Q9Y618 (NCOR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	NCOR2
Synonyms:	CTG26

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2525 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcriptional corepressor of NR4A2/NURR1 and acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in a repressed deacetylated state By similarity. 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.
Subunit structure	Interacts with BCL6, HDAC7 and C1D. Interacts with NR4A2; this interaction increases in the absence of PITX3 By similarity. 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 SRMT) 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. Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.23
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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat
Ligand	DNA-binding
Molecular function	Repressor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling pathway Traceable author statement. Source: Reactome cellular lipid metabolic process 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 transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome
Cellular_component	nuclear body Inferred from direct assay PubMed 16030140. Source: MGI nucleus Inferred from direct assay Ref.3. Source: MGI transcriptional repressor complex Inferred from direct assay PubMed 11804585. Source: BHF-UCL
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Inferred from electronic annotation. Source: InterPro transcription corepressor activity Inferred from mutant phenotype PubMed 12628926. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AHR	P35869	2	EBI-80830,EBI-80780
ARNT	P27540	2	EBI-80830,EBI-80809
E2F1	Q01094	2	EBI-80830,EBI-448924
HDAC1	Q13547	2	EBI-80830,EBI-301834
SNW1	Q13573	3	EBI-80830,EBI-632715

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2525

2525

Nuclear receptor corepressor 2

PRO_0000055622

Regions

Domain

427 – 478

52

SANT 1

Domain

610 – 661

52

SANT 2

Region

254 – 312

59

Interaction with SIN3A/B By similarity

Region

2139 – 2142

4

Required for interaction with RARA in the absence of its ligand

Coiled coil

174 – 215

42

Potential

Coiled coil

522 – 561

40

Potential

Motif

2147 – 2151

5

CORNR box of ID1

Motif

2350 – 2354

5

CORNR box of ID2

Compositional bias

494 – 510

17

Poly-Gln

Compositional bias

682 – 685

4

Poly-Lys

Compositional bias

778 – 820

43

Pro-rich

Compositional bias

995 – 1003

9

Poly-Pro

Compositional bias

1392 – 1397

6

Poly-Pro

Compositional bias

1850 – 1854

5

Poly-Gly

Compositional bias

2487 – 2490

4

Poly-Pro

Amino acid modifications

Modified residue

54

1

Phosphoserine Ref.19

Modified residue

67

1

Phosphoserine Ref.21

Modified residue

149

1

Phosphoserine Ref.18 Ref.20 Ref.21 Ref.24 Ref.26

Modified residue

152

1

Phosphoserine Ref.20 Ref.21 Ref.24 Ref.26

Modified residue

156

1

Phosphothreonine Ref.20

Modified residue

215

1

Phosphoserine Ref.18

Modified residue

553

1

Phosphothreonine Ref.21

Modified residue

554

1

Phosphoserine Ref.21 Ref.24

Modified residue

750

1

Phosphoserine Ref.20

Modified residue

753

1

Phosphoserine Ref.20

Modified residue

864

1

Phosphoserine By similarity

Modified residue

878

1

N6-acetyllysine Ref.22

Modified residue

939

1

Phosphoserine Ref.21

Modified residue

956

1

Phosphoserine Ref.24 Ref.26

Modified residue

959

1

N6-acetyllysine Ref.22

Modified residue

1218

1

N6-acetyllysine Ref.22

Modified residue

1248

1

N6-acetyllysine Ref.22

Modified residue

1259

1

Phosphoserine Ref.20

Modified residue

1331

1

Phosphoserine Ref.21

Modified residue

1391

1

Phosphothreonine Ref.18 Ref.20

Modified residue

1444

1

Phosphothreonine By similarity

Modified residue

1487

1

Phosphoserine Ref.20

Modified residue

1786

1

Phosphoserine Ref.26

Modified residue

1872

1

Phosphoserine Ref.24

Modified residue

1970

1

N6-acetyllysine Ref.22

Modified residue

2016

1

Phosphoserine Ref.18

Modified residue

2037

1

N6-acetyllysine Ref.22

Modified residue

2057

1

Phosphoserine Ref.21

Modified residue

2065

1

Phosphoserine Ref.20 Ref.21

Modified residue

2068

1

Phosphoserine Ref.21

Modified residue

2069

1

Phosphoserine Ref.21

Modified residue

2073

1

Phosphothreonine Ref.20

Modified residue

2214

1

Phosphoserine Ref.24

Modified residue

2234

1

Phosphoserine Ref.20 Ref.21 Ref.24

Modified residue

2269

1

Phosphoserine Ref.18 Ref.20 Ref.21 Ref.24 Ref.26

Modified residue

2463

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 1710

1710

Missing in isoform 2.

VSP_003412

Alternative sequence

724 – 740

17

Missing in isoform 4 and isoform 5.

VSP_036595

Alternative sequence

1034 – 1041

8

Missing in isoform 3.

VSP_036596

Alternative sequence

2361 – 2406

46

Missing in isoform 2 and isoform 5.

VSP_003413

Natural variant

781

1

G → E. Ref.6
Corresponds to variant rs7978237 [ dbSNP | Ensembl ].

VAR_060073

Natural variant

1707

1

A → T. Ref.2 Ref.3 Ref.4 Ref.8
Corresponds to variant rs2229840 [ dbSNP | Ensembl ].

VAR_054751

Natural variant

2012

1

P → S.
Corresponds to variant rs2230944 [ dbSNP | Ensembl ].

VAR_060074

Experimental info

Mutagenesis

2139

1

R → A: Abolishes interaction with the apo LBD of RARA. Restores some interaction on the addition of inverse agonist BMS493. Ref.23

Mutagenesis

2141

1

V → P: Abolishes interaction with the apo LBD of RARA. No change on interaction on the addition of inverse agonist BMS493. Ref.23

Mutagenesis

2142

1

T → G: Abolishes interaction with the apo LBD of RARA. Restores some interaction on the addition of inverse agonist BMS493. Ref.23

Sequence conflict

7

1

P → L in AAD20946. Ref.2

Sequence conflict

295

1

E → K in AAD20946. Ref.2

Sequence conflict

309

1

W → L in AAD20946. Ref.2

Sequence conflict

352

1

Missing in AAD22973. Ref.3

Sequence conflict

352

1

Missing in AAX77219. Ref.4

Sequence conflict

365

1

A → P in AAD22973. Ref.3

Sequence conflict

365

1

A → P in AAX77219. Ref.4

Sequence conflict

612 – 613

2

SS → EF in AAB91446. Ref.7

Sequence conflict

711

1

S → T in AAD22973. Ref.3

Sequence conflict

711

1

S → T in AAX77219. Ref.4

Sequence conflict

796

1

P → S in AAD22973. Ref.3

Sequence conflict

796

1

P → S in AAX77219. Ref.4

Sequence conflict

804

1

G → L in AAD22973. Ref.3

Sequence conflict

804

1

G → L in AAX77219. Ref.4

Sequence conflict

814

1

S → F in AAD22973. Ref.3

Sequence conflict

814

1

S → F in AAX77219. Ref.4

Sequence conflict

817

1

A → S in AAD22973. Ref.3

Sequence conflict

817

1

A → S in AAX77219. Ref.4

Sequence conflict

889

1

G → R in AAD22973. Ref.3

Sequence conflict

889

1

G → R in AAX77219. Ref.4

Sequence conflict

1570

1

T → M in AAD20946. Ref.2

Sequence conflict

1570

1

T → M in AAD22973. Ref.3

Sequence conflict

1570

1

T → M in AAX77219. Ref.4

Sequence conflict

1570

1

T → M in AAC50236. Ref.8

Sequence conflict

1902

1

T → K in AAD20946. Ref.2

Sequence conflict

1902

1

T → K in AAD22973. Ref.3

Sequence conflict

1902

1

T → K in AAX77219. Ref.4

Sequence conflict

1902

1

T → K in AAC50236. Ref.8

Sequence conflict

2502

1

P → A in AAB50847. Ref.1

Secondary structure

1

.

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2525

Helix Strand Turn

Details...

Beta strand

414 – 417

4

Helix

419 – 428

10

Helix

434 – 446

13

Helix

451 – 456

6

Turn

458 – 460

3

Helix

463 – 473

11

Turn

474 – 476

3

Helix

617 – 629

13

Turn

630 – 632

3

Helix

634 – 640

7

Beta strand

642 – 644

3

Helix

646 – 655

10

Helix

661 – 679

19

Beta strand

1116 – 1118

3

Beta strand

1424 – 1428

5

Helix

2351 – 2359

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (SMRT-alpha) (TRAC-2) [UniParc]. Last modified March 24, 2009. Version 2. Checksum: 9B8689CA013C4513	FASTA	2,525	274,804
	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
	Isoform 2 (TRAC-1) [UniParc]. Checksum: 399E0A5142E83975	FASTA	769	81,608
	10 20 30 40 50 60 MAQRADMLRG LSPRESSLAL NYAAGPRGII DLSQVPHLPV LVPPTPGTPA TAMDRLAYLP 70 80 90 100 110 120 TAPQPFSSRH SSSPLSPGGP THLTKPTTTS SSERERDRDR ERDRDREREK SILTSTTTVE 130 140 150 160 170 180 HAPIWRPGTE QSSGSSGSSG GGGGSSSRPA SHSHAHQHSP ISPRTQDALQ QRPSVLHNTG 190 200 210 220 230 240 MKGIITAVEP STPTVLRSTS TSSPVRPAAT FPPATHCPLG GTLDGVYPTL MEPVLLPKEA 250 260 270 280 290 300 PRVARPERPR ADTGHAFLAK PPARSGLEPA SSPSKGSEPR PLVPPVSGHA TIARTPAKNL 310 320 330 340 350 360 APHHASPDPP APPASASDPH REKTQSKPFS IQELELRSLG YHGSSYSPEG VEPVSPVSSP 370 380 390 400 410 420 SLTHDKGLPK HLEELDKSHL EGELRPKQPG PVKLGGEAAH LPHLRPLPES QPSSSPLLQT 430 440 450 460 470 480 APGVKGHQRV VTLAQHISEV ITQDYTRHHP QQLSAPLPAP LYSFPGASCP VLDLRRPPSD 490 500 510 520 530 540 LYLPPPDHGA PARGSPHSEG GKRSPEPNKT SVLGGGEDGI EPVSPPEGMT EPGHSRSAVY 550 560 570 580 590 600 PLLYRDGEQT EPSRMGSKSP GNTSQPPAFF SKLTESNSAM VKSKKQEINK KLNTHNRNEP 610 620 630 640 650 660 EYNISQPGTE IFNMPAITGT GLMTYRSQAV QEHASTNMGL EAIIRKALMG GGGKAKVSGR 670 680 690 700 710 720 PSSRKAKSPA PGLASGDRPP SVSSVHSEGD CNRRTPLTNR VWEDRPSSAG STPFPYNPLI 730 740 750 760 MRLQAGVMAS PPPPGLPAGS GPLAGPHHAW DEEPKPLLCS QYETLSDSE
	Isoform 3 (h-SMRT) [UniParc]. Checksum: D9616717A5C342DB	FASTA	2,517	273,888
	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 DKEAFAAEAQ KLPGDPPCWT SGLPFPVPPR EVIKASPHAP DPSAFSYAPP 1090 1100 1110 1120 1130 1140 GHPLPLGLHD TARPVLPRPP TISNPPPLIS SAKHPSVLER QIGAISQGMS VQLHVPYSEH 1150 1160 1170 1180 1190 1200 AKAPVGPVTM GLPLPMDPKK LAPFSGVKQE QLSPRGQAGP PESLGVPTAQ EASVLRGTAL 1210 1220 1230 1240 1250 1260 GSVPGGSITK GIPSTRVPSD SAITYRGSIT HGTPADVLYK GTITRIIGED SPSRLDRGRE 1270 1280 1290 1300 1310 1320 DSLPKGHVIY EGKKGHVLSY EGGMSVTQCS KEDGRSSSGP PHETAAPKRT YDMMEGRVGR 1330 1340 1350 1360 1370 1380 AISSASIEGL MGRAIPPERH SPHHLKEQHH IRGSITQGIP RSYVEAQEDY LRREAKLLKR 1390 1400 1410 1420 1430 1440 EGTPPPPPPS