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P70365

- NCOA1_MOUSE

UniProt

P70365 - NCOA1_MOUSE

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Protein

Nuclear receptor coactivator 1

Gene

Ncoa1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 3.4 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. DNA binding Source: MGI
  3. histone acetyltransferase activity Source: UniProtKB-EC
  4. ligand-dependent nuclear receptor transcription coactivator activity Source: Ensembl
  5. RNA polymerase II regulatory region DNA binding Source: Ensembl
  6. signal transducer activity Source: InterPro
  7. transcription coactivator activity Source: UniProtKB
  8. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. cellular response to hormone stimulus Source: Ensembl
  2. cerebellum development Source: Ensembl
  3. cerebral cortex development Source: Ensembl
  4. estrous cycle phase Source: Ensembl
  5. hippocampus development Source: Ensembl
  6. histone H4 acetylation Source: UniProtKB
  7. hypothalamus development Source: Ensembl
  8. labyrinthine layer morphogenesis Source: MGI
  9. lactation Source: Ensembl
  10. male gonad development Source: Ensembl
  11. male mating behavior Source: Ensembl
  12. ovulation cycle Source: Ensembl
  13. positive regulation of apoptotic process Source: UniProtKB
  14. positive regulation of female receptivity Source: Ensembl
  15. positive regulation of neuron differentiation Source: UniProtKB
  16. positive regulation of transcription, DNA-templated Source: UniProtKB
  17. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  18. positive regulation of transcription from RNA polymerase II promoter by galactose Source: UniProtKB
  19. regulation of cellular response to drug Source: UniProtKB
  20. regulation of RNA biosynthetic process Source: UniProtKB
  21. response to estradiol Source: Ensembl
  22. response to progesterone Source: Ensembl
  23. response to retinoic acid Source: Ensembl
  24. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_118837. Rora activates circadian gene expression.
REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_198351. RORA activates circadian gene expression.
REACT_198352. REV-ERBA represses gene expression.
REACT_198602. PPARA activates gene expression.
REACT_198969. Activation of gene expression by SREBF (SREBP).
REACT_203193. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_205251. Transcriptional activation of mitochondrial biogenesis.
REACT_207530. Synthesis of bile acids and bile salts.
REACT_226440. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_227038. Endogenous sterols.
REACT_239346. Recycling of bile acids and salts.
REACT_241925. Circadian Clock.
REACT_252217. Transcriptional regulation of white adipocyte differentiation.
REACT_257219. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_268398. Orphan transporters.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor coactivator 1 (EC:2.3.1.48)
Short name:
NCoA-1
Alternative name(s):
Nuclear receptor coactivator protein 1
Short name:
mNRC-1
Steroid receptor coactivator 1
Short name:
SRC-1
Gene namesi
Name:Ncoa1
Synonyms:Src1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:1276523. Ncoa1.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. neuron projection Source: Ensembl
  3. nuclear chromatin Source: Ensembl
  4. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi695 – 6984HRLL → AAAA: Abolishes the interactions with estrogen and retinoid-acids receptors. 1 Publication
Mutagenesisi756 – 7594RYLL → AAAA: Abolishes the interactions with estrogen and retinoid-acids receptors. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 14471446Nuclear receptor coactivator 1PRO_0000094401Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei22 – 221Phosphoserine1 Publication
Modified residuei372 – 3721Phosphoserine1 Publication
Modified residuei395 – 3951PhosphoserineBy similarity
Modified residuei518 – 5181PhosphoserineBy similarity
Modified residuei570 – 5701PhosphoserineBy similarity
Modified residuei702 – 7021Phosphoserine1 Publication
Cross-linki738 – 738Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki780 – 780Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei1039 – 10391PhosphoserineBy similarity
Modified residuei1185 – 11851PhosphothreonineBy similarity
Modified residuei1191 – 11911PhosphoserineBy similarity

Post-translational modificationi

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).By similarity
Ubiquitinated; leading to proteasome-mediated degradation. Ubiquitination and sumoylation take place at different sites (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP70365.
PaxDbiP70365.
PRIDEiP70365.

PTM databases

PhosphoSiteiP70365.

Expressioni

Tissue specificityi

Widely expressed.2 Publications

Gene expression databases

BgeeiP70365.
CleanExiMM_NCOA1.
GenevestigatoriP70365.

Interactioni

Subunit structurei

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. Interacts with PRMT6. Interacts (via LXXLL 1, 2 and 3 motifs) with RORC (via AF-2 motif). Interacts in a ligand-dependent fashion with RXRA.5 Publications

Protein-protein interaction databases

BioGridi201707. 14 interactions.
MINTiMINT-1530933.

