O60675 · MAFK_HUMAN

  • Protein
    Transcription factor MafK
  • Gene
    MAFK
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves (PubMed:9150357).
However, they act as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2, NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3, and recruiting them to specific DNA-binding sites (PubMed:8932385, PubMed:9150357).
Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor (PubMed:9150357).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchromatin
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular ComponentRNA polymerase II transcription regulator complex
Molecular FunctionDNA-binding transcription factor activity
Molecular FunctionDNA-binding transcription factor activity, RNA polymerase II-specific
Molecular FunctionDNA-binding transcription repressor activity, RNA polymerase II-specific
Molecular FunctionRNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Functionsequence-specific DNA binding
Molecular Functiontranscription cis-regulatory region binding
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processregulation of transcription by RNA polymerase II

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Transcription factor MafK
  • Alternative names
    • Erythroid transcription factor NF-E2 p18 subunit

Gene names

    • Name
      MAFK

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    O60675
  • Secondary accessions
    • A4D214

Proteomes

Organism-specific databases

Disease & Variants

Variants

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The viewer provides 174 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue, modified residue (large scale data), cross-link.

TypeIDPosition(s)SourceDescription
ChainPRO_00000765031-156UniProtTranscription factor MafK
Modified residue25UniProtPhosphoserine
Modified residue (large scale data)25PRIDEPhosphoserine
Cross-link130UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Homodimer or heterodimer. It can form high affinity heterodimers with members of the CNC-bZIP family such as NFE2, NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3 (PubMed:8932385, PubMed:9150357).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY O60675BACH2 Q9BYV94EBI-2559512, EBI-1642333
BINARY O60675NFE2L2 Q162367EBI-2559512, EBI-2007911
View interactors in UniProtKB
View CPX-2482 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region51-76Basic motif
Domain51-114bZIP
Region79-93Leucine-zipper

Sequence similarities

Belongs to the bZIP family. Maf subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    156
  • Mass (Da)
    17,523
  • Last updated
    1998-08-01 v1
  • Checksum
    39F98F8D550C168E
MTTNPKPNKALKVKKEAGENAPVLSDDELVSMSVRELNQHLRGLTKEEVTRLKQRRRTLKNRGYAASCRIKRVTQKEELERQRVELQQEVEKLARENSSMRLELDALRSKYEALQTFARTVARGPVAPSKVATTSVITIVKSTELSSTSVPFSAAS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF059194
EMBL· GenBank· DDBJ
AAC14426.1
EMBL· GenBank· DDBJ
mRNA
AK092414
EMBL· GenBank· DDBJ
BAG52549.1
EMBL· GenBank· DDBJ
mRNA
AC093734
EMBL· GenBank· DDBJ
AAP21866.1
EMBL· GenBank· DDBJ
Genomic DNA
CH236953
EMBL· GenBank· DDBJ
EAL23943.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471144
EMBL· GenBank· DDBJ
EAW87207.1
EMBL· GenBank· DDBJ
Genomic DNA
BC148265
EMBL· GenBank· DDBJ
AAI48266.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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