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Q9Y618

- NCOR2_HUMAN

UniProt

Q9Y618 - NCOR2_HUMAN

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Protein

Nuclear receptor corepressor 2

Gene

NCOR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Transcriptional corepressor. Mediates the transcriptional repression activity of some nuclear receptors by promoting chromatin condensation, thus preventing access of the basal transcription. Isoform 1 and isoform 5 have different affinities for different nuclear receptors. Involved in the regulation BCL6-dependent of the germinal center (GC) reactions, mainly through the control of the GC B-cells proliferation and survival.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 N-terminus binding Source: UniProtKB
  6. 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
Complete GO annotation...

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_228222. HDACs deacetylate histones.
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
Complete GO annotation...

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

BgeeiQ9Y618.
CleanExiHS_NCOR2.
ExpressionAtlasiQ9Y618. baseline and differential.
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. 106 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 – 1703Combined sources
Helixi171 – 20535Combined sources
Beta strandi414 – 4174Combined sources
Helixi419 – 42810Combined sources
Helixi434 – 44613Combined sources
Helixi451 – 4566Combined sources
Turni458 – 4603Combined sources
Helixi463 – 47311Combined sources
Turni474 – 4763Combined sources
Helixi617 – 62913Combined sources
Turni630 – 6323Combined sources
Helixi634 – 6407Combined sources
Beta strandi642 – 6443Combined sources
Helixi646 – 65510Combined sources
Helixi661 – 67919Combined sources
Beta strandi1116 – 11183Combined sources
Beta strandi1424 – 14285Combined sources
Helixi2351 – 23577Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4OARX-ray2.41B2346-2362[»]
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.
InParanoidiQ9Y618.
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

        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 AAC50236.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence AAD20946.1 differs from that shown. Reason: Frameshift at positions 787 and 794. Curated
The sequence BAD92326.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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:
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.
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:
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.
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
4OAR X-ray 2.41 B 2346-2362 [» ]
ProteinModelPortali Q9Y618.
SMRi Q9Y618. Positions 167-207, 408-476, 582-685.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114974. 106 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.
InParanoidi Q9Y618.
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_228222. HDACs deacetylate histones.
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

Bgeei Q9Y618.
CleanExi HS_NCOR2.
ExpressionAtlasi Q9Y618. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 166 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