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O15525

- MAFG_HUMAN

UniProt

O15525 - MAFG_HUMAN

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Protein
Transcription factor MafG
Gene
MAFG
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. sequence-specific DNA binding Source: InterPro
  2. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. adult behavior Source: Ensembl
  2. blood coagulation Source: Reactome
  3. in utero embryonic development Source: Ensembl
  4. regulation of cell proliferation Source: Ensembl
  5. regulation of cellular pH Source: Ensembl
  6. regulation of epidermal cell differentiation Source: Ensembl
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor MafG
Alternative name(s):
V-maf musculoaponeurotic fibrosarcoma oncogene homolog G
hMAF
Gene namesi
Name:MAFG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:6781. MAFG.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi53 – 531K → 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. 1 Publication
Mutagenesisi60 – 601K → 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. 1 Publication
Mutagenesisi71 – 711K → 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. 1 Publication
Mutagenesisi76 – 761K → 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. 1 Publication

Organism-specific databases

PharmGKBiPA30539.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 162162Transcription factor MafG
PRO_0000076500Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei53 – 531N6-acetyllysine Inferred
Modified residuei60 – 601N6-acetyllysine Inferred
Modified residuei71 – 711N6-acetyllysine Inferred
Modified residuei76 – 761N6-acetyllysine Inferred
Modified residuei124 – 1241Phosphoserine1 Publication

Post-translational modificationi

Acetylated in erythroid cells by CREB-binding protein (CBP). Acetylation augments the DNA-binding activity of NFE2, but has no effect on binding NFE2.1 Publication
Sumoylation at Lys-14 is required for active transcriptional repression By similarity.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO15525.
PaxDbiO15525.
PRIDEiO15525.

PTM databases

PhosphoSiteiO15525.

Expressioni

Tissue specificityi

Highly expressed in skeletal muscle. Also expressed in heart and brain.

Gene expression databases

ArrayExpressiO15525.
BgeeiO15525.
CleanExiHS_MAFG.
GenevestigatoriO15525.

Organism-specific databases

HPAiCAB025573.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi110272. 32 interactions.
IntActiO15525. 11 interactions.
MINTiMINT-1374809.
STRINGi9606.ENSP00000350369.

Structurei

3D structure databases

ProteinModelPortaliO15525.
SMRiO15525. Positions 21-111.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 11464bZIP
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 7624Basic motif By similarity
Add
BLAST
Regioni79 – 9315Leucine-zipper By similarity
Add
BLAST

Sequence similaritiesi

Belongs to the bZIP family. Maf subfamily.

Phylogenomic databases

eggNOGiNOG236209.
HOGENOMiHOG000045475.
HOVERGENiHBG001725.
InParanoidiO15525.
KOiK09037.
OMAiITASMGP.
OrthoDBiEOG7BGHMQ.
PhylomeDBiO15525.
TreeFamiTF325689.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR028551. MafG.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view]
PANTHERiPTHR10129. PTHR10129. 1 hit.
PTHR10129:SF15. PTHR10129:SF15. 1 hit.
PfamiPF03131. bZIP_Maf. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMiSSF47454. SSF47454. 1 hit.
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O15525-1 [UniParc]FASTAAdd to Basket

« Hide

MTTPNKGNKA LKVKREPGEN GTSLTDEELV TMSVRELNQH LRGLSKEEIV    50
QLKQRRRTLK NRGYAASCRV KRVTQKEELE KQKAELQQEV EKLASENASM 100
KLELDALRSK YEALQTFART VARSPVAPAR GPLAAGLGPL VPGKVAATSV 150
ITIVKSKTDA RS 162
Length:162
Mass (Da):17,850
Last modified:January 1, 1998 - v1
Checksum:iE49F1FBA230F8D30
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y11514 mRNA. Translation: CAA72284.1.
U84249 mRNA. Translation: AAC51737.1.
AF059195 mRNA. Translation: AAC14427.1.
BC012327 mRNA. Translation: AAH12327.1.
CCDSiCCDS11793.1.
RefSeqiNP_002350.1. NM_002359.3.
NP_116100.2. NM_032711.3.
UniGeneiHs.252229.
Hs.744113.

Genome annotation databases

EnsembliENST00000357736; ENSP00000350369; ENSG00000197063.
ENST00000392366; ENSP00000376173; ENSG00000197063.
GeneIDi4097.
KEGGihsa:4097.
UCSCiuc002kcm.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y11514 mRNA. Translation: CAA72284.1 .
U84249 mRNA. Translation: AAC51737.1 .
AF059195 mRNA. Translation: AAC14427.1 .
BC012327 mRNA. Translation: AAH12327.1 .
CCDSi CCDS11793.1.
RefSeqi NP_002350.1. NM_002359.3.
NP_116100.2. NM_032711.3.
UniGenei Hs.252229.
Hs.744113.

3D structure databases

ProteinModelPortali O15525.
SMRi O15525. Positions 21-111.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110272. 32 interactions.
IntActi O15525. 11 interactions.
MINTi MINT-1374809.
STRINGi 9606.ENSP00000350369.

PTM databases

PhosphoSitei O15525.

Proteomic databases

MaxQBi O15525.
PaxDbi O15525.
PRIDEi O15525.

Protocols and materials databases

DNASUi 4097.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000357736 ; ENSP00000350369 ; ENSG00000197063 .
ENST00000392366 ; ENSP00000376173 ; ENSG00000197063 .
GeneIDi 4097.
KEGGi hsa:4097.
UCSCi uc002kcm.3. human.

Organism-specific databases

CTDi 4097.
GeneCardsi GC17M079877.
HGNCi HGNC:6781. MAFG.
HPAi CAB025573.
MIMi 602020. gene.
neXtProti NX_O15525.
PharmGKBi PA30539.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG236209.
HOGENOMi HOG000045475.
HOVERGENi HBG001725.
InParanoidi O15525.
KOi K09037.
OMAi ITASMGP.
OrthoDBi EOG7BGHMQ.
PhylomeDBi O15525.
TreeFami TF325689.

Enzyme and pathway databases

Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSi MAFG. human.
GeneWikii MAFG.
GenomeRNAii 4097.
NextBioi 16068.
PROi O15525.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15525.
Bgeei O15525.
CleanExi HS_MAFG.
Genevestigatori O15525.

Family and domain databases

Gene3Di 1.10.880.10. 1 hit.
InterProi IPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR028551. MafG.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view ]
PANTHERi PTHR10129. PTHR10129. 1 hit.
PTHR10129:SF15. PTHR10129:SF15. 1 hit.
Pfami PF03131. bZIP_Maf. 1 hit.
[Graphical view ]
SMARTi SM00338. BRLZ. 1 hit.
[Graphical view ]
SUPFAMi SSF47454. SSF47454. 1 hit.
PROSITEi PS50217. BZIP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiMAFG_HUMAN
AccessioniPrimary (citable) accession number: O15525
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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