Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Repressor of RNA polymerase III transcription MAF1 homolog

Gene

MAF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.3 Publications

GO - Molecular functioni

  • RNA polymerase III core binding Source: GO_Central
  • RNA polymerase III type 1 promoter DNA binding Source: UniProtKB
  • RNA polymerase III type 2 promoter DNA binding Source: UniProtKB
  • RNA polymerase III type 3 promoter DNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

SIGNORiQ9H063.

Names & Taxonomyi

Protein namesi
Recommended name:
Repressor of RNA polymerase III transcription MAF1 homolog
Gene namesi
Name:MAF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:24966. MAF1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 351K → R: No interaction with RNA pol III and impaired recruitment to tRNA gene promoters. 1 Publication
Mutagenesisi60 – 601S → 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. 2 Publications
Mutagenesisi60 – 601S → D: No change. Weaker repressive effect on RNA polymerase III transcription; when associated with D-68 and D-75. 2 Publications
Mutagenesisi64 – 641T → A: Much stronger repressive effect on RNA polymerase III transcription and loss of phosphorylation; when associated with A-60, A-68 and A-75. 1 Publication
Mutagenesisi68 – 681S → 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. 2 Publications
Mutagenesisi68 – 681S → D: No change. Weaker repressive effect on RNA polymerase III transcription; when associated with D-60 and D-75. 2 Publications
Mutagenesisi75 – 751S → 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. 3 Publications
Mutagenesisi75 – 751S → D: No change. Weaker repressive effect on RNA polymerase III transcription; when associated with D-60 and D-68. 3 Publications

Organism-specific databases

PharmGKBiPA142671489.

Polymorphism and mutation databases

BioMutaiMAF1.
DMDMi296434582.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 256256Repressor of RNA polymerase III transcription MAF1 homologPRO_0000213973Add
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)
Modified residuei60 – 601Phosphoserine; by MTORCombined sources2 Publications
Modified residuei64 – 641Phosphothreonine2 Publications
Modified residuei65 – 651Phosphoserine1 Publication
Modified residuei68 – 681Phosphoserine; by MTOR2 Publications
Modified residuei70 – 701Phosphoserine1 Publication
Modified residuei75 – 751Phosphoserine; by MTORCombined sources4 Publications
Modified residuei212 – 2121Phosphothreonine1 Publication
Modified residuei214 – 2141PhosphoserineCombined sources1 Publication

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.4 Publications
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.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9H063.
MaxQBiQ9H063.
PaxDbiQ9H063.
PeptideAtlasiQ9H063.
PRIDEiQ9H063.

PTM databases

iPTMnetiQ9H063.
PhosphoSiteiQ9H063.

Expressioni

Gene expression databases

BgeeiQ9H063.
CleanExiHS_MAF1.
ExpressionAtlasiQ9H063. baseline and differential.
GenevisibleiQ9H063. HS.

Organism-specific databases

HPAiHPA024821.
HPA058548.

Interactioni

Subunit structurei

Interacts with BRF2.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi123965. 17 interactions.
DIPiDIP-53028N.
IntActiQ9H063. 5 interactions.
MINTiMINT-1424988.
STRINGi9606.ENSP00000318604.

Structurei

Secondary structure

256
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 44Combined sources
Helixi7 – 159Combined sources
Beta strandi27 – 348Combined sources
Helixi91 – 10414Combined sources
Turni105 – 1073Combined sources
Helixi115 – 1173Combined sources
Beta strandi118 – 1203Combined sources
Helixi124 – 13916Combined sources
Helixi140 – 1423Combined sources
Helixi143 – 15816Combined sources
Helixi160 – 1623Combined sources
Beta strandi164 – 1685Combined sources
Helixi172 – 1743Combined sources
Beta strandi183 – 19210Combined sources
Turni193 – 1964Combined sources
Beta strandi197 – 2059Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NR5X-ray1.55A1-205[»]
ProteinModelPortaliQ9H063.
SMRiQ9H063. Positions 1-205.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H063.

Family & Domainsi

Sequence similaritiesi

Belongs to the MAF1 family.Curated

Phylogenomic databases

eggNOGiKOG3104. Eukaryota.
COG5046. LUCA.
GeneTreeiENSGT00390000006896.
HOGENOMiHOG000185242.
HOVERGENiHBG052395.
InParanoidiQ9H063.
OrthoDBiEOG776SQX.
PhylomeDBiQ9H063.
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.

Q9H063-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLENSSFE AINSQLTVET GDAHIIGRIE SYSCKMAGDD KHMFKQFCQE
60 70 80 90 100
GQPHVLEALS PPQTSGLSPS RLSKSQGGEE EGPLSDKCSR KTLFYLIATL
110 120 130 140 150
NESFRPDYDF STARSHEFSR EPSLSWVVNA VNCSLFSAVR EDFKDLKPQL
160 170 180 190 200
WNAVDEEICL AECDIYSYNP DLDSDPFGED GSLWSFNYFF YNKRLKRIVF
210 220 230 240 250
FSCRSISGST YTPSEAGNEL DMELGEEEVE EESRSGGSGA EETSTMEEDR

VPVICI
Length:256
Mass (Da):28,771
Last modified:May 18, 2010 - v2
Checksum:iD6C06D2E476753AA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti236 – 2361G → R.4 Publications
Corresponds to variant rs11546144 [ dbSNP | Ensembl ].
VAR_060408

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136937 mRNA. Translation: CAB66871.1.
CR533463 mRNA. Translation: CAG38494.1.
AC104592 Genomic DNA. No translation available.
CH471162 Genomic DNA. Translation: EAW82158.1.
CH471162 Genomic DNA. Translation: EAW82159.1.
BC014082 mRNA. Translation: AAH14082.1.
BC018714 mRNA. Translation: AAH18714.1.
BC031273 mRNA. Translation: AAH31273.1.
CCDSiCCDS6416.1.
RefSeqiNP_115648.2. NM_032272.4.
UniGeneiHs.19673.

Genome annotation databases

EnsembliENST00000322428; ENSP00000318604; ENSG00000179632.
ENST00000532522; ENSP00000436720; ENSG00000179632.
GeneIDi84232.
KEGGihsa:84232.
UCSCiuc003zbc.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL136937 mRNA. Translation: CAB66871.1.
CR533463 mRNA. Translation: CAG38494.1.
AC104592 Genomic DNA. No translation available.
CH471162 Genomic DNA. Translation: EAW82158.1.
CH471162 Genomic DNA. Translation: EAW82159.1.
BC014082 mRNA. Translation: AAH14082.1.
BC018714 mRNA. Translation: AAH18714.1.
BC031273 mRNA. Translation: AAH31273.1.
CCDSiCCDS6416.1.
RefSeqiNP_115648.2. NM_032272.4.
UniGeneiHs.19673.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NR5X-ray1.55A1-205[»]
ProteinModelPortaliQ9H063.
SMRiQ9H063. Positions 1-205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123965. 17 interactions.
DIPiDIP-53028N.
IntActiQ9H063. 5 interactions.
MINTiMINT-1424988.
STRINGi9606.ENSP00000318604.

PTM databases

iPTMnetiQ9H063.
PhosphoSiteiQ9H063.

Polymorphism and mutation databases

BioMutaiMAF1.
DMDMi296434582.

Proteomic databases

EPDiQ9H063.
MaxQBiQ9H063.
PaxDbiQ9H063.
PeptideAtlasiQ9H063.
PRIDEiQ9H063.

Protocols and materials databases

DNASUi84232.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322428; ENSP00000318604; ENSG00000179632.
ENST00000532522; ENSP00000436720; ENSG00000179632.
GeneIDi84232.
KEGGihsa:84232.
UCSCiuc003zbc.2. human.

Organism-specific databases

CTDi84232.
GeneCardsiMAF1.
H-InvDBHIX0022762.
HGNCiHGNC:24966. MAF1.
HPAiHPA024821.
HPA058548.
MIMi610210. gene.
neXtProtiNX_Q9H063.
PharmGKBiPA142671489.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3104. Eukaryota.
COG5046. LUCA.
GeneTreeiENSGT00390000006896.
HOGENOMiHOG000185242.
HOVERGENiHBG052395.
InParanoidiQ9H063.
OrthoDBiEOG776SQX.
PhylomeDBiQ9H063.
TreeFamiTF315149.

Enzyme and pathway databases

SIGNORiQ9H063.

Miscellaneous databases

ChiTaRSiMAF1. human.
EvolutionaryTraceiQ9H063.
GeneWikiiMAF1.
GenomeRNAii84232.
PROiQ9H063.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H063.
CleanExiHS_MAF1.
ExpressionAtlasiQ9H063. baseline and differential.
GenevisibleiQ9H063. HS.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-236.
    Tissue: Uterus.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-236.
  3. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-236.
  5. "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], VARIANT ARG-236.
    Tissue: Brain, Lung and Uterus.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Human Maf1 negatively regulates RNA polymerase III transcription via the TFIIB family members Brf1 and Brf2."
    Rollins J., Veras I., Cabarcas S., Willis I., Schramm L.
    Int. J. Biol. Sci. 3:292-302(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRF2.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Requirement of the mTOR kinase for the regulation of Maf1 phosphorylation and control of RNA polymerase III-dependent transcription in cancer cells."
    Shor B., Wu J., Shakey Q., Toral-Barza L., Shi C., Follettie M., Yu K.
    J. Biol. Chem. 285:15380-15392(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-60; THR-64; SER-68 AND SER-75, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-60; THR-64; SER-68 AND SER-75.
  11. Cited for: FUNCTION, PHOSPHORYLATION AT SER-60; SER-68 AND SER-75 BY MTOR, PHOSPHORYLATION AT THR-64; SER-65; SER-70; THR-212 AND SER-214, MUTAGENESIS OF SER-60; SER-68 AND SER-75.
  12. "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: FUNCTION, PHOSPHORYLATION AT SER-75, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-75.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Covalent small ubiquitin-like modifier (SUMO) modification of Maf1 protein controls RNA polymerase III-dependent transcription repression."
    Rohira A.D., Chen C.Y., Allen J.R., Johnson D.L.
    J. Biol. Chem. 288:19288-19295(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-35, PHOSPHORYLATION AT SER-75, MUTAGENESIS OF LYS-35.
  16. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMAF1_HUMAN
AccessioniPrimary (citable) accession number: Q9H063
Secondary accession number(s): D3DWL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: May 18, 2010
Last modified: July 6, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.