NCOA7_HUMAN
ID NCOA7_HUMAN Reviewed; 942 AA.
AC Q8NI08; B2RNS2; B7Z2C4; B9EH71; G8JL91; Q3LID6; Q4G0V1; Q5TF95; Q6IPQ4;
AC Q6NE83; Q86T89; Q8N1W4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Nuclear receptor coactivator 7;
DE AltName: Full=140 kDa estrogen receptor-associated protein;
DE AltName: Full=Estrogen nuclear receptor coactivator 1;
GN Name=NCOA7; Synonyms=ERAP140, ESNA1; ORFNames=Nbla00052, Nbla10993;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ESR1;
RP ESR2A; ESR2B; THRB; PPARG AND RARA, TISSUE SPECIFICITY, MUTAGENESIS OF
RP 511-LEU--LEU-517 AND 522-LEU-ILE-523, AND VARIANT ALA-399.
RX PubMed=11971969; DOI=10.1128/mcb.22.10.3358-3372.2002;
RA Shao W., Halachmi S., Brown M.;
RT "ERAP140, a conserved tissue-specific nuclear receptor coactivator.";
RL Mol. Cell. Biol. 22:3358-3372(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Neuroblastoma;
RX PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5;
RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA Hirato J., Nakagawara A.;
RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of the
RT genesis and biology of neuroblastoma.";
RL Cancer Lett. 197:63-68(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7), AND VARIANT
RP ALA-399.
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, Fetal kidney, and Spinal cord;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-399.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 6), AND VARIANT
RP ALA-399.
RC TISSUE=Brain, Kidney, Lung, Muscle, Placenta, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH HETERODIMER AHR-ARNT.
RX PubMed=10395741; DOI=10.1006/abbi.1999.1282;
RA Nguyen T.A., Hoivik D., Lee J.-E., Safe S.;
RT "Interactions of nuclear receptor coactivator/corepressor proteins with the
RT aryl hydrocarbon receptor complex.";
RL Arch. Biochem. Biophys. 367:250-257(1999).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-441, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179; SER-208 AND SER-211, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208 AND SER-211, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; THR-134; SER-179;
RP SER-208; SER-211 AND SER-502, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208 AND SER-211, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Enhances the transcriptional activities of several nuclear
CC receptors. Involved in the coactivation of different nuclear receptors,
CC such as ESR1, THRB, PPARG and RARA. {ECO:0000269|PubMed:11971969}.
CC -!- SUBUNIT: Interacts with ESR1, ESR2A, ESR2B, THRB, PPARG and RARA in a
CC ligand-inducible manner. Interacts with the heterodimer AHR-ARNT.
CC {ECO:0000269|PubMed:10395741, ECO:0000269|PubMed:11971969}.
CC -!- INTERACTION:
CC Q8NI08; P35869: AHR; NbExp=2; IntAct=EBI-80799, EBI-80780;
CC Q8NI08; P27540: ARNT; NbExp=2; IntAct=EBI-80799, EBI-80809;
CC Q8NI08; O95166: GABARAP; NbExp=4; IntAct=EBI-80799, EBI-712001;
CC Q8NI08; Q9H0R8: GABARAPL1; NbExp=2; IntAct=EBI-80799, EBI-746969;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q8NI08-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NI08-2; Sequence=VSP_019638;
CC Name=3;
CC IsoId=Q8NI08-3; Sequence=VSP_019637;
CC Name=4;
CC IsoId=Q8NI08-4; Sequence=VSP_019635, VSP_019636;
CC Name=5;
CC IsoId=Q8NI08-5; Sequence=VSP_019632, VSP_019639;
CC Name=6;
CC IsoId=Q8NI08-6; Sequence=VSP_019633, VSP_019634;
CC Name=7;
CC IsoId=Q8NI08-7; Sequence=VSP_044859, VSP_019638;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Weakly expressed in
CC mammary gland, ovary, uterus, prostate, stomach, bladder, spinal cord
CC and pancreas. Expressed in cancer cell line.
