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O15525 (MAFG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor MafG
Alternative name(s):
V-maf musculoaponeurotic fibrosarcoma oncogene homolog G
hMAF
Gene names
Name:MAFG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length162 AA.
Sequence statusComplete.
Protein existenceEvidence 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 transactivation 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. Ref.7

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 162162Transcription factor MafG
PRO_0000076500

Regions

Domain51 – 11464bZIP
Region53 – 7624Basic motif By similarity
Region79 – 9315Leucine-zipper By similarity

Amino acid modifications

Modified residue531N6-acetyllysine Probable
Modified residue601N6-acetyllysine Probable
Modified residue711N6-acetyllysine Probable
Modified residue761N6-acetyllysine Probable
Modified residue1241Phosphoserine Ref.8
Cross-link14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Experimental info

Mutagenesis531K → 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
Mutagenesis601K → 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
Mutagenesis711K → 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
Mutagenesis761K → 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 LengthMass (Da)Tools
O15525 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E49F1FBA230F8D30

FASTA16217,850
        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 

« Hide

References

« Hide '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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
RefSeqNP_002350.1. NM_002359.3.
NP_116100.2. NM_032711.3.
UniGeneHs.252229.
Hs.744113.

3D structure databases

ProteinModelPortalO15525.
SMRO15525. Positions 21-111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110272. 32 interactions.
IntActO15525. 11 interactions.
MINTMINT-1374809.
STRING9606.ENSP00000350369.

PTM databases

PhosphoSiteO15525.

Proteomic databases

PaxDbO15525.
PRIDEO15525.

Protocols and materials databases

DNASU4097.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357736; ENSP00000350369; ENSG00000197063.
ENST00000392366; ENSP00000376173; ENSG00000197063.
GeneID4097.
KEGGhsa:4097.
UCSCuc002kcm.3. human.

Organism-specific databases

CTD4097.
GeneCardsGC17M079877.
HGNCHGNC:6781. MAFG.
HPACAB025573.
MIM602020. gene.
neXtProtNX_O15525.
PharmGKBPA30539.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG236209.
HOGENOMHOG000045475.
HOVERGENHBG001725.
InParanoidO15525.
KOK09037.
OMAITASMGP.
OrthoDBEOG7BGHMQ.
PhylomeDBO15525.
TreeFamTF325689.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressO15525.
BgeeO15525.
CleanExHS_MAFG.
GenevestigatorO15525.

Family and domain databases

Gene3D1.10.880.10. 1 hit.
InterProIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR028551. MafG.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view]
PANTHERPTHR10129. PTHR10129. 1 hit.
PTHR10129:SF15. PTHR10129:SF15. 1 hit.
PfamPF03131. bZIP_Maf. 1 hit.
[Graphical view]
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMSSF47454. SSF47454. 1 hit.
PROSITEPS50217. BZIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAFG. human.
GeneWikiMAFG.
GenomeRNAi4097.
NextBio16068.
PROO15525.
SOURCESearch...

Entry information

Entry nameMAFG_HUMAN
AccessionPrimary (citable) accession number: O15525
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: March 19, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM