O00268 · TAF4_HUMAN
- ProteinTranscription initiation factor TFIID subunit 4
- GeneTAF4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1085 (go to sequence)
- Protein existenceEvidence at protein 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 (PubMed:33795473).
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) (PubMed:33795473).
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 (PubMed:10594036, PubMed:33795473, PubMed:8942982).
TAF4 may maintain an association between the TFIID and TFIIA complexes, while bound to the promoter, together with TBP, during PIC assembly (PubMed:33795473).
Potentiates transcriptional activation by the AF-2S of the retinoic acid, vitamin D3 and thyroid hormone (PubMed:9192867).
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) (PubMed:33795473).
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 (PubMed:10594036, PubMed:33795473, PubMed:8942982).
TAF4 may maintain an association between the TFIID and TFIIA complexes, while bound to the promoter, together with TBP, during PIC assembly (PubMed:33795473).
Potentiates transcriptional activation by the AF-2S of the retinoic acid, vitamin D3 and thyroid hormone (PubMed:9192867).
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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Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTranscription initiation factor TFIID subunit 4
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00268
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Intellectual developmental disorder, autosomal dominant 73 (MRD73)
- Note
- DescriptionAn autosomal dominant disorder characterized by intellectual disability ranging from mild to severe, developmental delay, speech delay, behavioral abnormalities, and non-specific dysmorphic facial features.
- See alsoMIM:620450
Natural variants in MRD73
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_088796 | 450-1085 | missing | in MRD73; likely pathogenic | |
VAR_088797 | 677-1085 | missing | in MRD73; likely pathogenic | |
VAR_088798 | 729-1085 | missing | in MRD73; likely pathogenic | |
VAR_088799 | 949-1085 | missing | in MRD73; likely pathogenic |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_088796 | 450-1085 | in MRD73; likely pathogenic | |||
Sequence: Missing | ||||||
Natural variant | VAR_052258 | 651 | in dbSNP:rs6089604 | |||
Sequence: P → L | ||||||
Natural variant | VAR_088797 | 677-1085 | in MRD73; likely pathogenic | |||
Sequence: Missing | ||||||
Natural variant | VAR_088798 | 729-1085 | in MRD73; likely pathogenic | |||
Sequence: Missing | ||||||
Natural variant | VAR_088799 | 949-1085 | in MRD73; likely pathogenic | |||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,335 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000118869 | 1-1085 | UniProt | Transcription initiation factor TFIID subunit 4 | |||
Sequence: MAAGSDLLDEVFFNSEVDEKVVSDLVGSLESQLAASAAHHHHLAPRTPEVRAAAAGALGNHVVSGSPAGAAGAGPAAPAEGAPGAAPEPPPAGRARPGGGGPQRPGPPSPRRPLVPAGPAPPAAKLRPPPEGSAGSCAPVPAAAAVAAGPEPAPAGPAKPAGPAALAARAGPGPGPGPGPGPGPGPGKPAGPGAAQTLNGSAALLNSHHAAAPAVSLVNNGPAALLPLPKPAAPGTVIQTPPFVGAAAPPAPAAPSPPAAPAPAAPAAAPPPPPPAPATLARPPGHPAGPPTAAPAVPPPAAAQNGGSAGAAPAPAPAAGGPAGVSGQPGPGAAAAAPAPGVKAESPKRVVQAAPPAAQTLAASGPASTAASMVIGPTMQGALPSPAAVPPPAPGTPTGLPKGAAGAVTQSLSRTPTATTSGIRATLTPTVLAPRLPQPPQNPTNIQNFQLPPGMVLVRSENGQLLMIPQQALAQMQAQAHAQPQTTMAPRPATPTSAPPVQISTVQAPGTPIIARQVTPTTIIKQVSQAQTTVQPSATLQRSPGVQPQLVLGGAAQTASLGTATAVQTGTPQRTVPGATTTSSAATETMENVKKCKNFLSTLIKLASSGKQSTETAANVKELVQNLLDGKIEAEDFTSRLYRELNSSPQPYLVPFLKRSLPALRQLTPDSAAFIQQSQQQPPPPTSQATTALTAVVLSSSVQRTAGKTAATVTSALQPPVLSLTQPTQVGVGKQGQPTPLVIQQPPKPGALIRPPQVTLTQTPMVALRQPHNRIMLTTPQQIQLNPLQPVPVVKPAVLPGTKALSAVSAQAAAAQKNKLKEPGGGSFRDDDDINDVASMAGVNLSEESARILATNSELVGTLTRSCKDETFLLQAPLQRRILEIGKKHGITELHPDVVSYVSHATQQRLQNLVEKISETAQQKNFSYKDDDRYEQASDVRAQLKFFEQLDQIEKQRKDEQEREILMRAAKSRSRQEDPEQLRLKQKAKEMQQQELAQMRQRDANLTALAAIGPRKKRKVDCPGPGSGAEGSGPGSVVPGSSGVGTPRQFTRQRITRVNLRDLIFCLENERETSHSLLLYKAFLK | |||||||
Modified residue (large scale data) | 15 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 109 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 109 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 424 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue | 435 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 543 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 558 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 571 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 594 | UniProt | N6,N6-dimethyllysine | ||||
Sequence: K | |||||||
Modified residue | 595 | UniProt | N6,N6-dimethyllysine | ||||
Sequence: K | |||||||
Modified residue | 597 | UniProt | N6,N6-dimethyllysine | ||||
Sequence: K | |||||||
Modified residue | 605 | UniProt | N6,N6-dimethyllysine | ||||
Sequence: K | |||||||
Modified residue | 611 | UniProt | N6,N6-dimethyllysine | ||||
Sequence: K | |||||||
Modified residue | 621 | UniProt | N6,N6-dimethyllysine | ||||
Sequence: K | |||||||
Modified residue | 631 | UniProt | N6,N6-dimethyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 648 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 658 | UniProt | N6,N6-dimethyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 1027 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1042 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1046 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
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 (PubMed:10594036, PubMed:33795473).
Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TADA3L, SUPT3H, TAF2, TAF4, TAF5, GCN5L2/GCN5, TAF10, TAF12 and TRRAP (PubMed:10373431, PubMed:12601814).
Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15960975).
Interacts with ATF7; the interaction inhibits ATF7-mediated tranactivation (PubMed:15735663).
Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TADA3L, SUPT3H, TAF2, TAF4, TAF5, GCN5L2/GCN5, TAF10, TAF12 and TRRAP (PubMed:10373431, PubMed:12601814).
Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15960975).
Interacts with ATF7; the interaction inhibits ATF7-mediated tranactivation (PubMed:15735663).
(Microbial infection) Interacts with SV40 Large T antigen.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O00268 | CREB3 O43889 | 2 | EBI-1034261, EBI-625002 | |
BINARY | O00268 | CREBZF Q9NS37 | 2 | EBI-1034261, EBI-632965 | |
BINARY | O00268 | TAF12 Q16514 | 4 | EBI-1034261, EBI-1034238 | |
BINARY | O00268 | TAF12 Q16514-1 | 16 | EBI-1034261, EBI-1034253 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 66-204 | Disordered | ||||
Sequence: SPAGAAGAGPAAPAEGAPGAAPEPPPAGRARPGGGGPQRPGPPSPRRPLVPAGPAPPAAKLRPPPEGSAGSCAPVPAAAAVAAGPEPAPAGPAKPAGPAALAARAGPGPGPGPGPGPGPGPGKPAGPGAAQTLNGSAAL | ||||||
Compositional bias | 82-128 | Pro residues | ||||
Sequence: APGAAPEPPPAGRARPGGGGPQRPGPPSPRRPLVPAGPAPPAAKLRP | ||||||
Compositional bias | 173-189 | Pro residues | ||||
Sequence: GPGPGPGPGPGPGPGKP | ||||||
Region | 243-341 | Disordered | ||||
Sequence: FVGAAAPPAPAAPSPPAAPAPAAPAAAPPPPPPAPATLARPPGHPAGPPTAAPAVPPPAAAQNGGSAGAAPAPAPAAGGPAGVSGQPGPGAAAAAPAPG | ||||||
Compositional bias | 245-298 | Pro residues | ||||
Sequence: GAAAPPAPAAPSPPAAPAPAAPAAAPPPPPPAPATLARPPGHPAGPPTAAPAVP | ||||||
Region | 383-425 | Disordered | ||||
Sequence: LPSPAAVPPPAPGTPTGLPKGAAGAVTQSLSRTPTATTSGIRA | ||||||
Compositional bias | 384-398 | Pro residues | ||||
Sequence: PSPAAVPPPAPGTPT | ||||||
Compositional bias | 408-425 | Polar residues | ||||
Sequence: VTQSLSRTPTATTSGIRA | ||||||
Region | 479-499 | Disordered | ||||
Sequence: QAHAQPQTTMAPRPATPTSAP | ||||||
Region | 566-586 | Disordered | ||||
Sequence: AVQTGTPQRTVPGATTTSSAA | ||||||
Domain | 590-687 | TAFH | ||||
Sequence: MENVKKCKNFLSTLIKLASSGKQSTETAANVKELVQNLLDGKIEAEDFTSRLYRELNSSPQPYLVPFLKRSLPALRQLTPDSAAFIQQSQQQPPPPTS | ||||||
Region | 870-913 | Minimal region required to interact with TAF12 | ||||
Sequence: ETFLLQAPLQRRILEIGKKHGITELHPDVVSYVSHATQQRLQNL | ||||||
Region | 1015-1049 | Disordered | ||||
Sequence: RKKRKVDCPGPGSGAEGSGPGSVVPGSSGVGTPRQ |
Sequence similarities
Belongs to the TAF4 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,085
- Mass (Da)110,114
- Last updated2004-12-07 v2
- ChecksumBC2F5B5F143DB145
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2JRY5 | A0A0G2JRY5_HUMAN | TAF4 | 457 | ||
V9GY03 | V9GY03_HUMAN | TAF4 | 79 | ||
V9GY14 | V9GY14_HUMAN | TAF4 | 215 | ||
A0A8I5KRH3 | A0A8I5KRH3_HUMAN | TAF4 | 323 | ||
A0A8I5KW49 | A0A8I5KW49_HUMAN | TAF4 | 27 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 82-128 | Pro residues | ||||
Sequence: APGAAPEPPPAGRARPGGGGPQRPGPPSPRRPLVPAGPAPPAAKLRP | ||||||
Sequence conflict | 105-117 | in Ref. 5; AAC50901 | ||||
Sequence: PGPPSPRRPLVPA → GRGLLQQRGGRES | ||||||
Sequence conflict | 136 | in Ref. 1; CAA72189 and 5; AAC50901 | ||||
Sequence: S → A | ||||||
Compositional bias | 173-189 | Pro residues | ||||
Sequence: GPGPGPGPGPGPGPGKP | ||||||
Sequence conflict | 186-187 | in Ref. 1; CAA72189 and 5; AAC50901 | ||||
Sequence: Missing | ||||||
Sequence conflict | 235-266 | in Ref. 5; AAC50901 | ||||
Sequence: Missing | ||||||
Compositional bias | 245-298 | Pro residues | ||||
Sequence: GAAAPPAPAAPSPPAAPAPAAPAAAPPPPPPAPATLARPPGHPAGPPTAAPAVP | ||||||
Sequence conflict | 295 | in Ref. 5; AAC50901 | ||||
Sequence: P → L | ||||||
Compositional bias | 384-398 | Pro residues | ||||
Sequence: PSPAAVPPPAPGTPT | ||||||
Compositional bias | 408-425 | Polar residues | ||||
Sequence: VTQSLSRTPTATTSGIRA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y11354 EMBL· GenBank· DDBJ | CAA72189.1 EMBL· GenBank· DDBJ | mRNA | ||
AY623115 EMBL· GenBank· DDBJ | AAT38111.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL109911 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL137077 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471077 EMBL· GenBank· DDBJ | EAW75407.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U75308 EMBL· GenBank· DDBJ | AAC50901.1 EMBL· GenBank· DDBJ | mRNA |