O15525 (MAFG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor MafG

Alternative name(s):
V-maf musculoaponeurotic fibrosarcoma oncogene homolog G
hMAF

Gene names

Name:

MAFG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	162 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves. However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins and recruiting them to specific DNA-binding sites. Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor. Transcription factor, component of erythroid-specific transcription factor NF-E2. Activates globin gene expression when associated with NF-E2. May be involved in signal transduction of extracellular H+ By similarity. Ref.7
Subunit structure	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. Interacts with NFE2; the interaction results in tranactivation activation. Interacts with CREBBP; the interaction leads to acetylation of the basic region of MAFG and stimulation of NFE2 transcriptional activity through increased DNA binding. Ref.7
Subcellular location	Nucleus Ref.7.
Tissue specificity	Highly expressed in skeletal muscle. Also expressed in heart and brain.
Post-translational modification	Acetylated in erythroid cells by CREB-binding protein (CBP). Acetylation augments the DNA-binding activity of NFE2, but has no effect on binding NFE2. Sumoylation at Lys-14 is required for active transcriptional repression By similarity.
Sequence similarities	Belongs to the bZIP family. Maf subfamily. Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adult behavior Inferred from electronic annotation. Source: Compara blood coagulation Traceable author statement. Source: Reactome in utero embryonic development Inferred from electronic annotation. Source: Compara regulation of cell proliferation Inferred from electronic annotation. Source: Compara regulation of cellular pH Inferred from electronic annotation. Source: Compara regulation of epidermal cell differentiation Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Non-traceable author statement Ref.3. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 162	162	Transcription factor MafG		PRO_0000076500
Regions
	Domain	51 – 114	64	bZIP
	Region	53 – 76	24	Basic motif By similarity
	Region	79 – 93	15	Leucine-zipper By similarity
Amino acid modifications
	Modified residue	53	1	N6-acetyllysine Probable
	Modified residue	60	1	N6-acetyllysine Probable
	Modified residue	71	1	N6-acetyllysine Probable
	Modified residue	76	1	N6-acetyllysine Probable
	Modified residue	124	1	Phosphoserine Ref.8
	Cross-link	14		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Experimental info
	Mutagenesis	53	1	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. Ref.7
	Mutagenesis	60	1	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. Ref.7
	Mutagenesis	71	1	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. Ref.7
	Mutagenesis	76	1	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. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	O15525 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: E49F1FBA230F8D30	FASTA	162	17,850
	10 20 30 40 50 60 MTTPNKGNKA LKVKREPGEN GTSLTDEELV TMSVRELNQH LRGLSKEEIV QLKQRRRTLK 70 80 90 100 110 120 NRGYAASCRV KRVTQKEELE KQKAELQQEV EKLASENASM KLELDALRSK YEALQTFART 130 140 150 160 VARSPVAPAR GPLAAGLGPL VPGKVAATSV ITIVKSKTDA RS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"hMAF, a small human transcription factor that heterodimerizes specifically with Nrf1 and Nrf2." Marini M.G., Chan K., Casula L., Kan Y.W., Cao A., Moi P. J. Biol. Chem. 272:16490-16497(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Human MafG is a functional partner for p45 NF-E2 in activating globin gene expression." Blank V., Kim M.J., Andrews N.C. Blood 89:3925-3935(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Muscle.
[3]	"Molecular characterization and localization of the human MAFG gene." Blank V., Knoll J.H.M., Andrews N.C. Genomics 44:147-149(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Muscle.
[4]	"Human small Maf proteins form heterodimers with CNC family transcription factors and recognize the NF-E2 motif." Toki T., Itoh J., Kitazawa J., Arai K., Hatakeyama K., Akasaka J., Igarashi K., Nomura N., Yokoyama M., Yamamoto M., Ito E. Oncogene 14:1901-1910(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	Ito E., Toki T. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[7]	"Stimulation of NF-E2 DNA binding by CREB-binding protein (CBP)-mediated acetylation." Hung H.-L., Kim A.Y., Hong W., Rakowski C., Blobel G.A. J. Biol. Chem. 276:10715-10721(2001) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-53; LYS-60; LYS-71 AND LYS-76, FUNCTION, INTERACTION WITH NFE2 AND CREBBP, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-53; LYS-60; LYS-71 AND LYS-76.
[8]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y11514 mRNA. Translation: CAA72284.1. U84249 mRNA. Translation: AAC51737.1. AF059195 mRNA. Translation: AAC14427.1. BC012327 mRNA. Translation: AAH12327.1.
IPI	IPI00007311.
RefSeq	NP_002350.1. NM_002359.3. NP_116100.2. NM_032711.3.
UniGene	Hs.252229. Hs.731947.
3D structure databases
ProteinModelPortal	O15525.
ModBase	Search...
Protein-protein interaction databases
IntAct	O15525. 11 interactions.
MINT	MINT-1374809.
STRING	9606.ENSP00000350369.
PTM databases
PhosphoSite	O15525.
Proteomic databases
PaxDb	O15525.
PRIDE	O15525.
Protocols and materials databases
DNASU	4097.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000357736; ENSP00000350369; ENSG00000197063. ENST00000392366; ENSP00000376173; ENSG00000197063.
GeneID	4097.
KEGG	hsa:4097.
UCSC	uc002kcm.3. human.
Organism-specific databases
CTD	4097.
GeneCards	GC17M079877.
HGNC	HGNC:6781. MAFG.
HPA	CAB025573.
MIM	602020. gene.
neXtProt	NX_O15525.
PharmGKB	PA30539.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG236209.
HOGENOM	HOG000045475.
HOVERGEN	HBG001725.
InParanoid	O15525.
KO	K09037.
OMA	ITASMGP.
OrthoDB	EOG4C5CKX.
PhylomeDB	O15525.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	O15525.
Bgee	O15525.
CleanEx	HS_MAFG.
Genevestigator	O15525.
GermOnline	ENSG00000197063. Homo sapiens.
Family and domain databases
Gene3D	1.10.880.10. 1 hit.
InterPro	IPR004827. bZIP. IPR004826. bZIP_Maf. IPR008917. Euk_TF_DNA-bd. IPR024874. Transciption_factor_Maf. [Graphical view]
PANTHER	PTHR10129. PTHR10129. 1 hit.
Pfam	PF03131. bZIP_Maf. 1 hit. [Graphical view]
SMART	SM00338. BRLZ. 1 hit. [Graphical view]
SUPFAM	SSF47454. Euk_transcr_DNA. 1 hit.
PROSITE	PS50217. BZIP. 1 hit. PS00036. BZIP_BASIC. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MAFG. human.
GenomeRNAi	4097.
NextBio	16068.
SOURCE	Search...

Entry information

Entry name

MAFG_HUMAN

Accession

Primary (citable) accession number: O15525

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.