Q9EQH4 · TAF8_MOUSE
- ProteinTranscription initiation factor TFIID subunit 8
- GeneTaf8
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids308 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (By similarity).
TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (By similarity).
The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (By similarity).
The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C (By similarity).
TAF8 is involved in forming the TFIID-B module, together with TAF5 (By similarity).
Mediates both basal and activator-dependent transcription (By similarity).
Plays a role in the differentiation of preadipocyte fibroblasts to adipocytes, however, does not seem to play a role in differentiation of myoblasts (PubMed:14580349).
Required for the integration of TAF10 in the TAF complex (By similarity).
May be important for survival of cells of the inner cell mass which constitute the pluripotent cell population of the early embryo (PubMed:11076765).
TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (By similarity).
The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (By similarity).
The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C (By similarity).
TAF8 is involved in forming the TFIID-B module, together with TAF5 (By similarity).
Mediates both basal and activator-dependent transcription (By similarity).
Plays a role in the differentiation of preadipocyte fibroblasts to adipocytes, however, does not seem to play a role in differentiation of myoblasts (PubMed:14580349).
Required for the integration of TAF10 in the TAF complex (By similarity).
May be important for survival of cells of the inner cell mass which constitute the pluripotent cell population of the early embryo (PubMed:11076765).
Miscellaneous
'Taube nuss' means 'empty nut' in German.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | transcription factor TFIID complex | |
Molecular Function | protein heterodimerization activity | |
Biological Process | cell differentiation | |
Biological Process | DNA-templated transcription open complex formation | |
Biological Process | inner cell mass cell proliferation | |
Biological Process | maintenance of protein location in nucleus | |
Biological Process | mRNA transcription by RNA polymerase II | |
Biological Process | positive regulation of transcription initiation by RNA polymerase II | |
Biological Process | regulation of fat cell differentiation | |
Biological Process | RNA polymerase II preinitiation complex assembly | |
Biological Process | transcription initiation at RNA polymerase II promoter |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTranscription initiation factor TFIID subunit 8
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9EQH4
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Death during early embryonic development. The inner cell mass cells of mutant embryos died of apoptosis.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 11 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000315398 | 2-308 | Transcription initiation factor TFIID subunit 8 | |||
Sequence: ADTAAGPGGSGTRPGSKQSTNPADNYHLARRRTLQVVVSSLLTEAGFESAEKASVETLTEMLQSYISEIGRSAKSYCEHTARTQPTLSDIVVTLVEMGFNVDTLPAYAKRSQRMVITAPPVTNQPVTPKALTAGQNRPHPPHIPSHFPEFPDPHTYIKTPTYREPVSDYQILREKAASQRRDVERALTRFMAKTGETQSLFKDDVSTFPLIAARPFTIPYLTALLPSELEIQQMEETDSSEQEEQTDTENNALHISTDDSGAEKESASVLQQSSSLSGSRNGEESVIDNPYLRPVKKPKIRRKKSLS | ||||||
Modified residue | 128 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 269 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Low level of expression throughout the brain with slightly higher expression in the hippocampus.
Developmental stage
Expressed ubiquitously at very low levels throughout embryonic development. Higher levels of expression seen in inner cell mass and heart.
Gene expression databases
Interaction
Subunit
Component of the TFIID basal transcription factor complex, composed of TATA-box-binding protein TBP, and a number of TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. Interacts with TBP, TAF1, TAF6, TAF10, TAF11 and TAF13. Component also of a small TAF complex (SMAT) containing TAF8, TAF10 and SUPT7L. Forms a heterodimer with TAF10. Interaction with TAF10 is mediated mainly via its histone fold domain while interaction with SUPT7L is via its C-terminal region.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-29 | Disordered | ||||
Sequence: MADTAAGPGGSGTRPGSKQSTNPADNYHL | ||||||
Compositional bias | 13-27 | Polar residues | ||||
Sequence: TRPGSKQSTNPADNY | ||||||
Domain | 35-102 | Histone-fold | ||||
Sequence: LQVVVSSLLTEAGFESAEKASVETLTEMLQSYISEIGRSAKSYCEHTARTQPTLSDIVVTLVEMGFNV | ||||||
Region | 235-308 | Disordered | ||||
Sequence: MEETDSSEQEEQTDTENNALHISTDDSGAEKESASVLQQSSSLSGSRNGEESVIDNPYLRPVKKPKIRRKKSLS | ||||||
Compositional bias | 250-285 | Polar residues | ||||
Sequence: ENNALHISTDDSGAEKESASVLQQSSSLSGSRNGEE | ||||||
Motif | 292-305 | Nuclear localization signal | ||||
Sequence: YLRPVKKPKIRRKK |
Sequence similarities
Belongs to the TAF8 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
Q9EQH4-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length308
- Mass (Da)33,988
- Last updated2001-03-01 v1
- ChecksumFD527CD7905CC8D9
Q9EQH4-2
- Name2
- Differences from canonical
- 306-308: Missing
Q9EQH4-3
- Name3
Q9EQH4-4
- Name4
- Differences from canonical
- 259-308: DDSGAEKESASVLQQSSSLSGSRNGEESVIDNPYLRPVKKPKIRRKKSLS → VGPPLLPASQQSQNSLSHILPLPLGTEQGLPQVSGWLLQACMMGCVSSLHHETHLLGSHTFSRW
Q9EQH4-5
- Name5
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 13-27 | Polar residues | ||||
Sequence: TRPGSKQSTNPADNY | ||||||
Sequence conflict | 127 | in Ref. 2; BAC36363 | ||||
Sequence: V → L | ||||||
Sequence conflict | 153 | in Ref. 2; BAC34001 | ||||
Sequence: D → V | ||||||
Alternative sequence | VSP_030550 | 213-221 | in isoform 5 | |||
Sequence: AARPFTIPY → SDQHLIKAP | ||||||
Alternative sequence | VSP_030551 | 222-308 | in isoform 5 | |||
Sequence: Missing | ||||||
Sequence conflict | 236 | in Ref. 2; BAC34001 | ||||
Sequence: E → G | ||||||
Compositional bias | 250-285 | Polar residues | ||||
Sequence: ENNALHISTDDSGAEKESASVLQQSSSLSGSRNGEE | ||||||
Alternative sequence | VSP_030553 | 259-265 | in isoform 3 | |||
Sequence: DDSGAEK → GHPEASA | ||||||
Alternative sequence | VSP_030552 | 259-308 | in isoform 4 | |||
Sequence: DDSGAEKESASVLQQSSSLSGSRNGEESVIDNPYLRPVKKPKIRRKKSLS → VGPPLLPASQQSQNSLSHILPLPLGTEQGLPQVSGWLLQACMMGCVSSLHHETHLLGSHTFSRW | ||||||
Alternative sequence | VSP_030554 | 266-308 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_030555 | 306-308 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF222802 EMBL· GenBank· DDBJ | AAG01682.1 EMBL· GenBank· DDBJ | mRNA | ||
AK045108 EMBL· GenBank· DDBJ | BAC32225.1 EMBL· GenBank· DDBJ | mRNA | ||
AK049949 EMBL· GenBank· DDBJ | BAC34001.1 EMBL· GenBank· DDBJ | mRNA | ||
AK076486 EMBL· GenBank· DDBJ | BAC36363.1 EMBL· GenBank· DDBJ | mRNA | ||
AK086656 EMBL· GenBank· DDBJ | BAC39712.1 EMBL· GenBank· DDBJ | mRNA | ||
AK162110 EMBL· GenBank· DDBJ | BAE36731.1 EMBL· GenBank· DDBJ | mRNA | ||
BC057895 EMBL· GenBank· DDBJ | AAH57895.1 EMBL· GenBank· DDBJ | mRNA |