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Q15361 (TTF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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
Gene names
Name:TTF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length905 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

Subunit structure

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

Subcellular location

Nucleus. Nucleusnucleolus By similarity.

Domain

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

Sequence similarities

Contains 2 Myb-like domains.

Sequence caution

The sequence AAH62692.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAI04640.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAI27670.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

The sequence AAI27671.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

The sequence AAI43049.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

The sequence AAI43050.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

The sequence CAA58807.1 differs from that shown. Reason: Frameshift at position 875.

The sequence CAA58807.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Transcription termination
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandDNA-binding
   Molecular functionDNA replication inhibitor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA-templated transcription, termination

Non-traceable author statement Ref.1. Source: UniProtKB

chromatin remodeling

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

negative regulation of DNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

termination of RNA polymerase I transcription

Traceable author statement. Source: Reactome

transcription from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase I promoter

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Non-traceable author statement Ref.1. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 905905Transcription termination factor 1
PRO_0000250472

Regions

Domain612 – 66150Myb-like 1
Domain661 – 74585Myb-like 2
Region1 – 223223N-terminal region (NRD) By similarity
Compositional bias17 – 215Poly-Lys
Compositional bias216 – 22510Poly-Lys
Compositional bias272 – 28211Poly-Lys
Compositional bias329 – 33810Poly-Lys

Amino acid modifications

Modified residue651Phosphoserine Ref.6 Ref.9
Modified residue2401Phosphoserine Ref.5
Modified residue4031Phosphoserine Ref.6
Modified residue4761Phosphotyrosine Ref.8
Modified residue4781Phosphoserine Ref.10
Modified residue4811Phosphoserine Ref.6 Ref.8 Ref.10
Modified residue4871Phosphoserine Ref.6 Ref.8 Ref.9 Ref.10
Modified residue8721Phosphoserine Ref.9 Ref.10

Natural variations

Natural variant351E → K. Ref.3
Corresponds to variant rs11550314 [ dbSNP | Ensembl ].
VAR_027563
Natural variant2901A → S.
Corresponds to variant rs8999 [ dbSNP | Ensembl ].
VAR_027564
Natural variant3031V → A.
Corresponds to variant rs3739914 [ dbSNP | Ensembl ].
VAR_027565
Natural variant3601G → V.
Corresponds to variant rs3739915 [ dbSNP | Ensembl ].
VAR_027566
Natural variant4011R → Q.
Corresponds to variant rs3739916 [ dbSNP | Ensembl ].
VAR_027567
Natural variant4731E → K.
Corresponds to variant rs12336746 [ dbSNP | Ensembl ].
VAR_050201
Natural variant8851A → V.
Corresponds to variant rs1752676 [ dbSNP | Ensembl ].
VAR_061363

Experimental info

Sequence conflict2811K → T in AAH50734. Ref.3
Sequence conflict6491S → R in CAA58807. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q15361 [UniParc].

Last modified September 11, 2007. Version 3.
Checksum: 12F829CEFDDF96E8

FASTA905103,051
        10         20         30         40         50         60 
MEGESSRFEI HTPVSDKKKK KCSIHKERPQ KHSHEIFRDS SLVNEQSQIT RRKKRKKDFQ 

        70         80         90        100        110        120 
HLISSPLKKS RICDETANAT STLKKRKKRR YSALEVDEEA GVTVVLVDKE NINNTPKHFR 

       130        140        150        160        170        180 
KDVDVVCVDM SIEQKLPRKP KTDKFQVLAK SHAHKSEALH SKVREKKNKK HQRKAASWES 

       190        200        210        220        230        240 
QRARDTLPQS ESHQEESWLS VGPGGEITEL PASAHKNKSK KKKKKSSNRE YETLAMPEGS 

       250        260        270        280        290        300 
QAGREAGTDM QESQPTVGLD DETPQLLGPT HKKKSKKKKK KKSNHQEFEA LAMPEGSQVG 

       310        320        330        340        350        360 
SEVGADMQES RPAVGLHGET AGIPAPAYKN KSKKKKKKSN HQEFEAVAMP ESLESAYPEG 

       370        380        390        400        410        420 
SQVGSEVGTV EGSTALKGFK ESNSTKKKSK KRKLTSVKRA RVSGDDFSVP SKNSESTLFD 

       430        440        450        460        470        480 
SVEGDGAMME EGVKSRPRQK KTQACLASKH VQEAPRLEPA NEEHNVETAE DSEIRYLSAD 

       490        500        510        520        530        540 
SGDADDSDAD LGSAVKQLQE FIPNIKDRAT STIKRMYRDD LERFKEFKAQ GVAIKFGKFS 

       550        560        570        580        590        600 
VKENKQLEKN VEDFLALTGI ESADKLLYTD RYPEEKSVIT NLKRRYSFRL HIGRNIARPW 

       610        620        630        640        650        660 
KLIYYRAKKM FDVNNYKGRY SEGDTEKLKM YHSLLGNDWK TIGEMVARSS LSVALKFSQI 

       670        680        690        700        710        720 
SSQRNRGAWS KSETRKLIKA VEEVILKKMS PQELKEVDSK LQENPESCLS IVREKLYKGI 

       730        740        750        760        770        780 
SWVEVEAKVQ TRNWMQCKSK WTEILTKRMT NGRRIYYGMN ALRAKVSLIE RLYEINVEDT 

       790        800        810        820        830        840 
NEIDWEDLAS AIGDVPPSYV QTKFSRLKAV YVPFWQKKTF PEIIDYLYET TLPLLKEKLE 

       850        860        870        880        890        900 
KMMEKKGTKI QTPAAPKQVF PFRDIFYYED DSEGEDIEKE SEGQAPCMAH ACNSSTLGGQ 


GRWII 

« Hide

References

« Hide 'large scale' references
[1]"Molecular evolution of mammalian ribosomal gene terminator sequences and the transcription termination factor TTF-1."
Evers R., Grummt I.
Proc. Natl. Acad. Sci. U.S.A. 92:5827-5831(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] OF 1-338 AND 457-905, VARIANT LYS-35.
Tissue: Uterus.
[4]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-403; SER-481 AND SER-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"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 TYR-476; SER-481 AND SER-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"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-65; SER-487 AND SER-872, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-478; SER-481; SER-487 AND SER-872, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83973 mRNA. Translation: CAA58807.1. Sequence problems.
AL353701 Genomic DNA. Translation: CAI94997.2.
BC050734 mRNA. Translation: AAH50734.1.
BC062692 mRNA. Translation: AAH62692.1. Sequence problems.
BC104639 mRNA. Translation: AAI04640.1. Sequence problems.
BC127669 mRNA. Translation: AAI27670.1. Sequence problems.
BC127670 mRNA. Translation: AAI27671.1. Sequence problems.
BC143048 mRNA. Translation: AAI43049.1. Sequence problems.
BC143049 mRNA. Translation: AAI43050.1. Sequence problems.
CCDSCCDS6948.1.
PIRI38182.
RefSeqNP_001192225.1. NM_001205296.1.
NP_031370.2. NM_007344.3.
UniGeneHs.54780.
Hs.732733.

3D structure databases

ProteinModelPortalQ15361.
SMRQ15361. Positions 613-667.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113121. 9 interactions.
IntActQ15361. 2 interactions.
MINTMINT-1181965.
STRING9606.ENSP00000333920.

PTM databases

PhosphoSiteQ15361.

Polymorphism databases

DMDM158518534.

Proteomic databases

MaxQBQ15361.
PaxDbQ15361.
PRIDEQ15361.

Protocols and materials databases

DNASU7270.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334270; ENSP00000333920; ENSG00000125482.
GeneID7270.
KEGGhsa:7270.
UCSCuc004cbl.3. human.

Organism-specific databases

CTD7270.
GeneCardsGC09M135250.
H-InvDBHIX0201412.
HGNCHGNC:12397. TTF1.
HPACAB053633.
HPA051105.
HPA054837.
MIM600777. gene.
neXtProtNX_Q15361.
PharmGKBPA37062.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262979.
HOGENOMHOG000231811.
HOVERGENHBG104803.
InParanoidQ15361.
KOK15225.
OMADYLYETT.
OrthoDBEOG7ZKS9N.
PhylomeDBQ15361.
TreeFamTF333537.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

BgeeQ15361.
CleanExHS_TTF1.
GenevestigatorQ15361.

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

GeneWikiTranscription_termination_factor,_RNA_polymerase_I.
GenomeRNAi7270.
NextBio28421.
PROQ15361.
SOURCESearch...

Entry information

Entry nameTTF1_HUMAN
AccessionPrimary (citable) accession number: Q15361
Secondary accession number(s): A1L160 expand/collapse secondary AC list , Q4VXF3, Q58EY2, Q6P5T5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: September 11, 2007
Last modified: July 9, 2014
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM