O15525 (MAFG_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 108.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Transcription factor MafG Alternative name(s): V-maf musculoaponeurotic fibrosarcoma oncogene homolog G hMAF | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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 | |
| 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 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Cellular component | Nucleus |
| Ligand | DNA-binding |
| Molecular function | Repressor |
| PTM | Acetylation Isopeptide bond Ubl conjugation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | blood coagulation Traceable author statement. Source: Reactome transcription, DNA-dependentInferred 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 activityNon-traceable author statement. 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 | 86 – 114 | 29 | Leucine-zipper | ||||||
| DNA binding | 53 – 83 | 31 | Basic motif | ||||||
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 | ||||||
| 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
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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: 9195958] [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: 9166829] [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: 9286713] [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: 9150357] [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: 15489334] [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: 11154691] [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. |
| + | 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. |
3D structure databases | |
| ProteinModelPortal | O15525. |
| SMR | O15525. Positions 21-111. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | O15525. 9 interactions. |
| MINT | MINT-1374809. |
| STRING | O15525. |
PTM databases | |
| PhosphoSite | O15525. |
Proteomic databases | |
| PRIDE | O15525. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000357736; ENSP00000350369; ENSG00000197063. ENST00000392366; ENSP00000376173; ENSG00000197063. |
| GeneID | 4097. |
| KEGG | hsa:4097. |
| UCSC | uc002kcm.1. human. |
Organism-specific databases | |
| CTD | 4097. |
| GeneCards | GC17M079877. |
| H-InvDB | HIX0202478. |
| HGNC | HGNC:6781. MAFG. |
| HPA | CAB025573. |
| MIM | 602020. gene. |
| neXtProt | NX_O15525. |
| PharmGKB | PA30539. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG11941. |
| GeneTree | ENSGT00550000074549. |
| HOGENOM | HBG715194. |
| HOVERGEN | HBG001725. |
| InParanoid | O15525. |
| OMA | SKGNKAL. |
| 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 | |
| InterPro | IPR004827. bZIP. IPR004826. bZIP_Maf. IPR008917. Euk_TF_DNA-bd. IPR024874. Transciption_factor_Maf. [Graphical view] |
| Gene3D | G3DSA:1.10.880.10. G3DSA:1.10.880.10. 1 hit. |
| KO | K09037. |
| 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 | |
| NextBio | 16068. |
| SOURCE | Search... |
Entry information
| Entry name | MAFG_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O15525 | ||||||||
| Entry history |
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| 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. | ||||||||
Relevant documents
| Human chromosome 17 Human chromosome 17: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with