MAFG_HUMAN
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 03-AUG-2022, entry version 188.
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:8932385, PubMed:9421508,
CC PubMed:11154691). Small Maf proteins heterodimerize with Fos and may
CC act 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:8932385, PubMed:9421508, PubMed:11154691).
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=6; IntAct=EBI-713514, EBI-1263541;
CC O15525; Q9BYV9: BACH2; NbExp=5; 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=4; IntAct=EBI-713514, EBI-2804436;
CC O15525; Q14494-2: NFE2L1; NbExp=3; IntAct=EBI-713514, EBI-11745778;
CC O15525; Q16236: NFE2L2; NbExp=12; IntAct=EBI-713514, EBI-2007911;
CC O15525; Q9Y4A8: NFE2L3; NbExp=5; 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}.
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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 AlphaFoldDB; O15525; -.
DR SMR; O15525; -.
DR BioGRID; 110272; 39.
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; 26.
DR MINT; O15525; -.
DR STRING; 9606.ENSP00000350369; -.
DR iPTMnet; O15525; -.
DR PhosphoSitePlus; O15525; -.
DR BioMuta; MAFG; -.
DR EPD; O15525; -.
DR jPOST; O15525; -.
DR MassIVE; O15525; -.
DR MaxQB; O15525; -.
DR PaxDb; O15525; -.
DR PeptideAtlas; O15525; -.
DR PRIDE; O15525; -.
DR ProteomicsDB; 48725; -.
DR Antibodypedia; 19851; 131 antibodies from 26 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 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; IREQEHP; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; O15525; -.
DR TreeFam; TF325689; -.
DR PathwayCommons; O15525; -.
DR Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; O15525; -.
DR SIGNOR; O15525; -.
DR BioGRID-ORCS; 4097; 49 hits in 1093 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 183 other tissues.
DR ExpressionAtlas; O15525; baseline and differential.
DR Genevisible; O15525; HS.
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:0046982; F:protein heterodimerization activity; IEA:InterPro.
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; IC: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:0030641; P:regulation of cellular pH; 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 InterPro; IPR004827; bZIP.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR028551; MafG.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR InterPro; IPR024874; Transcription_factor_Maf_fam.
DR PANTHER; PTHR10129; PTHR10129; 1.
DR PANTHER; PTHR10129:SF15; PTHR10129:SF15; 1.
DR Pfam; PF03131; bZIP_Maf; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW 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"
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