RDLTEAYKTQ ALGPLKLKPA HEGLVATVKE AGRSIHEIPR EELRHTPELP 1450 1460 1470 1480 1490 1500 LAPRPLKEGS ITQGTPLKYD TGASTTGSKK HDVRSLIGSP GRTFPPVHPL DVMADARALE 1510 1520 1530 1540 1550 1560 RACYEESLKS RPGTASSSGG SIARGAPVIV PELGKPRQSP LTYEDHGAPF AGHLPRGSPV 1570 1580 1590 1600 1610 1620 TTREPTPRLQ EGSLSSSKAS QDRKLTSTPR EIAKSPHSTV PEHHPHPISP YEHLLRGVSG 1630 1640 1650 1660 1670 1680 VDLYRSHIPL AFDPTSIPRG IPLDAAAAYY LPRHLAPNPT YPHLYPPYLI RGYPDTAALE 1690 1700 1710 1720 1730 1740 NRQTIINDYI TSQQMHHNAA TAMAQRADML RGLSPRESSL ALNYAAGPRG IIDLSQVPHL 1750 1760 1770 1780 1790 1800 PVLVPPTPGT PATAMDRLAY LPTAPQPFSS RHSSSPLSPG GPTHLTKPTT TSSSERERDR 1810 1820 1830 1840 1850 1860 DRERDRDRER EKSILTSTTT VEHAPIWRPG TEQSSGSSGS SGGGGGSSSR PASHSHAHQH 1870 1880 1890 1900 1910 1920 SPISPRTQDA LQQRPSVLHN TGMKGIITAV EPSTPTVLRS TSTSSPVRPA ATFPPATHCP 1930 1940 1950 1960 1970 1980 LGGTLDGVYP TLMEPVLLPK EAPRVARPER PRADTGHAFL AKPPARSGLE PASSPSKGSE 1990 2000 2010 2020 2030 2040 PRPLVPPVSG HATIARTPAK NLAPHHASPD PPAPPASASD PHREKTQSKP FSIQELELRS 2050 2060 2070 2080 2090 2100 LGYHGSSYSP EGVEPVSPVS SPSLTHDKGL PKHLEELDKS HLEGELRPKQ PGPVKLGGEA 2110 2120 2130 2140 2150 2160 AHLPHLRPLP ESQPSSSPLL QTAPGVKGHQ RVVTLAQHIS EVITQDYTRH HPQQLSAPLP 2170 2180 2190 2200 2210 2220 APLYSFPGAS CPVLDLRRPP SDLYLPPPDH GAPARGSPHS EGGKRSPEPN KTSVLGGGED 2230 2240 2250 2260 2270 2280 GIEPVSPPEG MTEPGHSRSA VYPLLYRDGE QTEPSRMGSK SPGNTSQPPA FFSKLTESNS 2290 2300 2310 2320 2330 2340 AMVKSKKQEI NKKLNTHNRN EPEYNISQPG TEIFNMPAIT GTGLMTYRSQ AVQEHASTNM 2350 2360 2370 2380 2390 2400 GLEAIIRKAL MGKYDQWEES PPLSANAFNP LNASASLPAA MPITAADGRS DHTLTSPGGG 2410 2420 2430 2440 2450 2460 GKAKVSGRPS SRKAKSPAPG LASGDRPPSV SSVHSEGDCN RRTPLTNRVW EDRPSSAGST 2470 2480 2490 2500 2510 PFPYNPLIMR LQAGVMASPP PPGLPAGSGP LAGPHHAWDE EPKPLLCSQY ETLSDSE
	Isoform 4 (SMRTe) [UniParc]. Checksum: 8738AABD508422AA	FASTA	2,508	273,141
	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 AEATVNNSSD TESIPSPHTE AAKDTGQNGP KPPATLGADG PPPGPPTPPP EDIPAPTEPT 790 800 810 820 830 840 PASEATGAPT PPPAPPSPSA PPPVVPKEEK EEETAAAPPV EEGEEQKPPA AEELAVDTGK 850 860 870 880 890 900 AEEPVKSECT EEAEEGPAKG KDAEAAEATA EGALKAEKKE GGSGRATTAK SSGAPQDSDS 910 920 930 940 950 960 SATCSADEVD EAEGGDKNRL LSPRPSLLTP TGDPRANASP QKPLDLKQLK QRAAAIPPIQ 970 980 990 1000 1010 1020 VTKVHEPPRE DAAPTKPAPP APPPPQNLQP ESDAPQQPGS SPRGKSRSPA PPADKEAEKP 1030 1040 1050 1060 1070 1080 VFFPAFAAEA QKLPGDPPCW TSGLPFPVPP REVIKASPHA PDPSAFSYAP PGHPLPLGLH 1090 1100 1110 1120 1130 1140 DTARPVLPRP PTISNPPPLI SSAKHPSVLE RQIGAISQGM SVQLHVPYSE HAKAPVGPVT 1150 1160 1170 1180 1190 1200 MGLPLPMDPK KLAPFSGVKQ EQLSPRGQAG PPESLGVPTA QEASVLRGTA LGSVPGGSIT 1210 1220 1230 1240 1250 1260 KGIPSTRVPS DSAITYRGSI THGTPADVLY KGTITRIIGE DSPSRLDRGR EDSLPKGHVI 1270 1280 1290 1300 1310 1320 YEGKKGHVLS YEGGMSVTQC SKEDGRSSSG PPHETAAPKR TYDMMEGRVG RAISSASIEG 1330 1340 1350 1360 1370 1380 LMGRAIPPER HSPHHLKEQH HIRGSITQGI PRSYVEAQED YLRREAKLLK REGTPPPPPP 1390 1400 1410 1420 1430 1440 SRDLTEAYKT QALGPLKLKP AHEGLVATVK EAGRSIHEIP REELRHTPEL PLAPRPLKEG 1450 1460 1470 1480 1490 1500 SITQGTPLKY DTGASTTGSK KHDVRSLIGS PGRTFPPVHP LDVMADARAL ERACYEESLK 1510 1520 1530 1540 1550 1560 SRPGTASSSG GSIARGAPVI VPELGKPRQS PLTYEDHGAP FAGHLPRGSP VTTREPTPRL 1570 1580 1590 1600 1610 1620 QEGSLSSSKA SQDRKLTSTP REIAKSPHST VPEHHPHPIS PYEHLLRGVS GVDLYRSHIP 1630 1640 1650 1660 1670 1680 LAFDPTSIPR GIPLDAAAAY YLPRHLAPNP TYPHLYPPYL IRGYPDTAAL ENRQTIINDY 1690 1700 1710 1720 1730 1740 ITSQQMHHNA ATAMAQRADM LRGLSPRESS LALNYAAGPR GIIDLSQVPH LPVLVPPTPG 1750 1760 1770 1780 1790 1800 TPATAMDRLA YLPTAPQPFS SRHSSSPLSP GGPTHLTKPT TTSSSERERD RDRERDRDRE 1810 1820 1830 1840 1850 1860 REKSILTSTT TVEHAPIWRP GTEQSSGSSG SSGGGGGSSS RPASHSHAHQ HSPISPRTQD 1870 1880 1890 1900 1910 1920 ALQQRPSVLH NTGMKGIITA VEPSTPTVLR STSTSSPVRP AATFPPATHC PLGGTLDGVY 1930 1940 1950 1960 1970 1980 PTLMEPVLLP KEAPRVARPE RPRADTGHAF LAKPPARSGL EPASSPSKGS EPRPLVPPVS 1990 2000 2010 2020 2030 2040 GHATIARTPA KNLAPHHASP DPPAPPASAS DPHREKTQSK PFSIQELELR SLGYHGSSYS 2050 2060 2070 2080 2090 2100 PEGVEPVSPV SSPSLTHDKG LPKHLEELDK SHLEGELRPK QPGPVKLGGE AAHLPHLRPL 2110 2120 2130 2140 2150 2160 PESQPSSSPL LQTAPGVKGH QRVVTLAQHI SEVITQDYTR HHPQQLSAPL PAPLYSFPGA 2170 2180 2190 2200 2210 2220 SCPVLDLRRP PSDLYLPPPD HGAPARGSPH SEGGKRSPEP NKTSVLGGGE DGIEPVSPPE 2230 2240 2250 2260 2270 2280 GMTEPGHSRS AVYPLLYRDG EQTEPSRMGS KSPGNTSQPP AFFSKLTESN SAMVKSKKQE 2290 2300 2310 2320 2330 2340 INKKLNTHNR NEPEYNISQP GTEIFNMPAI TGTGLMTYRS QAVQEHASTN MGLEAIIRKA 2350 2360 2370 2380 2390 2400 LMGKYDQWEE SPPLSANAFN PLNASASLPA AMPITAADGR SDHTLTSPGG GGKAKVSGRP 2410 2420 2430 2440 2450 2460 SSRKAKSPAP GLASGDRPPS VSSVHSEGDC NRRTPLTNRV WEDRPSSAGS TPFPYNPLIM 2470 2480 2490 2500 RLQAGVMASP PPPGLPAGSG PLAGPHHAWD EEPKPLLCSQ YETLSDSE
	Isoform 5 (SMRT-tau) [UniParc]. Checksum: 31DC105B162AFD57	FASTA	2,462	268,361
	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 AEATVNNSSD TESIPSPHTE AAKDTGQNGP KPPATLGADG PPPGPPTPPP EDIPAPTEPT 790 800 810 820 830 840 PASEATGAPT PPPAPPSPSA PPPVVPKEEK EEETAAAPPV EEGEEQKPPA AEELAVDTGK 850 860 870 880 890 900 AEEPVKSECT EEAEEGPAKG KDAEAAEATA EGALKAEKKE GGSGRATTAK SSGAPQDSDS 910 920 930 940 950 960 SATCSADEVD EAEGGDKNRL LSPRPSLLTP TGDPRANASP QKPLDLKQLK QRAAAIPPIQ 970 980 990 1000 1010 1020 VTKVHEPPRE DAAPTKPAPP APPPPQNLQP ESDAPQQPGS SPRGKSRSPA PPADKEAEKP 1030 1040 1050 1060 1070 1080 VFFPAFAAEA QKLPGDPPCW TSGLPFPVPP REVIKASPHA PDPSAFSYAP PGHPLPLGLH 1090 1100 1110 1120 1130 1140 DTARPVLPRP PTISNPPPLI SSAKHPSVLE RQIGAISQGM SVQLHVPYSE HAKAPVGPVT 1150 1160 1170 1180 1190 1200 MGLPLPMDPK KLAPFSGVKQ EQLSPRGQAG PPESLGVPTA QEASVLRGTA LGSVPGGSIT 1210 1220 1230 1240 1250 1260 KGIPSTRVPS DSAITYRGSI THGTPADVLY KGTITRIIGE DSPSRLDRGR EDSLPKGHVI 1270 1280 1290 1300 1310 1320 YEGKKGHVLS YEGGMSVTQC SKEDGRSSSG PPHETAAPKR TYDMMEGRVG RAISSASIEG 1330 1340 1350 1360 1370 1380 LMGRAIPPER HSPHHLKEQH HIRGSITQGI PRSYVEAQED YLRREAKLLK REGTPPPPPP 1390 1400 1410 1420 1430 1440 SRDLTEAYKT QALGPLKLKP AHEGLVATVK EAGRSIHEIP REELRHTPEL PLAPRPLKEG 1450 1460 1470 1480 1490 1500 SITQGTPLKY DTGASTTGSK KHDVRSLIGS PGRTFPPVHP LDVMADARAL ERACYEESLK 1510 1520 1530 1540 1550 1560 SRPGTASSSG GSIARGAPVI VPELGKPRQS PLTYEDHGAP FAGHLPRGSP VTTREPTPRL 1570 1580 1590 1600 1610 1620 QEGSLSSSKA SQDRKLTSTP REIAKSPHST VPEHHPHPIS PYEHLLRGVS GVDLYRSHIP 1630 1640 1650 1660 1670 1680 LAFDPTSIPR GIPLDAAAAY YLPRHLAPNP TYPHLYPPYL IRGYPDTAAL ENRQTIINDY 1690 1700 1710 1720 1730 1740 ITSQQMHHNA ATAMAQRADM LRGLSPRESS LALNYAAGPR GIIDLSQVPH LPVLVPPTPG 1750 1760 1770 1780 1790 1800 TPATAMDRLA YLPTAPQPFS SRHSSSPLSP GGPTHLTKPT TTSSSERERD RDRERDRDRE 1810 1820 1830 1840 1850 1860 REKSILTSTT TVEHAPIWRP GTEQSSGSSG SSGGGGGSSS RPASHSHAHQ HSPISPRTQD 1870 1880 1890 1900 1910 1920 ALQQRPSVLH NTGMKGIITA VEPSTPTVLR STSTSSPVRP AATFPPATHC PLGGTLDGVY 1930 1940 1950 1960 1970 1980 PTLMEPVLLP KEAPRVARPE RPRADTGHAF LAKPPARSGL EPASSPSKGS EPRPLVPPVS 1990 2000 2010 2020 2030 2040 GHATIARTPA KNLAPHHASP DPPAPPASAS DPHREKTQSK PFSIQELELR SLGYHGSSYS 2050 2060 2070 2080 2090 2100 PEGVEPVSPV SSPSLTHDKG LPKHLEELDK SHLEGELRPK QPGPVKLGGE AAHLPHLRPL 2110 2120 2130 2140 2150 2160 PESQPSSSPL LQTAPGVKGH QRVVTLAQHI SEVITQDYTR HHPQQLSAPL PAPLYSFPGA 2170 2180 2190 2200 2210 2220 SCPVLDLRRP PSDLYLPPPD HGAPARGSPH SEGGKRSPEP NKTSVLGGGE DGIEPVSPPE 2230 2240 2250 2260 2270 2280 GMTEPGHSRS AVYPLLYRDG EQTEPSRMGS KSPGNTSQPP AFFSKLTESN SAMVKSKKQE 2290 2300 2310 2320 2330 2340 INKKLNTHNR NEPEYNISQP GTEIFNMPAI TGTGLMTYRS QAVQEHASTN MGLEAIIRKA 2350 2360 2370 2380 2390 2400 LMGGGGKAKV SGRPSSRKAK SPAPGLASGD RPPSVSSVHS EGDCNRRTPL TNRVWEDRPS 2410 2420 2430 2440 2450 2460 SAGSTPFPYN PLIMRLQAGV MASPPPPGLP AGSGPLAGPH HAWDEEPKPL LCSQYETLSD SE

References

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[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.
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[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]	"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.
[17]	"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).
[18]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[22]	"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, MASS SPECTROMETRY.
[23]	"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.
[24]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"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].
[26]	"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, MASS SPECTROMETRY.
[27]	"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.

IPI

IPI00001735.
IPI00878336.
IPI00923436.
IPI00923531.
IPI00923596.

PIR

S60255.

RefSeq

NP_001070729.2. NM_001077261.3.
NP_001193583.1. NM_001206654.1.
NP_006303.4. NM_006312.5.

UniGene

Hs.137510.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
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	[»]

ProteinModelPortal

Q9Y618.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-951N.

IntAct

Q9Y618. 25 interactions.

MINT

MINT-129997.

STRING

9606.ENSP00000348551.

PTM databases

PhosphoSite

Q9Y618.

Polymorphism databases

DMDM

226713806.

Proteomic databases

PaxDb

Q9Y618.

PRIDE

Q9Y618.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356219; ENSP00000348551; ENSG00000196498.

GeneID

9612.

KEGG

hsa:9612.

UCSC

uc001ugj.1. human.
uc010tax.2. human.

Organism-specific databases

CTD

9612.

GeneCards

GC12M124808.

H-InvDB

HIX0026341.

HGNC

HGNC:7673. NCOR2.

HPA

HPA001928.

MIM

600848. gene.

neXtProt

NX_Q9Y618.

PharmGKB

PA31478.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOVERGEN

HBG052587.

KO

K06065.

Enzyme and pathway databases

Pathway_Interaction_DB

retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.
rxr_vdr_pathway. RXR and RAR hetrodimerization with other nuclear receptor.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q9Y618.

Bgee

Q9Y618.

CleanEx

HS_NCOR2.

Genevestigator

Q9Y618.

GermOnline

ENSG00000196498. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.60. 1 hit.

InterPro

IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]

Pfam

PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]

SMART

SM00717. SANT. 2 hits.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 2 hits.

PROSITE

PS51293. SANT. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9Y618.

ChEMBL

CHEMBL5949.

ChiTaRS

NCOR2. human.

EvolutionaryTrace

Q9Y618.

GenomeRNAi

9612.

NextBio

36061.

SOURCE

Search...

Entry information

Entry name

NCOR2_HUMAN

Accession

Primary (citable) accession number: Q9Y618
Secondary accession number(s): O00613 , O15416, O15421, Q13354, Q56D06, Q59GM0, Q9Y5U0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	March 24, 2009
Last modified:	May 1, 2013
This is version 148 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.