ID MAFG_HUMAN Reviewed; 162 AA. AC O15525; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 02-OCT-2024, entry version 200. DE RecName: Full=Transcription factor MafG; DE AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog G; DE AltName: Full=hMAF; GN Name=MAFG; 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]. RX PubMed=9195958; DOI=10.1074/jbc.272.26.16490; RA Marini M.G., Chan K., Casula L., Kan Y.W., Cao A., Moi P.; RT "hMAF, a small human transcription factor that heterodimerizes specifically RT with Nrf1 and Nrf2."; RL J. Biol. Chem. 272:16490-16497(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Muscle; RX PubMed=9166829; RA Blank V., Kim M.J., Andrews N.C.; RT "Human MafG is a functional partner for p45 NF-E2 in activating globin gene RT expression."; RL Blood 89:3925-3935(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Muscle; RX PubMed=9286713; DOI=10.1006/geno.1997.4847; RA Blank V., Knoll J.H.M., Andrews N.C.; RT "Molecular characterization and localization of the human MAFG gene."; RL Genomics 44:147-149(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9150357; DOI=10.1038/sj.onc.1201024; RA Toki T., Itoh J., Kitazawa J., Arai K., Hatakeyama K., Akasaka J., RA Igarashi K., Nomura N., Yokoyama M., Yamamoto M., Ito E.; RT "Human small Maf proteins form heterodimers with CNC family transcription RT factors and recognize the NF-E2 motif."; RL Oncogene 14:1901-1910(1997). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Ito E., Toki T.; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [7] RP FUNCTION, DNA-BINDING, AND INTERACTION WITH NFE2L1. RX PubMed=8932385; DOI=10.1093/nar/24.21.4289; RA Johnsen O., Skammelsrud N., Luna L., Nishizawa M., Prydz H., Kolstoe A.B.; RT "Small Maf proteins interact with the human transcription factor RT TCF11/Nrf1/LCR-F1."; RL Nucleic Acids Res. 24:4289-4297(1996). RN [8] RP FUNCTION, DNA-BINDING, AND INTERACTION WITH NFE2L1. RX PubMed=9421508; DOI=10.1093/nar/26.2.512; RA Johnsen O., Murphy P., Prydz H., Kolsto A.B.; RT "Interaction of the CNC-bZIP factor TCF11/LCR-F1/Nrf1 with MafG: binding- RT site selection and regulation of transcription."; RL Nucleic Acids Res. 26:512-520(1998). RN [9] RP ACETYLATION AT LYS-53; LYS-60; LYS-71 AND LYS-76, FUNCTION, INTERACTION RP WITH NFE2 AND CREBBP, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-53; RP LYS-60; LYS-71 AND LYS-76. RX PubMed=11154691; DOI=10.1074/jbc.m007846200; RA Hung H.-L., Kim A.Y., Hong W., Rakowski C., Blobel G.A.; RT "Stimulation of NF-E2 DNA binding by CREB-binding protein (CBP)-mediated RT acetylation."; RL J. Biol. Chem. 276:10715-10721(2001). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY RP 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY RP MASS SPECTROMETRY [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 [12] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [13] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14, 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: Since they lack a putative transactivation domain, the small CC Mafs behave as transcriptional repressors when they dimerize among CC themselves (PubMed:11154691). However, they seem to serve as CC transcriptional activators by dimerizing with other (usually larger) CC basic-zipper proteins, such as NFE2, NFE2L1 and NFE2L2, and recruiting CC them to specific DNA-binding sites (PubMed:11154691, PubMed:8932385, CC PubMed:9421508). Small Maf proteins heterodimerize with Fos and may act CC as competitive repressors of the NFE2L2 transcription factor CC (PubMed:11154691). Transcription factor, component of erythroid- CC specific transcription factor NFE2L2 (PubMed:11154691). Activates CC globin gene expression when associated with NFE2L2 (PubMed:11154691). CC May be involved in signal transduction of extracellular H(+) (By CC similarity). {ECO:0000250|UniProtKB:Q76MX4, CC ECO:0000269|PubMed:11154691, ECO:0000269|PubMed:8932385, CC ECO:0000269|PubMed:9421508}. CC -!- SUBUNIT: Homodimer or heterodimer. Homodimerization leads to CC transcriptional repression. Forms high affinity heterodimers with CC members of the CNC-bZIP family such as NFE2, NFE2L1/NRF1, NFE2L2/NRF2 CC and NFE2L3/NRF3 (PubMed:11154691, PubMed:8932385, PubMed:9421508). CC Interacts with CREBBP; the interaction leads to acetylation of the CC basic region of MAFG and stimulation of NFE2 transcriptional activity CC through increased DNA binding. {ECO:0000269|PubMed:11154691, CC ECO:0000269|PubMed:8932385, ECO:0000269|PubMed:9421508}. CC -!- INTERACTION: CC O15525; O14867: BACH1; NbExp=8; IntAct=EBI-713514, EBI-1263541; CC O15525; Q9BYV9: BACH2; NbExp=6; IntAct=EBI-713514, EBI-1642333; CC O15525; Q9NR55: BATF3; NbExp=2; IntAct=EBI-713514, EBI-10312707; CC O15525; Q9ULX9: MAFF; NbExp=2; IntAct=EBI-713514, EBI-721128; CC O15525; O15525: MAFG; NbExp=2; IntAct=EBI-713514, EBI-713514; CC O15525; Q14494: NFE2L1; NbExp=5; IntAct=EBI-713514, EBI-2804436; CC O15525; Q14494-2: NFE2L1; NbExp=3; IntAct=EBI-713514, EBI-11745778; CC O15525; Q16236: NFE2L2; NbExp=16; IntAct=EBI-713514, EBI-2007911; CC O15525; Q9Y4A8: NFE2L3; NbExp=6; IntAct=EBI-713514, EBI-10890629; CC O15525; Q16649: NFIL3; NbExp=2; IntAct=EBI-713514, EBI-3951858; CC O15525; P0C746: HBZ; Xeno; NbExp=3; IntAct=EBI-713514, EBI-10890294; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, CC ECO:0000269|PubMed:11154691}. CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Also expressed CC in heart and brain. CC -!- PTM: Acetylated in erythroid cells by CREB-binding protein (CBP). CC Acetylation augments the DNA-binding activity of NFE2, but has no CC effect on binding NFE2. {ECO:0000269|PubMed:11154691}. CC -!- PTM: Sumoylation at Lys-14 is required for active transcriptional CC repression. {ECO:0000250|UniProtKB:O54790}. CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y11514; CAA72284.1; -; mRNA. DR EMBL; U84249; AAC51737.1; -; mRNA. DR EMBL; AF059195; AAC14427.1; -; mRNA. DR EMBL; BC012327; AAH12327.1; -; mRNA. DR CCDS; CCDS11793.1; -. DR RefSeq; NP_002350.1; NM_002359.3. DR RefSeq; NP_116100.2; NM_032711.3. DR RefSeq; XP_011521880.1; XM_011523578.1. DR PDB; 7X5E; X-ray; 2.30 A; A/E=21-123. DR PDB; 7X5F; X-ray; 2.60 A; A/E=21-123. DR PDB; 7X5G; X-ray; 2.30 A; A/E=21-123. DR PDBsum; 7X5E; -. DR PDBsum; 7X5F; -. DR PDBsum; 7X5G; -. DR AlphaFoldDB; O15525; -. DR SMR; O15525; -. DR BioGRID; 110272; 42. DR ComplexPortal; CPX-2485; bZIP transcription factor complex, BACH2-MAFG. DR ComplexPortal; CPX-2872; bZIP transcription factor complex, BACH1-MAFG. DR ComplexPortal; CPX-6481; bZIP transcription factor complex, ATF3-MAFG. DR ComplexPortal; CPX-7105; bZIP transcription factor complex, BATF3-MAFG. DR ELM; O15525; -. DR IntAct; O15525; 29. DR MINT; O15525; -. DR STRING; 9606.ENSP00000350369; -. DR GlyGen; O15525; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O15525; -. DR PhosphoSitePlus; O15525; -. DR BioMuta; MAFG; -. DR jPOST; O15525; -. DR MassIVE; O15525; -. DR PaxDb; 9606-ENSP00000350369; -. DR PeptideAtlas; O15525; -. DR ProteomicsDB; 48725; -. DR Pumba; O15525; -. DR Antibodypedia; 19851; 156 antibodies from 27 providers. DR DNASU; 4097; -. DR Ensembl; ENST00000357736.9; ENSP00000350369.4; ENSG00000197063.11. DR Ensembl; ENST00000392366.7; ENSP00000376173.3; ENSG00000197063.11. DR GeneID; 4097; -. DR KEGG; hsa:4097; -. DR MANE-Select; ENST00000357736.9; ENSP00000350369.4; NM_002359.4; NP_002350.1. DR UCSC; uc002kcm.4; human. DR AGR; HGNC:6781; -. DR CTD; 4097; -. DR DisGeNET; 4097; -. DR GeneCards; MAFG; -. DR HGNC; HGNC:6781; MAFG. DR HPA; ENSG00000197063; Low tissue specificity. DR MIM; 602020; gene. DR neXtProt; NX_O15525; -. DR OpenTargets; ENSG00000197063; -. DR PharmGKB; PA30539; -. DR VEuPathDB; HostDB:ENSG00000197063; -. DR eggNOG; KOG4196; Eukaryota. DR GeneTree; ENSGT00940000160070; -. DR HOGENOM; CLU_112948_0_0_1; -. DR InParanoid; O15525; -. DR OMA; QHSRYRF; -. DR OrthoDB; 2958941at2759; -. DR PhylomeDB; O15525; -. DR TreeFam; TF325689; -. DR PathwayCommons; O15525; -. DR Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2. DR Reactome; R-HSA-9818028; NFE2L2 regulates pentose phosphate pathway genes. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; O15525; -. DR SIGNOR; O15525; -. DR BioGRID-ORCS; 4097; 50 hits in 1165 CRISPR screens. DR ChiTaRS; MAFG; human. DR GeneWiki; MAFG; -. DR GenomeRNAi; 4097; -. DR Pharos; O15525; Tbio. DR PRO; PR:O15525; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; O15525; protein. DR Bgee; ENSG00000197063; Expressed in secondary oocyte and 185 other cell types or tissues. DR ExpressionAtlas; O15525; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl. DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:ProtInc. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0030534; P:adult behavior; IEA:Ensembl. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0045604; P:regulation of epidermal cell differentiation; IBA:GO_Central. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd14717; bZIP_Maf_small; 1. DR Gene3D; 1.20.5.170; -; 1. DR InterPro; IPR004827; bZIP. DR InterPro; IPR004826; bZIP_Maf. DR InterPro; IPR046347; bZIP_sf. DR InterPro; IPR008917; TF_DNA-bd_sf. DR InterPro; IPR024874; Transcription_factor_Maf_fam. DR PANTHER; PTHR10129; TRANSCRIPTION FACTOR MAF; 1. DR PANTHER; PTHR10129:SF15; TRANSCRIPTION FACTOR MAFG; 1. DR Pfam; PF03131; bZIP_Maf; 1. DR SMART; SM00338; BRLZ; 1. DR SUPFAM; SSF47454; A DNA-binding domain in eukaryotic transcription factors; 1. DR SUPFAM; SSF57959; Leucine zipper domain; 1. DR PROSITE; PS50217; BZIP; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; DNA-binding; Isopeptide bond; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; Repressor; KW Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1..162 FT /note="Transcription factor MafG" FT /id="PRO_0000076500" FT DOMAIN 51..114 FT /note="bZIP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 53..76 FT /note="Basic motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT REGION 79..93 FT /note="Leucine-zipper" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978" FT MOD_RES 53 FT /note="N6-acetyllysine" FT /evidence="ECO:0000305|PubMed:11154691" FT MOD_RES 60 FT /note="N6-acetyllysine" FT /evidence="ECO:0000305|PubMed:11154691" FT MOD_RES 71 FT /note="N6-acetyllysine" FT /evidence="ECO:0000305|PubMed:11154691" FT MOD_RES 76 FT /note="N6-acetyllysine" FT /evidence="ECO:0000305|PubMed:11154691" FT MOD_RES 124 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 14 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT CROSSLNK 14 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT MUTAGEN 53 FT /note="K->A: Abolishes acetylation. Has no effect on FT binding to NFE2 but impairs the DNA binding and FT transcriptional activities of NFE2; when associated with A- FT 60; A-71 and A-76." FT /evidence="ECO:0000269|PubMed:11154691" FT MUTAGEN 60 FT /note="K->A: Abolishes acetylation. Has no effect on FT binding to NFE2 but impairs the DNA binding and FT transcriptional activities of NFE2; when associated with A- FT 53; A-71 and A-76." FT /evidence="ECO:0000269|PubMed:11154691" FT MUTAGEN 71 FT /note="K->A: Abolishes acetylation. Has no effect on FT binding to NFE2 but impairs the DNA binding and FT transcriptional activities of NFE2; when associated with A- FT 53; A-60; and A-76." FT /evidence="ECO:0000269|PubMed:11154691" FT MUTAGEN 76 FT /note="K->A: Abolishes acetylation. Has no effect on FT binding to NFE2 but impairs the DNA binding and FT transcriptional activities of NFE2; when associated with A- FT 53; A-60 and A-71." FT /evidence="ECO:0000269|PubMed:11154691" FT HELIX 26..30 FT /evidence="ECO:0007829|PDB:7X5E" FT HELIX 34..37 FT /evidence="ECO:0007829|PDB:7X5E" FT HELIX 38..40 FT /evidence="ECO:0007829|PDB:7X5G" FT HELIX 46..120 FT /evidence="ECO:0007829|PDB:7X5E" SQ SEQUENCE 162 AA; 17850 MW; E49F1FBA230F8D30 CRC64; MTTPNKGNKA LKVKREPGEN GTSLTDEELV TMSVRELNQH LRGLSKEEIV QLKQRRRTLK NRGYAASCRV KRVTQKEELE KQKAELQQEV EKLASENASM KLELDALRSK YEALQTFART VARSPVAPAR GPLAAGLGPL VPGKVAATSV ITIVKSKTDA RS //