P70365 (NCOA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear receptor coactivator 1
Short name=NCoA-1
EC=2.3.1.48

Alternative name(s):
Nuclear receptor coactivator protein 1
Short name=mNRC-1
Steroid receptor coactivator 1
Short name=SRC-1

Gene names

Name:	Ncoa1
Synonyms:	Src1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1447 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. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3. Ref.1 Ref.8 Ref.10
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Interacts with NCOA6 and NCOA2. Interacts with the FDL motif of STAT5A and STAT5B. Interacts with the LXXLL motif of STAT6. Interacts with STAT3 following IL-6 stimulation. Interacts with the basal transcription factor GTF2B. Interacts with COPS5, NR3C1, PCAF and TTLL5/STAMP. Interacts with the histone acetyltransferases EP300 and CREBBP, and the methyltransferase CARM1. Interacts with PSMB9. Interacts with UBE2L3; they functionally interact to regulate progesterone receptor transcriptional activity. Interacts with PRMT2 and DDX5. Interacts with ASXL1 By similarity. Ref.1 Ref.3 Ref.9
Subcellular location	Nucleus Ref.3.
Tissue specificity	Widely expressed. Ref.3 Ref.7
Domain	The C-terminal (1113-1447) part mediates the histone acetyltransferase (HAT) activity By similarity. Contains 7 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. LXXLL motifs 3, 4 and 5 are essential for the association with nuclear receptors. LXXLL motif 7, which is not present in isoform 2, increases the affinity for steroid receptors in vitro.
Post-translational modification	Sumoylated; sumoylation increases its interaction with PGR and prolongs its retention in the nucleus. It does not prevent its ubiquitination and does not exert a clear effect on the stability of the protein By similarity. Ubiquitinated; leading to proteasome-mediated degradation. Ubiquitination and sumoylation take place at different sites By similarity.
Disruption phenotype	Mice show partial hormone resistance: target organs such as uterus, prostate, testis and mammary gland exhibiting decreased growth and development in response to steroid hormones. Moreover, such mice are prone to obesity due to reduced energy expenditure. Ref.8
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	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	Activator Acyltransferase Transferase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	histone H4 acetylation Inferred from mutant phenotype PubMed 16723356. Source: UniProtKB positive regulation of apoptotic process Inferred from mutant phenotype PubMed 16723356. Source: UniProtKB positive regulation of neuron differentiation Inferred from mutant phenotype PubMed 16723356. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter by galactose Inferred from mutant phenotype PubMed 16723356. Source: UniProtKB regulation of cellular response to drug Inferred from mutant phenotype PubMed 16723356. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nuclear chromatin Inferred from electronic annotation. Source: Compara nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA binding Inferred from direct assay PubMed 15681609. Source: MGI chromatin binding Inferred from direct assay PubMed 12446761PubMed 16109736. Source: MGI histone acetyltransferase activity Inferred from electronic annotation. Source: EC ligand-dependent nuclear receptor transcription coactivator activity Inferred from electronic annotation. Source: Compara signal transducer activity Inferred from electronic annotation. Source: InterPro transcription coactivator activity Inferred from mutant phenotype PubMed 16723356. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P70365-1)

Also known as: SRC-1A; SRC1a;

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: P70365-2)

Also known as: SRC-1E; SRC1e;

The sequence of this isoform differs from the canonical sequence as follows:
     1392-1447: QVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQLLTE → DKKTEEFFSVVTTD

Isoform 3 (identifier: P70365-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1392-1447: QVQQVQVFAD...KSLLQQLLTE → VSKKDNPSAELADSITLDTWRTSHGIC

Note: No experimental confirmation available.

Isoform 4 (identifier: P70365-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1300-1376: NVFSQAVQSQ...LRHTGLYCNQ → KWKRKHSEHESNDGPDANELSADARDEYCVL
     1377-1447: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1447

1447

Nuclear receptor coactivator 1

PRO_0000094401

Regions

Domain

23 – 80

58

bHLH

Domain

109 – 180

72

PAS

Region

361 – 568

208

Interaction with STAT3

Region

787 – 994

208

Interaction with CREBBP

Motif

46 – 50

5

LXXLL motif 1

Motif

112 – 116

5

LXXLL motif 2

Motif

637 – 641

5

LXXLL motif 3

Motif

694 – 698

5

LXXLL motif 4

Motif

755 – 759

5

LXXLL motif 5

Motif

919 – 923

5

LXXLL motif 6

Motif

1441 – 1445

5

LXXLL motif 7

Compositional bias

389 – 686

298

Ser-rich

Compositional bias

1059 – 1144

86

Gln-rich

Amino acid modifications

Modified residue

22

1

Phosphoserine Ref.11

Modified residue

372

1

Phosphoserine By similarity

Modified residue

395

1

Phosphoserine By similarity

Modified residue

518

1

Phosphoserine By similarity

Modified residue

570

1

Phosphoserine By similarity

Modified residue

1039

1

Phosphoserine By similarity

Modified residue

1185

1

Phosphothreonine By similarity

Modified residue

1191

1

Phosphoserine By similarity

Cross-link

738

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Cross-link

780

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence

1300 – 1376

77

NVFSQ…LYCNQ → KWKRKHSEHESNDGPDANEL SADARDEYCVL in isoform 4.

VSP_027855

Alternative sequence

1377 – 1447

71

Missing in isoform 4.

VSP_027856

Alternative sequence

1392 – 1447

56

QVQQV…QLLTE → DKKTEEFFSVVTTD in isoform 2.

VSP_011740

Alternative sequence

1392 – 1447

56

QVQQV…QLLTE → VSKKDNPSAELADSITLDTW RTSHGIC in isoform 3.

VSP_011741

Experimental info

Mutagenesis

695 – 698

4

HRLL → AAAA: Abolishes the interactions with estrogen and retinoid-acids receptors. Ref.7

Mutagenesis

756 – 759

4

RYLL → AAAA: Abolishes the interactions with estrogen and retinoid-acids receptors. Ref.7

Sequence conflict

45

1

E → G in AAB01228. Ref.1

Sequence conflict

223

1

C → R in AAB06177. Ref.2

Sequence conflict

234

1

E → G in AAB06177. Ref.2

Sequence conflict

237

1

E → K in AAH80866. Ref.5

Sequence conflict

465 – 466

2

SS → TT in AAB01228. Ref.1

Sequence conflict

699

1

Q → P in AAB06177. Ref.2

Sequence conflict

1115

1

L → M in BAC29244. Ref.4

Sequence conflict

1130

1

R → K in AAB01228. Ref.1

Sequence conflict

1137 – 1138

2

RA → KP in AAB01228. Ref.1

Sequence conflict

1142

1

R → K in AAB01228. Ref.1

Sequence conflict

1162

1

T → D in AAB01228. Ref.1

Sequence conflict

1164

1

R → S in AAB06177. Ref.2

Sequence conflict

1166

1

P → L in AAB01228. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1447

Helix Strand Turn

Details...

