P35269 · T2FA_HUMAN
- ProteinGeneral transcription factor IIF subunit 1
- GeneGTF2F1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids517 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGeneral transcription factor IIF subunit 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP35269
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_039004 | 3 | in dbSNP:rs34826931 | |||
Sequence: A → V | ||||||
Mutagenesis | 385 | Eliminates putative kinase activity; when associated with A-389. | ||||
Sequence: S → A | ||||||
Mutagenesis | 389 | Eliminates putative kinase activity; when associated with A-385. | ||||
Sequence: T → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 610 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000211231 | 2-517 | UniProt | General transcription factor IIF subunit 1 | |||
Sequence: AALGPSSQNVTEYVVRVPKNTTKKYNIMAFNAADKVNFATWNQARLERDLSNKKIYQEEEMPESGAGSEFNRKLREEARRKKYGIVLKEFRPEDQPWLLRVNGKSGRKFKGIKKGGVTENTSYYIFTQCPDGAFEAFPVHNWYNFTPLARHRTLTAEEAEEEWERRNKVLNHFSIMQQRRLKDQDQDEDEEEKEKRGRRKASELRIHDLEDDLEMSSDASDASGEEGGRVPKAKKKAPLAKGGRKKKKKKGSDDEAFEDSDDGDFEGQEVDYMSDGSSSSQEEPESKAKAPQQEEGPKGVDEQSDSSEESEEEKPPEEDKEEEEEKKAPTPQEKKRRKDSSEESDSSEESDIDSEASSALFMAKKKTPPKRERKPSGGSSRGNSRPGTPSAEGGSTSSTLRAAASKLEQGKRVSEMPAAKRLRLDTGPQSLSGKSTPQPPSGKTTPNSGDVQVTEDAVRRYLTRKPMTTKDLLKKFQTKKTGLSSEQTVNVLAQILKRLNPERKMINDKMHFSLKE | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 65 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 154 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 156 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 156 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 217 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 217 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 218 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 218 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 221 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 221 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 224 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 224 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 305 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 307 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 308 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 311 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 331 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 331 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 377 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 377 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 380 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 381 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 385 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 385 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 389 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 389 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 391 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 391 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 396 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 407 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 427 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 431 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 431 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 433 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 433 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 436 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 436 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 437 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 437 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 442 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 445 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 446 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 446 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 449 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 449 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on Ser and other residues by TAF1 and casein kinase II-like kinases.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Up-regulated in response to enterovirus 71 (EV71) infection.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Heterodimer of an alpha and a beta subunit. Interacts with GTF2F2, CTDP1, TAF6/TAFII80 and URI1. Interacts with GTF2B (via C-terminus and preferentially via acetylated form); this interaction prevents binding of GTF2B to GTF2F2 (PubMed:12931194, PubMed:8662660).
Part of TBP-based Pol II pre-initiation complex (PIC), in which Pol II core assembles with general transcription factors and other specific initiation factors including GTF2E1, GTF2E2, GTF2F1, GTF2F2, TCEA1, ERCC2, ERCC3, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2A1, GTF2A2, GTF2B and TBP; this large multi-subunit PIC complex mediates DNA unwinding and targets Pol II core to the transcription start site where the first phosphodiester bond forms
Part of TBP-based Pol II pre-initiation complex (PIC), in which Pol II core assembles with general transcription factors and other specific initiation factors including GTF2E1, GTF2E2, GTF2F1, GTF2F2, TCEA1, ERCC2, ERCC3, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2A1, GTF2A2, GTF2B and TBP; this large multi-subunit PIC complex mediates DNA unwinding and targets Pol II core to the transcription start site where the first phosphodiester bond forms
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P35269 | CTDP1 Q9Y5B0 | 2 | EBI-457886, EBI-2807555 | |
BINARY | P35269 | GTF2F2 P13984 | 28 | EBI-457886, EBI-1030560 | |
BINARY | P35269 | SRF P11831 | 2 | EBI-457886, EBI-493034 | |
BINARY | P35269 | TAF1 P21675 | 3 | EBI-457886, EBI-491289 | |
BINARY | P35269 | URI1 O94763 | 3 | EBI-457886, EBI-357067 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 178-466 | Disordered | ||||
Sequence: QQRRLKDQDQDEDEEEKEKRGRRKASELRIHDLEDDLEMSSDASDASGEEGGRVPKAKKKAPLAKGGRKKKKKKGSDDEAFEDSDDGDFEGQEVDYMSDGSSSSQEEPESKAKAPQQEEGPKGVDEQSDSSEESEEEKPPEEDKEEEEEKKAPTPQEKKRRKDSSEESDSSEESDIDSEASSALFMAKKKTPPKRERKPSGGSSRGNSRPGTPSAEGGSTSSTLRAAASKLEQGKRVSEMPAAKRLRLDTGPQSLSGKSTPQPPSGKTTPNSGDVQVTEDAVRRYLTRK | ||||||
Compositional bias | 179-214 | Basic and acidic residues | ||||
Sequence: QRRLKDQDQDEDEEEKEKRGRRKASELRIHDLEDDL | ||||||
Compositional bias | 273-287 | Polar residues | ||||
Sequence: YMSDGSSSSQEEPES | ||||||
Compositional bias | 288-305 | Basic and acidic residues | ||||
Sequence: KAKAPQQEEGPKGVDEQS | ||||||
Compositional bias | 306-320 | Acidic residues | ||||
Sequence: DSSEESEEEKPPEED | ||||||
Compositional bias | 321-345 | Basic and acidic residues | ||||
Sequence: KEEEEEKKAPTPQEKKRRKDSSEES | ||||||
Compositional bias | 380-405 | Polar residues | ||||
Sequence: SSRGNSRPGTPSAEGGSTSSTLRAAA | ||||||
Compositional bias | 429-453 | Polar residues | ||||
Sequence: PQSLSGKSTPQPPSGKTTPNSGDVQ |
Sequence similarities
Belongs to the TFIIF alpha subunit family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length517
- Mass (Da)58,240
- Last updated2004-04-13 v2
- Checksum1032B04A36BDC24F
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 179-214 | Basic and acidic residues | ||||
Sequence: QRRLKDQDQDEDEEEKEKRGRRKASELRIHDLEDDL | ||||||
Sequence conflict | 231 | in Ref. 2; CAA45404 | ||||
Sequence: V → I | ||||||
Compositional bias | 273-287 | Polar residues | ||||
Sequence: YMSDGSSSSQEEPES | ||||||
Compositional bias | 288-305 | Basic and acidic residues | ||||
Sequence: KAKAPQQEEGPKGVDEQS | ||||||
Compositional bias | 306-320 | Acidic residues | ||||
Sequence: DSSEESEEEKPPEED | ||||||
Compositional bias | 321-345 | Basic and acidic residues | ||||
Sequence: KEEEEEKKAPTPQEKKRRKDSSEES | ||||||
Sequence conflict | 361 | in Ref. 1; CAA45408 | ||||
Sequence: L → F | ||||||
Compositional bias | 380-405 | Polar residues | ||||
Sequence: SSRGNSRPGTPSAEGGSTSSTLRAAA | ||||||
Compositional bias | 429-453 | Polar residues | ||||
Sequence: PQSLSGKSTPQPPSGKTTPNSGDVQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X64037 EMBL· GenBank· DDBJ | CAA45408.1 EMBL· GenBank· DDBJ | mRNA | ||
X64002 EMBL· GenBank· DDBJ | CAA45404.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007097 EMBL· GenBank· DDBJ | AAP35761.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315240 EMBL· GenBank· DDBJ | BAG37667.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471139 EMBL· GenBank· DDBJ | EAW69098.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000120 EMBL· GenBank· DDBJ | AAH00120.1 EMBL· GenBank· DDBJ | mRNA | ||
BC013007 EMBL· GenBank· DDBJ | AAH13007.1 EMBL· GenBank· DDBJ | mRNA |