Structurei

Secondary structure

1
1447
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi261 – 2666Combined sources
Beta strandi272 – 2765Combined sources
Helixi278 – 2814Combined sources
Helixi288 – 29912Combined sources
Helixi309 – 32012Combined sources
Beta strandi321 – 3244Combined sources
Beta strandi328 – 3314Combined sources
Beta strandi337 – 34711Combined sources
Beta strandi357 – 3659Combined sources
Turni687 – 6904Combined sources
Helixi693 – 6997Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OJ5X-ray2.20A257-385[»]
2O9IX-ray2.80C/D686-700[»]
4DMAX-ray2.30E/F690-704[»]
ProteinModelPortaliP70365.
SMRiP70365. Positions 29-367, 926-980.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP70365.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 8058bHLHPROSITE-ProRule annotationAdd
BLAST
Domaini109 – 18072PASPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni361 – 568208Interaction with STAT3Add
BLAST
Regioni787 – 994208Interaction with CREBBPAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi46 – 505LXXLL motif 1
Motifi112 – 1165LXXLL motif 2
Motifi637 – 6415LXXLL motif 3
Motifi694 – 6985LXXLL motif 4
Motifi755 – 7595LXXLL motif 5
Motifi919 – 9235LXXLL motif 6
Motifi1441 – 14455LXXLL motif 7

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi389 – 686298Ser-richAdd
BLAST
Compositional biasi1059 – 114486Gln-richAdd
BLAST

Domaini

The C-terminal (1113-1447) part mediates the histone acetyltransferase (HAT) activity.By similarity

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation
Contains 1 PAS (PER-ARNT-SIM) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG315556.
GeneTreeiENSGT00530000063109.
HOGENOMiHOG000230947.
HOVERGENiHBG052583.
InParanoidiP70365.
KOiK09101.
OMAiQITPQPP.
OrthoDBiEOG789C9C.
PhylomeDBiP70365.
TreeFamiTF332652.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
4.10.630.10. 2 hits.
InterProiIPR011598. bHLH_dom.
IPR010011. DUF1518.
IPR028819. NCOA1.
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]
PANTHERiPTHR10684. PTHR10684. 1 hit.
PTHR10684:SF1. PTHR10684:SF1. 1 hit.
PfamiPF07469. DUF1518. 2 hits.
PF08815. Nuc_rec_co-act. 1 hit.
PF00989. PAS. 1 hit.
PF08832. SRC-1. 1 hit.
[Graphical view]
PIRSFiPIRSF038181. Nuclear_receptor_coactivator. 1 hit.
SMARTiSM00353. HLH. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P70365-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL
60 70 80 90 100
SANISDIDSL SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS
110 120 130 140 150
SSSQGVIEKE SLGPLLLEAL DGFFFVVNCE GRIVFVSENV TSYLGYNQEE
160 170 180 190 200
LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG VPWPQEATRR NSHTFNCRML
210 220 230 240 250
IHPPEDPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ SCLICIARRL
260 270 280 290 300
PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF
310 320 330 340 350
QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ
360 370 380 390 400
SPDMQPFIMG IHIIDREHSG LSPQDDSNSG MSIPRINPSV NPGISPAHGV
410 420 430 440 450
TRSSTLPPSN NNMVSARVNR QQSSDLNSSS SHTNSSNNQG NFGCSPGNQI
460 470 480 490 500
VANVALNQGQ AGSQSSNPSL NLNNSPMEGT GIALSQFMSP RRQANSGLAT
510 520 530 540 550
RARMSNNSFP PNIPTLSSPV GITSGACNNN NRSYSNIPVT SLQGMNEGPN
560 570 580 590 600
NSVGFSAGSP VLRQMSSQNS PSRLSMQPAK AESKDSKEIA SILNEMIQSD
610 620 630 640 650
NSDNSANEGK PLDSGLLHNN DRLSEGDSKY SQTSHKLVQL LTTTAEQQLR
660 670 680 690 700
HADIDTSCKD VLSCTGTSSS ASSNPSGGTC PSSHSSLTER HKILHRLLQE
710 720 730 740 750
GSPSDITTLS VEPEKKDSVP ASTAVSVSGQ SQGSASIKLE LDAAKKKESK
760 770 780 790 800
DHQLLRYLLD KDEKDLRSTP NLCLDDVKVK VEKKEQMDPC NTNPTPMTKP
810 820 830 840 850
APEEVKLESQ SQFTADLDQF DQLLPTLEKA AQLPSLCETD RMDGAVTGVS
860 870 880 890 900
IKAEVLPASL QPTTARAAPR LSRLPELELE AIDNQFGQPG AGDQIPWANN
910 920 930 940 950
TLTTINQNKP EDQCISSQLD ELLCPPTTVE GRNDEKALLE QLVSFLSGKD
960 970 980 990 1000
ETELAELDRA LGIDKLVQGG GLDVLSERFP PQQATPPLMM EDRPTLYSQP
1010 1020 1030 1040 1050
YSSPSPTAGL SGPFQGMVRQ KPSLGAMPVQ VTPPRGTFSP NMGMQPRQTL
1060 1070 1080 1090 1100
NRPPAAPNQL RLQLQQRLQG QQQLMHQNRQ AILNQFAANA PVGMNMRSGM
1110 1120 1130 1140 1150
QQQITPQPPL NAQMLAQRQR ELYSQQHRQR QIIQQQRAML MRHQSFGNNI
1160 1170 1180 1190 1200
PPSSGLPVQM GTPRLPQGAP QQFPYPPNYG TNPGTPPAST SPFSQLAANP
1210 1220 1230 1240 1250
EASLATRSSM VNRGMAGNMG GQFGAGISPQ MQQNVFQYPG PGLVPQGEAT
1260 1270 1280 1290 1300
FAPSLSPGSS MVPMPVPPPQ SSLLQQTPPT SGYQSPDMKA WQQGTMGNNN
1310 1320 1330 1340 1350
VFSQAVQSQP APAQPGVYNN MSITVSMAGG NANIQNMNPM MGQMQMSSLQ
1360 1370 1380 1390 1400
MPGMNTVCSE QMNDPALRHT GLYCNQLSST DLLKTDADGN QQVQQVQVFA
1410 1420 1430 1440
DVQCTVNLVG GDPYLNQPGP LGTQKPTSGP QTPQAQQKSL LQQLLTE
Length:1,447
Mass (Da):157,016
Last modified:October 11, 2004 - v2
Checksum:i65C08AFFCF14241D
GO
Isoform 2 (identifier: P70365-2) [UniParc]FASTAAdd to Basket

