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Transcription factor MafG (V-maf musculoaponeurotic fibrosarcoma oncogene homolog G) (hMAF)

 MAFG_HUMAN              Reviewed;         162 AA.
O15525;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
05-DEC-2018, entry version 166.
RecName: Full=Transcription factor MafG;
AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog G;
AltName: Full=hMAF;
Name=MAFG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9195958; DOI=10.1074/jbc.272.26.16490;
Marini M.G., Chan K., Casula L., Kan Y.W., Cao A., Moi P.;
"hMAF, a small human transcription factor that heterodimerizes
specifically with Nrf1 and Nrf2.";
J. Biol. Chem. 272:16490-16497(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Muscle;
PubMed=9166829;
Blank V., Kim M.J., Andrews N.C.;
"Human MafG is a functional partner for p45 NF-E2 in activating globin
gene expression.";
Blood 89:3925-3935(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Muscle;
PubMed=9286713; DOI=10.1006/geno.1997.4847;
Blank V., Knoll J.H.M., Andrews N.C.;
"Molecular characterization and localization of the human MAFG gene.";
Genomics 44:147-149(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9150357; DOI=10.1038/sj.onc.1201024;
Toki T., Itoh J., Kitazawa J., Arai K., Hatakeyama K., Akasaka J.,
Igarashi K., Nomura N., Yokoyama M., Yamamoto M., Ito E.;
"Human small Maf proteins form heterodimers with CNC family
transcription factors and recognize the NF-E2 motif.";
Oncogene 14:1901-1910(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
Ito E., Toki T.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, DNA-BINDING, AND INTERACTION WITH NFE2L1.
PubMed=8932385;
Johnsen O., Skammelsrud N., Luna L., Nishizawa M., Prydz H.,
Kolstoe A.B.;
"Small Maf proteins interact with the human transcription factor
TCF11/Nrf1/LCR-F1.";
Nucleic Acids Res. 24:4289-4297(1996).
[8]
FUNCTION, DNA-BINDING, AND INTERACTION WITH NFE2L1.
PubMed=9421508;
Johnsen O., Murphy P., Prydz H., Kolsto A.B.;
"Interaction of the CNC-bZIP factor TCF11/LCR-F1/Nrf1 with MafG:
binding-site selection and regulation of transcription.";
Nucleic Acids Res. 26:512-520(1998).
[9]
ACETYLATION AT LYS-53; LYS-60; LYS-71 AND LYS-76, FUNCTION,
INTERACTION WITH NFE2 AND CREBBP, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF LYS-53; LYS-60; LYS-71 AND LYS-76.
PubMed=11154691; DOI=10.1074/jbc.M007846200;
Hung H.-L., Kim A.Y., Hong W., Rakowski C., Blobel G.A.;
"Stimulation of NF-E2 DNA binding by CREB-binding protein (CBP)-
mediated acetylation.";
J. Biol. Chem. 276:10715-10721(2001).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[13]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Since they lack a putative transactivation domain, the
small Mafs behave as transcriptional repressors when they dimerize
among themselves (PubMed:11154691). However, they seem to serve as
transcriptional activators by dimerizing with other (usually
larger) basic-zipper proteins, such as NFE2, NFE2L1 and NFE2L2,
and recruiting them to specific DNA-binding sites (PubMed:8932385,
PubMed:9421508, PubMed:11154691). Small Maf proteins
heterodimerize with Fos and may act as competitive repressors of
the NFE2L2 transcription factor (PubMed:11154691). Transcription
factor, component of erythroid-specific transcription factor
NFE2L2 (PubMed:11154691). Activates globin gene expression when
associated with NFE2L2 (PubMed:11154691). May be involved in
signal transduction of extracellular H(+) (By similarity).
{ECO:0000250|UniProtKB:Q76MX4, ECO:0000269|PubMed:11154691,
ECO:0000269|PubMed:8932385, ECO:0000269|PubMed:9421508}.
-!- SUBUNIT: Homodimer or heterodimer. Homodimerization leads to
transcriptional repression. Forms high affinity heterodimers with
members of the CNC-bZIP family such as NFE2, NFE2L1/NRF1,
NFE2L2/NRF2 and NFE2L3/NRF3 (PubMed:8932385, PubMed:9421508,
PubMed:11154691). Interacts with CREBBP; the interaction leads to
acetylation of the basic region of MAFG and stimulation of NFE2
transcriptional activity through increased DNA binding.
{ECO:0000269|PubMed:11154691, ECO:0000269|PubMed:8932385,
ECO:0000269|PubMed:9421508}.
-!- INTERACTION:
O14867:BACH1; NbExp=3; IntAct=EBI-713514, EBI-1263541;
P0C746:HBZ (xeno); NbExp=3; IntAct=EBI-713514, EBI-10890294;
Q14494:NFE2L1; NbExp=2; IntAct=EBI-713514, EBI-2804436;
Q16236:NFE2L2; NbExp=5; IntAct=EBI-713514, EBI-2007911;
Q9Y4A8:NFE2L3; NbExp=2; IntAct=EBI-713514, EBI-10890629;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00978, ECO:0000269|PubMed:11154691}.
-!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Also
expressed in heart and brain.
-!- PTM: Acetylated in erythroid cells by CREB-binding protein (CBP).
Acetylation augments the DNA-binding activity of NFE2, but has no
effect on binding NFE2. {ECO:0000269|PubMed:11154691}.
-!- PTM: Sumoylation at Lys-14 is required for active transcriptional
repression. {ECO:0000250|UniProtKB:O54790}.
-!- SIMILARITY: Belongs to the bZIP family. Maf subfamily.
{ECO:0000305}.
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EMBL; Y11514; CAA72284.1; -; mRNA.
EMBL; U84249; AAC51737.1; -; mRNA.
EMBL; AF059195; AAC14427.1; -; mRNA.
EMBL; BC012327; AAH12327.1; -; mRNA.
CCDS; CCDS11793.1; -.
RefSeq; NP_002350.1; NM_002359.3.
RefSeq; NP_116100.2; NM_032711.3.
RefSeq; XP_011521880.1; XM_011523578.1.
UniGene; Hs.252229; -.
UniGene; Hs.744113; -.
ProteinModelPortal; O15525; -.
SMR; O15525; -.
BioGrid; 110272; 30.
ELM; O15525; -.
IntAct; O15525; 17.
MINT; O15525; -.
STRING; 9606.ENSP00000350369; -.
iPTMnet; O15525; -.
PhosphoSitePlus; O15525; -.
BioMuta; MAFG; -.
EPD; O15525; -.
MaxQB; O15525; -.
PaxDb; O15525; -.
PeptideAtlas; O15525; -.
PRIDE; O15525; -.
ProteomicsDB; 48725; -.
DNASU; 4097; -.
Ensembl; ENST00000357736; ENSP00000350369; ENSG00000197063.
Ensembl; ENST00000392366; ENSP00000376173; ENSG00000197063.
GeneID; 4097; -.
KEGG; hsa:4097; -.
UCSC; uc002kcm.4; human.
CTD; 4097; -.
DisGeNET; 4097; -.
EuPathDB; HostDB:ENSG00000197063.10; -.
GeneCards; MAFG; -.
HGNC; HGNC:6781; MAFG.
HPA; CAB025573; -.
MIM; 602020; gene.
neXtProt; NX_O15525; -.
OpenTargets; ENSG00000197063; -.
PharmGKB; PA30539; -.
eggNOG; ENOG410ISHW; Eukaryota.
eggNOG; ENOG4111HFT; LUCA.
GeneTree; ENSGT00940000160070; -.
HOGENOM; HOG000045475; -.
HOVERGEN; HBG001725; -.
InParanoid; O15525; -.
KO; K09037; -.
OMA; ITASMGP; -.
OrthoDB; EOG091G0H46; -.
PhylomeDB; O15525; -.
TreeFam; TF325689; -.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SIGNOR; O15525; -.
ChiTaRS; MAFG; human.
GeneWiki; MAFG; -.
GenomeRNAi; 4097; -.
PRO; PR:O15525; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000197063; Expressed in 208 organ(s), highest expression level in amniotic fluid.
CleanEx; HS_MAFG; -.
ExpressionAtlas; O15525; baseline and differential.
Genevisible; O15525; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISM:NTNU_SB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0001077; F:proximal promoter DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0030534; P:adult behavior; IEA:Ensembl.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0030641; P:regulation of cellular pH; IEA:Ensembl.
GO; GO:0045604; P:regulation of epidermal cell differentiation; IBA:GO_Central.
InterPro; IPR004827; bZIP.
InterPro; IPR004826; bZIP_Maf.
InterPro; IPR028551; MafG.
InterPro; IPR008917; TF_DNA-bd_sf.
InterPro; IPR024874; Transciption_factor_Maf_fam.
PANTHER; PTHR10129; PTHR10129; 1.
PANTHER; PTHR10129:SF15; PTHR10129:SF15; 1.
Pfam; PF03131; bZIP_Maf; 1.
SMART; SM00338; BRLZ; 1.
SUPFAM; SSF47454; SSF47454; 1.
PROSITE; PS50217; BZIP; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 162 Transcription factor MafG.
/FTId=PRO_0000076500.
DOMAIN 51 114 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 53 76 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 79 93 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOD_RES 53 53 N6-acetyllysine.
{ECO:0000305|PubMed:11154691}.
MOD_RES 60 60 N6-acetyllysine.
{ECO:0000305|PubMed:11154691}.
MOD_RES 71 71 N6-acetyllysine.
{ECO:0000305|PubMed:11154691}.
MOD_RES 76 76 N6-acetyllysine.
{ECO:0000305|PubMed:11154691}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
MUTAGEN 53 53 K->A: Abolishes acetylation. Has no
effect on binding to NFE2 but impairs the
DNA binding and transcriptional
activities of NFE2; when associated with
A-60; A-71 and A-76.
{ECO:0000269|PubMed:11154691}.
MUTAGEN 60 60 K->A: Abolishes acetylation. Has no
effect on binding to NFE2 but impairs the
DNA binding and transcriptional
activities of NFE2; when associated with
A-53; A-71 and A-76.
{ECO:0000269|PubMed:11154691}.
MUTAGEN 71 71 K->A: Abolishes acetylation. Has no
effect on binding to NFE2 but impairs the
DNA binding and transcriptional
activities of NFE2; when associated with
A-53; A-60; and A-76.
{ECO:0000269|PubMed:11154691}.
MUTAGEN 76 76 K->A: Abolishes acetylation. Has no
effect on binding to NFE2 but impairs the
DNA binding and transcriptional
activities of NFE2; when associated with
A-53; A-60 and A-71.
{ECO:0000269|PubMed:11154691}.
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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