NRF1_HUMAN
ID NRF1_HUMAN Reviewed; 503 AA.
AC Q16656; A8K4C6; B4DDV6; Q15305; Q96AN2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Nuclear respiratory factor 1;
DE Short=NRF-1;
DE AltName: Full=Alpha palindromic-binding protein;
DE Short=Alpha-pal;
GN Name=NRF1;
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 LONG), AND PROTEIN SEQUENCE OF 161-186
RP AND 256-263.
RX PubMed=8253388; DOI=10.1101/gad.7.12a.2431;
RA Virbasius C.A., Virbasius J.V., Scarpulla R.C.;
RT "NRF-1, an activator involved in nuclear-mitochondrial interactions,
RT utilizes a new DNA-binding domain conserved in a family of developmental
RT regulators.";
RL Genes Dev. 7:2431-2445(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND PROTEIN SEQUENCE OF 161-183
RP AND 231-253.
RX PubMed=8034649; DOI=10.1016/s0021-9258(17)32255-x;
RA Efiok B.J.S., Chiorini J.A., Safer B.;
RT "A key transcription factor for eukaryotic initiation factor-2 alpha is
RT strongly homologous to developmental transcription factors and may link
RT metabolic genes to cellular growth and development.";
RL J. Biol. Chem. 269:18921-18930(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=7629110; DOI=10.1074/jbc.270.30.18019;
RA Gopalakrishnan L., Scarpulla R.C.;
RT "Structure, expression, and chromosomal assignment of the human gene
RT encoding nuclear respiratory factor 1.";
RL J. Biol. Chem. 270:18019-18025(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Hepatoma;
RA Yang S.J., Li K.N., Zhang Y.Q.;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND 3).
RC TISSUE=Urinary bladder;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Duodenum;
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 [10]
RP ALTERNATIVE SPLICING.
RX PubMed=8541844; DOI=10.1093/hmg/4.9.1591;
RA Spelbrink J.N., Van den Bogert C.;
RT "The pre-mRNA of nuclear respiratory factor 1, a regulator of mitochondrial
RT biogenesis, is alternatively spliced in human tissues and cell lines.";
RL Hum. Mol. Genet. 4:1591-1596(1995).
RN [11]
RP IDENTIFICATION OF DOMAINS, AND PHOSPHORYLATION AT SER-39; SER-44; SER-46;
RP SER-47 AND SER-52.
RX PubMed=9228045; DOI=10.1074/jbc.272.30.18732;
RA Gugneja S., Scarpulla R.C.;
RT "Serine phosphorylation within a concise amino-terminal domain in nuclear
RT respiratory factor 1 enhances DNA binding.";
RL J. Biol. Chem. 272:18732-18739(1997).
RN [12]
RP INTERACTION WITH PPRC1.
RX PubMed=11340167; DOI=10.1128/mcb.21.11.3738-3749.2001;
RA Andersson U., Scarpulla R.C.;
RT "Pgc-1-related coactivator, a novel, serum-inducible coactivator of nuclear
RT respiratory factor 1-dependent transcription in mammalian cells.";
RL Mol. Cell. Biol. 21:3738-3749(2001).
RN [13]
RP INTERACTION WITH PPRC1.
RX PubMed=16908542; DOI=10.1128/mcb.00585-06;
RA Vercauteren K., Pasko R.A., Gleyzer N., Marino V.M., Scarpulla R.C.;
RT "PGC-1-related coactivator: immediate early expression and characterization
RT of a CREB/NRF-1 binding domain associated with cytochrome c promoter
RT occupancy and respiratory growth.";
RL Mol. Cell. Biol. 26:7409-7419(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-139, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Transcription factor that activates the expression of the
CC EIF2S1 (EIF2-alpha) gene. Links the transcriptional modulation of key
CC metabolic genes to cellular growth and development. Implicated in the
CC control of nuclear genes required for respiration, heme biosynthesis,
CC and mitochondrial DNA transcription and replication.
CC -!- SUBUNIT: Homodimer. Binds DNA as a dimer. Interacts with PPRC1.
CC {ECO:0000269|PubMed:11340167, ECO:0000269|PubMed:16908542}.
CC -!- INTERACTION:
CC Q16656; P24385: CCND1; NbExp=2; IntAct=EBI-2547810, EBI-375001;
CC Q16656; Q14192: FHL2; NbExp=3; IntAct=EBI-2547810, EBI-701903;
CC Q16656; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-2547810, EBI-1389308;
CC Q16656; Q9NRC8: SIRT7; NbExp=2; IntAct=EBI-2547810, EBI-716046;
CC Q16656; Q02446: SP4; NbExp=3; IntAct=EBI-2547810, EBI-10198587;
CC Q16656; Q12933: TRAF2; NbExp=3; IntAct=EBI-2547810, EBI-355744;
CC Q16656-4; O95994: AGR2; NbExp=5; IntAct=EBI-11742836, EBI-712648;
CC Q16656-4; Q92870-2: APBB2; NbExp=3; IntAct=EBI-11742836, EBI-21535880;
CC Q16656-4; Q9BXC9: BBS2; NbExp=3; IntAct=EBI-11742836, EBI-748297;
CC Q16656-4; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-11742836, EBI-1012434;
CC Q16656-4; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-11742836, EBI-10693038;
CC Q16656-4; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-11742836, EBI-12809220;
CC Q16656-4; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-11742836, EBI-18036948;
CC Q16656-4; P17540: CKMT2; NbExp=3; IntAct=EBI-11742836, EBI-712973;
CC Q16656-4; Q03692: COL10A1; NbExp=3; IntAct=EBI-11742836, EBI-2528309;
CC Q16656-4; P67870: CSNK2B; NbExp=3; IntAct=EBI-11742836, EBI-348169;
CC Q16656-4; Q9NQ30: ESM1; NbExp=3; IntAct=EBI-11742836, EBI-12260294;
CC Q16656-4; Q14192: FHL2; NbExp=3; IntAct=EBI-11742836, EBI-701903;
CC Q16656-4; Q96JK4-2: HHIPL1; NbExp=3; IntAct=EBI-11742836, EBI-12083878;
CC Q16656-4; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-11742836, EBI-9089060;
CC Q16656-4; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-11742836, EBI-2796400;
CC Q16656-4; P78385: KRT83; NbExp=3; IntAct=EBI-11742836, EBI-10221390;
CC Q16656-4; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-11742836, EBI-739909;
CC Q16656-4; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-11742836, EBI-11985629;
CC Q16656-4; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-11742836, EBI-12039345;
CC Q16656-4; A0A0S2Z5S9: LHX4; NbExp=3; IntAct=EBI-11742836, EBI-16429099;
CC Q16656-4; Q9UPM6: LHX6; NbExp=3; IntAct=EBI-11742836, EBI-10258746;
CC Q16656-4; P61968: LMO4; NbExp=3; IntAct=EBI-11742836, EBI-2798728;
CC Q16656-4; Q14764: MVP; NbExp=3; IntAct=EBI-11742836, EBI-2816254;
CC Q16656-4; O14561: NDUFAB1; NbExp=3; IntAct=EBI-11742836, EBI-1246261;
CC Q16656-4; Q495U3: PANX2; NbExp=3; IntAct=EBI-11742836, EBI-17242559;
CC Q16656-4; Q7Z3K3: POGZ; NbExp=7; IntAct=EBI-11742836, EBI-1389308;
CC Q16656-4; Q8N1D0-2: SLC22A18AS; NbExp=3; IntAct=EBI-11742836, EBI-12829638;
CC Q16656-4; Q02086-2: SP2; NbExp=3; IntAct=EBI-11742836, EBI-9088579;
CC Q16656-4; Q02446: SP4; NbExp=3; IntAct=EBI-11742836, EBI-10198587;
CC Q16656-4; Q99619: SPSB2; NbExp=3; IntAct=EBI-11742836, EBI-2323209;
CC Q16656-4; Q8NEQ6: SRARP; NbExp=3; IntAct=EBI-11742836, EBI-17858294;
CC Q16656-4; Q9Y4I5-2: TESMIN; NbExp=3; IntAct=EBI-11742836, EBI-12840664;
CC Q16656-4; Q6ZNM6: TEX43; NbExp=3; IntAct=EBI-11742836, EBI-18115728;
CC Q16656-4; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-11742836, EBI-74615;
CC Q16656-4; Q12933: TRAF2; NbExp=3; IntAct=EBI-11742836, EBI-355744;
CC Q16656-4; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-11742836, EBI-17716262;
CC Q16656-4; Q14119: VEZF1; NbExp=3; IntAct=EBI-11742836, EBI-11980193;
CC Q16656-4; O95789-4: ZMYM6; NbExp=3; IntAct=EBI-11742836, EBI-12949277;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Long;
CC IsoId=Q16656-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q16656-2; Sequence=VSP_003598;
CC Name=3;
CC IsoId=Q16656-3; Sequence=VSP_054330;
CC Name=4;
CC IsoId=Q16656-4; Sequence=VSP_054331;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with strongest expression in
CC skeletal muscle.
CC -!- PTM: Phosphorylation enhances DNA binding.
CC {ECO:0000269|PubMed:9228045}.
CC -!- SIMILARITY: Belongs to the NRF1/Ewg family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NRF1ID44233ch7q32.html";
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DR EMBL; L22454; AAA16918.1; -; mRNA.
DR EMBL; U02683; AAA21647.1; -; mRNA.
DR EMBL; U18383; AAA79013.1; -; Genomic_DNA.
DR EMBL; U18375; AAA79013.1; JOINED; Genomic_DNA.
DR EMBL; U18376; AAA79013.1; JOINED; Genomic_DNA.
DR EMBL; U18377; AAA79013.1; JOINED; Genomic_DNA.
DR EMBL; U18378; AAA79013.1; JOINED; Genomic_DNA.
DR EMBL; U18379; AAA79013.1; JOINED; Genomic_DNA.
DR EMBL; U18380; AAA79013.1; JOINED; Genomic_DNA.
DR EMBL; U18381; AAA79013.1; JOINED; Genomic_DNA.
DR EMBL; U18382; AAA79013.1; JOINED; Genomic_DNA.
DR EMBL; EU159452; ABV90872.1; -; mRNA.
DR EMBL; AK290891; BAF83580.1; -; mRNA.
DR EMBL; AK293351; BAG56867.1; -; mRNA.
DR EMBL; AC078846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236950; EAL24100.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83728.1; -; Genomic_DNA.
DR EMBL; BC016925; AAH16925.1; -; mRNA.
DR CCDS; CCDS5813.2; -. [Q16656-1]
DR CCDS; CCDS78273.1; -. [Q16656-4]
DR PIR; A54868; A54868.
DR RefSeq; NP_001035199.1; NM_001040110.1. [Q16656-1]
DR RefSeq; NP_001280092.1; NM_001293163.1. [Q16656-4]
DR RefSeq; NP_001280093.1; NM_001293164.1. [Q16656-3]
DR RefSeq; NP_005002.3; NM_005011.4. [Q16656-1]
DR AlphaFoldDB; Q16656; -.
DR BioGRID; 110955; 66.
DR DIP; DIP-56958N; -.
DR IntAct; Q16656; 52.
DR MINT; Q16656; -.
DR STRING; 9606.ENSP00000376924; -.
DR GlyGen; Q16656; 7 sites, 2 O-linked glycans (7 sites).
DR iPTMnet; Q16656; -.
DR PhosphoSitePlus; Q16656; -.
DR BioMuta; NRF1; -.
DR DMDM; 12643732; -.
DR EPD; Q16656; -.
DR jPOST; Q16656; -.
DR MassIVE; Q16656; -.
DR MaxQB; Q16656; -.
DR PaxDb; Q16656; -.
DR PeptideAtlas; Q16656; -.
DR PRIDE; Q16656; -.
DR ProteomicsDB; 3895; -.
DR ProteomicsDB; 61015; -. [Q16656-1]
DR ProteomicsDB; 61016; -. [Q16656-2]
DR ProteomicsDB; 75975; -.
DR Antibodypedia; 17908; 477 antibodies from 37 providers.
DR DNASU; 4899; -.
DR Ensembl; ENST00000223190.8; ENSP00000223190.4; ENSG00000106459.15. [Q16656-1]
DR Ensembl; ENST00000311967.6; ENSP00000309826.2; ENSG00000106459.15. [Q16656-4]
DR Ensembl; ENST00000353868.5; ENSP00000342351.5; ENSG00000106459.15. [Q16656-4]
DR Ensembl; ENST00000393230.6; ENSP00000376922.2; ENSG00000106459.15. [Q16656-1]
DR Ensembl; ENST00000393232.6; ENSP00000376924.1; ENSG00000106459.15. [Q16656-1]
DR GeneID; 4899; -.
DR KEGG; hsa:4899; -.
DR MANE-Select; ENST00000393232.6; ENSP00000376924.1; NM_005011.5; NP_005002.3.
DR UCSC; uc003voz.4; human. [Q16656-1]
DR CTD; 4899; -.
DR DisGeNET; 4899; -.
DR GeneCards; NRF1; -.
DR HGNC; HGNC:7996; NRF1.
DR HPA; ENSG00000106459; Low tissue specificity.
DR MIM; 600879; gene.
DR neXtProt; NX_Q16656; -.
DR OpenTargets; ENSG00000106459; -.
DR PharmGKB; PA31775; -.
DR VEuPathDB; HostDB:ENSG00000106459; -.
DR eggNOG; ENOG502QTK1; Eukaryota.
DR GeneTree; ENSGT00390000006835; -.
DR HOGENOM; CLU_018156_3_1_1; -.
DR InParanoid; Q16656; -.
DR OMA; EVEPSWA; -.
DR PhylomeDB; Q16656; -.
DR TreeFam; TF105308; -.
DR PathwayCommons; Q16656; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR SignaLink; Q16656; -.
DR SIGNOR; Q16656; -.
DR BioGRID-ORCS; 4899; 800 hits in 1119 CRISPR screens.
DR ChiTaRS; NRF1; human.
DR GeneWiki; NRF1; -.
DR GenomeRNAi; 4899; -.
DR Pharos; Q16656; Tbio.
DR PRO; PR:Q16656; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q16656; protein.
DR Bgee; ENSG00000106459; Expressed in cerebellar hemisphere and 147 other tissues.
DR ExpressionAtlas; Q16656; baseline and differential.
DR Genevisible; Q16656; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:AgBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR039142; NRF1/Ewg.
DR InterPro; IPR019526; Nrf1_activation-bd.
DR InterPro; IPR019525; Nrf1_NLS/DNA-bd_dimer.
DR PANTHER; PTHR20338; PTHR20338; 1.
DR Pfam; PF10492; Nrf1_activ_bdg; 1.
DR Pfam; PF10491; Nrf1_DNA-bind; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..503
FT /note="Nuclear respiratory factor 1"
FT /id="PRO_0000100208"
FT DNA_BIND 109..305
FT REGION 1..78
FT /note="Dimerization"
FT REGION 36..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..476
FT /note="Required for transcriptional activation"
FT MOTIF 88..116
FT /note="Nuclear localization signal"
FT MOD_RES 39
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:9228045"
FT MOD_RES 44
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:9228045"
FT MOD_RES 46
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:9228045"
FT MOD_RES 47
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:9228045"
FT MOD_RES 52
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:9228045"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..161
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054330"
FT VAR_SEQ 256..321
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_003598"
FT VAR_SEQ 449
FT /note="N -> NGLFMADRAGRKWILTDKAT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_054331"
FT CONFLICT 322
FT /note="V -> VV (in Ref. 3; AAA79013)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="T -> A (in Ref. 5; BAG56867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 53541 MW; F31C358278371929 CRC64;
MEEHGVTQTE HMATIEAHAV AQQVQQVHVA TYTEHSMLSA DEDSPSSPED TSYDDSDILN
STAADEVTAH LAAAGPVGMA AAAAVATGKK RKRPHVFESN PSIRKRQQTR LLRKLRATLD
EYTTRVGQQA IVLCISPSKP NPVFKVFGAA PLENVVRKYK SMILEDLESA LAEHAPAPQE
VNSELPPLTI DGIPVSVDKM TQAQLRAFIP EMLKYSTGRG KPGWGKESCK PIWWPEDIPW
ANVRSDVRTE EQKQRVSWTQ ALRTIVKNCY KQHGREDLLY AFEDQQTQTQ ATATHSIAHL
VPSQTVVQTF SNPDGTVSLI QVGTGATVAT LADASELPTT VTVAQVNYSA VADGEVEQNW
ATLQGGEMTI QTTQASEATQ AVASLAEAAV AASQEMQQGA TVTMALNSEA AAHAVATLAE
ATLQGGGQIV LSGETAAAVG ALTGVQDANG LVQIPVSMYQ TVVTSLAQGN GPVQVAMAPV
TTRISDSAVT MDGQAVEVVT LEQ
