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Protein

Transcription factor MafG

Gene

MAFG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:G66-31685-MONOMER.
ReactomeiR-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SIGNORiO15525.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:6781. MAFG.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi53K → 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 Publication1
Mutagenesisi60K → 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 Publication1
Mutagenesisi71K → 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 Publication1
Mutagenesisi76K → 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 Publication1

Organism-specific databases

DisGeNETi4097.
OpenTargetsiENSG00000197063.
PharmGKBiPA30539.

Polymorphism and mutation databases

BioMutaiMAFG.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000765001 – 162Transcription factor MafGAdd BLAST162

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei53N6-acetyllysine1 Publication1
Modified residuei60N6-acetyllysine1 Publication1
Modified residuei71N6-acetyllysine1 Publication1
Modified residuei76N6-acetyllysine1 Publication1
Modified residuei124PhosphoserineCombined sources1

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

EPDiO15525.
MaxQBiO15525.
PaxDbiO15525.
PeptideAtlasiO15525.
PRIDEiO15525.

PTM databases

iPTMnetiO15525.
PhosphoSitePlusiO15525.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000197063.
CleanExiHS_MAFG.
ExpressionAtlasiO15525. baseline and differential.
GenevisibleiO15525. HS.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
BACH1O148673EBI-713514,EBI-1263541
HBZP0C7463EBI-713514,EBI-10890294From a different organism.
NFE2L1Q144942EBI-713514,EBI-2804436
NFE2L2Q162365EBI-713514,EBI-2007911
NFE2L3Q9Y4A82EBI-713514,EBI-10890629

Protein-protein interaction databases

BioGridi110272. 28 interactors.
IntActiO15525. 17 interactors.
MINTiMINT-1374809.
STRINGi9606.ENSP00000350369.

Structurei

3D structure databases

ProteinModelPortaliO15525.
SMRiO15525.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini51 – 114bZIPPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni53 – 76Basic motifPROSITE-ProRule annotationAdd BLAST24
Regioni79 – 93Leucine-zipperPROSITE-ProRule annotationAdd BLAST15

Sequence similaritiesi

Belongs to the bZIP family. Maf subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410ISHW. Eukaryota.
ENOG4111HFT. LUCA.
GeneTreeiENSGT00550000074549.
HOGENOMiHOG000045475.
HOVERGENiHBG001725.
InParanoidiO15525.
KOiK09037.
OMAiITASMGP.
OrthoDBiEOG091G0H46.
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_fam.
[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

        10         20         30         40         50
MTTPNKGNKA LKVKREPGEN GTSLTDEELV TMSVRELNQH LRGLSKEEIV
60 70 80 90 100
QLKQRRRTLK NRGYAASCRV KRVTQKEELE KQKAELQQEV EKLASENASM
110 120 130 140 150
KLELDALRSK YEALQTFART VARSPVAPAR GPLAAGLGPL VPGKVAATSV
160
ITIVKSKTDA RS
Length:162
Mass (Da):17,850
Last modified:January 1, 1998 - v1
Checksum:iE49F1FBA230F8D30
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
XP_011521880.1. XM_011523578.1.
UniGeneiHs.252229.
Hs.744113.

Genome annotation databases

EnsembliENST00000357736; ENSP00000350369; ENSG00000197063.
ENST00000392366; ENSP00000376173; ENSG00000197063.
GeneIDi4097.
KEGGihsa:4097.
UCSCiuc002kcm.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
XP_011521880.1. XM_011523578.1.
UniGeneiHs.252229.
Hs.744113.

3D structure databases

ProteinModelPortaliO15525.
SMRiO15525.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110272. 28 interactors.
IntActiO15525. 17 interactors.
MINTiMINT-1374809.
STRINGi9606.ENSP00000350369.

PTM databases

iPTMnetiO15525.
PhosphoSitePlusiO15525.

Polymorphism and mutation databases

BioMutaiMAFG.

Proteomic databases

EPDiO15525.
MaxQBiO15525.
PaxDbiO15525.
PeptideAtlasiO15525.
PRIDEiO15525.

Protocols and materials databases

DNASUi4097.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357736; ENSP00000350369; ENSG00000197063.
ENST00000392366; ENSP00000376173; ENSG00000197063.
GeneIDi4097.
KEGGihsa:4097.
UCSCiuc002kcm.4. human.

Organism-specific databases

CTDi4097.
DisGeNETi4097.
GeneCardsiMAFG.
HGNCiHGNC:6781. MAFG.
HPAiCAB025573.
MIMi602020. gene.
neXtProtiNX_O15525.
OpenTargetsiENSG00000197063.
PharmGKBiPA30539.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ISHW. Eukaryota.
ENOG4111HFT. LUCA.
GeneTreeiENSGT00550000074549.
HOGENOMiHOG000045475.
HOVERGENiHBG001725.
InParanoidiO15525.
KOiK09037.
OMAiITASMGP.
OrthoDBiEOG091G0H46.
PhylomeDBiO15525.
TreeFamiTF325689.

Enzyme and pathway databases

BioCyciZFISH:G66-31685-MONOMER.
ReactomeiR-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SIGNORiO15525.

Miscellaneous databases

ChiTaRSiMAFG. human.
GeneWikiiMAFG.
GenomeRNAii4097.
PROiO15525.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197063.
CleanExiHS_MAFG.
ExpressionAtlasiO15525. baseline and differential.
GenevisibleiO15525. HS.

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_fam.
[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]
ProtoNetiSearch...

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: November 30, 2016
This is version 150 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.