Q9Y6Q9 (NCOA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear receptor coactivator 3
Short name=NCoA-3
EC=2.3.1.48

Alternative name(s):
ACTR
Amplified in breast cancer 1 protein
Short name=AIB-1
CBP-interacting protein
Short name=pCIP
Class E basic helix-loop-helix protein 42
Short name=bHLHe42
Receptor-associated coactivator 3
Short name=RAC-3
Steroid receptor coactivator protein 3
Short name=SRC-3
Thyroid hormone receptor activator molecule 1
Short name=TRAM-1

Gene names

Name:	NCOA3
Synonyms:	AIB1, BHLHE42, RAC3, TRAM1

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	1424 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit. Interacts with PSMB9.
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.2
Enzyme regulation	Coactivator activity on nuclear receptors and NF-kappa-B pathways is enhanced by various hormones, and the TNF cytokine, respectively. TNF stimulation probably enhances phosphorylation, which in turn activates coactivator function. In contrast, acetylation by CREBBP apparently suppresses coactivation of target genes by disrupting its association with nuclear receptors. Binds to CSNK1D.
Subunit structure	Interacts with CARM1 By similarity. Present in a complex containing NCOA2, IKKA, IKKB, IKBKG and the histone acetyltransferase protein CREBBP. Interacts with CASP8AP2, NR3C1 and PCAF. Interacts with ATAD2 and this interaction is enhanced by estradiol. Found in a complex containing NCOA3, AR and MAK. Interacts with DDX5. Ref.1 Ref.3 Ref.4 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21
Subcellular location	Cytoplasm. Nucleus. Note: Mainly cytoplasmic and weakly nuclear. Upon TNF activation and subsequent phosphorylation, it translocates from the cytoplasm to the nucleus.
Tissue specificity	Widely expressed. High expression in heart, skeletal muscle, pancreas and placenta. Low expression in brain, and very low in lung, liver and kidney.
Domain	Contains three Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Motifs 1 and 2 are essential for the association with nuclear receptors, and constitute the RID domain (Receptor-interacting domain).
Post-translational modification	Acetylated by CREBBP. Acetylation occurs in the RID domain, and disrupts the interaction with nuclear receptors and regulates its function. Methylated by CARM1 By similarity. Phosphorylated by IKK complex. Regulated its function. Phosphorylation at Ser-601 by CK1 promotes coactivator function. Ref.13 Ref.21
Polymorphism	The length of the poly-Gln region is polymorphic in the normal population.
Miscellaneous	NCOA3 is frequently amplified or overexpressed in breast and ovarian cancers.
Sequence similarities	Belongs to the SRC/p160 nuclear receptor coactivator family. Contains 1 bHLH (basic helix-loop-helix) domain. Contains 1 PAS (PER-ARNT-SIM) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Molecular function	Activator Acyltransferase Transferase
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	androgen receptor signaling pathway Non-traceable author statement PubMed 15572661. Source: UniProtKB cellular lipid metabolic process Traceable author statement. Source: Reactome developmental growth Inferred from electronic annotation. Source: Compara mammary gland branching involved in thelarche Inferred from electronic annotation. Source: Compara multicellular organism growth Inferred from electronic annotation. Source: Compara positive regulation of keratinocyte differentiation Inferred from mutant phenotype PubMed 17082781PubMed 17223341. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.2. Source: UniProtKB receptor transactivation Traceable author statement PubMed 17223341. Source: UniProtKB small molecule metabolic process Traceable author statement. Source: Reactome transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW vagina development Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay PubMed 17223341. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	androgen receptor binding Non-traceable author statement PubMed 15572661. Source: UniProtKB chromatin binding Inferred from electronic annotation. Source: Compara histone acetyltransferase activity Inferred from direct assay Ref.2. Source: UniProtKB signal transducer activity Inferred from electronic annotation. Source: InterPro thyroid hormone receptor binding Non-traceable author statement Ref.1. Source: UniProtKB transcription coactivator activity Inferred from direct assay Ref.4Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DDX17	Q92841	2	EBI-81196,EBI-746012
ESR1	P03372	2	EBI-81196,EBI-78473
IKBKB	O14920	3	EBI-81196,EBI-81266
PSME3	P61289	5	EBI-81196,EBI-355546
SPOP	O43791	6	EBI-81196,EBI-743549
Vdr	P48281	2	EBI-81196,EBI-346797	From a different organism.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9Y6Q9-1)

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: Q9Y6Q9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     903-917: Missing.

Isoform 3 (identifier: Q9Y6Q9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     321-321: E → EVTSDGIFSPT
     903-917: Missing.
     1214-1217: Missing.

Isoform 4 (identifier: Q9Y6Q9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     321-321: E → EVTSDGIFSPT
     837-901: Missing.
     903-917: Missing.
     1214-1217: Missing.

Isoform 5 (identifier: Q9Y6Q9-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1214-1217: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1424

1424

Nuclear receptor coactivator 3

PRO_0000094406

Regions

Domain

25 – 82

58

bHLH

Domain

110 – 180

71

PAS

Region

1023 – 1093

71

Interaction with CREBBP

Region

1097 – 1304

208

Acetyltransferase

Motif

685 – 689

5

LXXLL motif 1

Motif

738 – 742

5

LXXLL motif 2

Motif

1057 – 1061

5

LXXLL motif 3

Compositional bias

505 – 671

167

Ser-rich

Compositional bias

976 – 980

5

Poly-Gln

Compositional bias

1248 – 1278

31

Poly-Gln

Compositional bias

1392 – 1417

26

Met-rich

Amino acid modifications

Modified residue

214

1

Phosphoserine Ref.20 Ref.24

Modified residue

551

1

Phosphoserine Ref.20

Modified residue

601

1

Phosphoserine; by CK1 Ref.21

Modified residue

616

1

N6-acetyllysine; by CREBBP

Modified residue

619

1

N6-acetyllysine; by CREBBP

Modified residue

620

1

N6-acetyllysine; by CREBBP

Modified residue

687

1

N6-acetyllysine Ref.23

Modified residue

728

1

Phosphoserine Ref.20

Modified residue

857

1

Phosphoserine Ref.18 Ref.20 Ref.22 Ref.24

Modified residue

867

1

Phosphoserine Ref.18 Ref.24

Modified residue

1042

1

Phosphoserine By similarity

Natural variations

Alternative sequence

321

1

E → EVTSDGIFSPT in isoform 3 and isoform 4.

VSP_003405

Alternative sequence

837 – 901

65

Missing in isoform 4.

VSP_003406

Alternative sequence

903 – 917

15

Missing in isoform 2, isoform 3 and isoform 4.

VSP_003407

Alternative sequence

1214 – 1217

4

Missing in isoform 3, isoform 4 and isoform 5.

VSP_003408

Natural variant

218

1

R → C. Ref.5
Corresponds to variant rs6094752 [ dbSNP | Ensembl ].

VAR_053527

Natural variant

220

1

R → I. Ref.5

VAR_060695

Natural variant

369

1

L → F.
Corresponds to variant rs6094756 [ dbSNP | Ensembl ].

VAR_053528

Natural variant

460

1

G → R.
Corresponds to variant rs1052765 [ dbSNP | Ensembl ].

VAR_013831

Natural variant

556

1

I → V. Ref.5

VAR_060696

Natural variant

559

1

P → S. Ref.5
Corresponds to variant rs2230781 [ dbSNP | Ensembl ].

VAR_013832

Natural variant

586

1

Q → H. Ref.5
Corresponds to variant rs2230782 [ dbSNP | Ensembl ].

VAR_013833

Natural variant

777

1

S → A. Ref.5
Corresponds to variant rs2230783 [ dbSNP | Ensembl ].

VAR_053529

Natural variant

1247

1

M → K. Ref.5

VAR_060697

Natural variant

1247

1

M → L. Ref.5

VAR_060698

Natural variant

1248 – 1250

3

Missing.

VAR_013834

Experimental info

Mutagenesis

616

1

K → Q: Strongly reduces acetylation by CREBBP. Ref.10

Mutagenesis

619 – 620

2

KK → QQ: Abolishes acetylation by CREBBP.

Mutagenesis

647

1

K → Q: Does not affect acetylation by CREBBP. Ref.10

Mutagenesis

681

1

K → Q: Does not affect acetylation by CREBBP. Ref.10

Mutagenesis

687

1

K → Q: Does not affect acetylation by CREBBP. Ref.10

Mutagenesis

700

1

K → Q: Does not affect acetylation by CREBBP. Ref.10

Mutagenesis

708

1

K → Q: Does not affect acetylation by CREBBP. Ref.10

Sequence conflict

131 – 132

2

DG → EA in AAC51663. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

1424

Helix Strand Turn

Details...

Helix

619 – 626

8

Helix

736 – 743

8

Helix

1049 – 1060

12

Helix

1069 – 1075

7

Helix

1078 – 1084

7

Helix

1086 – 1088

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 732CDF0423161679	FASTA	1,424	155,293
	10 20 30 40 50 60 MSGLGENLDP LASDSRKRKL PCDTPGQGLT CSGEKRRREQ ESKYIEELAE LISANLSDID 70 80 90 100 110 120 NFNVKPDKCA ILKETVRQIR QIKEQGKTIS NDDDVQKADV SSTGQGVIDK DSLGPLLLQA 130 140 150 160 170 180 LDGFLFVVNR DGNIVFVSEN VTQYLQYKQE DLVNTSVYNI LHEEDRKDFL KNLPKSTVNG 190 200 210 220 230 240 VSWTNETQRQ KSHTFNCRML MKTPHDILED INASPEMRQR YETMQCFALS QPRAMMEEGE 250 260 270 280 290 300 DLQSCMICVA RRITTGERTF PSNPESFITR HDLSGKVVNI DTNSLRSSMR PGFEDIIRRC 310 320 330 340 350 360 IQRFFSLNDG QSWSQKRHYQ EAYLNGHAET PVYRFSLADG TIVTAQTKSK LFRNPVTNDR 370 380 390 400 410 420 HGFVSTHFLQ REQNGYRPNP NPVGQGIRPP MAGCNSSVGG MSMSPNQGLQ MPSSRAYGLA 430 440 450 460 470 480 DPSTTGQMSG ARYGGSSNIA SLTPGPGMQS PSSYQNNNYG LNMSSPPHGS PGLAPNQQNI 490 500 510 520 530 540 MISPRNRGSP KIASHQFSPV AGVHSPMASS GNTGNHSFSS SSLSALQAIS EGVGTSLLST 550 560 570 580 590 600 LSSPGPKLDN SPNMNITQPS KVSNQDSKSP LGFYCDQNPV ESSMCQSNSR DHLSDKESKE 610 620 630 640 650 660 SSVEGAENQR GPLESKGHKK LLQLLTCSSD DRGHSSLTNS PLDSSCKESS VSVTSPSGVS 670 680 690 700 710 720 SSTSGGVSST SNMHGSLLQE KHRILHKLLQ NGNSPAEVAK ITAEATGKDT SSITSCGDGN 730 740 750 760 770 780 VVKQEQLSPK KKENNALLRY LLDRDDPSDA LSKELQPQVE GVDNKMSQCT SSTIPSSSQE 790 800 810 820 830 840 KDPKIKTETS EEGSGDLDNL DAILGDLTSS DFYNNSISSN GSHLGTKQQV FQGTNSLGLK 850 860 870 880 890 900 SSQSVQSIRP PYNRAVSLDS PVSVGSSPPV KNISAFPMLP KQPMLGGNPR MMDSQENYGS 910 920 930 940 950 960 SMGGPNRNVT VTQTPSSGDW GLPNSKAGRM EPMNSNSMGR PGGDYNTSLP RPALGGSIPT 970 980 990 1000 1010 1020 LPLRSNSIPG ARPVLQQQQQ MLQMRPGEIP MGMGANPYGQ AAASNQLGSW PDGMLSMEQV 1030 1040 1050 1060 1070 1080 SHGTQNRPLL RNSLDDLVGP PSNLEGQSDE RALLDQLHTL LSNTDATGLE EIDRALGIPE 1090 1100 1110 1120 1130 1140 LVNQGQALEP KQDAFQGQEA AVMMDQKAGL YGQTYPAQGP PMQGGFHLQG QSPSFNSMMN 1150 1160 1170 1180 1190 1200 QMNQQGNFPL QGMHPRANIM RPRTNTPKQL RMQLQQRLQG QQFLNQSRQA LELKMENPTA 1210 1220 1230 1240 1250 1260 GGAAVMRPMM QPQVSSQQGF LNAQMVAQRS RELLSHHFRQ QRVAMMMQQQ QQQQQQQQQQ 1270 1280 1290 1300 1310 1320 QQQQQQQQQQ QQQQQQTQAF SPPPNVTASP SMDGLLAGPT MPQAPPQQFP YQPNYGMGQQ 1330 1340 1350 1360 1370 1380 PDPAFGRVSS PPNAMMSSRM GPSQNPMMQH PQAASIYQSS EMKGWPSGNL ARNSSFSQQQ 1390 1400 1410 1420 FAHQGNPAVY SMVHMNGSSG HMGQMNMNPM PMSGMPMGPD QKYC
	Isoform 2 [UniParc]. Checksum: 04B4DF09150BD916	FASTA	1,409	153,797
	10 20 30 40 50 60 MSGLGENLDP LASDSRKRKL PCDTPGQGLT CSGEKRRREQ ESKYIEELAE LISANLSDID 70 80 90 100 110 120 NFNVKPDKCA ILKETVRQIR QIKEQGKTIS NDDDVQKADV SSTGQGVIDK DSLGPLLLQA 130 140 150 160 170 180 LDGFLFVVNR DGNIVFVSEN VTQYLQYKQE DLVNTSVYNI LHEEDRKDFL KNLPKSTVNG 190 200 210 220 230 240 VSWTNETQRQ KSHTFNCRML MKTPHDILED INASPEMRQR YETMQCFALS QPRAMMEEGE 250 260 270 280 290 300 DLQSCMICVA RRITTGERTF PSNPESFITR HDLSGKVVNI DTNSLRSSMR PGFEDIIRRC 310 320 330 340 350 360 IQRFFSLNDG QSWSQKRHYQ EAYLNGHAET PVYRFSLADG TIVTAQTKSK LFRNPVTNDR 370 380 390 400 410 420 HGFVSTHFLQ REQNGYRPNP NPVGQGIRPP MAGCNSSVGG MSMSPNQGLQ MPSSRAYGLA 430 440 450 460 470 480 DPSTTGQMSG ARYGGSSNIA SLTPGPGMQS PSSYQNNNYG LNMSSPPHGS PGLAPNQQNI 490 500 510 520 530 540 MISPRNRGSP KIASHQFSPV AGVHSPMASS GNTGNHSFSS SSLSALQAIS EGVGTSLLST 550 560 570 580 590 600 LSSPGPKLDN SPNMNITQPS KVSNQDSKSP LGFYCDQNPV ESSMCQSNSR DHLSDKESKE 610 620 630 640 650 660 SSVEGAENQR GPLESKGHKK LLQLLTCSSD DRGHSSLTNS PLDSSCKESS VSVTSPSGVS 670 680 690 700 710 720 SSTSGGVSST SNMHGSLLQE KHRILHKLLQ NGNSPAEVAK ITAEATGKDT SSITSCGDGN 730 740 750 760 770 780 VVKQEQLSPK KKENNALLRY LLDRDDPSDA LSKELQPQVE GVDNKMSQCT SSTIPSSSQE 790 800 810 820 830 840 KDPKIKTETS EEGSGDLDNL DAILGDLTSS DFYNNSISSN GSHLGTKQQV FQGTNSLGLK 850 860 870 880 890 900 SSQSVQSIRP PYNRAVSLDS PVSVGSSPPV KNISAFPMLP KQPMLGGNPR MMDSQENYGS 910 920 930 940 950 960 SMGDWGLPNS KAGRMEPMNS NSMGRPGGDY NTSLPRPALG GSIPTLPLRS NSIPGARPVL 970 980 990 1000 1010 1020 QQQQQMLQMR PGEIPMGMGA NPYGQAAASN QLGSWPDGML SMEQVSHGTQ NRPLLRNSLD 1030 1040 1050 1060 1070 1080 DLVGPPSNLE GQSDERALLD QLHTLLSNTD ATGLEEIDRA LGIPELVNQG QALEPKQDAF 1090 1100 1110 1120 1130 1140 QGQEAAVMMD QKAGLYGQTY PAQGPPMQGG FHLQGQSPSF NSMMNQMNQQ GNFPLQGMHP 1150 1160 1170 1180 1190 1200 RANIMRPRTN TPKQLRMQLQ QRLQGQQFLN QSRQALELKM ENPTAGGAAV MRPMMQPQVS 1210 1220 1230 1240 1250 1260 SQQGFLNAQM VAQRSRELLS HHFRQQRVAM MMQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ 1270 1280 1290 1300 1310 1320 QTQAFSPPPN VTASPSMDGL LAGPTMPQAP PQQFPYQPNY GMGQQPDPAF GRVSSPPNAM 1330 1340 1350 1360 1370 1380 MSSRMGPSQN PMMQHPQAAS IYQSSEMKGW PSGNLARNSS FSQQQFAHQG NPAVYSMVHM 1390 1400 NGSSGHMGQM NMNPMPMSGM PMGPDQKYC
	Isoform 3 [UniParc]. Checksum: 4A162AB05BA34062	FASTA	1,415	154,400
	10 20 30 40 50 60 MSGLGENLDP LASDSRKRKL PCDTPGQGLT CSGEKRRREQ ESKYIEELAE LISANLSDID 70 80 90 100 110 120 NFNVKPDKCA ILKETVRQIR QIKEQGKTIS NDDDVQKADV SSTGQGVIDK DSLGPLLLQA 130 140 150 160 170 180 LDGFLFVVNR DGNIVFVSEN VTQYLQYKQE DLVNTSVYNI LHEEDRKDFL KNLPKSTVNG 190 200 210 220 230 240 VSWTNETQRQ KSHTFNCRML MKTPHDILED INASPEMRQR YETMQCFALS QPRAMMEEGE 250 260 270 280 290 300 DLQSCMICVA RRITTGERTF PSNPESFITR HDLSGKVVNI DTNSLRSSMR PGFEDIIRRC 310 320 330 340 350 360 IQRFFSLNDG QSWSQKRHYQ EVTSDGIFSP TAYLNGHAET PVYRFSLADG TIVTAQTKSK 370 380 390 400 410 420 LFRNPVTNDR HGFVSTHFLQ REQNGYRPNP NPVGQGIRPP MAGCNSSVGG MSMSPNQGLQ 430 440 450 460 470 480 MPSSRAYGLA DPSTTGQMSG ARYGGSSNIA SLTPGPGMQS PSSYQNNNYG LNMSSPPHGS 490 500 510 520 530 540 PGLAPNQQNI MISPRNRGSP KIASHQFSPV AGVHSPMASS GNTGNHSFSS SSLSALQAIS 550 560 570 580 590 600 EGVGTSLLST LSSPGPKLDN SPNMNITQPS KVSNQDSKSP LGFYCDQNPV ESSMCQSNSR 610 620 630 640 650 660 DHLSDKESKE SSVEGAENQR GPLESKGHKK LLQLLTCSSD DRGHSSLTNS PLDSSCKESS 670 680 690 700 710 720 VSVTSPSGVS SSTSGGVSST SNMHGSLLQE KHRILHKLLQ NGNSPAEVAK ITAEATGKDT 730 740 750 760 770 780 SSITSCGDGN VVKQEQLSPK KKENNALLRY LLDRDDPSDA LSKELQPQVE GVDNKMSQCT 790 800 810 820 830 840 SSTIPSSSQE KDPKIKTETS EEGSGDLDNL DAILGDLTSS DFYNNSISSN GSHLGTKQQV 850 860 870 880 890 900 FQGTNSLGLK SSQSVQSIRP PYNRAVSLDS PVSVGSSPPV KNISAFPMLP KQPMLGGNPR 910 920 930 940 950 960 MMDSQENYGS SMGDWGLPNS KAGRMEPMNS NSMGRPGGDY NTSLPRPALG GSIPTLPLRS 970 980 990 1000 1010 1020 NSIPGARPVL QQQQQMLQMR PGEIPMGMGA NPYGQAAASN QLGSWPDGML SMEQVSHGTQ 1030 1040 1050 1060 1070 1080 NRPLLRNSLD DLVGPPSNLE GQSDERALLD QLHTLLSNTD ATGLEEIDRA LGIPELVNQG 1090 1100 1110 1120 1130 1140 QALEPKQDAF QGQEAAVMMD QKAGLYGQTY PAQGPPMQGG FHLQGQSPSF NSMMNQMNQQ 1150 1160 1170 1180 1190 1200 GNFPLQGMHP RANIMRPRTN TPKQLRMQLQ QRLQGQQFLN QSRQALELKM ENPTAGGAAV 1210 1220 1230 1240 1250 1260 MRPMMQPQQG FLNAQMVAQR SRELLSHHFR QQRVAMMMQQ QQQQQQQQQQ QQQQQQQQQQ 1270 1280 1290 1300 1310 1320 QQQQQQQTQA FSPPPNVTAS PSMDGLLAGP TMPQAPPQQF PYQPNYGMGQ QPDPAFGRVS 1330 1340 1350 1360 1370 1380 SPPNAMMSSR MGPSQNPMMQ HPQAASIYQS SEMKGWPSGN LARNSSFSQQ QFAHQGNPAV 1390 1400 1410 YSMVHMNGSS GHMGQMNMNP MPMSGMPMGP DQKYC
	Isoform 4 [UniParc]. Checksum: F75584B329A892C4	FASTA	1,350	147,499
	10 20 30 40 50 60 MSGLGENLDP LASDSRKRKL PCDTPGQGLT CSGEKRRREQ ESKYIEELAE LISANLSDID 70 80 90 100 110 120 NFNVKPDKCA ILKETVRQIR QIKEQGKTIS NDDDVQKADV SSTGQGVIDK DSLGPLLLQA 130 140 150 160 170 180 LDGFLFVVNR DGNIVFVSEN VTQYLQYKQE DLVNTSVYNI LHEEDRKDFL KNLPKSTVNG 190 200 210 220 230 240 VSWTNETQRQ KSHTFNCRML MKTPHDILED INASPEMRQR YETMQCFALS QPRAMMEEGE 250 260 270 280 290 300 DLQSCMICVA RRITTGERTF PSNPESFITR HDLSGKVVNI DTNSLRSSMR PGFEDIIRRC 310 320 330 340 350 360 IQRFFSLNDG QSWSQKRHYQ EVTSDGIFSP TAYLNGHAET PVYRFSLADG TIVTAQTKSK 370 380 390 400 410 420 LFRNPVTNDR HGFVSTHFLQ REQNGYRPNP NPVGQGIRPP MAGCNSSVGG MSMSPNQGLQ 430 440 450 460 470 480 MPSSRAYGLA DPSTTGQMSG ARYGGSSNIA SLTPGPGMQS PSSYQNNNYG LNMSSPPHGS 490 500 510 520 530 540 PGLAPNQQNI MISPRNRGSP KIASHQFSPV AGVHSPMASS GNTGNHSFSS SSLSALQAIS 550 560 570 580 590 600 EGVGTSLLST LSSPGPKLDN SPNMNITQPS KVSNQDSKSP LGFYCDQNPV ESSMCQSNSR 610 620 630 640 650 660 DHLSDKESKE SSVEGAENQR GPLESKGHKK LLQLLTCSSD DRGHSSLTNS PLDSSCKESS 670 680 690 700 710 720 VSVTSPSGVS SSTSGGVSST SNMHGSLLQE KHRILHKLLQ NGNSPAEVAK ITAEATGKDT 730 740 750 760 770 780 SSITSCGDGN VVKQEQLSPK KKENNALLRY LLDRDDPSDA LSKELQPQVE GVDNKMSQCT 790 800 810 820 830 840 SSTIPSSSQE KDPKIKTETS EEGSGDLDNL DAILGDLTSS DFYNNSISSN GSHLGTKQQV 850 860 870 880 890 900 FQGTNSMGDW GLPNSKAGRM EPMNSNSMGR PGGDYNTSLP RPALGGSIPT LPLRSNSIPG 910 920 930 940 950 960 ARPVLQQQQQ MLQMRPGEIP MGMGANPYGQ AAASNQLGSW PDGMLSMEQV SHGTQNRPLL 970 980 990 1000 1010 1020 RNSLDDLVGP PSNLEGQSDE RALLDQLHTL LSNTDATGLE EIDRALGIPE LVNQGQALEP 1030 1040 1050 1060 1070 1080 KQDAFQGQEA AVMMDQKAGL YGQTYPAQGP PMQGGFHLQG QSPSFNSMMN QMNQQGNFPL 1090 1100 1110 1120 1130 1140 QGMHPRANIM RPRTNTPKQL RMQLQQRLQG QQFLNQSRQA LELKMENPTA GGAAVMRPMM 1150 1160 1170 1180 1190 1200 QPQQGFLNAQ MVAQRSRELL SHHFRQQRVA MMMQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ 1210 1220 1230 1240 1250 1260 QQTQAFSPPP NVTASPSMDG LLAGPTMPQA PPQQFPYQPN YGMGQQPDPA FGRVSSPPNA 1270 1280 1290 1300 1310 1320 MMSSRMGPSQ NPMMQHPQAA SIYQSSEMKG WPSGNLARNS SFSQQQFAHQ GNPAVYSMVH 1330 1340 1350 MNGSSGHMGQ MNMNPMPMSG MPMGPDQKYC
	Isoform 5 [UniParc]. Checksum: 654343CEA0855C60	FASTA	1,420	154,892
	10 20 30 40 50 60 MSGLGENLDP LASDSRKRKL PCDTPGQGLT CSGEKRRREQ ESKYIEELAE LISANLSDID 70 80 90 100 110 120 NFNVKPDKCA ILKETVRQIR QIKEQGKTIS NDDDVQKADV SSTGQGVIDK DSLGPLLLQA 130 140 150 160 170 180 LDGFLFVVNR DGNIVFVSEN VTQYLQYKQE DLVNTSVYNI LHEEDRKDFL KNLPKSTVNG 190 200 210 220 230 240 VSWTNETQRQ KSHTFNCRML MKTPHDILED INASPEMRQR YETMQCFALS QPRAMMEEGE 250 260 270 280 290 300 DLQSCMICVA RRITTGERTF PSNPESFITR HDLSGKVVNI DTNSLRSSMR PGFEDIIRRC 310 320 330 340 350 360 IQRFFSLNDG QSWSQKRHYQ EAYLNGHAET PVYRFSLADG TIVTAQTKSK LFRNPVTNDR 370 380 390 400 410 420 HGFVSTHFLQ REQNGYRPNP NPVGQGIRPP MAGCNSSVGG MSMSPNQGLQ MPSSRAYGLA 430 440 450 460 470 480 DPSTTGQMSG ARYGGSSNIA SLTPGPGMQS PSSYQNNNYG LNMSSPPHGS PGLAPNQQNI 490 500 510 520 530 540 MISPRNRGSP KIASHQFSPV AGVHSPMASS GNTGNHSFSS SSLSALQAIS EGVGTSLLST 550 560 570 580 590 600 LSSPGPKLDN SPNMNITQPS KVSNQDSKSP LGFYCDQNPV ESSMCQSNSR DHLSDKESKE 610 620 630 640 650 660 SSVEGAENQR GPLESKGHKK LLQLLTCSSD DRGHSSLTNS PLDSSCKESS VSVTSPSGVS 670 680 690 700 710 720 SSTSGGVSST SNMHGSLLQE KHRILHKLLQ NGNSPAEVAK ITAEATGKDT SSITSCGDGN 730 740 