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Protein

Repressor of RNA polymerase III transcription MAF1 homolog

Gene

Maf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Element of the mTORC1 signaling pathway that acts as a mediator of diverse signals and that represses RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Repressor of RNA polymerase III transcription MAF1 homolog
Gene namesi
Name:Maf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1916127. Maf1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 258258Repressor of RNA polymerase III transcription MAF1 homologPRO_0000213974Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki35 – 35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1 and SUMO2)By similarity
Modified residuei60 – 601Phosphoserine; by MTORBy similarity
Modified residuei64 – 641PhosphothreonineBy similarity
Modified residuei65 – 651PhosphoserineBy similarity
Modified residuei68 – 681Phosphoserine; by MTORBy similarity
Modified residuei70 – 701PhosphoserineBy similarity
Modified residuei75 – 751Phosphoserine; by MTORBy similarity
Modified residuei212 – 2121PhosphothreonineBy similarity
Modified residuei214 – 2141PhosphoserineBy similarity

Post-translational modificationi

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).By similarity
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).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9D0U6.
MaxQBiQ9D0U6.
PaxDbiQ9D0U6.
PRIDEiQ9D0U6.

PTM databases

iPTMnetiQ9D0U6.
PhosphoSiteiQ9D0U6.

Expressioni

Gene expression databases

BgeeiQ9D0U6.
CleanExiMM_MAF1.
ExpressionAtlasiQ9D0U6. baseline and differential.
GenevisibleiQ9D0U6. MM.

Interactioni

Subunit structurei

Interacts with BRF2.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023212.

Structurei

3D structure databases

ProteinModelPortaliQ9D0U6.
SMRiQ9D0U6. Positions 1-205.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MAF1 family.Curated

Phylogenomic databases

eggNOGiKOG3104. Eukaryota.
COG5046. LUCA.
GeneTreeiENSGT00390000006896.
HOGENOMiHOG000185242.
HOVERGENiHBG052395.
InParanoidiQ9D0U6.
OMAiRCYCTSK.
OrthoDBiEOG776SQX.
PhylomeDBiQ9D0U6.
TreeFamiTF315149.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9D0U6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLENSSFE AINSQLTVET GDAHIIGRIE SYSCKMAGDD KHMFKQFCQE
60 70 80 90 100
GQPHVLEALS PPQTSGLSPS RLSKSQGGED ESPLSDKCSR KTLFYLIATL
110 120 130 140 150
NESFRPDYDF STARSHEFSR EPSLRWVVNA VNCSLFSAVR EDFKALKPQL
160 170 180 190 200
WNAVDEEICL AECDIYSYNP DLDSDPFGED GSLWSFNYFF YNKRLKRIVF
210 220 230 240 250
FSCRSISGST YTPSEAGNAL DLELGAEEAD EESGGGGGEG RAEETSTMEE

DRVPVICM
Length:258
Mass (Da):28,780
Last modified:June 1, 2001 - v1
Checksum:i5CE8AE117604B27F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791E → D in AAH16260 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004406 mRNA. Translation: BAB23294.1.
AK042913 mRNA. Translation: BAC31403.1.
AK154047 mRNA. Translation: BAE32337.1.
BC016260 mRNA. Translation: AAH16260.1.
CCDSiCCDS27568.1.
RefSeqiNP_001158079.1. NM_001164607.1.
NP_001158080.1. NM_001164608.1.
NP_081135.3. NM_026859.3.
UniGeneiMm.289680.

Genome annotation databases

EnsembliENSMUST00000023212; ENSMUSP00000023212; ENSMUSG00000022553.
ENSMUST00000160853; ENSMUSP00000124893; ENSMUSG00000022553.
ENSMUST00000161527; ENSMUSP00000125387; ENSMUSG00000022553.
GeneIDi68877.
KEGGimmu:68877.
UCSCiuc007wjw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004406 mRNA. Translation: BAB23294.1.
AK042913 mRNA. Translation: BAC31403.1.
AK154047 mRNA. Translation: BAE32337.1.
BC016260 mRNA. Translation: AAH16260.1.
CCDSiCCDS27568.1.
RefSeqiNP_001158079.1. NM_001164607.1.
NP_001158080.1. NM_001164608.1.
NP_081135.3. NM_026859.3.
UniGeneiMm.289680.

3D structure databases

ProteinModelPortaliQ9D0U6.
SMRiQ9D0U6. Positions 1-205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023212.

PTM databases

iPTMnetiQ9D0U6.
PhosphoSiteiQ9D0U6.

Proteomic databases

EPDiQ9D0U6.
MaxQBiQ9D0U6.
PaxDbiQ9D0U6.
PRIDEiQ9D0U6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023212; ENSMUSP00000023212; ENSMUSG00000022553.
ENSMUST00000160853; ENSMUSP00000124893; ENSMUSG00000022553.
ENSMUST00000161527; ENSMUSP00000125387; ENSMUSG00000022553.
GeneIDi68877.
KEGGimmu:68877.
UCSCiuc007wjw.2. mouse.

Organism-specific databases

CTDi84232.
MGIiMGI:1916127. Maf1.

Phylogenomic databases

eggNOGiKOG3104. Eukaryota.
COG5046. LUCA.
GeneTreeiENSGT00390000006896.
HOGENOMiHOG000185242.
HOVERGENiHBG052395.
InParanoidiQ9D0U6.
OMAiRCYCTSK.
OrthoDBiEOG776SQX.
PhylomeDBiQ9D0U6.
TreeFamiTF315149.

Miscellaneous databases

ChiTaRSiMaf1. mouse.
NextBioi328101.
PROiQ9D0U6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D0U6.
CleanExiMM_MAF1.
ExpressionAtlasiQ9D0U6. baseline and differential.
GenevisibleiQ9D0U6. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Cerebellum and Thymus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Salivary gland.
  3. "mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes, and targets their repressor Maf1."
    Kantidakis T., Ramsbottom B.A., Birch J.L., Dowding S.N., White R.J.
    Proc. Natl. Acad. Sci. U.S.A. 107:11823-11828(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiMAF1_MOUSE
AccessioniPrimary (citable) accession number: Q9D0U6
Secondary accession number(s): Q3U4U3, Q91W84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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.