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Q62187 (TTF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription termination factor 1

Short name=TTF-1
Alternative name(s):
RNA polymerase I termination factor
Transcription termination factor I
Short name=TTF-I
Short name=mTFF-I
Gene names
Name:Ttf1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length859 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Multifunctional nucleolar protein that terminates ribosomal gene transcription, mediates replication fork arrest and regulates RNA polymerase I transcription on chromatin. Plays a dual role in rDNA regulation, being involved in both activation and silencing of rDNA transcription. Interaction with BAZ2A/TIP5 recovers DNA-binding activity. Ref.1 Ref.5 Ref.6 Ref.7

Subunit structure

Oligomer. The oligomeric structure enables to interact simultaneously with two separatee DNA fragments. Interacts with BAZ2A/TIP5. Ref.4 Ref.7

Subcellular location

Nucleus. Nucleusnucleolus Ref.1.

Domain

The N-terminal region (NRD) inhibits DNA-binding via its interaction with the C-terminal region.

Sequence similarities

Contains 2 Myb-like domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 859859Transcription termination factor 1
PRO_0000250473

Regions

Domain585 – 63450Myb-like 1
Domain634 – 71885Myb-like 2
Region1 – 210210N-terminal region (NRD)
Compositional bias359 – 36810Poly-Lys

Amino acid modifications

Modified residue2271Phosphoserine By similarity
Modified residue3751Phosphoserine By similarity
Modified residue4511Phosphoserine By similarity
Modified residue4571Phosphoserine Ref.8
Modified residue4601Phosphoserine Ref.8
Modified residue8451Phosphoserine By similarity

Experimental info

Sequence conflict72 – 9625Missing in CAA58808. Ref.1
Sequence conflict305 – 3073KKS → RSL in CAA58808. Ref.1
Sequence conflict3481Missing in CAA58808. Ref.1
Sequence conflict4961R → L AA sequence Ref.1
Sequence conflict7621A → C in CAA58808. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q62187 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: D47950ECB3A08DCD

FASTA85997,723
        10         20         30         40         50         60 
MKGGTSKFKT HTETLYKKKK WSSVSEKRPQ KCPSQCLESK QPQVSVLGKR RRASQTPAQE 

        70         80         90        100        110        120 
TLESEWPQKA KRKKRRREPQ TPAQETLESE WPQKAKKKKR RGEPQTPTQE SLESEQPPVS 

       130        140        150        160        170        180 
LLGKRRRESQ TPAQENSESE QPRKAKRRRK KRKGSQQPTS SLLKTPETFL KAKKTTSAHK 

       190        200        210        220        230        240 
KKKNSVLEVD METGIILVDK ENMENLLETS RKDVDIVYVD MSKGQRSAKV RETGELPAAK 

       250        260        270        280        290        300 
PQEHGCRELL GDVRSRKKQK HLQKVAPWDV VQGSQPESIS LPPSEPLSSE DLEGKSTEAA 

       310        320        330        340        350        360 
VFCKKKSKKN VFRSQELEPI PDSLDDSETI SERLDSTHHG GAVGAGEECE STKESHSIKK 

       370        380        390        400        410        420 
KSKKKKHKSV ALATSSDSAS VTDSKAKNAL VDSSEGSGAV REEDVDHRPA EAEAQACSTE 

       430        440        450        460        470        480 
KHREAMQRLE PTHEEESNSE SASNSAARHI SEDRRESDDS DVDLGSAVRQ LREFIPDIQE 

       490        500        510        520        530        540 
RAATTIRRMY RDDLGRFKEF KAQGVAIRFG KFSAKENKQI EKNVQDFLSL TGIESADKLL 

       550        560        570        580        590        600 
YTDRYPEEKT LITNLKRKHA FRLHIGKGIA RPWKLVYYRA KKIFDVNNYK GRYNEEDTKK 

       610        620        630        640        650        660 
LKAYHSLHGN DWKKIGAMVA RSSLSVALKF SQIGGTRNQG AWSKAETQRL IKAVEDVILK 

