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O54790 (MAFG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. 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
Gene names
Name:Mafg
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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.1 Ref.3

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 By similarity.

Subcellular location

Nucleus By similarity.

Developmental stage

Expressed throughout the embryo up until E8.5 with strong expression in the neural tube. Expression continues throughout the embryo with some intense expression also in the epithelium of the intestine, skeletal muscle, lens, retina, cranial nerve, and dorsal root ganglion cells. After birth, strong expression in the epidermis, hair follicles, epithelium of the digestive and respiratory tracts, and kidney tubules. Ref.1

Post-translational modification

Acetylated in erythroid cells by CREB-binding protein (CBP). Acetylation augments the DNA-binding activity of NF-E2.

Sumoylation at Lys-14 is required for active transcriptional repression. Ref.3

Disruption phenotype

Mice, although viable and fertile, exhibit abnormal megakaryocyte proliferation as well as age-dependent behavioral defects. Megakaryocytes display both anti-glycoprotein IIb immunoreactivity and anti-acetylcholinesterase activity. Ref.1

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_0000076501

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 By similarity
Cross-link14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.3

Secondary structure

............... 162
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O54790 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: C7FF19614EB95C7D

FASTA16217,877
        10         20         30         40         50         60 
MTTPNKGNKA LKVKREPGEN GTSLTDEELV TMSVRELNQH LRGLSKEEII QLKQRRRTLK 

        70         80         90        100        110        120 
NRGYAASCRV KRVTQKEELE KQKAELQQEV EKLASENASM KLELDALRSK YEALQNFART 

       130        140        150        160 
VARSPVAPAR GPLAAGLGPL VPGKVAATSV ITIVKSKTDA RS 

« Hide

References

« Hide 'large scale' references
[1]"Impaired megakaryopoiesis and behavioral defects in mafG-null mutant mice."
Shavit J.A., Motohashi H., Onodera K., Akasaka J., Yamamoto M., Engel J.D.
Genes Dev. 12:2164-2174(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, FUNCTION.
Strain: 129/SvJ.
[2]"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].
Strain: C57BL/6J.
Tissue: Mammary gland and Olfactory epithelium.
[3]"MafG sumoylation is required for active transcriptional repression."
Motohashi H., Katsuoka F., Miyoshi C., Uchimura Y., Saitoh H., Francastel C., Engel J.D., Yamamoto M.
Mol. Cell. Biol. 26:4652-4663(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-14, FUNCTION.
[4]"Solution structure of the DNA-binding domain of MafG."
Kusunoki H., Motohashi H., Katsuoka F., Morohashi A., Yamamoto M., Tanaka T.
Nat. Struct. Biol. 9:252-256(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 24-64.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB009693 Genomic DNA. Translation: BAA24028.1.
BC002092 mRNA. Translation: AAH02092.1.
BC052633 mRNA. Translation: AAH52633.1.
CCDSCCDS25748.1.
RefSeqNP_034886.1. NM_010756.3.
UniGeneMm.268010.
Mm.292957.
Mm.393664.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K1VNMR-A24-64[»]
3A5TX-ray2.80A/B21-123[»]
ProteinModelPortalO54790.
SMRO54790. Positions 21-111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201283. 3 interactions.
DIPDIP-46344N.
IntActO54790. 1 interaction.
MINTMINT-4101043.

PTM databases

PhosphoSiteO54790.

Proteomic databases

PaxDbO54790.
PRIDEO54790.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000058162; ENSMUSP00000053899; ENSMUSG00000051510.
ENSMUST00000106180; ENSMUSP00000101786; ENSMUSG00000051510.
ENSMUST00000106181; ENSMUSP00000101787; ENSMUSG00000051510.
ENSMUST00000106182; ENSMUSP00000101788; ENSMUSG00000051510.
GeneID17134.
KEGGmmu:17134.
UCSCuc007mtu.2. mouse.

Organism-specific databases

CTD4097.
MGIMGI:96911. Mafg.

Phylogenomic databases

eggNOGNOG236209.
GeneTreeENSGT00550000074549.
HOGENOMHOG000045475.
HOVERGENHBG001725.
InParanoidO54790.
KOK09037.
OMAITASMGP.
OrthoDBEOG7BGHMQ.
PhylomeDBO54790.
TreeFamTF325689.

Gene expression databases

BgeeO54790.
GenevestigatorO54790.

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

EvolutionaryTraceO54790.
NextBio291340.
PROO54790.
SOURCESearch...

Entry information

Entry nameMAFG_MOUSE
AccessionPrimary (citable) accession number: O54790
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot