MAF1_HUMAN
ID MAF1_HUMAN Reviewed; 256 AA.
AC Q9H063; D3DWL4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Repressor of RNA polymerase III transcription MAF1 homolog;
GN Name=MAF1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-236.
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-236.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-236.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-236.
RC TISSUE=Brain, Lung, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP FUNCTION.
RX PubMed=17499043; DOI=10.1016/j.molcel.2007.03.021;
RA Johnson S.S., Zhang C., Fromm J., Willis I.M., Johnson D.L.;
RT "Mammalian Maf1 is a negative regulator of transcription by all three
RT nuclear RNA polymerases.";
RL Mol. Cell 26:367-379(2007).
RN [8]
RP INTERACTION WITH BRF2, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17505538; DOI=10.7150/ijbs.3.292;
RA Rollins J., Veras I., Cabarcas S., Willis I., Schramm L.;
RT "Human Maf1 negatively regulates RNA polymerase III transcription via the
RT TFIIB family members Brf1 and Brf2.";
RL Int. J. Biol. Sci. 3:292-302(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-75, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH POLR3F; BRF1 AND GTF3C1.
RX PubMed=18377933; DOI=10.1016/j.jmb.2008.02.060;
RA Goodfellow S.J., Graham E.L., Kantidakis T., Marshall L., Coppins B.A.,
RA Oficjalska-Pham D., Gerard M., Lefebvre O., White R.J.;
RT "Regulation of RNA polymerase III transcription by Maf1 in mammalian
RT cells.";
RL J. Mol. Biol. 378:481-491(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP FUNCTION, PHOSPHORYLATION AT SER-60; THR-64; SER-68 AND SER-75, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF SER-60; THR-64; SER-68 AND SER-75.
RX PubMed=20233713; DOI=10.1074/jbc.m109.071639;
RA Shor B., Wu J., Shakey Q., Toral-Barza L., Shi C., Follettie M., Yu K.;
RT "Requirement of the mTOR kinase for the regulation of Maf1 phosphorylation
RT and control of RNA polymerase III-dependent transcription in cancer
RT cells.";
RL J. Biol. Chem. 285:15380-15392(2010).
RN [13]
RP FUNCTION, PHOSPHORYLATION AT SER-60; SER-68 AND SER-75 BY MTOR,
RP PHOSPHORYLATION AT THR-64; SER-65; SER-70; THR-212 AND SER-214, AND
RP MUTAGENESIS OF SER-60; SER-68 AND SER-75.
RX PubMed=20516213; DOI=10.1128/mcb.00319-10;
RA Michels A.A., Robitaille A.M., Buczynski-Ruchonnet D., Hodroj W.,
RA Reina J.H., Hall M.N., Hernandez N.;
RT "mTORC1 directly phosphorylates and regulates human MAF1.";
RL Mol. Cell. Biol. 30:3749-3757(2010).
RN [14]
RP FUNCTION, PHOSPHORYLATION AT SER-75, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF SER-75.
RX PubMed=20543138; DOI=10.1073/pnas.1005188107;
RA Kantidakis T., Ramsbottom B.A., Birch J.L., Dowding S.N., White R.J.;
RT "mTOR associates with TFIIIC, is found at tRNA and 5S rRNA genes, and
RT targets their repressor Maf1.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11823-11828(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-75, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP SUMOYLATION AT LYS-35, PHOSPHORYLATION AT SER-75, AND MUTAGENESIS OF
RP LYS-35.
RX PubMed=23673667; DOI=10.1074/jbc.m113.473744;
RA Rohira A.D., Chen C.Y., Allen J.R., Johnson D.L.;
RT "Covalent small ubiquitin-like modifier (SUMO) modification of Maf1 protein
RT controls RNA polymerase III-dependent transcription repression.";
RL J. Biol. Chem. 288:19288-19295(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-214, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP FUNCTION.
RX PubMed=26941251; DOI=10.1101/gr.201400.115;
RA Orioli A., Praz V., Lhote P., Hernandez N.;
RT "Human MAF1 targets and represses active RNA polymerase III genes by
RT preventing recruitment rather than inducing long-term transcriptional
RT arrest.";
RL Genome Res. 26:624-635(2016).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1-205, AND FUNCTION.
RX PubMed=20887893; DOI=10.1016/j.cell.2010.09.002;
RA Vannini A., Ringel R., Kusser A.G., Berninghausen O., Kassavetis G.A.,
RA Cramer P.;
RT "Molecular basis of RNA polymerase III transcription repression by Maf1.";
RL Cell 143:59-70(2010).
CC -!- FUNCTION: Plays a role in the repression of RNA polymerase III-mediated
CC transcription in response to changing nutritional, environmental and
CC cellular stress conditions to balance the production of highly abundant
CC tRNAs, 5S rRNA, and other small non-coding RNAs with cell growth and
CC maintenance (PubMed:18377933, PubMed:20233713, PubMed:20516213,
CC PubMed:20543138). Also plays a key role in cell fate determination by
CC promoting mesorderm induction and adipocyte differentiation (By
CC similarity). Mechanistically, associates with the RNA polymerase III
CC clamp and thereby impairs its recruitment to the complex made of the
CC promoter DNA, TBP and the initiation factor TFIIIB (PubMed:20887893,
CC PubMed:17505538). When nutrients are available and mTOR kinase is
CC active, MAF1 is hyperphosphorylated and RNA polymerase III is engaged
CC in transcription. Stress-induced MAF1 dephosphorylation results in
CC nuclear localization, increased targeting of gene-bound RNA polymerase
CC III and a decrease in the transcriptional readout (PubMed:26941251).
CC Additionally, may also regulate RNA polymerase I and RNA polymerase II-
CC dependent transcription through its ability to regulate expression of
CC the central initiation factor TBP (PubMed:17499043).
CC {ECO:0000250|UniProtKB:Q9D0U6, ECO:0000269|PubMed:17499043,
CC ECO:0000269|PubMed:17505538, ECO:0000269|PubMed:18377933,
CC ECO:0000269|PubMed:20233713, ECO:0000269|PubMed:20516213,
CC ECO:0000269|PubMed:20543138, ECO:0000269|PubMed:20887893,
CC ECO:0000269|PubMed:26941251}.
CC -!- SUBUNIT: Interacts with TFIIIB subunits BRF1 and BRF2 (PubMed:17505538,
CC PubMed:18377933). Interacts with Pol III subunit POLR3F. Interacts with
CC TFIIIC subunit GTF3C1 (PubMed:18377933). {ECO:0000269|PubMed:17505538,
CC ECO:0000269|PubMed:18377933}.
CC -!- INTERACTION:
CC Q9H063; Q9UH62: ARMCX3; NbExp=3; IntAct=EBI-720354, EBI-717832;
CC Q9H063; P42858: HTT; NbExp=3; IntAct=EBI-720354, EBI-466029;
CC Q9H063; P12004: PCNA; NbExp=4; IntAct=EBI-720354, EBI-358311;
CC Q9H063; O76024: WFS1; NbExp=3; IntAct=EBI-720354, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17505538,
CC ECO:0000269|PubMed:20233713}. Cytoplasm {ECO:0000269|PubMed:20233713}.
CC -!- PTM: Phosphorylated at Ser-60, Ser-68 and Ser-75; the major sites of
CC phosphorylation. Nuclear accumulation correlates with a concomitant
CC dephosphorylation. Phosphorylation may attenuate its RNA polymerase
CC III-repressive function. {ECO:0000269|PubMed:20233713,
CC ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20543138,
CC ECO:0000269|PubMed:23673667}.
CC -!- PTM: Sumoylated with SUMO1 and SUMO2, mainly on Lys-35. Desumoylated by
CC SENP1. SUMOylation promotes the ability of MAF1 to repress
CC transcription and suppress colony formation.
CC {ECO:0000269|PubMed:23673667}.
CC -!- SIMILARITY: Belongs to the MAF1 family. {ECO:0000305}.
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DR EMBL; AL136937; CAB66871.1; -; mRNA.
DR EMBL; CR533463; CAG38494.1; -; mRNA.
DR EMBL; AC104592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471162; EAW82158.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82159.1; -; Genomic_DNA.
DR EMBL; BC014082; AAH14082.1; -; mRNA.
DR EMBL; BC018714; AAH18714.1; -; mRNA.
DR EMBL; BC031273; AAH31273.1; -; mRNA.
DR CCDS; CCDS6416.1; -.
DR RefSeq; NP_115648.2; NM_032272.4.
DR RefSeq; XP_016869393.1; XM_017013904.1.
DR PDB; 3NR5; X-ray; 1.55 A; A=1-205.
DR PDBsum; 3NR5; -.
DR AlphaFoldDB; Q9H063; -.
DR SMR; Q9H063; -.
DR BioGRID; 123965; 25.
DR DIP; DIP-53028N; -.
DR IntAct; Q9H063; 18.
DR MINT; Q9H063; -.
DR STRING; 9606.ENSP00000318604; -.
DR iPTMnet; Q9H063; -.
DR PhosphoSitePlus; Q9H063; -.
DR BioMuta; MAF1; -.
DR DMDM; 296434582; -.
DR EPD; Q9H063; -.
DR jPOST; Q9H063; -.
DR MassIVE; Q9H063; -.
DR MaxQB; Q9H063; -.
DR PaxDb; Q9H063; -.
DR PeptideAtlas; Q9H063; -.
DR PRIDE; Q9H063; -.
DR ProteomicsDB; 80206; -.
DR Antibodypedia; 28301; 185 antibodies from 29 providers.
DR DNASU; 84232; -.
DR Ensembl; ENST00000322428.10; ENSP00000318604.5; ENSG00000179632.10.
DR Ensembl; ENST00000532522.5; ENSP00000436720.1; ENSG00000179632.10.
DR GeneID; 84232; -.
DR KEGG; hsa:84232; -.
DR MANE-Select; ENST00000322428.10; ENSP00000318604.5; NM_032272.5; NP_115648.2.
DR UCSC; uc003zbc.2; human.
DR CTD; 84232; -.
DR DisGeNET; 84232; -.
DR GeneCards; MAF1; -.
DR HGNC; HGNC:24966; MAF1.
DR HPA; ENSG00000179632; Low tissue specificity.
DR MIM; 610210; gene.
DR neXtProt; NX_Q9H063; -.
DR OpenTargets; ENSG00000179632; -.
DR PharmGKB; PA142671489; -.
DR VEuPathDB; HostDB:ENSG00000179632; -.
DR eggNOG; KOG3104; Eukaryota.
DR GeneTree; ENSGT00390000006896; -.
DR InParanoid; Q9H063; -.
DR OrthoDB; 939345at2759; -.
DR PhylomeDB; Q9H063; -.
DR TreeFam; TF315149; -.
DR PathwayCommons; Q9H063; -.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR SignaLink; Q9H063; -.
DR SIGNOR; Q9H063; -.
DR BioGRID-ORCS; 84232; 19 hits in 1079 CRISPR screens.
DR ChiTaRS; MAF1; human.
DR EvolutionaryTrace; Q9H063; -.
DR GeneWiki; MAF1; -.
DR GenomeRNAi; 84232; -.
DR Pharos; Q9H063; Tbio.
DR PRO; PR:Q9H063; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9H063; protein.
DR Bgee; ENSG00000179632; Expressed in hindlimb stylopod muscle and 179 other tissues.
DR ExpressionAtlas; Q9H063; baseline and differential.
DR Genevisible; Q9H063; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000994; F:RNA polymerase III core binding; IBA:GO_Central.
DR GO; GO:0001002; F:RNA polymerase III type 1 promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001003; F:RNA polymerase III type 2 promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IDA:CACAO.
DR GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; IDA:UniProtKB.
DR Gene3D; 3.40.1000.50; -; 2.
DR InterPro; IPR015257; Maf1.
DR InterPro; IPR038564; Maf1_sf.
DR PANTHER; PTHR22504; PTHR22504; 1.
DR Pfam; PF09174; Maf1; 1.
DR PIRSF; PIRSF037240; RNA_polIII_Trep_MAF1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..256
FT /note="Repressor of RNA polymerase III transcription MAF1
FT homolog"
FT /id="PRO_0000213973"
FT REGION 58..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine; by MTOR"
FT /evidence="ECO:0000269|PubMed:20233713,
FT ECO:0000269|PubMed:20516213, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20233713,
FT ECO:0000269|PubMed:20516213"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20516213"
FT MOD_RES 68
FT /note="Phosphoserine; by MTOR"
FT /evidence="ECO:0000269|PubMed:20233713,
FT ECO:0000269|PubMed:20516213"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20516213"
FT MOD_RES 75
FT /note="Phosphoserine; by MTOR"
FT /evidence="ECO:0000269|PubMed:20233713,
FT ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20543138,
FT ECO:0000269|PubMed:23673667, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20516213"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20516213,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1 and SUMO2)"
FT VARIANT 236
FT /note="G -> R (in dbSNP:rs11546144)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.4"
FT /id="VAR_060408"
FT MUTAGEN 35
FT /note="K->R: No interaction with RNA pol III and impaired
FT recruitment to tRNA gene promoters."
FT /evidence="ECO:0000269|PubMed:23673667"
FT MUTAGEN 60
FT /note="S->A: Stronger repressive effect on RNA polymerase
FT III transcription; when associated with A-68 and A-75. Much
FT stronger repressive effect on RNA polymerase III
FT transcription and loss of phosphorylation; when associated
FT with A-64, A-68 and A-75."
FT /evidence="ECO:0000269|PubMed:20233713,
FT ECO:0000269|PubMed:20516213"
FT MUTAGEN 60
FT /note="S->D: No change. Weaker repressive effect on RNA
FT polymerase III transcription; when associated with D-68 and
FT D-75."
FT /evidence="ECO:0000269|PubMed:20233713,
FT ECO:0000269|PubMed:20516213"
FT MUTAGEN 64
FT /note="T->A: Much stronger repressive effect on RNA
FT polymerase III transcription and loss of phosphorylation;
FT when associated with A-60, A-68 and A-75."
FT /evidence="ECO:0000269|PubMed:20233713"
FT MUTAGEN 68
FT /note="S->A: Stronger repressive effect on RNA polymerase
FT III transcription; when associated with A-60 and A-75. Much
FT stronger repressive effect on RNA polymerase III
FT transcription and loss of phosphorylation; when associated
FT with A-60, A-64 and A-75."
FT /evidence="ECO:0000269|PubMed:20233713,
FT ECO:0000269|PubMed:20516213"
FT MUTAGEN 68
FT /note="S->D: No change. Weaker repressive effect on RNA
FT polymerase III transcription; when associated with D-60 and
FT D-75."
FT /evidence="ECO:0000269|PubMed:20233713,
FT ECO:0000269|PubMed:20516213"
FT MUTAGEN 75
FT /note="S->A: Stronger repressive effect on RNA polymerase
FT III transcription. Stronger repressive effect on RNA
FT polymerase III transcription; when associated with A-60 and
FT A-68. Much stronger repressive effect on RNA polymerase III
FT transcription and loss of phosphorylation; when associated
FT with A-60, A-64 and A-68."
FT /evidence="ECO:0000269|PubMed:20233713,
FT ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20543138"
FT MUTAGEN 75
FT /note="S->D: No change. Weaker repressive effect on RNA
FT polymerase III transcription; when associated with D-60 and
FT D-68."
FT /evidence="ECO:0000269|PubMed:20233713,
FT ECO:0000269|PubMed:20516213, ECO:0000269|PubMed:20543138"
FT STRAND 1..4
FT /evidence="ECO:0007829|PDB:3NR5"
FT HELIX 7..15
FT /evidence="ECO:0007829|PDB:3NR5"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:3NR5"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:3NR5"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:3NR5"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3NR5"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3NR5"
FT HELIX 124..139
FT /evidence="ECO:0007829|PDB:3NR5"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:3NR5"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:3NR5"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3NR5"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:3NR5"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:3NR5"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:3NR5"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:3NR5"
FT STRAND 197..205
FT /evidence="ECO:0007829|PDB:3NR5"
SQ SEQUENCE 256 AA; 28771 MW; D6C06D2E476753AA CRC64;
MKLLENSSFE AINSQLTVET GDAHIIGRIE SYSCKMAGDD KHMFKQFCQE GQPHVLEALS
PPQTSGLSPS RLSKSQGGEE EGPLSDKCSR KTLFYLIATL NESFRPDYDF STARSHEFSR
EPSLSWVVNA VNCSLFSAVR EDFKDLKPQL WNAVDEEICL AECDIYSYNP DLDSDPFGED
GSLWSFNYFF YNKRLKRIVF FSCRSISGST YTPSEAGNEL DMELGEEEVE EESRSGGSGA
EETSTMEEDR VPVICI
