Maf1
entrez
68877
canonical
uniprot
Q9D0U6
canonical
ensembl
ENSMUSG00000022553
resolver
ensp
ENSMUSP00000023212
resolver
ensp
ENSMUSP00000124893
resolver
ensp
ENSMUSP00000125387
resolver
enst
ENSMUST00000023212
resolver
enst
ENSMUST00000160853
resolver
enst
ENSMUST00000161527
resolver
genesymbol
Maf1
resolver
uniprot
Q3U4U3
resolver
uniprot
Q91W84
resolver
uniprot_entry
MAF1_MOUSE
resolver
uniprot_sec
Q3U4U3
resolver
uniprot_sec
Q91W84
resolver
amino_acid_sequence
MKLLENSSFEAINSQLTVETGDAHIIGRIESYSCKMAGDDKHMFKQFCQEGQPHVLEALSPPQTSGLSPSRLSKSQGGEDESPLSDKCSRKTLFYLIATLNESFRPDYDFSTARSHEFSREPSLRWVVNAVNCSLFSAVREDFKALKPQLWNAVDEEICLAECDIYSYNPDLDSDPFGEDGSLWSFNYFFYNKRLKRIVFFSCRSISGSTYTPSEAGNALDLELGAEEADEESGGGGGEGRAEETSTMEEDRVPVICM
uniprot
proteins
function
FUNCTION: Plays a role in the repression of RNA polymerase III-mediated transcription in response to changing nutritional, environmental and cellular stress conditions to balance the production of highly abundant tRNAs, 5S rRNA, and other small non-coding RNAs with cell growth and maintenance (By similarity). Also plays a key role in cell fate determination by promoting mesorderm induction and adipocyte differentiation (PubMed:30110641). Mechanistically, associates with the RNA polymerase III clamp and thereby impairs its recruitment to the complex made of the promoter DNA, TBP and the initiation factor TFIIIB. When nutrients are available and mTOR kinase is active, MAF1 is hyperphosphorylated and RNA polymerase III is engaged in transcription. Stress-induced MAF1 dephosphorylation results in nuclear localization, increased targeting of gene-bound RNA polymerase III and a decrease in the transcriptional readout. Additionally, may also regulate RNA polymerase I and RNA polymerase II-dependent transcription through its ability to regulate expression of the central initiation factor TBP (By similarity). {ECO:0000250|UniProtKB:Q9H063, ECO:0000269|PubMed:30110641}.
uniprot
proteins
mass_dalton
28780
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-60, Ser-68 and Ser-75; the major sites of phosphorylation. Nuclear accumulation correlates with a concomitant dephosphorylation. Phosphorylation may attenuate its RNA polymerase III-repressive function (By similarity). {ECO:0000250}.; PTM: Sumoylated with SUMO1 and SUMO2, mainly on Lys-35. Desumoylated by SENP1. SUMOylation promotes the ability of MAF1 to repress transcription and suppress colony formation (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
MAF1 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
20543138
uniprot
proteins
pubmed
25934505
uniprot
proteins
pubmed
30110641
uniprot
proteins
pubmed
30429315
uniprot
proteins
sequence_length
258
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20543138}. Cytoplasm {ECO:0000250|UniProtKB:Q9H063}.
uniprot
proteins