDSA ITYRGSITHG TPADVLYKGT 1250
    ITRIIGEDSP SRLDRGREDS LPKGHVIYEG KKGHVLSYEG GMSVTQCSKE 1300
    DGRSSSGPPH ETAAPKRTYD MMEGRVGRAI SSASIEGLMG RAIPPERHSP 1350
    HHLKEQHHIR GSITQGIPRS YVEAQEDYLR REAKLLKREG TPPPPPPSRD 1400
    LTEAYKTQAL GPLKLKPAHE GLVATVKEAG RSIHEIPREE LRHTPELPLA 1450
    PRPLKEGSIT QGTPLKYDTG ASTTGSKKHD VRSLIGSPGR TFPPVHPLDV 1500
    MADARALERA CYEESLKSRP GTASSSGGSI ARGAPVIVPE LGKPRQSPLT 1550
    YEDHGAPFAG HLPRGSPVTT REPTPRLQEG SLSSSKASQD RKLTSTPREI 1600
    AKSPHSTVPE HHPHPISPYE HLLRGVSGVD LYRSHIPLAF DPTSIPRGIP 1650
    LDAAAAYYLP RHLAPNPTYP HLYPPYLIRG YPDTAALENR QTIINDYITS 1700
    QQMHHNAATA MAQRADMLRG LSPRESSLAL NYAAGPRGII DLSQVPHLPV 1750
    LVPPTPGTPA TAMDRLAYLP TAPQPFSSRH SSSPLSPGGP THLTKPTTTS 1800
    SSERERDRDR ERDRDREREK SILTSTTTVE HAPIWRPGTE QSSGSSGSSG 1850
    GGGGSSSRPA SHSHAHQHSP ISPRTQDALQ QRPSVLHNTG MKGIITAVEP 1900
    STPTVLRSTS TSSPVRPAAT FPPATHCPLG GTLDGVYPTL MEPVLLPKEA 1950
    PRVARPERPR ADTGHAFLAK PPARSGLEPA SSPSKGSEPR PLVPPVSGHA 2000
    TIARTPAKNL APHHASPDPP APPASASDPH REKTQSKPFS IQELELRSLG 2050
    YHGSSYSPEG VEPVSPVSSP SLTHDKGLPK HLEELDKSHL EGELRPKQPG 2100
    PVKLGGEAAH LPHLRPLPES QPSSSPLLQT APGVKGHQRV VTLAQHISEV 2150
    ITQDYTRHHP QQLSAPLPAP LYSFPGASCP VLDLRRPPSD LYLPPPDHGA 2200
    PARGSPHSEG GKRSPEPNKT SVLGGGEDGI EPVSPPEGMT EPGHSRSAVY 2250
    PLLYRDGEQT EPSRMGSKSP GNTSQPPAFF SKLTESNSAM VKSKKQEINK 2300
    KLNTHNRNEP EYNISQPGTE IFNMPAITGT GLMTYRSQAV QEHASTNMGL 2350
    EAIIRKALMG KYDQWEESPP LSANAFNPLN ASASLPAAMP ITAADGRSDH 2400
    TLTSPGGGGK AKVSGRPSSR KAKSPAPGLA SGDRPPSVSS VHSEGDCNRR 2450
    TPLTNRVWED RPSSAGSTPF PYNPLIMRLQ AGVMASPPPP GLPAGSGPLA 2500
    GPHHAWDEEP KPLLCSQYET LSDSE 2525
    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 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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71P → L in AAD20946. (PubMed:10077563)Curated
    Sequence conflicti295 – 2951E → K in AAD20946. (PubMed:10077563)Curated
    Sequence conflicti309 – 3091W → L in AAD20946. (PubMed:10077563)Curated
    Sequence conflicti352 – 3521Missing in AAD22973. (PubMed:10097068)Curated
    Sequence conflicti352 – 3521Missing in AAX77219. 1 PublicationCurated
    Sequence conflicti365 – 3651A → P in AAD22973. (PubMed:10097068)Curated
    Sequence conflicti365 – 3651A → P in AAX77219. 1 PublicationCurated
    Sequence conflicti612 – 6132SS → EF in AAB91446. (PubMed:9225980)Curated
    Sequence conflicti711 – 7111S → T in AAD22973. (PubMed:10097068)Curated
    Sequence conflicti711 – 7111S → T in AAX77219. 1 PublicationCurated
    Sequence conflicti796 – 7961P → S in AAD22973. (PubMed:10097068)Curated
    Sequence conflicti796 – 7961P → S in AAX77219. 1 PublicationCurated
    Sequence conflicti804 – 8041G → L in AAD22973. (PubMed:10097068)Curated
    Sequence conflicti804 – 8041G → L in AAX77219. 1 PublicationCurated
    Sequence conflicti814 – 8141S → F in AAD22973. (PubMed:10097068)Curated
    Sequence conflicti814 – 8141S → F in AAX77219. 1 PublicationCurated
    Sequence conflicti817 – 8171A → S in AAD22973. (PubMed:10097068)Curated
    Sequence conflicti817 – 8171A → S in AAX77219. 1 PublicationCurated
    Sequence conflicti889 – 8891G → R in AAD22973. (PubMed:10097068)Curated
    Sequence conflicti889 – 8891G → R in AAX77219. 1 PublicationCurated
    Sequence conflicti1570 – 15701T → M in AAD20946. (PubMed:10077563)Curated
    Sequence conflicti1570 – 15701T → M in AAD22973. (PubMed:10097068)Curated
    Sequence conflicti1570 – 15701T → M in AAX77219. 1 PublicationCurated
    Sequence conflicti1570 – 15701T → M in AAC50236. (PubMed:7566127)Curated
    Sequence conflicti1902 – 19021T → K in AAD20946. (PubMed:10077563)Curated
    Sequence conflicti1902 – 19021T → K in AAD22973. (PubMed:10097068)Curated
    Sequence conflicti1902 – 19021T → K in AAX77219. 1 PublicationCurated
    Sequence conflicti1902 – 19021T → K in AAC50236. (PubMed:7566127)Curated
    Sequence conflicti2502 – 25021P → A in AAB50847. (PubMed:8813722)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti781 – 7811G → E.1 Publication
    Corresponds to variant rs7978237 [ dbSNP | Ensembl ].
    VAR_060073
    Natural varianti1707 – 17071A → T.4 Publications
    Corresponds to variant rs2229840 [ dbSNP | Ensembl ].
    VAR_054751
    Natural varianti2012 – 20121P → S.
    Corresponds to variant rs2230944 [ dbSNP | Ensembl ].
    VAR_060074

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 17101710Missing in isoform 2. 1 PublicationVSP_003412Add
    BLAST
    Alternative sequencei724 – 74017Missing in isoform 4 and isoform 5. 2 PublicationsVSP_036595Add
    BLAST
    Alternative sequencei1034 – 10418Missing in isoform 3. 1 PublicationVSP_036596
    Alternative sequencei2361 – 240646Missing in isoform 2 and isoform 5. 2 PublicationsVSP_003413Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    UCSCiuc001ugj.1. human. [Q9Y618-1]
    uc010tax.2. human. [Q9Y618-2]

    Polymorphism databases

    DMDMi226713806.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    PIRi S60255.
    RefSeqi NP_001070729.2. NM_001077261.3.
    NP_001193583.1. NM_001206654.1.
    NP_006303.4. NM_006312.5.
    UniGenei Hs.137510.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KKQ X-ray 3.00 E/F/G/H 2347-2365 [» ]
    1R2B X-ray 2.20 C/D 1422-1438 [» ]
    1XC5 NMR - A 412-480 [» ]
    2GPV X-ray 2.85 G/H/I 2346-2367 [» ]
    2L5G NMR - B 167-207 [» ]
    2LTP NMR - A 615-685 [» ]
    2ODD NMR - B 1109-1121 [» ]
    2RT5 NMR - B 2518-2525 [» ]
    3R29 X-ray 2.90 C/D 2346-2361 [» ]
    3R2A X-ray 3.00 E/F 2346-2361 [» ]
    4A69 X-ray 2.06 C/D 389-480 [» ]
    ProteinModelPortali Q9Y618.
    SMRi Q9Y618. Positions 167-207, 408-476, 582-685.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114974. 104 interactions.
    DIPi DIP-951N.
    IntActi Q9Y618. 32 interactions.
    MINTi MINT-129997.
    STRINGi 9606.ENSP00000348551.

    Chemistry

    BindingDBi Q9Y618.
    ChEMBLi CHEMBL2096976.

    PTM databases

    PhosphoSitei Q9Y618.

    Polymorphism databases

    DMDMi 226713806.

    Proteomic databases

    MaxQBi Q9Y618.
    PaxDbi Q9Y618.
    PRIDEi Q9Y618.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356219 ; ENSP00000348551 ; ENSG00000196498 .
    GeneIDi 9612.
    KEGGi hsa:9612.
    UCSCi uc001ugj.1. human. [Q9Y618-1 ]
    uc010tax.2. human. [Q9Y618-2 ]

    Organism-specific databases

    CTDi 9612.
    GeneCardsi GC12M124808.
    H-InvDB HIX0026341.
    HGNCi HGNC:7673. NCOR2.
    HPAi HPA001928.
    MIMi 600848. gene.
    neXtProti NX_Q9Y618.
    PharmGKBi PA31478.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG052587.
    KOi K06065.
    PhylomeDBi Q9Y618.

    Enzyme and pathway databases

    Reactomei REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinki Q9Y618.

    Miscellaneous databases

    ChiTaRSi NCOR2. human.
    EvolutionaryTracei Q9Y618.
    GeneWikii Nuclear_receptor_co-repressor_2.
    GenomeRNAii 9612.
    NextBioi 36061.
    PROi Q9Y618.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y618.
    Bgeei Q9Y618.
    CleanExi HS_NCOR2.
    Genevestigatori Q9Y618.

    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

    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.
      , 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. 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. Cited for: FUNCTION AS BCL6 COREPRESSOR, INTERACTION WITH BCL6.
    22. 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. "The basic helix-loop-helix proteins differentiated embryo chondrocyte (DEC) 1 and DEC2 function as corepressors of retinoid X receptors."
      Cho Y., Noshiro M., Choi M., Morita K., Kawamoto T., Fujimoto K., Kato Y., Makishima M.
      Mol. Pharmacol. 76:1360-1369(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RXRA.
    25. "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.
    26. "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].
    27. "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.
    28. "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.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "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].
    31. Cited for: FUNCTION AS BCL6 COREPRESSOR, INTERACTION WITH BCL6 AND HDAC3, IDENTIFICATION IN A COMPLEX WITH BCL6 AND BCOR.
    32. Cited for: INTERACTION WITH DEAF1.
    33. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1422-1438 IN COMPLEX WITH BL6.

    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: October 1, 2014
    This is version 164 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

    External Data

    Dasty 3