Beta strand

261 – 266

6

Beta strand

272 – 276

5

Helix

278 – 281

4

Helix

288 – 299

12

Helix

309 – 320

12

Beta strand

321 – 324

4

Beta strand

328 – 331

4

Beta strand

337 – 347

11

Beta strand

357 – 365

9

Turn

687 – 690

4

Helix

693 – 699

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (SRC-1A) (SRC1a) [UniParc]. Last modified October 11, 2004. Version 2. Checksum: 65C08AFFCF14241D	FASTA	1,447	157,016
	10 20 30 40 50 60 MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL SANISDIDSL 70 80 90 100 110 120 SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS SSSQGVIEKE SLGPLLLEAL 130 140 150 160 170 180 DGFFFVVNCE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG 190 200 210 220 230 240 VPWPQEATRR NSHTFNCRML IHPPEDPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ 250 260 270 280 290 300 SCLICIARRL PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF 310 320 330 340 350 360 QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ SPDMQPFIMG 370 380 390 400 410 420 IHIIDREHSG LSPQDDSNSG MSIPRINPSV NPGISPAHGV TRSSTLPPSN NNMVSARVNR 430 440 450 460 470 480 QQSSDLNSSS SHTNSSNNQG NFGCSPGNQI VANVALNQGQ AGSQSSNPSL NLNNSPMEGT 490 500 510 520 530 540 GIALSQFMSP RRQANSGLAT RARMSNNSFP PNIPTLSSPV GITSGACNNN NRSYSNIPVT 550 560 570 580 590 600 SLQGMNEGPN NSVGFSAGSP VLRQMSSQNS PSRLSMQPAK AESKDSKEIA SILNEMIQSD 610 620 630 640 650 660 NSDNSANEGK PLDSGLLHNN DRLSEGDSKY SQTSHKLVQL LTTTAEQQLR HADIDTSCKD 670 680 690 700 710 720 VLSCTGTSSS ASSNPSGGTC PSSHSSLTER HKILHRLLQE GSPSDITTLS VEPEKKDSVP 730 740 750 760 770 780 ASTAVSVSGQ SQGSASIKLE LDAAKKKESK DHQLLRYLLD KDEKDLRSTP NLCLDDVKVK 790 800 810 820 830 840 VEKKEQMDPC NTNPTPMTKP APEEVKLESQ SQFTADLDQF DQLLPTLEKA AQLPSLCETD 850 860 870 880 890 900 RMDGAVTGVS IKAEVLPASL QPTTARAAPR LSRLPELELE AIDNQFGQPG AGDQIPWANN 910 920 930 940 950 960 TLTTINQNKP EDQCISSQLD ELLCPPTTVE GRNDEKALLE QLVSFLSGKD ETELAELDRA 970 980 990 1000 1010 1020 LGIDKLVQGG GLDVLSERFP PQQATPPLMM EDRPTLYSQP YSSPSPTAGL SGPFQGMVRQ 1030 1040 1050 1060 1070 1080 KPSLGAMPVQ VTPPRGTFSP NMGMQPRQTL NRPPAAPNQL RLQLQQRLQG QQQLMHQNRQ 1090 1100 1110 1120 1130 1140 AILNQFAANA PVGMNMRSGM QQQITPQPPL NAQMLAQRQR ELYSQQHRQR QIIQQQRAML 1150 1160 1170 1180 1190 1200 MRHQSFGNNI PPSSGLPVQM GTPRLPQGAP QQFPYPPNYG TNPGTPPAST SPFSQLAANP 1210 1220 1230 1240 1250 1260 EASLATRSSM VNRGMAGNMG GQFGAGISPQ MQQNVFQYPG PGLVPQGEAT FAPSLSPGSS 1270 1280 1290 1300 1310 1320 MVPMPVPPPQ SSLLQQTPPT SGYQSPDMKA WQQGTMGNNN VFSQAVQSQP APAQPGVYNN 1330 1340 1350 1360 1370 1380 MSITVSMAGG NANIQNMNPM MGQMQMSSLQ MPGMNTVCSE QMNDPALRHT GLYCNQLSST 1390 1400 1410 1420 1430 1440 DLLKTDADGN QQVQQVQVFA DVQCTVNLVG GDPYLNQPGP LGTQKPTSGP QTPQAQQKSL LQQLLTE
	Isoform 2 (SRC-1E) (SRC1e) [UniParc]. Checksum: 92088DAE1A6A7F77	FASTA	1,405	152,644
	10 20 30 40 50 60 MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL SANISDIDSL 70 80 90 100 110 120 SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS SSSQGVIEKE SLGPLLLEAL 130 140 150 160 170 180 DGFFFVVNCE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG 190 200 210 220 230 240 VPWPQEATRR NSHTFNCRML IHPPEDPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ 250 260 270 280 290 300 SCLICIARRL PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF 310 320 330 340 350 360 QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ SPDMQPFIMG 370 380 390 400 410 420 IHIIDREHSG LSPQDDSNSG MSIPRINPSV NPGISPAHGV TRSSTLPPSN NNMVSARVNR 430 440 450 460 470 480 QQSSDLNSSS SHTNSSNNQG NFGCSPGNQI VANVALNQGQ AGSQSSNPSL NLNNSPMEGT 490 500 510 520 530 540 GIALSQFMSP RRQANSGLAT RARMSNNSFP PNIPTLSSPV GITSGACNNN NRSYSNIPVT 550 560 570 580 590 600 SLQGMNEGPN NSVGFSAGSP VLRQMSSQNS PSRLSMQPAK AESKDSKEIA SILNEMIQSD 610 620 630 640 650 660 NSDNSANEGK PLDSGLLHNN DRLSEGDSKY SQTSHKLVQL LTTTAEQQLR HADIDTSCKD 670 680 690 700 710 720 VLSCTGTSSS ASSNPSGGTC PSSHSSLTER HKILHRLLQE GSPSDITTLS VEPEKKDSVP 730 740 750 760 770 780 ASTAVSVSGQ SQGSASIKLE LDAAKKKESK DHQLLRYLLD KDEKDLRSTP NLCLDDVKVK 790 800 810 820 830 840 VEKKEQMDPC NTNPTPMTKP APEEVKLESQ SQFTADLDQF DQLLPTLEKA AQLPSLCETD 850 860 870 880 890 900 RMDGAVTGVS IKAEVLPASL QPTTARAAPR LSRLPELELE AIDNQFGQPG AGDQIPWANN 910 920 930 940 950 960 TLTTINQNKP EDQCISSQLD ELLCPPTTVE GRNDEKALLE QLVSFLSGKD ETELAELDRA 970 980 990 1000 1010 1020 LGIDKLVQGG GLDVLSERFP PQQATPPLMM EDRPTLYSQP YSSPSPTAGL SGPFQGMVRQ 1030 1040 1050 1060 1070 1080 KPSLGAMPVQ VTPPRGTFSP NMGMQPRQTL NRPPAAPNQL RLQLQQRLQG QQQLMHQNRQ 1090 1100 1110 1120 1130 1140 AILNQFAANA PVGMNMRSGM QQQITPQPPL NAQMLAQRQR ELYSQQHRQR QIIQQQRAML 1150 1160 1170 1180 1190 1200 MRHQSFGNNI PPSSGLPVQM GTPRLPQGAP QQFPYPPNYG TNPGTPPAST SPFSQLAANP 1210 1220 1230 1240 1250 1260 EASLATRSSM VNRGMAGNMG GQFGAGISPQ MQQNVFQYPG PGLVPQGEAT FAPSLSPGSS 1270 1280 1290 1300 1310 1320 MVPMPVPPPQ SSLLQQTPPT SGYQSPDMKA WQQGTMGNNN VFSQAVQSQP APAQPGVYNN 1330 1340 1350 1360 1370 1380 MSITVSMAGG NANIQNMNPM MGQMQMSSLQ MPGMNTVCSE QMNDPALRHT GLYCNQLSST 1390 1400 DLLKTDADGN QDKKTEEFFS VVTTD
	Isoform 3 [UniParc]. Checksum: 2AE9E75D49E5D1DC	FASTA	1,418	153,943
	10 20 30 40 50 60 MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL SANISDIDSL 70 80 90 100 110 120 SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS SSSQGVIEKE SLGPLLLEAL 130 140 150 160 170 180 DGFFFVVNCE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG 190 200 210 220 230 240 VPWPQEATRR NSHTFNCRML IHPPEDPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ 250 260 270 280 290 300 SCLICIARRL PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF 310 320 330 340 350 360 QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ SPDMQPFIMG 370 380 390 400 410 420 IHIIDREHSG LSPQDDSNSG MSIPRINPSV NPGISPAHGV TRSSTLPPSN NNMVSARVNR 430 440 450 460 470 480 QQSSDLNSSS SHTNSSNNQG NFGCSPGNQI VANVALNQGQ AGSQSSNPSL NLNNSPMEGT 490 500 510 520 530 540 GIALSQFMSP RRQANSGLAT RARMSNNSFP PNIPTLSSPV GITSGACNNN NRSYSNIPVT 550 560 570 580 590 600 SLQGMNEGPN NSVGFSAGSP VLRQMSSQNS PSRLSMQPAK AESKDSKEIA SILNEMIQSD 610 620 630 640 650 660 NSDNSANEGK PLDSGLLHNN DRLSEGDSKY SQTSHKLVQL LTTTAEQQLR HADIDTSCKD 670 680 690 700 710 720 VLSCTGTSSS ASSNPSGGTC PSSHSSLTER HKILHRLLQE GSPSDITTLS VEPEKKDSVP 730 740 750 760 770 780 ASTAVSVSGQ SQGSASIKLE LDAAKKKESK DHQLLRYLLD KDEKDLRSTP NLCLDDVKVK 790 800 810 820 830 840 VEKKEQMDPC NTNPTPMTKP APEEVKLESQ SQFTADLDQF DQLLPTLEKA AQLPSLCETD 850 860 870 880 890 900 RMDGAVTGVS IKAEVLPASL QPTTARAAPR LSRLPELELE AIDNQFGQPG AGDQIPWANN 910 920 930 940 950 960 TLTTINQNKP EDQCISSQLD ELLCPPTTVE GRNDEKALLE QLVSFLSGKD ETELAELDRA 970 980 990 1000 1010 1020 LGIDKLVQGG GLDVLSERFP PQQATPPLMM EDRPTLYSQP YSSPSPTAGL SGPFQGMVRQ 1030 1040 1050 1060 1070 1080 KPSLGAMPVQ VTPPRGTFSP NMGMQPRQTL NRPPAAPNQL RLQLQQRLQG QQQLMHQNRQ 1090 1100 1110 1120 1130 1140 AILNQFAANA PVGMNMRSGM QQQITPQPPL NAQMLAQRQR ELYSQQHRQR QIIQQQRAML 1150 1160 1170 1180 1190 1200 MRHQSFGNNI PPSSGLPVQM GTPRLPQGAP QQFPYPPNYG TNPGTPPAST SPFSQLAANP 1210 1220 1230 1240 1250 1260 EASLATRSSM VNRGMAGNMG GQFGAGISPQ MQQNVFQYPG PGLVPQGEAT FAPSLSPGSS 1270 1280 1290 1300 1310 1320 MVPMPVPPPQ SSLLQQTPPT SGYQSPDMKA WQQGTMGNNN VFSQAVQSQP APAQPGVYNN 1330 1340 1350 1360 1370 1380 MSITVSMAGG NANIQNMNPM MGQMQMSSLQ MPGMNTVCSE QMNDPALRHT GLYCNQLSST 1390 1400 1410 DLLKTDADGN QVSKKDNPSA ELADSITLDT WRTSHGIC
	Isoform 4 [UniParc]. Checksum: D7787C36638B2D94	FASTA	1,330	144,762
	10 20 30 40 50 60 MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL SANISDIDSL 70 80 90 100 110 120 SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS SSSQGVIEKE SLGPLLLEAL 130 140 150 160 170 180 DGFFFVVNCE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG 190 200 210 220 230 240 VPWPQEATRR NSHTFNCRML IHPPEDPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ 250 260 270 280 290 300 SCLICIARRL PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF 310 320 330 340 350 360 QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ SPDMQPFIMG 370 380 390 400 410 420 IHIIDREHSG LSPQDDSNSG MSIPRINPSV NPGISPAHGV TRSSTLPPSN NNMVSARVNR 430 440 450 460 470 480 QQSSDLNSSS SHTNSSNNQG NFGCSPGNQI VANVALNQGQ AGSQSSNPSL NLNNSPMEGT 490 500 510 520 530 540 GIALSQFMSP RRQANSGLAT RARMSNNSFP PNIPTLSSPV GITSGACNNN NRSYSNIPVT 550 560 570 580 590 600 SLQGMNEGPN NSVGFSAGSP VLRQMSSQNS PSRLSMQPAK AESKDSKEIA SILNEMIQSD 610 620 630 640 650 660 NSDNSANEGK PLDSGLLHNN DRLSEGDSKY SQTSHKLVQL LTTTAEQQLR HADIDTSCKD 670 680 690 700 710 720 VLSCTGTSSS ASSNPSGGTC PSSHSSLTER HKILHRLLQE GSPSDITTLS VEPEKKDSVP 730 740 750 760 770 780 ASTAVSVSGQ SQGSASIKLE LDAAKKKESK DHQLLRYLLD KDEKDLRSTP NLCLDDVKVK 790 800 810 820 830 840 VEKKEQMDPC NTNPTPMTKP APEEVKLESQ SQFTADLDQF DQLLPTLEKA AQLPSLCETD 850 860 870 880 890 900 RMDGAVTGVS IKAEVLPASL QPTTARAAPR LSRLPELELE AIDNQFGQPG AGDQIPWANN 910 920 930 940 950 960 TLTTINQNKP EDQCISSQLD ELLCPPTTVE GRNDEKALLE QLVSFLSGKD ETELAELDRA 970 980 990 1000 1010 1020 LGIDKLVQGG GLDVLSERFP PQQATPPLMM EDRPTLYSQP YSSPSPTAGL SGPFQGMVRQ 1030 1040 1050 1060 1070 1080 KPSLGAMPVQ VTPPRGTFSP NMGMQPRQTL NRPPAAPNQL RLQLQQRLQG QQQLMHQNRQ 1090 1100 1110 1120 1130 1140 AILNQFAANA PVGMNMRSGM QQQITPQPPL NAQMLAQRQR ELYSQQHRQR QIIQQQRAML 1150 1160 1170 1180 1190 1200 MRHQSFGNNI PPSSGLPVQM GTPRLPQGAP QQFPYPPNYG TNPGTPPAST SPFSQLAANP 1210 1220 1230 1240 1250 1260 EASLATRSSM VNRGMAGNMG GQFGAGISPQ MQQNVFQYPG PGLVPQGEAT FAPSLSPGSS 1270 1280 1290 1300 1310 1320 MVPMPVPPPQ SSLLQQTPPT SGYQSPDMKA WQQGTMGNNK WKRKHSEHES NDGPDANELS 1330 ADARDEYCVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors." Kamei Y., Xu L., Heinzel T., Torchia J., Kurokawa R., Gloss B., Lin S.-C., Heyman R.A., Rose D.W., Glass C.K., Rosenfeld M.G. Cell 85:403-414(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH EP300 AND CREBBP.
[2]	"Cloning and identification of mouse steroid receptor coactivator-1 (mSRC-1), as a coactivator of peroxisome proliferator-activated receptor gamma." Zhu Y., Qi C., Calandra C., Rao M.S., Reddy J.K. Gene Expr. 6:185-195(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"The nuclear hormone receptor coactivator SRC-1 is a specific target of p300." Yao T.-P., Ku G., Zhou N., Scully R., Livingston D.M. Proc. Natl. Acad. Sci. U.S.A. 93:10626-10631(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH EP300 AND RAR.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Strain: C57BL/6J. Tissue: Cerebellum.
[5]	"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] (ISOFORMS 2 AND 4). Strain: C57BL/6. Tissue: Brain and Eye.
[6]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 21-33, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[7]	"The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function." Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., Rosenfeld M.G. Nature 387:677-684(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE OF LXXLL MOTIFS, TISSUE SPECIFICITY, MUTAGENESIS OF 695-HIS--LEU-698 AND 756-ARG--LEU-759.
[8]	"Partial hormone resistance in mice with disruption of the steroid receptor coactivator-1 (SRC-1) gene." Xu J., Qiu Y., DeMayo F.J., Tsai S.Y., Tsai M.-J., O'Malley B.W. Science 279:1922-1925(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[9]	"Regulation of transcription by a protein methyltransferase." Chen D., Ma H., Hong H., Koh S.S., Huang S.-M., Schurter B.T., Aswad D.W., Stallcup M.R. Science 284:2174-2177(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CARM1.
[10]	"SRC-1 and TIF2 control energy balance between white and brown adipose tissues." Picard F., Gehin M., Annicotte J.-S., Rocchi S., Champy M.-F., O'Malley B.W., Chambon P., Auwerx J. Cell 111:931-941(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, MASS SPECTROMETRY. Tissue: Macrophage.
[12]	"Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain." Razeto A., Ramakrishnan V., Litterst C.M., Giller K., Griesinger C., Carlomagno T., Lakomek N., Heimburg T., Lodrini M., Pfitzner E., Becker S. J. Mol. Biol. 336:319-329(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 257-385 IN COMPLEX WITH STAT6.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U56920 mRNA. Translation: AAB01228.1.
U64606 mRNA. Translation: AAB06177.1.
U64828 mRNA. Translation: AAB38841.1.
AK035922 mRNA. Translation: BAC29244.1.
BC068177 mRNA. Translation: AAH68177.1.
BC080866 mRNA. Translation: AAH80866.1.

IPI

IPI00117839.
IPI00471393.
IPI00471395.
IPI00857158.

RefSeq

NP_035011.1. NM_010881.2.

UniGene

Mm.301039.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OJ5	X-ray	2.20	A	257-385	[»]
2O9I	X-ray	2.80	C/D	686-700	[»]
4DMA	X-ray	2.30	E/F	690-704	[»]

ProteinModelPortal

P70365.

SMR

P70365. Positions 29-367, 926-980.

ModBase

Search...

PTM databases

PhosphoSite

P70365.

Proteomic databases

PaxDb

P70365.

PRIDE

P70365.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000085814; ENSMUSP00000082971; ENSMUSG00000020647.

GeneID

17977.

KEGG

mmu:17977.

UCSC

uc007mxr.2. mouse.
uc007mxs.2. mouse.
uc007mxu.1. mouse.

Organism-specific databases

CTD

8648.

MGI

MGI:1276523. Ncoa1.

Phylogenomic databases

eggNOG

NOG315556.

GeneTree

ENSGT00530000063109.

HOGENOM

HOG000230947.

HOVERGEN

HBG052583.

InParanoid

P70365.

KO

K09101.

OMA

QITPQPP.

OrthoDB

EOG40K7Z6.

Enzyme and pathway databases

Reactome

REACT_127416. Developmental Biology.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Gene expression databases

Bgee

P70365.

CleanEx

MM_NCOA1.

Genevestigator

P70365.

GermOnline

ENSMUSG00000020647. Mus musculus.

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. 2 hits.
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

ChiTaRS

NCOA1. mouse.

EvolutionaryTrace

P70365.

NextBio

292937.

SOURCE

Search...

Entry information

Entry name

NCOA1_MOUSE

Accession

Primary (citable) accession number: P70365
Secondary accession number(s): P70366 , Q61202, Q66JL7, Q8CBI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program