750 760 770 780 VVKQEQLSPK KKENNALLRY LLDRDDPSDA LSKELQPQVE GVDNKMSQCT SSTIPSSSQE 790 800 810 820 830 840 KDPKIKTETS EEGSGDLDNL DAILGDLTSS DFYNNSISSN GSHLGTKQQV FQGTNSLGLK 850 860 870 880 890 900 SSQSVQSIRP PYNRAVSLDS PVSVGSSPPV KNISAFPMLP KQPMLGGNPR MMDSQENYGS 910 920 930 940 950 960 SMGGPNRNVT VTQTPSSGDW GLPNSKAGRM EPMNSNSMGR PGGDYNTSLP RPALGGSIPT 970 980 990 1000 1010 1020 LPLRSNSIPG ARPVLQQQQQ MLQMRPGEIP MGMGANPYGQ AAASNQLGSW PDGMLSMEQV 1030 1040 1050 1060 1070 1080 SHGTQNRPLL RNSLDDLVGP PSNLEGQSDE RALLDQLHTL LSNTDATGLE EIDRALGIPE 1090 1100 1110 1120 1130 1140 LVNQGQALEP KQDAFQGQEA AVMMDQKAGL YGQTYPAQGP PMQGGFHLQG QSPSFNSMMN 1150 1160 1170 1180 1190 1200 QMNQQGNFPL QGMHPRANIM RPRTNTPKQL RMQLQQRLQG QQFLNQSRQA LELKMENPTA 1210 1220 1230 1240 1250 1260 GGAAVMRPMM QPQQGFLNAQ MVAQRSRELL SHHFRQQRVA MMMQQQQQQQ QQQQQQQQQQ 1270 1280 1290 1300 1310 1320 QQQQQQQQQQ QQTQAFSPPP NVTASPSMDG LLAGPTMPQA PPQQFPYQPN YGMGQQPDPA 1330 1340 1350 1360 1370 1380 FGRVSSPPNA MMSSRMGPSQ NPMMQHPQAA SIYQSSEMKG WPSGNLARNS SFSQQQFAHQ 1390 1400 1410 1420 GNPAVYSMVH MNGSSGHMGQ MNMNPMPMSG MPMGPDQKYC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1." Takeshita A., Cardona G.R., Koibuchi N., Suen C.-S., Chin W.W. J. Biol. Chem. 272:27629-27634(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH CREBBP; PCAF; RARA; RXRA; THRA AND ESR. Tissue: Pituitary.
[2]	"Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300." Chen H., Lin R.J., Schiltz R.L., Chakravarti D., Nash A., Nagy L., Privalsky M.L., Nakatani Y., Evans R.M. Cell 90:569-580(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), ENZYME ACTIVITY, VARIANT 1248-GLN--GLN-1250 DEL. Tissue: Leukemia.
[3]	"AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer." Anzick S.L., Kononen J., Walker R.L., Azorsa D.O., Tanner M.M., Guan X.-Y., Sauter G., Kallioniemi O.-P., Trent J.M., Meltzer P.S. Science 277:965-968(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), INTERACTION WITH ESR. Tissue: Lung.
[4]	"RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2." Li H., Gomes P.J., Chen J.D. Proc. Natl. Acad. Sci. U.S.A. 94:8479-8484(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), INTERACTION WITH VDR; RARA; PPARA; RXRA; THRA AND ESR, VARIANT 1248-GLN--GLN-1250 DEL. Tissue: Brain.
[5]	NIEHS SNPs program Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-218; ILE-220; VAL-556; SER-559; HIS-586; ALA-777; LEU-1247 AND LYS-1247.
[6]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[9]	"Polymorphic exonic CAG microsatellites in the gene amplified in breast cancer (AIB1 gene)." Shirazi S.K., Bober M.A., Coetzee G.A. Clin. Genet. 54:102-103(1998) [PubMed] [Europe PMC] [Abstract] Cited for: POLYMORPHISM OF POLY-GLN REGION.
[10]	"Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase." Chen H., Lin R.J., Xie W., Wilpitz D., Evans R.M. Cell 98:675-686(1999) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION BY CREBBP, MUTAGENESIS OF LYS-616; 619-LYS-LYS-620; LYS-647; LYS-681; LYS-687; LYS-700 AND LYS-708.
[11]	"RAC-3 is a NF-kappa B coactivator." Werbajh S., Nojek I., Lanz R., Costas M.A. FEBS Lett. 485:195-199(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NFKB1.
[12]	"A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor alpha coactivator through the N-terminal activation domain (AF-1) with an RNA coactivator, SRA." Watanabe M., Yanagisawa J., Kitagawa H., Takeyama K., Ogawa S., Arao Y., Suzawa M., Kobayashi Y., Yano T., Yoshikawa H., Masuhiro Y., Kato S. EMBO J. 20:1341-1352(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DDX5.
[13]	"Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase." Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J., O'Malley B.W. Mol. Cell. Biol. 22:3549-3561(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT OF A COMPLEX CONTAINING CREBBP; NCOA2; IKKA; IKKB AND IKBKG, PHOSPHORYLATION.
[14]	"BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation." Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K. Mol. Cell. Biol. 23:6210-6220(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NR3C1.
[15]	"FLASH interacts with p160 coactivator subtypes and differentially suppresses transcriptional activity of steroid hormone receptors." Kino T., Ichijo T., Chrousos G.P. J. Steroid Biochem. Mol. Biol. 92:357-363(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CASP8AP2.
[16]	"Male germ cell-associated kinase, a male-specific kinase regulated by androgen, is a coactivator of androgen receptor in prostate cancer cells." Ma A.H., Xia L., Desai S.J., Boucher D.L., Guan Y., Shih H.M., Shi X.B., deVere White R.W., Chen H.W., Tepper C.G., Kung H.J. Cancer Res. 66:8439-8447(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[17]	"The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription." Zhang H., Sun L., Liang J., Yu W., Zhang Y., Wang Y., Chen Y., Li R., Sun X., Shang Y. EMBO J. 25:4223-4233(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PSMB9.
[18]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857 AND SER-867, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"ANCCA, an estrogen-regulated AAA+ ATPase coactivator for ERalpha, is required for coregulator occupancy and chromatin modification." Zou J.X., Revenko A.S., Li L.B., Gemo A.T., Chen H.-W. Proc. Natl. Acad. Sci. U.S.A. 104:18067-18072(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATAD2.
[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-214; SER-551; SER-728 AND SER-857, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"CK1delta modulates the transcriptional activity of ERalpha via AIB1 in an estrogen-dependent manner and regulates ERalpha-AIB1 interactions." Giamas G., Castellano L., Feng Q., Knippschild U., Jacob J., Thomas R.S., Coombes R.C., Smith C.L., Jiao L.R., Stebbing J. Nucleic Acids Res. 37:3110-3123(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-601 BY CSNK1D/CK1, INTERACTION WITH CSNK1D.
[22]	"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-857, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[23]	"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-687, MASS SPECTROMETRY.
[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-214; SER-857 AND SER-867, 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].
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF016031 mRNA. Translation: AAC51849.1.
AF036892 mRNA. Translation: AAB92368.1.
AF012108 mRNA. Translation: AAC51677.1.
AF010227 mRNA. Translation: AAC51663.1.
EF488684 Genomic DNA. Translation: ABO43042.1.
AL034418 Genomic DNA. Translation: CAB40662.1.
AL034418 Genomic DNA. Translation: CAC17693.1.
AL034418 Genomic DNA. Translation: CAI42141.1.
CH471077 Genomic DNA. Translation: EAW75698.1.
CH471077 Genomic DNA. Translation: EAW75702.1.
BC119001 mRNA. Translation: AAI19002.1.

IPI

IPI00220079.
IPI00220080.
IPI00220081.
IPI00220082.
IPI00748532.

PIR

T03851.

RefSeq

NP_001167559.1. NM_001174088.1.
NP_006525.2. NM_006534.3.
NP_858045.1. NM_181659.2.

UniGene

Hs.592142.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KBH	NMR	-	A	1045-1091	[»]
3L3X	X-ray	1.55	B	618-629	[»]
3L3Z	X-ray	2.00	B	735-746	[»]

DisProt

DP00343.

ProteinModelPortal

Q9Y6Q9.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-30876N.

IntAct

Q9Y6Q9. 34 interactions.

MINT

MINT-231818.

PTM databases

PhosphoSite

Q9Y6Q9.

Polymorphism databases

DMDM

23396777.

Proteomic databases

PaxDb

Q9Y6Q9.

PRIDE

Q9Y6Q9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371997; ENSP00000361065; ENSG00000124151.
ENST00000371998; ENSP00000361066; ENSG00000124151.
ENST00000372004; ENSP00000361073; ENSG00000124151.

GeneID

8202.

KEGG

hsa:8202.

UCSC

uc002xtk.3. human.
uc002xtl.3. human.
uc010ght.2. human.

Organism-specific databases

CTD

8202.

GeneCards

GC20P046130.

HGNC

HGNC:7670. NCOA3.

HPA

CAB009800.
HPA024210.

MIM

601937. gene.

neXtProt

NX_Q9Y6Q9.

PharmGKB

PA31472.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG315556.

HOVERGEN

HBG052583.

InParanoid

Q9Y6Q9.

KO

K11256.

OMA

DGNIVFV.

PhylomeDB

Q9Y6Q9.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3apathway. FOXA1 transcription factor network.
retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.

Reactome

REACT_111045. Developmental Biology.
REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

Q9Y6Q9.

Bgee

Q9Y6Q9.

CleanEx

HS_NCOA3.
HS_RAC3.
HS_TRAM1.

Genevestigator

Q9Y6Q9.

GermOnline

ENSG00000124151. Homo sapiens.

Family and domain databases

Gene3D

4.10.280.10. 1 hit.
4.10.630.10. 2 hits.

InterPro

IPR011598. bHLH_dom.
IPR010011. DUF1518.
IPR009110. Nuc_rcpt_coact.
IPR014920. Nuc_rcpt_coact_Ncoa-typ.
IPR017426. Nuclear_rcpt_coactivator.
IPR000014. PAS.
IPR013767. PAS_fold.
IPR014935. SRC-1.
IPR008955. Src1_rcpt_coact.
[Graphical view]

Pfam

PF07469. DUF1518. 1 hit.
PF08815. Nuc_rec_co-act. 1 hit.
PF00989. PAS. 1 hit.
PF08832. SRC-1. 1 hit.
[Graphical view]

PIRSF

PIRSF038181. Nuclear_receptor_coactivator. 1 hit.

SMART

SM00353. HLH. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]

SUPFAM

SSF47459. HLH_basic. 1 hit.
SSF69125. Nuc_recept_coact. 1 hit.

PROSITE

PS50888. BHLH. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9Y6Q9.

ChEMBL

CHEMBL1615382.

ChiTaRS

NCOA3. human.

EvolutionaryTrace

Q9Y6Q9.

GenomeRNAi

8202.

NextBio

30907.

SOURCE

Search...

Entry information

Entry name

NCOA3_HUMAN

Accession

Primary (citable) accession number: Q9Y6Q9
Secondary accession number(s): A4LAZ5 , Q0VF45, Q5JYD9, Q5JYE0, Q9BR49, Q9UPC9, Q9UPG4, Q9UPG7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 144 of the entry and version 1 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.