Q9H063 · MAF1_HUMAN
- ProteinRepressor of RNA polymerase III transcription MAF1 homolog
- GeneMAF1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids256 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | RNA polymerase III core binding | |
Molecular Function | RNA polymerase III type 1 promoter sequence-specific DNA binding | |
Molecular Function | RNA polymerase III type 2 promoter sequence-specific DNA binding | |
Molecular Function | RNA polymerase III type 3 promoter sequence-specific DNA binding | |
Biological Process | negative regulation of transcription by RNA polymerase I | |
Biological Process | negative regulation of transcription by RNA polymerase III |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRepressor of RNA polymerase III transcription MAF1 homolog
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H063
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 35 | No interaction with RNA pol III and impaired recruitment to tRNA gene promoters. | ||||
Sequence: K → R | ||||||
Mutagenesis | 60 | 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. | ||||
Sequence: S → A | ||||||
Mutagenesis | 60 | No change. Weaker repressive effect on RNA polymerase III transcription; when associated with D-68 and D-75. | ||||
Sequence: S → D | ||||||
Mutagenesis | 64 | Much stronger repressive effect on RNA polymerase III transcription and loss of phosphorylation; when associated with A-60, A-68 and A-75. | ||||
Sequence: T → A | ||||||
Mutagenesis | 68 | 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. | ||||
Sequence: S → A | ||||||
Mutagenesis | 68 | No change. Weaker repressive effect on RNA polymerase III transcription; when associated with D-60 and D-75. | ||||
Sequence: S → D | ||||||
Mutagenesis | 75 | 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. | ||||
Sequence: S → A | ||||||
Mutagenesis | 75 | No change. Weaker repressive effect on RNA polymerase III transcription; when associated with D-60 and D-68. | ||||
Sequence: S → D | ||||||
Natural variant | VAR_060408 | 236 | in dbSNP:rs11546144 | |||
Sequence: G → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 219 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, cross-link, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000213973 | 1-256 | UniProt | Repressor of RNA polymerase III transcription MAF1 homolog | |||
Sequence: MKLLENSSFEAINSQLTVETGDAHIIGRIESYSCKMAGDDKHMFKQFCQEGQPHVLEALSPPQTSGLSPSRLSKSQGGEEEGPLSDKCSRKTLFYLIATLNESFRPDYDFSTARSHEFSREPSLSWVVNAVNCSLFSAVREDFKDLKPQLWNAVDEEICLAECDIYSYNPDLDSDPFGEDGSLWSFNYFFYNKRLKRIVFFSCRSISGSTYTPSEAGNELDMELGEEEVEEESRSGGSGAEETSTMEEDRVPVICI | |||||||
Cross-link | 35 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1 and SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 60 | UniProt | Phosphoserine; by MTOR | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 60 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 64 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 64 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 65 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 68 | UniProt | Phosphoserine; by MTOR | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 68 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 70 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 70 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 73 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 75 | UniProt | Phosphoserine; by MTOR | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 75 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 212 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 214 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 214 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 238 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
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.
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.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with TFIIIB subunits BRF1 and BRF2 (PubMed:17505538, PubMed:18377933).
Interacts with Pol III subunit POLR3F. Interacts with TFIIIC subunit GTF3C1 (PubMed:18377933).
Interacts with Pol III subunit POLR3F. Interacts with TFIIIC subunit GTF3C1 (PubMed:18377933).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9H063 | ARMCX3 Q9UH62 | 4 | EBI-720354, EBI-717832 | |
BINARY | Q9H063 | CSNK2A1 P68400 | 2 | EBI-720354, EBI-347804 | |
BINARY | Q9H063 | HTT P42858 | 3 | EBI-720354, EBI-466029 | |
BINARY | Q9H063 | PCNA P12004 | 4 | EBI-720354, EBI-358311 | |
BINARY | Q9H063 | WFS1 O76024 | 3 | EBI-720354, EBI-720609 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 58-75 | Polar residues | ||||
Sequence: ALSPPQTSGLSPSRLSKS | ||||||
Region | 58-85 | Disordered | ||||
Sequence: ALSPPQTSGLSPSRLSKSQGGEEEGPLS | ||||||
Region | 212-252 | Disordered | ||||
Sequence: TPSEAGNELDMELGEEEVEEESRSGGSGAEETSTMEEDRVP | ||||||
Compositional bias | 231-248 | Basic and acidic residues | ||||
Sequence: EESRSGGSGAEETSTMEE |
Sequence similarities
Belongs to the MAF1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length256
- Mass (Da)28,771
- Last updated2010-05-18 v2
- ChecksumD6C06D2E476753AA
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 58-75 | Polar residues | ||||
Sequence: ALSPPQTSGLSPSRLSKS | ||||||
Compositional bias | 231-248 | Basic and acidic residues | ||||
Sequence: EESRSGGSGAEETSTMEE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL136937 EMBL· GenBank· DDBJ | CAB66871.1 EMBL· GenBank· DDBJ | mRNA | ||
CR533463 EMBL· GenBank· DDBJ | CAG38494.1 EMBL· GenBank· DDBJ | mRNA | ||
AC104592 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471162 EMBL· GenBank· DDBJ | EAW82158.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471162 EMBL· GenBank· DDBJ | EAW82159.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC014082 EMBL· GenBank· DDBJ | AAH14082.1 EMBL· GenBank· DDBJ | mRNA | ||
BC018714 EMBL· GenBank· DDBJ | AAH18714.1 EMBL· GenBank· DDBJ | mRNA | ||
BC031273 EMBL· GenBank· DDBJ | AAH31273.1 EMBL· GenBank· DDBJ | mRNA |