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Protein

Repressor of RNA polymerase III transcription MAF1

Gene

MAF1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Mediator of diverse signals that repress RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA.1 Publication

GO - Molecular functioni

  • RNA polymerase III core binding Source: SGD

GO - Biological processi

  • negative regulation of transcription from RNA polymerase III promoter Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
  • transcription factor TFIIIB complex assembly Source: GO_Central
  • transfer RNA gene-mediated silencing Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-29627-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Repressor of RNA polymerase III transcription MAF1
Gene namesi
Name:MAF1
Ordered Locus Names:YDR005C
ORF Names:YD8119.11C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR005C.
SGDiS000002412. MAF1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • nucleolus Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395Repressor of RNA polymerase III transcription MAF1PRO_0000213972Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei90 – 901PhosphoserineCombined sources
Modified residuei209 – 2091PhosphoserineCombined sources
Modified residuei210 – 2101PhosphoserineCombined sources
Modified residuei347 – 3471PhosphothreonineCombined sources

Post-translational modificationi

Phosphorylated by PKA in a TORC1-dependent manner. Phosphorylation at PKA consensus sites RRxS/T decreases upon rapamycin treatment.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP41910.

PTM databases

iPTMnetiP41910.

Interactioni

GO - Molecular functioni

  • RNA polymerase III core binding Source: SGD

Protein-protein interaction databases

BioGridi32058. 118 interactions.
DIPiDIP-5133N.
IntActiP41910. 13 interactions.
MINTiMINT-543690.

Structurei

3D structure databases

ProteinModelPortaliP41910.
SMRiP41910. Positions 225-336.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MAF1 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000006896.
HOGENOMiHOG000065964.
InParanoidiP41910.
OMAiCDIFTTK.
OrthoDBiEOG7SN8PR.

Family and domain databases

InterProiIPR015257. Maf1.
[Graphical view]
PANTHERiPTHR22504. PTHR22504. 2 hits.
PfamiPF09174. Maf1. 1 hit.
[Graphical view]
PIRSFiPIRSF037240. RNA_polIII_Trep_MAF1. 1 hit.

Sequencei

Sequence statusi: Complete.

P41910-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFIDELDIE RVNQTLNFET NDCKIVGSCD IFTTKAVASD RKLYKTIDQH
60 70 80 90 100
LDTILQENEN YNATLQQQLA APETNQSPCS SPFYSNRRDS NSFWEQKRRI
110 120 130 140 150
SFSEYNSNNN TNNSNGNSSN NNNYSGPNGS SPATFPKSAK LNDQNLKELV
160 170 180 190 200
SNYDSGSMSS SSLDSSSKND ERIRRRSSSS ISSFKSGKSS NNNYSSGTAT
210 220 230 240 250
NNVNKRRKSS INERPSNLSL GPFGPINEPS SRKIFAYLIA ILNASYPDHD
260 270 280 290 300
FSSVEPTDFV KTSLKTFISK FENTLYSLGR QPEEWVWEVI NSHMTLSDCV
310 320 330 340 350
LFQYSPSNSF LEDEPGYLWN LIGFLYNRKR KRVAYLYLIC SRLNSSTGEV
360 370 380 390
EDALAKKPQG KLIIDDGSNE YEGEYDFTYD ENVIDDKSDQ EESLQ
Length:395
Mass (Da):44,733
Last modified:November 1, 1995 - v1
Checksum:i1AE6262D0BEBBB1D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19492 Genomic DNA. Translation: AAB51655.1.
Z48008 Genomic DNA. Translation: CAA88065.1.
BK006938 Genomic DNA. Translation: DAA11853.1.
PIRiS50986.
RefSeqiNP_010288.1. NM_001180313.1.

Genome annotation databases

EnsemblFungiiYDR005C; YDR005C; YDR005C.
GeneIDi851568.
KEGGisce:YDR005C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19492 Genomic DNA. Translation: AAB51655.1.
Z48008 Genomic DNA. Translation: CAA88065.1.
BK006938 Genomic DNA. Translation: DAA11853.1.
PIRiS50986.
RefSeqiNP_010288.1. NM_001180313.1.

3D structure databases

ProteinModelPortaliP41910.
SMRiP41910. Positions 225-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32058. 118 interactions.
DIPiDIP-5133N.
IntActiP41910. 13 interactions.
MINTiMINT-543690.

PTM databases

iPTMnetiP41910.

Proteomic databases

MaxQBiP41910.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR005C; YDR005C; YDR005C.
GeneIDi851568.
KEGGisce:YDR005C.

Organism-specific databases

EuPathDBiFungiDB:YDR005C.
SGDiS000002412. MAF1.

Phylogenomic databases

GeneTreeiENSGT00390000006896.
HOGENOMiHOG000065964.
InParanoidiP41910.
OMAiCDIFTTK.
OrthoDBiEOG7SN8PR.

Enzyme and pathway databases

BioCyciYEAST:G3O-29627-MONOMER.

Miscellaneous databases

PROiP41910.

Family and domain databases

InterProiIPR015257. Maf1.
[Graphical view]
PANTHERiPTHR22504. PTHR22504. 2 hits.
PfamiPF09174. Maf1. 1 hit.
[Graphical view]
PIRSFiPIRSF037240. RNA_polIII_Trep_MAF1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mutation in a new gene MAF1 affects tRNA suppressor efficiency in Saccharomyces cerevisiae."
    Boguta M., Czerska K., Zoladek T.
    Gene 185:291-296(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: T8-1D.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Maf1 is an essential mediator of diverse signals that repress RNA polymerase III transcription."
    Upadhya R., Lee J., Willis I.M.
    Mol. Cell 10:1489-1494(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209 AND SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND THR-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates."
    Soulard A., Cremonesi A., Moes S., Schutz F., Jeno P., Hall M.N.
    Mol. Biol. Cell 21:3475-3486(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY PKA.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAF1_YEAST
AccessioniPrimary (citable) accession number: P41910
Secondary accession number(s): D6VRZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 6, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1720 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.