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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
 
 
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