MAF1
entrez
84232
canonical
uniprot
Q9H063
canonical
ensembl
ENSG00000179632
resolver
ensp
ENSP00000318604
resolver
ensp
ENSP00000436720
resolver
ensp
ENSP00000520454
resolver
ensp
ENSP00000546724
resolver
ensp
ENSP00000546725
resolver
ensp
ENSP00000546727
resolver
ensp
ENSP00000546733
resolver
ensp
ENSP00000546734
resolver
ensp
ENSP00000546735
resolver
ensp
ENSP00000634402
resolver
ensp
ENSP00000634404
resolver
ensp
ENSP00000634409
resolver
enst
ENST00000322428
resolver
enst
ENST00000532522
resolver
enst
ENST00000715465
resolver
enst
ENST00000876665
resolver
enst
ENST00000876666
resolver
enst
ENST00000876668
resolver
enst
ENST00000876674
resolver
enst
ENST00000876675
resolver
enst
ENST00000876676
resolver
enst
ENST00000964343
resolver
enst
ENST00000964345
resolver
enst
ENST00000964350
resolver
genesymbol
MAF1
resolver
hgnc
HGNC:24966
resolver
uniprot
D3DWL4
resolver
uniprot_entry
MAF1_HUMAN
resolver
uniprot_sec
D3DWL4
resolver
amino_acid_sequence
MKLLENSSFEAINSQLTVETGDAHIIGRIESYSCKMAGDDKHMFKQFCQEGQPHVLEALSPPQTSGLSPSRLSKSQGGEEEGPLSDKCSRKTLFYLIATLNESFRPDYDFSTARSHEFSREPSLSWVVNAVNCSLFSAVREDFKDLKPQLWNAVDEEICLAECDIYSYNPDLDSDPFGEDGSLWSFNYFFYNKRLKRIVFFSCRSISGSTYTPSEAGNELDMELGEEEVEEESRSGGSGAEETSTMEEDRVPVICI
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 (PubMed:18377933, PubMed:20233713, PubMed:20516213, PubMed:20543138). Also plays a key role in cell fate determination by promoting mesorderm induction and adipocyte differentiation (By similarity). 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 (PubMed:17505538, PubMed:20887893). 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 (PubMed:26941251). 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 (PubMed:17499043). {ECO:0000250|UniProtKB:Q9D0U6, ECO:0000269|PubMed:17499043, ECO:0000269|PubMed:17505538, ECO:0000269|PubMed:18377933, ECO:0000269|PubMed:20233713, ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20543138, ECO:0000269|PubMed:20887893, ECO:0000269|PubMed:26941251}.
uniprot
proteins
mass_dalton
28771
uniprot
proteins
mutagenesis
MUTAGEN 35; /note="K->R: No interaction with RNA pol III and impaired recruitment to tRNA gene promoters."; /evidence="ECO:0000269|PubMed:23673667"; MUTAGEN 60; /note="S->A: Stronger repressive effect on RNA polymerase III transcription; when associated with A-68 and A-75. Much stronger repressive effect on RNA polymerase III transcription and loss of phosphorylation; when associated with A-64, A-68 and A-75."; /evidence="ECO:0000269|PubMed:20233713, ECO:0000269|PubMed:20516213"; MUTAGEN 60; /note="S->D: No change. Weaker repressive effect on RNA polymerase III transcription; when associated with D-68 and D-75."; /evidence="ECO:0000269|PubMed:20233713, ECO:0000269|PubMed:20516213"; MUTAGEN 64; /note="T->A: Much stronger repressive effect on RNA polymerase III transcription and loss of phosphorylation; when associated with A-60, A-68 and A-75."; /evidence="ECO:0000269|PubMed:20233713"; MUTAGEN 68; /note="S->A: Stronger repressive effect on RNA polymerase III transcription; when associated with A-60 and A-75. Much stronger repressive effect on RNA polymerase III transcription and loss of phosphorylation; when associated with A-60, A-64 and A-75."; /evidence="ECO:0000269|PubMed:20233713, ECO:0000269|PubMed:20516213"; MUTAGEN 68; /note="S->D: No change. Weaker repressive effect on RNA polymerase III transcription; when associated with D-60 and D-75."; /evidence="ECO:0000269|PubMed:20233713, ECO:0000269|PubMed:20516213"; MUTAGEN 75; /note="S->A: Stronger repressive effect on RNA polymerase III transcription. Stronger repressive effect on RNA polymerase III transcription; when associated with A-60 and A-68. Much stronger repressive effect on RNA polymerase III transcription and loss of phosphorylation; when associated with A-60, A-64 and A-68."; /evidence="ECO:0000269|PubMed:20233713, ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20543138"; MUTAGEN 75; /note="S->D: No change. Weaker repressive effect on RNA polymerase III transcription; when associated with D-60 and D-68."; /evidence="ECO:0000269|PubMed:20233713, ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20543138
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. {ECO:0000269|PubMed:20233713, ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20543138, ECO:0000269|PubMed:23673667}.; 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. {ECO:0000269|PubMed:23673667}.
uniprot
proteins
protein_family
MAF1 family
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17499043
uniprot
proteins
pubmed
17505538
uniprot
proteins
pubmed
18377933
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20233713
uniprot
proteins
pubmed
20516213
uniprot
proteins
pubmed
20543138
uniprot
proteins
pubmed
20887893
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23673667
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26941251
uniprot
proteins
sequence_length
256
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17505538, ECO:0000269|PubMed:20233713}. Cytoplasm {ECO:0000269|PubMed:20233713}.
uniprot
proteins