CC {ECO:0000269|PubMed:11971969}.
CC -!- SIMILARITY: Belongs to the OXR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD89948.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF493978; AAM27392.1; -; mRNA.
DR EMBL; AB074157; BAE45732.1; -; mRNA.
DR EMBL; AK094706; BAC04402.1; -; mRNA.
DR EMBL; AK294558; BAH11810.1; -; mRNA.
DR EMBL; BX537385; CAD97627.1; -; mRNA.
DR EMBL; AL832628; CAD89948.1; ALT_FRAME; mRNA.
DR EMBL; AL035689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL078594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48133.1; -; Genomic_DNA.
DR EMBL; BC036461; AAH36461.1; -; mRNA.
DR EMBL; BC071782; AAH71782.1; -; mRNA.
DR EMBL; BC137094; AAI37095.1; -; mRNA.
DR EMBL; BC137095; AAI37096.1; -; mRNA.
DR CCDS; CCDS5132.1; -. [Q8NI08-1]
DR CCDS; CCDS56448.1; -. [Q8NI08-7]
DR CCDS; CCDS83125.1; -. [Q8NI08-5]
DR RefSeq; NP_001116314.1; NM_001122842.2. [Q8NI08-2]
DR RefSeq; NP_001186548.1; NM_001199619.1. [Q8NI08-1]
DR RefSeq; NP_001186549.1; NM_001199620.1. [Q8NI08-1]
DR RefSeq; NP_001186550.1; NM_001199621.1. [Q8NI08-7]
DR RefSeq; NP_001186551.1; NM_001199622.1. [Q8NI08-5]
DR RefSeq; NP_861447.3; NM_181782.4. [Q8NI08-1]
DR RefSeq; XP_005266879.1; XM_005266822.4. [Q8NI08-1]
DR RefSeq; XP_006715403.1; XM_006715340.3. [Q8NI08-1]
DR RefSeq; XP_011533757.1; XM_011535455.2. [Q8NI08-1]
DR RefSeq; XP_016865758.1; XM_017010269.1. [Q8NI08-1]
DR RefSeq; XP_016865759.1; XM_017010270.1. [Q8NI08-2]
DR RefSeq; XP_016865760.1; XM_017010271.1. [Q8NI08-2]
DR RefSeq; XP_016865761.1; XM_017010272.1. [Q8NI08-2]
DR RefSeq; XP_016865762.1; XM_017010273.1. [Q8NI08-2]
DR RefSeq; XP_016865763.1; XM_017010274.1. [Q8NI08-2]
DR PDB; 7OBP; X-ray; 1.80 A; A/B/C/D/E/F=777-942.
DR PDBsum; 7OBP; -.
DR AlphaFoldDB; Q8NI08; -.
DR SMR; Q8NI08; -.
DR BioGRID; 126419; 33.
DR IntAct; Q8NI08; 12.
DR MINT; Q8NI08; -.
DR STRING; 9606.ENSP00000376269; -.
DR TCDB; 8.A.126.1.1; the nuclear receptor coactivator 7 (ncoa7) family.
DR GlyGen; Q8NI08; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NI08; -.
DR PhosphoSitePlus; Q8NI08; -.
DR SwissPalm; Q8NI08; -.
DR BioMuta; NCOA7; -.
DR DMDM; 110287684; -.
DR EPD; Q8NI08; -.
DR jPOST; Q8NI08; -.
DR MassIVE; Q8NI08; -.
DR MaxQB; Q8NI08; -.
DR PaxDb; Q8NI08; -.
DR PeptideAtlas; Q8NI08; -.
DR PRIDE; Q8NI08; -.
DR ProteomicsDB; 34153; -.
DR ProteomicsDB; 73795; -. [Q8NI08-1]
DR ProteomicsDB; 73796; -. [Q8NI08-2]
DR ProteomicsDB; 73797; -. [Q8NI08-3]
DR ProteomicsDB; 73798; -. [Q8NI08-4]
DR ProteomicsDB; 73799; -. [Q8NI08-5]
DR ProteomicsDB; 73800; -. [Q8NI08-6]
DR Antibodypedia; 32708; 212 antibodies from 30 providers.
DR DNASU; 135112; -.
DR Ensembl; ENST00000229634.13; ENSP00000229634.9; ENSG00000111912.20. [Q8NI08-7]
DR Ensembl; ENST00000368357.7; ENSP00000357341.3; ENSG00000111912.20. [Q8NI08-1]
DR Ensembl; ENST00000392477.7; ENSP00000376269.2; ENSG00000111912.20. [Q8NI08-1]
DR Ensembl; ENST00000438495.6; ENSP00000398268.2; ENSG00000111912.20. [Q8NI08-5]
DR GeneID; 135112; -.
DR KEGG; hsa:135112; -.
DR MANE-Select; ENST00000392477.7; ENSP00000376269.2; NM_181782.5; NP_861447.3.
DR UCSC; uc003qae.5; human. [Q8NI08-1]
DR CTD; 135112; -.
DR DisGeNET; 135112; -.
DR GeneCards; NCOA7; -.
DR HGNC; HGNC:21081; NCOA7.
DR HPA; ENSG00000111912; Low tissue specificity.
DR MIM; 609752; gene.
DR neXtProt; NX_Q8NI08; -.
DR OpenTargets; ENSG00000111912; -.
DR PharmGKB; PA134905581; -.
DR VEuPathDB; HostDB:ENSG00000111912; -.
DR eggNOG; KOG2372; Eukaryota.
DR GeneTree; ENSGT00940000155141; -.
DR HOGENOM; CLU_007095_2_0_1; -.
DR InParanoid; Q8NI08; -.
DR OMA; SEDNCKF; -.
DR OrthoDB; 767847at2759; -.
DR PhylomeDB; Q8NI08; -.
DR TreeFam; TF313530; -.
DR PathwayCommons; Q8NI08; -.
DR SignaLink; Q8NI08; -.
DR BioGRID-ORCS; 135112; 16 hits in 1089 CRISPR screens.
DR ChiTaRS; NCOA7; human.
DR GeneWiki; NCOA7; -.
DR GenomeRNAi; 135112; -.
DR Pharos; Q8NI08; Tbio.
DR PRO; PR:Q8NI08; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8NI08; protein.
DR Bgee; ENSG00000111912; Expressed in kidney epithelium and 186 other tissues.
DR ExpressionAtlas; Q8NI08; baseline and differential.
DR Genevisible; Q8NI08; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016922; F:nuclear receptor binding; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:UniProtKB.
DR GO; GO:1900408; P:negative regulation of cellular response to oxidative stress; IEA:Ensembl.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IEA:Ensembl.
DR GO; GO:1902083; P:negative regulation of peptidyl-cysteine S-nitrosylation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR006571; TLDc_dom.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF07534; TLD; 1.
DR SMART; SM00257; LysM; 1.
DR SMART; SM00584; TLDc; 1.
DR SUPFAM; SSF54106; SSF54106; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS51886; TLDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Coiled coil;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..942
FT /note="Nuclear receptor coactivator 7"
FT /id="PRO_0000245229"
FT DOMAIN 114..157
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 781..942
FT /note="TLDc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01234"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..29
FT /evidence="ECO:0000255"
FT COMPBIAS 27..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 134
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFV7"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DFV7"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..723
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019632"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044859"
FT VAR_SEQ 91..102
FT /note="DDNQNKTHDKKE -> GEYSWRYCSIFI (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019633"
FT VAR_SEQ 103..942
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019634"
FT VAR_SEQ 234..249
FT /note="GVVGGVMIVTPNNIMF -> VYSNVICFLSLKSMKN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019635"
FT VAR_SEQ 250..942
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019636"
FT VAR_SEQ 296..942
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12880961"
FT /id="VSP_019637"
FT VAR_SEQ 296..306
FT /note="Missing (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_019638"
FT VAR_SEQ 724..748
FT /note="FVVVEKEELNMIDNFFSEPTTKSWE -> MRGQRLPLDIQIFYCARPDEEPF
FT VK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019639"
FT VARIANT 399
FT /note="S -> A (in dbSNP:rs6919947)"
FT /evidence="ECO:0000269|PubMed:11971969,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.6"
FT /id="VAR_026965"
FT VARIANT 533
FT /note="G -> R (in dbSNP:rs35223550)"
FT /id="VAR_050438"
FT VARIANT 942
FT /note="D -> E (in dbSNP:rs1567)"
FT /id="VAR_026966"
FT MUTAGEN 511..517
FT /note="LNIHEDL->ANAHEDA: No action on the E2-induced ESR1
FT binding."
FT /evidence="ECO:0000269|PubMed:11971969"
FT MUTAGEN 522..523
FT /note="LI->AA: Abolishes completely the E2-induced ESR1
FT binding."
FT /evidence="ECO:0000269|PubMed:11971969"
FT CONFLICT 32
FT /note="S -> T (in Ref. 2; BAE45732)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="A -> T (in Ref. 4; CAD89948)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="T -> A (in Ref. 1; AAM27392)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="Y -> H (in Ref. 4; CAD89948)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="F -> C (in Ref. 1; AAM27392)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="Y -> H (in Ref. 4; CAD97627)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="I -> T (in Ref. 1; AAM27392)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="E -> G (in Ref. 4; CAD89948)"
FT /evidence="ECO:0000305"
FT CONFLICT 723
FT /note="G -> S (in Ref. 3; BAH11810)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="V -> A (in Ref. 4; CAD89948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 942 AA; 106162 MW; AFD13F06F38C6C5D CRC64;
MDTKEEKKER KQSYFARLKK KKQAKQNAET ASAVATRTHT GKEDNNTVVL EPDKCNIAVE
EEYMTDEKKK RKSNQLKEIR RTELKRYYSI DDNQNKTHDK KEKKMVVQKP HGTMEYTAGN
QDTLNSIALK FNITPNKLVE LNKLFTHTIV PGQVLFVPDA NSPSSTLRLS SSSPGATVSP
SSSDAEYDKL PDADLARKAL KPIERVLSST SEEDEPGVVK FLKMNCRYFT DGKGVVGGVM
IVTPNNIMFD PHKSDPLVIE NGCEEYGLIC PMEEVVSIAL YNDISHMKIK DALPSDLPQD
LCPLYRPGEW EDLASEKDIN PFSKFKSINK EKRQQNGEKI MTSDSRPIVP LEKSTGHTPT
KPSGSSVSEK LKKLDSSRET SHGSPTVTKL SKEPSDTSSA FESTAKENFL GEDDDFVDLE
ELSSQTGGGM HKKDTLKECL SLDPEERKKA ESQINNSAVE MQVQSALAFL GTENDVELKG
ALDLETCEKQ DIMPEVDKQS GSPESRVENT LNIHEDLDKV KLIEYYLTKN KEGPQVSENL
QKTELSDGKS IEPGGIDITL SSSLSQAGDP ITEGNKEPDK TWVKKGEPLP VKLNSSTEAN
VIKEALDSSL ESTLDNSCQG AQMDNKSEVQ LWLLKRIQVP IEDILPSKEE KSKTPPMFLC
IKVGKPMRKS FATHTAAMVQ QYGKRRKQPE YWFAVPRERV DHLYTFFVQW SPDVYGKDAK
EQGFVVVEKE ELNMIDNFFS EPTTKSWEII TVEEAKRRKS TCSYYEDEDE EVLPVLRPHS
ALLENMHIEQ LARRLPARVQ GYPWRLAYST LEHGTSLKTL YRKSASLDSP VLLVIKDMDN
QIFGAYATHP FKFSDHYYGT GETFLYTFSP HFKVFKWSGE NSYFINGDIS SLELGGGGGR
FGLWLDADLY HGRSNSCSTF NNDILSKKED FIVQDLEVWA FD
