RGD Reference Report - Molecular cloning of a novel 120-kDa TBP-interacting protein. - Rat Genome Database

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Molecular cloning of a novel 120-kDa TBP-interacting protein.

Authors: Yogosawa, S  Makino, Y  Yoshida, T  Kishimoto, T  Muramatsu, M  Tamura, T 
Citation: Yogosawa S, etal., Biochem Biophys Res Commun 1996 Dec 13;229(2):612-7.
RGD ID: 634479
Pubmed: PMID:8954946   (View Abstract at PubMed)

TATA-binding protein (TBP) is a central component for transcriptional regulation and is a target for various transcription regulators. Using histidine-tagged TBP as a ligand for affinity-purification of proteins bound to TBP, we purified a 120-kD protein, termed TBP-interacting protein 120 (TIP120), from rat liver nuclear extracts. The entire cDNA sequence of TIP120 contained an open reading frame encoding a novel polypeptide of 1230 amino acids. The recombinant TIP120 interacted directly with TBP under a physiological condition in vitro. Immunoprecipitation analysis indicated that TIP120 was associated with TBP in nuclear extracts. Interestingly, the N-terminal region of TIP120 exhibited sequence similarity to that of Drosophila TAF80, which was shown to bind directly to TBP. This novel TBP-binding protein is considered to participate in transcription regulation through the interaction with TBP.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
TBP-class protein binding  IDA 634479 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Cand1  (cullin-associated and neddylation-dissociated 1)

Objects referenced in this article
Gene Tbp TATA box binding protein Rattus norvegicus

Additional Information