       670        680        690        700        710        720 
KMSPQELREL DSKLQEDPEG RLSIVREKLY KGISWVEVEA RVETRNWMQC KSKWTEILTK 

       730        740        750        760        770        780 
RMTHGGFVYR GVNALQAKIT LIERLYELNV NDANEIDWED LASAIGDVPP PFVQAKFYKL 

       790        800        810        820        830        840 
KAACVPFWQK KTFPEIIDYL YKNSLPLLKE KLDKKMKKKD GQIQTPAAPK QDFLFKDIFH 

       850 
CDDDSDEGSP EEPSASDVQ 

« Hide

References

« Hide 'large scale' references
[1]"Different domains of the murine RNA polymerase I-specific termination factor mTTF-I serve distinct functions in transcription termination."
Evers R., Smid A., Rudloff U., Lottspeich F., Gummt I.
EMBO J. 14:1248-1256(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 394-400 AND 457-498, FUNCTION, SUBCELLULAR LOCATION.
Tissue: Ehrlich ascites tumor cell.
[2]Hu Q., Rothblum L.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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: C57BL/6.
Tissue: Brain.
[4]"Oligomerization of the transcription termination factor TTF-I: implications for the structural organization of ribosomal transcription units."
Sander E.E., Grummt I.
Nucleic Acids Res. 25:1142-1147(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[5]"Termination of mammalian rDNA replication: polar arrest of replication fork movement by transcription termination factor TTF-I."
Gerber J.-K., Goegel E., Berger C., Wallisch M., Mueller F., Grummt I., Grummt F.
Cell 90:559-567(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"RNA polymerase I transcription on nucleosomal templates: the transcription termination factor TTF-I induces chromatin remodeling and relieves transcriptional repression."
Laengst G., Blank T.A., Becker P.B., Grummt I.
EMBO J. 16:760-768(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"The chromatin remodeling complex NoRC and TTF-I cooperate in the regulation of the mammalian rRNA genes in vivo."
Nemeth A., Strohner R., Grummt I., Laengst G.
Nucleic Acids Res. 32:4091-4099(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAZ2A, FUNCTION.
[8]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457 AND SER-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83974 mRNA. Translation: CAA58808.1.
AF237703 mRNA. Translation: AAF43448.1.
BC059011 mRNA. Translation: AAH59011.1.
CCDSCCDS38089.1.
PIRS54776.
RefSeqNP_033468.2. NM_009442.2.
XP_006497915.1. XM_006497852.1.
UniGeneMm.252195.

3D structure databases

ProteinModelPortalQ62187.
SMRQ62187. Positions 586-640, 694-719.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204361. 2 interactions.

Proteomic databases

PaxDbQ62187.
PRIDEQ62187.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000100237; ENSMUSP00000097809; ENSMUSG00000026803.
GeneID22130.
KEGGmmu:22130.
UCSCuc008izk.1. mouse.

Organism-specific databases

CTD7270.
MGIMGI:105044. Ttf1.

Phylogenomic databases

eggNOGNOG262979.
GeneTreeENSGT00530000063659.
HOGENOMHOG000231811.
HOVERGENHBG084694.
InParanoidQ62187.
KOK15225.
OMATLESEWP.
OrthoDBEOG7ZKS9N.
PhylomeDBQ62187.
TreeFamTF333537.

Enzyme and pathway databases

ReactomeREACT_200794. Mus musculus biological processes.

Gene expression databases

BgeeQ62187.
CleanExMM_TTF1.
GenevestigatorQ62187.

Family and domain databases

Gene3D1.10.10.60. 2 hits.
InterProIPR009057. Homeodomain-like.
IPR017877. Myb-like_dom.
IPR001005. SANT/Myb.
[Graphical view]
SMARTSM00717. SANT. 2 hits.
[Graphical view]
PROSITEPS50090. MYB_LIKE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio302001.
PROQ62187.
SOURCESearch...

Entry information

Entry nameTTF1_MOUSE
AccessionPrimary (citable) accession number: Q62187
Secondary accession number(s): Q9JKK5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: July 9, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot