TTF1_MOUSE
ID TTF1_MOUSE Reviewed; 859 AA.
AC Q62187; Q9JKK5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Transcription termination factor 1;
DE Short=TTF-1;
DE AltName: Full=RNA polymerase I termination factor;
DE AltName: Full=Transcription termination factor I;
DE Short=TTF-I;
DE Short=mTFF-I;
GN Name=Ttf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 394-400 AND 457-498,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Ehrlich ascites tumor cell;
RX PubMed=7720715; DOI=10.1002/j.1460-2075.1995.tb07108.x;
RA Evers R., Smid A., Rudloff U., Lottspeich F., Gummt I.;
RT "Different domains of the murine RNA polymerase I-specific termination
RT factor mTTF-I serve distinct functions in transcription termination.";
RL EMBO J. 14:1248-1256(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hu Q., Rothblum L.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP SUBUNIT.
RX PubMed=9092622; DOI=10.1093/nar/25.6.1142;
RA Sander E.E., Grummt I.;
RT "Oligomerization of the transcription termination factor TTF-I:
RT implications for the structural organization of ribosomal transcription
RT units.";
RL Nucleic Acids Res. 25:1142-1147(1997).
RN [5]
RP FUNCTION.
RX PubMed=9267035; DOI=10.1016/s0092-8674(00)80515-2;
RA Gerber J.-K., Goegel E., Berger C., Wallisch M., Mueller F., Grummt I.,
RA Grummt F.;
RT "Termination of mammalian rDNA replication: polar arrest of replication
RT fork movement by transcription termination factor TTF-I.";
RL Cell 90:559-567(1997).
RN [6]
RP FUNCTION.
RX PubMed=9049305; DOI=10.1093/emboj/16.4.760;
RA Laengst G., Blank T.A., Becker P.B., Grummt I.;
RT "RNA polymerase I transcription on nucleosomal templates: the transcription
RT termination factor TTF-I induces chromatin remodeling and relieves
RT transcriptional repression.";
RL EMBO J. 16:760-768(1997).
RN [7]
RP INTERACTION WITH CAVIN1.
RX PubMed=9582279; DOI=10.1093/emboj/17.10.2855;
RA Jansa P., Mason S.W., Hoffmann-Rohrer U., Grummt I.;
RT "Cloning and functional characterization of PTRF, a novel protein which
RT induces dissociation of paused ternary transcription complexes.";
RL EMBO J. 17:2855-2864(1998).
RN [8]
RP INTERACTION WITH BAZ2A, AND FUNCTION.
RX PubMed=15292447; DOI=10.1093/nar/gkh732;
RA Nemeth A., Strohner R., Grummt I., Laengst G.;
RT "The chromatin remodeling complex NoRC and TTF-I cooperate in the
RT regulation of the mammalian rRNA genes in vivo.";
RL Nucleic Acids Res. 32:4091-4099(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457 AND SER-460, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437; SER-457 AND SER-460, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION, INTERACTION WITH CDKN2A/ARF AND NPM1, AND SUBCELLULAR LOCATION.
RX PubMed=20513429; DOI=10.1016/j.molcel.2010.03.015;
RA Lessard F., Morin F., Ivanchuk S., Langlois F., Stefanovsky V., Rutka J.,
RA Moss T.;
RT "The ARF tumor suppressor controls ribosome biogenesis by regulating the
RT RNA polymerase I transcription factor TTF-I.";
RL Mol. Cell 38:539-550(2010).
RN [12]
RP INTERACTION WITH CAVIN1.
RX PubMed=27528195; DOI=10.7554/elife.17508;
RA Liu L., Pilch P.F.;
RT "PTRF/Cavin-1 promotes efficient ribosomal RNA transcription in response to
RT metabolic challenges.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Multifunctional nucleolar protein that terminates ribosomal
CC gene transcription, mediates replication fork arrest and regulates RNA
CC polymerase I transcription on chromatin (PubMed:7720715,
CC PubMed:9267035, PubMed:15292447, PubMed:9049305). Plays a dual role in
CC rDNA regulation, being involved in both activation and silencing of
CC rDNA transcription (PubMed:15292447, PubMed:20513429). Interaction with
CC BAZ2A/TIP5 recovers DNA-binding activity (PubMed:15292447).
CC {ECO:0000269|PubMed:15292447, ECO:0000269|PubMed:20513429,
CC ECO:0000269|PubMed:7720715, ECO:0000269|PubMed:9049305,
CC ECO:0000269|PubMed:9267035}.
CC -!- SUBUNIT: Oligomer. The oligomeric structure enables to interact
CC simultaneously with two separate DNA fragments (PubMed:9092622).
CC Interacts with BAZ2A/TIP5 (PubMed:15292447). Interacts with CAVIN1
CC (PubMed:9582279, PubMed:27528195). Interacts (via the N-terminal region
CC (NRD) and a C-terminal region) with CDKN2A/ARF; the interaction is
CC direct (PubMed:20513429). Interacts (via C-terminal region) with
CC NPM1/B23 (PubMed:20513429). {ECO:0000269|PubMed:15292447,
CC ECO:0000269|PubMed:27528195, ECO:0000269|PubMed:9092622,
CC ECO:0000269|PubMed:9582279}.
CC -!- INTERACTION:
CC Q62187; Q9UIF9: BAZ2A; Xeno; NbExp=3; IntAct=EBI-11705418, EBI-934890;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7720715}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:20513429, ECO:0000269|PubMed:7720715}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:20513429}. Note=May be
CC localized to the nucleolus in an NPM1/B23-dependent manner
CC (PubMed:20513429). May be displaced from the nucleolus into the
CC nucleoplasm in an CDKN2A/ARF-dependent manner (PubMed:20513429). May
CC shuttle back and forth from nucleoplasm to nucleolus (PubMed:20513429).
CC {ECO:0000269|PubMed:20513429}.
CC -!- DOMAIN: The N-terminal region (NRD) inhibits DNA-binding via its
CC interaction with the C-terminal region.
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DR EMBL; X83974; CAA58808.1; -; mRNA.
DR EMBL; AF237703; AAF43448.1; -; mRNA.
DR EMBL; BC059011; AAH59011.1; -; mRNA.
DR CCDS; CCDS38089.1; -.
DR PIR; S54776; S54776.
DR RefSeq; NP_033468.2; NM_009442.2.
DR RefSeq; XP_006497915.1; XM_006497852.1.
DR AlphaFoldDB; Q62187; -.
DR BioGRID; 204361; 3.
DR IntAct; Q62187; 1.
DR STRING; 10090.ENSMUSP00000097809; -.
DR iPTMnet; Q62187; -.
DR PhosphoSitePlus; Q62187; -.
DR EPD; Q62187; -.
DR MaxQB; Q62187; -.
DR PaxDb; Q62187; -.
DR PeptideAtlas; Q62187; -.
DR PRIDE; Q62187; -.
DR ProteomicsDB; 297677; -.
DR Antibodypedia; 45229; 246 antibodies from 32 providers.
DR DNASU; 22130; -.
DR Ensembl; ENSMUST00000100237; ENSMUSP00000097809; ENSMUSG00000026803.
DR GeneID; 22130; -.
DR KEGG; mmu:22130; -.
DR UCSC; uc008izk.1; mouse.
DR CTD; 7270; -.
DR MGI; MGI:105044; Ttf1.
DR VEuPathDB; HostDB:ENSMUSG00000026803; -.
DR eggNOG; KOG0051; Eukaryota.
DR GeneTree; ENSGT00940000159729; -.
DR HOGENOM; CLU_016962_1_0_1; -.
DR InParanoid; Q62187; -.
DR OMA; MQESRPA; -.
DR OrthoDB; 1474117at2759; -.
DR PhylomeDB; Q62187; -.
DR TreeFam; TF333537; -.
DR Reactome; R-MMU-5683826; Surfactant metabolism.
DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination.
DR BioGRID-ORCS; 22130; 22 hits in 80 CRISPR screens.
DR ChiTaRS; Ttf1; mouse.
DR PRO; PR:Q62187; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q62187; protein.
DR Bgee; ENSMUSG00000026803; Expressed in gastrula and 223 other tissues.
DR Genevisible; Q62187; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IDA:MGI.
DR GO; GO:0008156; P:negative regulation of DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:MGI.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA:MGI.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR001005; SANT/Myb.
DR SMART; SM00717; SANT; 2.
DR PROSITE; PS50090; MYB_LIKE; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA replication inhibitor; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Transcription termination;
KW Ubl conjugation.
FT CHAIN 1..859
FT /note="Transcription termination factor 1"
FT /id="PRO_0000250473"
FT DOMAIN 585..634
FT /note="Myb-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT DOMAIN 634..718
FT /note="Myb-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 1..210
FT /note="N-terminal region (NRD)"
FT REGION 1..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..210
FT /note="May be involved in localization to the nucleolus and
FT interaction with ARF"
FT /evidence="ECO:0000269|PubMed:20513429"
FT REGION 225..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..859
FT /note="May be involved in interaction with ARF"
FT /evidence="ECO:0000269|PubMed:20513429"
FT COMPBIAS 11..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15361"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15361"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15361"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15361"
FT CROSSLNK 673
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15361"
FT CONFLICT 72..96
FT /note="Missing (in Ref. 1; CAA58808)"
FT /evidence="ECO:0000305"
FT CONFLICT 305..307
FT /note="KKS -> RSL (in Ref. 1; CAA58808)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="Missing (in Ref. 1; CAA58808)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="R -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="A -> C (in Ref. 1; CAA58808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 859 AA; 97723 MW; D47950ECB3A08DCD CRC64;
MKGGTSKFKT HTETLYKKKK WSSVSEKRPQ KCPSQCLESK QPQVSVLGKR RRASQTPAQE
TLESEWPQKA KRKKRRREPQ TPAQETLESE WPQKAKKKKR RGEPQTPTQE SLESEQPPVS
LLGKRRRESQ TPAQENSESE QPRKAKRRRK KRKGSQQPTS SLLKTPETFL KAKKTTSAHK
KKKNSVLEVD METGIILVDK ENMENLLETS RKDVDIVYVD MSKGQRSAKV RETGELPAAK
PQEHGCRELL GDVRSRKKQK HLQKVAPWDV VQGSQPESIS LPPSEPLSSE DLEGKSTEAA
VFCKKKSKKN VFRSQELEPI PDSLDDSETI SERLDSTHHG GAVGAGEECE STKESHSIKK
KSKKKKHKSV ALATSSDSAS VTDSKAKNAL VDSSEGSGAV REEDVDHRPA EAEAQACSTE
KHREAMQRLE PTHEEESNSE SASNSAARHI SEDRRESDDS DVDLGSAVRQ LREFIPDIQE
RAATTIRRMY RDDLGRFKEF KAQGVAIRFG KFSAKENKQI EKNVQDFLSL TGIESADKLL
YTDRYPEEKT LITNLKRKHA FRLHIGKGIA RPWKLVYYRA KKIFDVNNYK GRYNEEDTKK
LKAYHSLHGN DWKKIGAMVA RSSLSVALKF SQIGGTRNQG AWSKAETQRL IKAVEDVILK
KMSPQELREL DSKLQEDPEG RLSIVREKLY KGISWVEVEA RVETRNWMQC KSKWTEILTK
RMTHGGFVYR GVNALQAKIT LIERLYELNV NDANEIDWED LASAIGDVPP PFVQAKFYKL
KAACVPFWQK KTFPEIIDYL YKNSLPLLKE KLDKKMKKKD GQIQTPAAPK QDFLFKDIFH
CDDDSDEGSP EEPSASDVQ
