Reviewed, UniProtKB/Swiss-Prot Q9Y618 (NCOR2_HUMAN)

Names and origin

Protein names

Recommended name:
    Nuclear receptor corepressor 2
      Short name=N-CoR2
Alternative name(s):
    Silencing mediator of retinoic acid and thyroid hormone receptor
      Short name=SMRT
    Thyroid-, retinoic-acid-receptor-associated corepressor
    T3 receptor-associating factor
      Short name=TRAC
    CTG repeat protein 26
    SMAP270

Gene names

Name:	NCOR2
Synonyms:	CTG26

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

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

General annotation (Comments)

Function	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 HDAC7 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. Isoform SRMT interacts 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. Interacts with C1D By similarity. Interacts with ATXN1L. Interacts with BCL6; the interaction is direct. Ref.11 Ref.12 Ref.14 Ref.16
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: Miscellaneous discrepancy. 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.

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
Gene Ontology (GO)
Biological process	negative regulation of gene-specific transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nuclear body Inferred from direct assay. Source: MGI transcriptional repressor complex Inferred from direct assay. Source: UniProtKB
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW Notch binding Inferred from physical interaction. Source: UniProtKB protein N-terminus binding Inferred from physical interaction. Source: UniProtKB transcription corepressor activity Inferred from mutant phenotype. Source: UniProtKB transcription repressor binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AHR	P35869	1	EBI-80830,EBI-80780
ARNT	P27540	1	EBI-80830,EBI-80809
HDAC1	Q13547	1	EBI-80830,EBI-301834
HDAC10	Q969S8	1	EBI-80830,EBI-301762
PGR	P06401	1	EBI-80830,EBI-78539
THRA	P04625	1	EBI-80830,EBI-286261	From a different organism.

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

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.20

Modified residue

67

1

Phosphoserine Ref.23

Modified residue

149

1

Phosphoserine Ref.23 Ref.18 Ref.21

Modified residue

152

1

Phosphoserine Ref.23 Ref.18 Ref.21

Modified residue

156

1

Phosphothreonine Ref.21

Modified residue

215

1

Phosphoserine Ref.18

Modified residue

553

1

Phosphothreonine Ref.23

Modified residue

554

1

Phosphoserine Ref.23

Modified residue

745

1

Phosphoserine Ref.21

Modified residue

746

1

Phosphoserine Ref.21

Modified residue

750

1

Phosphoserine Ref.21

Modified residue

753

1

Phosphoserine Ref.21

Modified residue

864

1

Phosphoserine By similarity

Modified residue

878

1

N6-acetyllysine Ref.24

Modified residue

939

1

Phosphoserine Ref.23

Modified residue

956

1

Phosphoserine Ref.21 Ref.19

Modified residue

959

1

N6-acetyllysine Ref.24

Modified residue

1218

1

N6-acetyllysine Ref.24

Modified residue

1248

1

N6-acetyllysine Ref.24

Modified residue

1259

1

Phosphoserine Ref.21

Modified residue

1261

1

Phosphoserine Ref.18

Modified residue

1331

1

Phosphoserine Ref.23

Modified residue

1391

1

Phosphothreonine Ref.18 Ref.21 Ref.22

Modified residue

1444

1

Phosphothreonine By similarity

Modified residue

1487

1

Phosphoserine Ref.21

Modified residue

1584

1

Phosphoserine Ref.18

Modified residue

1786

1

Phosphoserine By similarity

Modified residue

1795

1

N6-acetyllysine Ref.24

Modified residue

1970

1

N6-acetyllysine Ref.24

Modified residue

1982

1

Phosphoserine Ref.15

Modified residue

2016

1

Phosphoserine Ref.18

Modified residue

2037

1

N6-acetyllysine Ref.24

Modified residue

2051

1

Phosphotyrosine Ref.21

Modified residue

2057

1

Phosphoserine Ref.23 Ref.18 Ref.21

Modified residue

2065

1

Phosphoserine Ref.23 Ref.21

Modified residue

2068

1

Phosphoserine Ref.23

Modified residue

2069

1

Phosphoserine Ref.23 Ref.18

Modified residue

2071

1

Phosphoserine Ref.21

Modified residue

2073

1

Phosphothreonine Ref.21

Modified residue

2205

1

Phosphoserine Ref.18

Modified residue

2208

1

Phosphoserine Ref.18

Modified residue

2234

1

Phosphoserine Ref.23 Ref.21

Modified residue

2269

1

Phosphoserine Ref.23 Ref.18 Ref.21 Ref.15

Modified residue

2463

1

Phosphoserine By similarity

Modified residue

2522

1

Phosphoserine Ref.18

Modified residue

2524

1

Phosphoserine Ref.18

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: dbSNP rs7978237. Ref.6

VAR_060073

Natural variant

1707

1

A → T: dbSNP rs2229840. Ref.2 Ref.3 Ref.4 Ref.8

VAR_054751

Natural variant

2012

1

P → S: dbSNP rs2230944.

VAR_060074

Experimental info

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

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2525

Helix Strand Turn

Details...

Turn

421 – 424

4

Turn

426 – 430

5

Turn

434 – 436

3

Helix

437 – 446

10

Beta strand

451 – 453

3

Helix

454 – 457

4

Turn

458 – 460

3

Helix

463 – 473

11

Turn

474 – 476

3

Beta strand

1424 – 1428

5

Helix

2351 – 2356

6

Beta strand

2357 – 2360

4

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). 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). 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). 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). 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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[8]	"A transcriptional co-repressor that interacts with nuclear hormone receptors." Chen J.D., Evans R.M. Nature 377:454-457(1995) [PubMed: 7566127] [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: 10809664] [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: 10944117] [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: 11331609] [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: 11533236] [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: 11931768] [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: 11739383] [Abstract] Cited for: INTERACTION WITH HDAC10.
[15]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1982 AND SER-2269, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 16121196] [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: 15632172] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-152; SER-215; SER-1261; THR-1391; SER-1584; SER-2016; SER-2057; SER-2054; SER-2069; SER-2205; SER-2208; SER-2269; SER-2522 AND SER-2524, MASS SPECTROMETRY. Tissue: Epithelium.
[19]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-956, MASS SPECTROMETRY.
[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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, MASS SPECTROMETRY.
[21]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-152; THR-156; SER-745; SER-746; SER-750; SER-753; SER-956; SER-1259; THR-1391; SER-1487; TYR-2051; SER-2057; SER-2065; SER-2071; THR-2073; SER-2234 AND SER-2269, MASS SPECTROMETRY.
[22]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1391, MASS SPECTROMETRY.
[23]	"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: 19690332] [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: T-cell.
[24]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-878; LYS-959; LYS-1218; LYS-1248; LYS-1795; LYS-1970 AND LYS-2037, MASS SPECTROMETRY.
[25]	"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: 14690607] [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_001070729.1.
NP_006303.3.

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	[»]
2ODD	NMR	-	B	1109-1121	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-951N.

IntAct

Q9Y618. 12 interactions.

STRING

Q9Y618.

PTM databases

PhosphoSite

Q9Y618.

Proteomic databases

PRIDE

Q9Y618.

Genome annotation databases

Ensembl

ENST00000356219; ENSP00000348551; ENSG00000196498; Homo sapiens. [Genome view]

GeneID

9612.

KEGG

hsa:9612.

Organism-specific databases

CTD

9612.

GeneCards

GC12M123333.

H-InvDB

HIX0026341.

HGNC

HGNC:7673. NCOR2.

HPA

HPA001928.

MIM

600848. gene.

PharmGKB

PA31478.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG21482.

HOVERGEN

Q9Y618.

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_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

Q9Y618.

Bgee

Q9Y618.

CleanEx

HS_NCOR2.

Genevestigator

Q9Y618.

GermOnline

ENSG00000196498. Homo sapiens.

Family and domain databases

InterPro

IPR009057. Homeodomain-like.
IPR012287. Homeodomain-rel.
IPR014778. Myb_DNA-bd.
IPR001005. SANT_DNA-bd.
IPR017884. SANT_eukarya.
[Graphical view]

Gene3D

G3DSA:1.10.10.60. Homeodomain-rel. 1 hit.

Pfam

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

SMART

SM00717. SANT. 2 hits.
[Graphical view]

PROSITE

PS51293. SANT. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

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:	February 9, 2010
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.