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P70365

- NCOA1_MOUSE

UniProt

P70365 - NCOA1_MOUSE

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Protein

Nuclear receptor coactivator 1

Gene
Ncoa1, Src1
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. protein binding Source: MGI
  6. RNA polymerase II regulatory region DNA binding Source: Ensembl
  7. signal transducer activity Source: InterPro
  8. transcription coactivator activity Source: UniProtKB
  9. 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. positive regulation of apoptotic process Source: UniProtKB
  13. positive regulation of female receptivity Source: Ensembl
  14. positive regulation of neuron differentiation Source: UniProtKB
  15. positive regulation of transcription, DNA-templated Source: UniProtKB
  16. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  17. positive regulation of transcription from RNA polymerase II promoter by galactose Source: UniProtKB
  18. regulation of cellular response to drug Source: UniProtKB
  19. regulation of RNA biosynthetic process Source: UniProtKB
  20. response to estradiol Source: Ensembl
  21. response to progesterone Source: Ensembl
  22. response to retinoic acid Source: Ensembl
  23. 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_205251. Transcriptional activation of mitochondrial biogenesis.
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 Publication

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 – 11Removed By similarity
Chaini2 – 14471446Nuclear receptor coactivator 1PRO_0000094401Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei22 – 221Phosphoserine1 Publication
Modified residuei372 – 3721Phosphoserine1 Publication
Modified residuei395 – 3951Phosphoserine By similarity
Modified residuei518 – 5181Phosphoserine By similarity
Modified residuei570 – 5701Phosphoserine By 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 – 10391Phosphoserine By similarity
Modified residuei1185 – 11851Phosphothreonine By similarity
Modified residuei1191 – 11911Phosphoserine By 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.
Ubiquitinated; leading to proteasome-mediated degradation. Ubiquitination and sumoylation take place at different sites By similarity.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

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.4 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 – 2666
Beta strandi272 – 2765
Helixi278 – 2814
Helixi288 – 29912
Helixi309 – 32012
Beta strandi321 – 3244
Beta strandi328 – 3314
Beta strandi337 – 34711
Beta strandi357 – 3659
Turni687 – 6904
Helixi693 – 6997

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP70365.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 8058bHLHAdd
BLAST
Domaini109 – 18072PASAdd
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

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

MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL     50
SANISDIDSL SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS 100
SSSQGVIEKE SLGPLLLEAL DGFFFVVNCE GRIVFVSENV TSYLGYNQEE 150
LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG VPWPQEATRR NSHTFNCRML 200
IHPPEDPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ SCLICIARRL 250
PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF 300
QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ 350
SPDMQPFIMG IHIIDREHSG LSPQDDSNSG MSIPRINPSV NPGISPAHGV 400
TRSSTLPPSN NNMVSARVNR QQSSDLNSSS SHTNSSNNQG NFGCSPGNQI 450
VANVALNQGQ AGSQSSNPSL NLNNSPMEGT GIALSQFMSP RRQANSGLAT 500
RARMSNNSFP PNIPTLSSPV GITSGACNNN NRSYSNIPVT SLQGMNEGPN 550
NSVGFSAGSP VLRQMSSQNS PSRLSMQPAK AESKDSKEIA SILNEMIQSD 600
NSDNSANEGK PLDSGLLHNN DRLSEGDSKY SQTSHKLVQL LTTTAEQQLR 650
HADIDTSCKD VLSCTGTSSS ASSNPSGGTC PSSHSSLTER HKILHRLLQE 700
GSPSDITTLS VEPEKKDSVP ASTAVSVSGQ SQGSASIKLE LDAAKKKESK 750
DHQLLRYLLD KDEKDLRSTP NLCLDDVKVK VEKKEQMDPC NTNPTPMTKP 800
APEEVKLESQ SQFTADLDQF DQLLPTLEKA AQLPSLCETD RMDGAVTGVS 850
IKAEVLPASL QPTTARAAPR LSRLPELELE AIDNQFGQPG AGDQIPWANN 900
TLTTINQNKP EDQCISSQLD ELLCPPTTVE GRNDEKALLE QLVSFLSGKD 950
ETELAELDRA LGIDKLVQGG GLDVLSERFP PQQATPPLMM EDRPTLYSQP 1000
YSSPSPTAGL SGPFQGMVRQ KPSLGAMPVQ VTPPRGTFSP NMGMQPRQTL 1050
NRPPAAPNQL RLQLQQRLQG QQQLMHQNRQ AILNQFAANA PVGMNMRSGM 1100
QQQITPQPPL NAQMLAQRQR ELYSQQHRQR QIIQQQRAML MRHQSFGNNI 1150
PPSSGLPVQM GTPRLPQGAP QQFPYPPNYG TNPGTPPAST SPFSQLAANP 1200
EASLATRSSM VNRGMAGNMG GQFGAGISPQ MQQNVFQYPG PGLVPQGEAT 1250
FAPSLSPGSS MVPMPVPPPQ SSLLQQTPPT SGYQSPDMKA WQQGTMGNNN 1300
VFSQAVQSQP APAQPGVYNN MSITVSMAGG NANIQNMNPM MGQMQMSSLQ 1350
MPGMNTVCSE QMNDPALRHT GLYCNQLSST DLLKTDADGN QQVQQVQVFA 1400
DVQCTVNLVG GDPYLNQPGP LGTQKPTSGP QTPQAQQKSL LQQLLTE 1447
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1300 – 137677NVFSQ…LYCNQ → KWKRKHSEHESNDGPDANEL SADARDEYCVL in isoform 4. VSP_027855Add
BLAST
Alternative sequencei1377 – 144771Missing in isoform 4. VSP_027856Add
BLAST
Alternative sequencei1392 – 144756QVQQV…QLLTE → DKKTEEFFSVVTTD in isoform 2. VSP_011740Add
BLAST
Alternative sequencei1392 – 144756QVQQV…QLLTE → VSKKDNPSAELADSITLDTW RTSHGIC in isoform 3. VSP_011741Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451E → G in AAB01228. 1 Publication
Sequence conflicti223 – 2231C → R in AAB06177. 1 Publication
Sequence conflicti234 – 2341E → G in AAB06177. 1 Publication
Sequence conflicti237 – 2371E → K in AAH80866. 1 Publication
Sequence conflicti465 – 4662SS → TT in AAB01228. 1 Publication
Sequence conflicti699 – 6991Q → P in AAB06177. 1 Publication
Sequence conflicti1115 – 11151L → M in BAC29244. 1 Publication
Sequence conflicti1130 – 11301R → K in AAB01228. 1 Publication
Sequence conflicti1137 – 11382RA → KP in AAB01228. 1 Publication
Sequence conflicti1142 – 11421R → K in AAB01228. 1 Publication
Sequence conflicti1162 – 11621T → D in AAB01228. 1 Publication
Sequence conflicti1164 – 11641R → S in AAB06177. 1 Publication
Sequence conflicti1166 – 11661P → L in AAB01228. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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

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_205251. Transcriptional activation of mitochondrial biogenesis.
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: September 3, 2014
This is version 142 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

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