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Subcellular localization database

JensenLab
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TAF1 localizations

TAF1 [ENSP00000406549]

Transcription initiation factor TFIID subunit 1; Largest component and core scaffold of the TFIID basal transcription factor complex . Contains novel N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors. Phosphorylates TP53 on 'Thr-55' which leads to MDM2-mediated degradation of TP53. Phosphorylates GTF2A1 and GTF2F1 on Ser residues. Possesses DNA-binding activity . Essential for progression of the G1 phase of the cell cycle (PubMed:11278496, PubMed:15053879, PubMed:2038334, PubMed:8450888, PubMed:8625415, PubMed:9660973, PubMed:9858607). Exhibits histone acetyltransferase activity towards histones H3 and H4 . ECO:0000269|PubMed:15870300, ECO:0000269|PubMed:2038334, ECO:0000269|PubMed:25412659, ECO:0000269|PubMed:27007846, ECO:0000269|PubMed:8450888, ECO:0000269|PubMed:8625415,; Belongs to the TAF1 family.

Synonyms:  TAF1,  TAF1p,  hTAF1,  H0Y8N6,  H0Y9L7 ...

Linkouts:  STRING  Pharos  UniProt

Extracellular space Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi Apparatus Nucleus Mitochondrion 0 1 2 3 4 5 Confidence

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The subcellular localizations are derived from database annotations, automatic text mining of the biomedical literature, and sequence-based predictions. The confidence of each association is signified by stars, where ★★★★★ is the highest confidence and ★☆☆☆☆ is the lowest.

Developed by Janos Binder, Sune Frankild, Kalliopi Tsafou, Christian Stolte, Sean O'Donoghue, Reinhard Schneider, and Lars Juhl Jensen from the Novo Nordisk Foundation Center for Protein Research (CPR), the Luxembourg Centre for Systems Biomedicine (LCSB), and the Commonwealth Scientific and Industrial Research Organisation (CSIRO).

Currently maintained by Qingyao Huang at Swiss Institute of Bioinformatics, University of Zurich. Licensed under CC BY 4.0.