Also known as: SRC-1E, SRC1e

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

Show »
Length:1,405
Mass (Da):152,644
Checksum:i92088DAE1A6A7F77
GO
Isoform 3 (identifier: P70365-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:1,418
Mass (Da):153,943
Checksum:i2AE9E75D49E5D1DC
GO
Isoform 4 (identifier: P70365-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,330
Mass (Da):144,762
Checksum:iD7787C36638B2D94
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451E → G in AAB01228. (PubMed:8616895)Curated
Sequence conflicti223 – 2231C → R in AAB06177. (PubMed:9041124)Curated
Sequence conflicti234 – 2341E → G in AAB06177. (PubMed:9041124)Curated
Sequence conflicti237 – 2371E → K in AAH80866. (PubMed:15489334)Curated
Sequence conflicti465 – 4662SS → TT in AAB01228. (PubMed:8616895)Curated
Sequence conflicti699 – 6991Q → P in AAB06177. (PubMed:9041124)Curated
Sequence conflicti1115 – 11151L → M in BAC29244. (PubMed:16141072)Curated
Sequence conflicti1130 – 11301R → K in AAB01228. (PubMed:8616895)Curated
Sequence conflicti1137 – 11382RA → KP in AAB01228. (PubMed:8616895)Curated
Sequence conflicti1142 – 11421R → K in AAB01228. (PubMed:8616895)Curated
Sequence conflicti1162 – 11621T → D in AAB01228. (PubMed:8616895)Curated
Sequence conflicti1164 – 11641R → S in AAB06177. (PubMed:9041124)Curated
Sequence conflicti1166 – 11661P → L in AAB01228. (PubMed:8616895)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1300 – 137677NVFSQ…LYCNQ → KWKRKHSEHESNDGPDANEL SADARDEYCVL in isoform 4. 1 PublicationVSP_027855Add
BLAST
Alternative sequencei1377 – 144771Missing in isoform 4. 1 PublicationVSP_027856Add
BLAST
Alternative sequencei1392 – 144756QVQQV…QLLTE → DKKTEEFFSVVTTD in isoform 2. 3 PublicationsVSP_011740Add
BLAST
Alternative sequencei1392 – 144756QVQQV…QLLTE → VSKKDNPSAELADSITLDTW RTSHGIC in isoform 3. 1 PublicationVSP_011741Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25789.1. [P70365-2]
RefSeqiNP_035011.1. NM_010881.2. [P70365-2]
XP_006515068.1. XM_006515005.1. [P70365-1]
XP_006515069.1. XM_006515006.1. [P70365-1]
XP_006515070.1. XM_006515007.1. [P70365-1]
XP_006515072.1. XM_006515009.1. [P70365-2]
UniGeneiMm.301039.

Genome annotation databases

EnsembliENSMUST00000085814; ENSMUSP00000082971; ENSMUSG00000020647. [P70365-2]
GeneIDi17977.
KEGGimmu:17977.
UCSCiuc007mxr.2. mouse. [P70365-1]
uc007mxs.2. mouse. [P70365-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS25789.1. [P70365-2 ]
RefSeqi NP_035011.1. NM_010881.2. [P70365-2 ]
XP_006515068.1. XM_006515005.1. [P70365-1 ]
XP_006515069.1. XM_006515006.1. [P70365-1 ]
XP_006515070.1. XM_006515007.1. [P70365-1 ]
XP_006515072.1. XM_006515009.1. [P70365-2 ]
UniGenei Mm.301039.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P70365.
SMRi P70365. Positions 29-367, 926-980.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201707. 14 interactions.
MINTi MINT-1530933.

PTM databases

PhosphoSitei P70365.

Proteomic databases

MaxQBi P70365.
PaxDbi P70365.
PRIDEi P70365.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000085814 ; ENSMUSP00000082971 ; ENSMUSG00000020647 . [P70365-2 ]
GeneIDi 17977.
KEGGi mmu:17977.
UCSCi uc007mxr.2. mouse. [P70365-1 ]
uc007mxs.2. mouse. [P70365-2 ]

Organism-specific databases

CTDi 8648.
MGIi MGI:1276523. Ncoa1.

Phylogenomic databases

eggNOGi NOG315556.
GeneTreei ENSGT00530000063109.
HOGENOMi HOG000230947.
HOVERGENi HBG052583.
InParanoidi P70365.
KOi K09101.
OMAi QITPQPP.
OrthoDBi EOG789C9C.
PhylomeDBi P70365.
TreeFami TF332652.

Enzyme and pathway databases

Reactomei REACT_118837. Rora activates circadian gene expression.
REACT_196516. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
REACT_198351. RORA activates circadian gene expression.
REACT_198352. REV-ERBA represses gene expression.
REACT_198602. PPARA activates gene expression.
REACT_198969. Activation of gene expression by SREBF (SREBP).
REACT_203193. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_205251. Transcriptional activation of mitochondrial biogenesis.
REACT_207530. Synthesis of bile acids and bile salts.
REACT_226440. Synthesis of bile acids and bile salts via 27-hydroxycholesterol.
REACT_227038. Endogenous sterols.
REACT_239346. Recycling of bile acids and salts.
REACT_241925. Circadian Clock.
REACT_252217. Transcriptional regulation of white adipocyte differentiation.
REACT_257219. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
REACT_268398. Orphan transporters.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

ChiTaRSi Ncoa1. mouse.
EvolutionaryTracei P70365.
NextBioi 292937.
PROi P70365.
SOURCEi Search...

Gene expression databases

Bgeei P70365.
CleanExi MM_NCOA1.
Genevestigatori P70365.

Family and domain databases

Gene3Di 4.10.280.10. 1 hit.
4.10.630.10. 2 hits.
InterProi IPR011598. bHLH_dom.
IPR010011. DUF1518.
IPR028819. NCOA1.
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 ]
PANTHERi PTHR10684. PTHR10684. 1 hit.
PTHR10684:SF1. PTHR10684:SF1. 1 hit.
Pfami PF07469. DUF1518. 2 hits.
PF08815. Nuc_rec_co-act. 1 hit.
PF00989. PAS. 1 hit.
PF08832. SRC-1. 1 hit.
[Graphical view ]
PIRSFi PIRSF038181. Nuclear_receptor_coactivator. 1 hit.
SMARTi SM00353. HLH. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view ]
SUPFAMi SSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEi PS50888. BHLH. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY 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. "RORgammat recruits steroid receptor coactivators to ensure thymocyte survival."
    Xie H., Sadim M.S., Sun Z.
    J. Immunol. 175:3800-3809(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS COACTIVATOR, INTERACTION WITH RORC.
  12. "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; SER-372 AND SER-702, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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.

Entry informationi

Entry nameiNCOA1_MOUSE
AccessioniPrimary (citable) accession number: P70365
Secondary accession number(s): P70366
, Q61202, Q66JL7, Q8CBI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 26, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3