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P70365 (NCOA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1447 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 Ref.11

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. Interacts with PRMT6. Interacts (via LXXLL 1, 2 and 3 motifs) with RORC (via AF-2 motif). Ref.1 Ref.3 Ref.9 Ref.11

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 processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   Molecular functionActivator
Acyltransferase
Transferase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to hormone stimulus

Inferred from electronic annotation. Source: Ensembl

cerebellum development

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from electronic annotation. Source: Ensembl

estrous cycle phase

Inferred from electronic annotation. Source: Ensembl

hippocampus development

Inferred from electronic annotation. Source: Ensembl

histone H4 acetylation

Inferred from mutant phenotype PubMed 16723356. Source: UniProtKB

hypothalamus development

Inferred from electronic annotation. Source: Ensembl

labyrinthine layer morphogenesis

Inferred from genetic interaction PubMed 20685850. Source: MGI

lactation

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from electronic annotation. Source: Ensembl

male mating behavior

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 16723356. Source: UniProtKB

positive regulation of female receptivity

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron differentiation

Inferred from mutant phenotype PubMed 16723356. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 10934189. Source: MGI

positive regulation of transcription from RNA polymerase II promoter by galactose

Inferred from mutant phenotype PubMed 16723356. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of RNA biosynthetic process

Inferred from mutant phenotype PubMed 16723356. Source: UniProtKB

regulation of cellular response to drug

Inferred from mutant phenotype PubMed 16723356. Source: UniProtKB

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from electronic annotation. Source: Ensembl

nuclear chromatin

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15681609. Source: MGI

RNA polymerase II regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from direct assay PubMed 12446761PubMed 16109736. Source: MGI

histone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

signal transducer activity

Inferred from electronic annotation. Source: InterPro

transcription coactivator activity

Inferred from direct assay Ref.11. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.11. 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 14471446Nuclear receptor coactivator 1
PRO_0000094401

Regions

Domain23 – 8058bHLH
Domain109 – 18072PAS
Region361 – 568208Interaction with STAT3
Region787 – 994208Interaction with CREBBP
Motif46 – 505LXXLL motif 1
Motif112 – 1165LXXLL motif 2
Motif637 – 6415LXXLL motif 3
Motif694 – 6985LXXLL motif 4
Motif755 – 7595LXXLL motif 5
Motif919 – 9235LXXLL motif 6
Motif1441 – 14455LXXLL motif 7
Compositional bias389 – 686298Ser-rich
Compositional bias1059 – 114486Gln-rich

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue221Phosphoserine Ref.12
Modified residue3721Phosphoserine Ref.12
Modified residue3951Phosphoserine By similarity
Modified residue5181Phosphoserine By similarity
Modified residue5701Phosphoserine By similarity
Modified residue7021Phosphoserine Ref.12
Modified residue10391Phosphoserine By similarity
Modified residue11851Phosphothreonine By similarity
Modified residue11911Phosphoserine By similarity
Cross-link738Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link780Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1300 – 137677NVFSQ…LYCNQ → KWKRKHSEHESNDGPDANEL SADARDEYCVL in isoform 4.
VSP_027855
Alternative sequence1377 – 144771Missing in isoform 4.
VSP_027856
Alternative sequence1392 – 144756QVQQV…QLLTE → DKKTEEFFSVVTTD in isoform 2.
VSP_011740
Alternative sequence1392 – 144756QVQQV…QLLTE → VSKKDNPSAELADSITLDTW RTSHGIC in isoform 3.
VSP_011741

Experimental info

Mutagenesis695 – 6984HRLL → AAAA: Abolishes the interactions with estrogen and retinoid-acids receptors. Ref.7
Mutagenesis756 – 7594RYLL → AAAA: Abolishes the interactions with estrogen and retinoid-acids receptors. Ref.7
Sequence conflict451E → G in AAB01228. Ref.1
Sequence conflict2231C → R in AAB06177. Ref.2
Sequence conflict2341E → G in AAB06177. Ref.2
Sequence conflict2371E → K in AAH80866. Ref.5
Sequence conflict465 – 4662SS → TT in AAB01228. Ref.1
Sequence conflict6991Q → P in AAB06177. Ref.2
Sequence conflict11151L → M in BAC29244. Ref.4
Sequence conflict11301R → K in AAB01228. Ref.1
Sequence conflict1137 – 11382RA → KP in AAB01228. Ref.1
Sequence conflict11421R → K in AAB01228. Ref.1
Sequence conflict11621T → D in AAB01228. Ref.1
Sequence conflict11641R → S in AAB06177. Ref.2
Sequence conflict11661P → L in AAB01228. Ref.1

Secondary structure

...................... 1447
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SRC-1A) (SRC1a) [UniParc].

Last modified October 11, 2004. Version 2.
Checksum: 65C08AFFCF14241D

FASTA1,447157,016
        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 

« Hide

Isoform 2 (SRC-1E) (SRC1e) [UniParc].

Checksum: 92088DAE1A6A7F77
Show »

FASTA1,405152,644
Isoform 3 [UniParc].

Checksum: 2AE9E75D49E5D1DC
Show »

FASTA1,418153,943
Isoform 4 [UniParc].

Checksum: D7787C36638B2D94
Show »

FASTA1,330144,762

References

« Hide '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. expand/collapse author list , 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.
+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.
RefSeqNP_035011.1. NM_010881.2.
XP_006515068.1. XM_006515005.1.
XP_006515069.1. XM_006515006.1.
XP_006515070.1. XM_006515007.1.
XP_006515072.1. XM_006515009.1.
UniGeneMm.301039.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OJ5X-ray2.20A257-385[»]
2O9IX-ray2.80C/D686-700[»]
4DMAX-ray2.30E/F690-704[»]
ProteinModelPortalP70365.
SMRP70365. Positions 29-367, 926-980.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201707. 14 interactions.
MINTMINT-1530933.

PTM databases

PhosphoSiteP70365.

Proteomic databases

PaxDbP70365.
PRIDEP70365.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000085814; ENSMUSP00000082971; ENSMUSG00000020647. [P70365-2]
GeneID17977.
KEGGmmu:17977.
UCSCuc007mxr.2. mouse. [P70365-1]
uc007mxs.2. mouse. [P70365-2]

Organism-specific databases

CTD8648.
MGIMGI:1276523. Ncoa1.

Phylogenomic databases

eggNOGNOG315556.
GeneTreeENSGT00530000063109.
HOGENOMHOG000230947.
HOVERGENHBG052583.
InParanoidP70365.
KOK09101.
OMAQITPQPP.
OrthoDBEOG789C9C.
PhylomeDBP70365.
TreeFamTF332652.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.
REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Gene expression databases

BgeeP70365.
CleanExMM_NCOA1.
GenevestigatorP70365.

Family and domain databases

Gene3D4.10.280.10. 1 hit.
4.10.630.10. 2 hits.
InterProIPR011598. 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]
PANTHERPTHR10684. PTHR10684. 1 hit.
PTHR10684:SF1. PTHR10684:SF1. 1 hit.
PfamPF07469. DUF1518. 2 hits.
PF08815. Nuc_rec_co-act. 1 hit.
PF00989. PAS. 1 hit.
PF08832. SRC-1. 1 hit.
[Graphical view]
PIRSFPIRSF038181. Nuclear_receptor_coactivator. 1 hit.
SMARTSM00353. HLH. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]
SUPFAMSSF47459. SSF47459. 1 hit.
SSF55785. SSF55785. 2 hits.
SSF69125. SSF69125. 1 hit.
PROSITEPS50888. BHLH. 1 hit.
PS50112. PAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNCOA1. mouse.
EvolutionaryTraceP70365.
NextBio292937.
PROP70365.
SOURCESearch...

Entry information

Entry nameNCOA1_MOUSE
AccessionPrimary (citable) accession number: P70365
Secondary accession number(s): P70366 expand/collapse secondary AC list , Q61202, Q66JL7, Q8CBI9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: April 16, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot