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Q62187

- TTF1_MOUSE

UniProt

Q62187 - TTF1_MOUSE

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Protein

Transcription termination factor 1

Gene
Ttf1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. DNA binding Source: MGI
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. chromatin remodeling Source: MGI
  2. negative regulation of DNA replication Source: UniProtKB-KW
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. termination of RNA polymerase I transcription Source: MGI
  5. transcription initiation from RNA polymerase I promoter Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

DNA replication inhibitor

Keywords - Biological processi

Transcription, Transcription regulation, Transcription termination

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_200667. NoRC negatively regulates rRNA expression.
REACT_214440. NoRC negatively regulates rRNA expression.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ttf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:105044. Ttf1.

Subcellular locationi

Nucleus. Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. nucleolus Source: UniProtKB-SubCell
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 859859Transcription termination factor 1PRO_0000250473Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei227 – 2271Phosphoserine By similarity
Modified residuei375 – 3751Phosphoserine By similarity
Modified residuei451 – 4511Phosphoserine By similarity
Modified residuei457 – 4571Phosphoserine1 Publication
Modified residuei460 – 4601Phosphoserine1 Publication
Modified residuei845 – 8451Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ62187.
PRIDEiQ62187.

Expressioni

Gene expression databases

BgeeiQ62187.
CleanExiMM_TTF1.
GenevestigatoriQ62187.

Interactioni

Subunit structurei

Oligomer. The oligomeric structure enables to interact simultaneously with two separatee DNA fragments. Interacts with BAZ2A/TIP5.2 Publications

Protein-protein interaction databases

BioGridi204361. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ62187.
SMRiQ62187. Positions 586-640, 694-719.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini585 – 63450Myb-like 1Add
BLAST
Domaini634 – 71885Myb-like 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 210210N-terminal region (NRD)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi359 – 36810Poly-Lys

Domaini

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

Sequence similaritiesi

Contains 2 Myb-like domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG262979.
GeneTreeiENSGT00530000063659.
HOGENOMiHOG000231811.
HOVERGENiHBG084694.
InParanoidiQ62187.
KOiK15225.
OMAiTLESEWP.
OrthoDBiEOG7ZKS9N.
PhylomeDBiQ62187.
TreeFamiTF333537.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
InterProiIPR009057. Homeodomain-like.
IPR017877. Myb-like_dom.
IPR001005. SANT/Myb.
[Graphical view]
SMARTiSM00717. SANT. 2 hits.
[Graphical view]
PROSITEiPS50090. MYB_LIKE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q62187-1 [UniParc]FASTAAdd to Basket

« Hide

MKGGTSKFKT HTETLYKKKK WSSVSEKRPQ KCPSQCLESK QPQVSVLGKR    50
RRASQTPAQE TLESEWPQKA KRKKRRREPQ TPAQETLESE WPQKAKKKKR 100
RGEPQTPTQE SLESEQPPVS LLGKRRRESQ TPAQENSESE QPRKAKRRRK 150
KRKGSQQPTS SLLKTPETFL KAKKTTSAHK KKKNSVLEVD METGIILVDK 200
ENMENLLETS RKDVDIVYVD MSKGQRSAKV RETGELPAAK PQEHGCRELL 250
GDVRSRKKQK HLQKVAPWDV VQGSQPESIS LPPSEPLSSE DLEGKSTEAA 300
VFCKKKSKKN VFRSQELEPI PDSLDDSETI SERLDSTHHG GAVGAGEECE 350
STKESHSIKK KSKKKKHKSV ALATSSDSAS VTDSKAKNAL VDSSEGSGAV 400
REEDVDHRPA EAEAQACSTE KHREAMQRLE PTHEEESNSE SASNSAARHI 450
SEDRRESDDS DVDLGSAVRQ LREFIPDIQE RAATTIRRMY RDDLGRFKEF 500
KAQGVAIRFG KFSAKENKQI EKNVQDFLSL TGIESADKLL YTDRYPEEKT 550
LITNLKRKHA FRLHIGKGIA RPWKLVYYRA KKIFDVNNYK GRYNEEDTKK 600
LKAYHSLHGN DWKKIGAMVA RSSLSVALKF SQIGGTRNQG AWSKAETQRL 650
IKAVEDVILK KMSPQELREL DSKLQEDPEG RLSIVREKLY KGISWVEVEA 700
RVETRNWMQC KSKWTEILTK RMTHGGFVYR GVNALQAKIT LIERLYELNV 750
NDANEIDWED LASAIGDVPP PFVQAKFYKL KAACVPFWQK KTFPEIIDYL 800
YKNSLPLLKE KLDKKMKKKD GQIQTPAAPK QDFLFKDIFH CDDDSDEGSP 850
EEPSASDVQ 859
Length:859
Mass (Da):97,723
Last modified:October 3, 2006 - v2
Checksum:iD47950ECB3A08DCD
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 9625Missing in CAA58808. 1 PublicationAdd
BLAST
Sequence conflicti305 – 3073KKS → RSL in CAA58808. 1 Publication
Sequence conflicti348 – 3481Missing in CAA58808. 1 Publication
Sequence conflicti496 – 4961R → L AA sequence 1 Publication
Sequence conflicti762 – 7621A → C in CAA58808. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83974 mRNA. Translation: CAA58808.1.
AF237703 mRNA. Translation: AAF43448.1.
BC059011 mRNA. Translation: AAH59011.1.
CCDSiCCDS38089.1.
PIRiS54776.
RefSeqiNP_033468.2. NM_009442.2.
XP_006497915.1. XM_006497852.1.
UniGeneiMm.252195.

Genome annotation databases

EnsembliENSMUST00000100237; ENSMUSP00000097809; ENSMUSG00000026803.
GeneIDi22130.
KEGGimmu:22130.
UCSCiuc008izk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X83974 mRNA. Translation: CAA58808.1 .
AF237703 mRNA. Translation: AAF43448.1 .
BC059011 mRNA. Translation: AAH59011.1 .
CCDSi CCDS38089.1.
PIRi S54776.
RefSeqi NP_033468.2. NM_009442.2.
XP_006497915.1. XM_006497852.1.
UniGenei Mm.252195.

3D structure databases

ProteinModelPortali Q62187.
SMRi Q62187. Positions 586-640, 694-719.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204361. 2 interactions.

Proteomic databases

PaxDbi Q62187.
PRIDEi Q62187.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000100237 ; ENSMUSP00000097809 ; ENSMUSG00000026803 .
GeneIDi 22130.
KEGGi mmu:22130.
UCSCi uc008izk.1. mouse.

Organism-specific databases

CTDi 7270.
MGIi MGI:105044. Ttf1.

Phylogenomic databases

eggNOGi NOG262979.
GeneTreei ENSGT00530000063659.
HOGENOMi HOG000231811.
HOVERGENi HBG084694.
InParanoidi Q62187.
KOi K15225.
OMAi TLESEWP.
OrthoDBi EOG7ZKS9N.
PhylomeDBi Q62187.
TreeFami TF333537.

Enzyme and pathway databases

Reactomei REACT_200667. NoRC negatively regulates rRNA expression.
REACT_214440. NoRC negatively regulates rRNA expression.

Miscellaneous databases

NextBioi 302001.
PROi Q62187.
SOURCEi Search...

Gene expression databases

Bgeei Q62187.
CleanExi MM_TTF1.
Genevestigatori Q62187.

Family and domain databases

Gene3Di 1.10.10.60. 2 hits.
InterProi IPR009057. Homeodomain-like.
IPR017877. Myb-like_dom.
IPR001005. SANT/Myb.
[Graphical view ]
SMARTi SM00717. SANT. 2 hits.
[Graphical view ]
PROSITEi PS50090. MYB_LIKE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457 AND SER-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTTF1_MOUSE
AccessioniPrimary (citable) accession number: Q62187
Secondary accession number(s): Q9JKK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: September 3, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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

External Data

Dasty 3

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