Version 5.4
Homo sapiens Protein: TTF2
Summary
InnateDB Protein IDBP-387896.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol TTF2
Protein Name transcription termination factor, RNA polymerase II
Synonyms HuF2; ZGRF6;
Species Homo sapiens
Ensembl Protein ENSP00000408111
InnateDB Gene IDBG-101430 (TTF2)
Protein Structure
UniProt Annotation
Function DsDNA-dependent ATPase which acts as a transcription termination factor by coupling ATP hydrolysis with removal of RNA polymerase II from the DNA template. May contribute to mitotic transcription repression. May also be involved in pre-mRNA splicing. {ECO:0000269PubMed:10455150, ECO:0000269PubMed:12927788, ECO:0000269PubMed:15125840, ECO:0000269PubMed:9748214}.
Subcellular Localization Cytoplasm {ECO:0000269PubMed:15125840}. Nucleus {ECO:0000269PubMed:15125840}. Note=Cytoplasmic during interphase. Relocates to the nucleus as cells enter mitosis.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 32 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Experimentally validated
Total 32 [view]
Protein-Protein 30 [view]
Protein-DNA 2 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003676 nucleic acid binding
GO:0004386 helicase activity
GO:0005524 ATP binding
Biological Process
GO:0008152 metabolic process
Cellular Component
Protein Structure and Domains
PDB ID
InterPro IPR001650 Helicase, C-terminal
IPR027417 P-loop containing nucleoside triphosphate hydrolase
PFAM PF00271
PRINTS
PIRSF
SMART SM00490
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-Q9UNY4
TrEMBL X6RI15
UniProt Splice Variant
Entrez Gene 8458
UniGene Hs.598918
RefSeq
HUGO HGNC:12398
OMIM 604718
CCDS
HPRD 05280
IMGT
EMBL AL139248 AL391476 AL445231
GenPept

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca