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Q15361

- TTF1_HUMAN

UniProt

Q15361 - TTF1_HUMAN

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Protein

Transcription termination factor 1

Gene
TTF1
Organism
Homo sapiens (Human)
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.1 Publication

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. chromatin remodeling Source: Ensembl
  2. DNA-templated transcription, termination Source: UniProtKB
  3. gene expression Source: Reactome
  4. negative regulation of DNA replication Source: UniProtKB-KW
  5. regulation of transcription, DNA-templated Source: UniProtKB-KW
  6. termination of RNA polymerase I transcription Source: Reactome
  7. transcription from RNA polymerase I promoter Source: Reactome
  8. transcription initiation from RNA polymerase I promoter Source: Ensembl
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_1074. RNA Polymerase I Transcription Termination.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_953. RNA Polymerase I Transcription Initiation.

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
Gene namesi
Name:TTF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:12397. TTF1.

Subcellular locationi

Nucleus. Nucleusnucleolus By similarity

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleolus Source: HPA
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37062.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 905905Transcription termination factor 1PRO_0000250472Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651Phosphoserine2 Publications
Modified residuei240 – 2401Phosphoserine1 Publication
Modified residuei403 – 4031Phosphoserine1 Publication
Modified residuei476 – 4761Phosphotyrosine1 Publication
Modified residuei478 – 4781Phosphoserine1 Publication
Modified residuei481 – 4811Phosphoserine3 Publications
Modified residuei487 – 4871Phosphoserine4 Publications
Modified residuei872 – 8721Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15361.
PaxDbiQ15361.
PRIDEiQ15361.

PTM databases

PhosphoSiteiQ15361.

Expressioni

Gene expression databases

BgeeiQ15361.
CleanExiHS_TTF1.
GenevestigatoriQ15361.

Organism-specific databases

HPAiCAB053633.
HPA051105.
HPA054837.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi113121. 9 interactions.
IntActiQ15361. 2 interactions.
MINTiMINT-1181965.
STRINGi9606.ENSP00000333920.

Structurei

3D structure databases

ProteinModelPortaliQ15361.
SMRiQ15361. Positions 613-667.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini612 – 66150Myb-like 1Add
BLAST
Domaini661 – 74585Myb-like 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 223223N-terminal region (NRD) By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi17 – 215Poly-Lys
Compositional biasi216 – 22510Poly-Lys
Compositional biasi272 – 28211Poly-LysAdd
BLAST
Compositional biasi329 – 33810Poly-Lys

Domaini

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

Sequence similaritiesi

Contains 2 Myb-like domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG262979.
HOGENOMiHOG000231811.
HOVERGENiHBG104803.
InParanoidiQ15361.
KOiK15225.
OMAiDYLYETT.
OrthoDBiEOG7ZKS9N.
PhylomeDBiQ15361.
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.

Q15361-1 [UniParc]FASTAAdd to Basket

« Hide

MEGESSRFEI HTPVSDKKKK KCSIHKERPQ KHSHEIFRDS SLVNEQSQIT    50
RRKKRKKDFQ HLISSPLKKS RICDETANAT STLKKRKKRR YSALEVDEEA 100
GVTVVLVDKE NINNTPKHFR KDVDVVCVDM SIEQKLPRKP KTDKFQVLAK 150
SHAHKSEALH SKVREKKNKK HQRKAASWES QRARDTLPQS ESHQEESWLS 200
VGPGGEITEL PASAHKNKSK KKKKKSSNRE YETLAMPEGS QAGREAGTDM 250
QESQPTVGLD DETPQLLGPT HKKKSKKKKK KKSNHQEFEA LAMPEGSQVG 300
SEVGADMQES RPAVGLHGET AGIPAPAYKN KSKKKKKKSN HQEFEAVAMP 350
ESLESAYPEG SQVGSEVGTV EGSTALKGFK ESNSTKKKSK KRKLTSVKRA 400
RVSGDDFSVP SKNSESTLFD SVEGDGAMME EGVKSRPRQK KTQACLASKH 450
VQEAPRLEPA NEEHNVETAE DSEIRYLSAD SGDADDSDAD LGSAVKQLQE 500
FIPNIKDRAT STIKRMYRDD LERFKEFKAQ GVAIKFGKFS VKENKQLEKN 550
VEDFLALTGI ESADKLLYTD RYPEEKSVIT NLKRRYSFRL HIGRNIARPW 600
KLIYYRAKKM FDVNNYKGRY SEGDTEKLKM YHSLLGNDWK TIGEMVARSS 650
LSVALKFSQI SSQRNRGAWS KSETRKLIKA VEEVILKKMS PQELKEVDSK 700
LQENPESCLS IVREKLYKGI SWVEVEAKVQ TRNWMQCKSK WTEILTKRMT 750
NGRRIYYGMN ALRAKVSLIE RLYEINVEDT NEIDWEDLAS AIGDVPPSYV 800
QTKFSRLKAV YVPFWQKKTF PEIIDYLYET TLPLLKEKLE KMMEKKGTKI 850
QTPAAPKQVF PFRDIFYYED DSEGEDIEKE SEGQAPCMAH ACNSSTLGGQ 900
GRWII 905
Length:905
Mass (Da):103,051
Last modified:September 11, 2007 - v3
Checksum:i12F829CEFDDF96E8
GO

Sequence cautioni

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: Contaminating sequence. Sequence of unknown origin in the C-terminal part.
The sequence CAA58807.1 differs from that shown. Reason: Frameshift at position 875.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti35 – 351E → K.1 Publication
Corresponds to variant rs11550314 [ dbSNP | Ensembl ].
VAR_027563
Natural varianti290 – 2901A → S.
Corresponds to variant rs8999 [ dbSNP | Ensembl ].
VAR_027564
Natural varianti303 – 3031V → A.
Corresponds to variant rs3739914 [ dbSNP | Ensembl ].
VAR_027565
Natural varianti360 – 3601G → V.
Corresponds to variant rs3739915 [ dbSNP | Ensembl ].
VAR_027566
Natural varianti401 – 4011R → Q.
Corresponds to variant rs3739916 [ dbSNP | Ensembl ].
VAR_027567
Natural varianti473 – 4731E → K.
Corresponds to variant rs12336746 [ dbSNP | Ensembl ].
VAR_050201
Natural varianti885 – 8851A → V.
Corresponds to variant rs1752676 [ dbSNP | Ensembl ].
VAR_061363

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti281 – 2811K → T in AAH50734. 1 Publication
Sequence conflicti649 – 6491S → R in CAA58807. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS6948.1.
PIRiI38182.
RefSeqiNP_001192225.1. NM_001205296.1.
NP_031370.2. NM_007344.3.
UniGeneiHs.54780.
Hs.732733.

Genome annotation databases

EnsembliENST00000334270; ENSP00000333920; ENSG00000125482.
GeneIDi7270.
KEGGihsa:7270.
UCSCiuc004cbl.3. human.

Polymorphism databases

DMDMi158518534.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS6948.1.
PIRi I38182.
RefSeqi NP_001192225.1. NM_001205296.1.
NP_031370.2. NM_007344.3.
UniGenei Hs.54780.
Hs.732733.

3D structure databases

ProteinModelPortali Q15361.
SMRi Q15361. Positions 613-667.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113121. 9 interactions.
IntActi Q15361. 2 interactions.
MINTi MINT-1181965.
STRINGi 9606.ENSP00000333920.

PTM databases

PhosphoSitei Q15361.

Polymorphism databases

DMDMi 158518534.

Proteomic databases

MaxQBi Q15361.
PaxDbi Q15361.
PRIDEi Q15361.

Protocols and materials databases

DNASUi 7270.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000334270 ; ENSP00000333920 ; ENSG00000125482 .
GeneIDi 7270.
KEGGi hsa:7270.
UCSCi uc004cbl.3. human.

Organism-specific databases

CTDi 7270.
GeneCardsi GC09M135250.
H-InvDB HIX0201412.
HGNCi HGNC:12397. TTF1.
HPAi CAB053633.
HPA051105.
HPA054837.
MIMi 600777. gene.
neXtProti NX_Q15361.
PharmGKBi PA37062.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG262979.
HOGENOMi HOG000231811.
HOVERGENi HBG104803.
InParanoidi Q15361.
KOi K15225.
OMAi DYLYETT.
OrthoDBi EOG7ZKS9N.
PhylomeDBi Q15361.
TreeFami TF333537.

Enzyme and pathway databases

Reactomei REACT_1074. RNA Polymerase I Transcription Termination.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_953. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

GeneWikii Transcription_termination_factor,_RNA_polymerase_I.
GenomeRNAii 7270.
NextBioi 28421.
PROi Q15361.
SOURCEi Search...

Gene expression databases

Bgeei Q15361.
CleanExi HS_TTF1.
Genevestigatori Q15361.

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. "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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  6. 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].

Entry informationi

Entry nameiTTF1_HUMAN
AccessioniPrimary (citable) accession number: Q15361
Secondary accession number(s): A1L160
, Q4VXF3, Q58EY2, Q6P5T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: September 11, 2007
Last modified: September 3, 2014
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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