Relation Results

Summary

Name GTF2A1
Full Name Transcription initiation factor IIA subunit 1
Synonyms General transcription factor IIA subunit 1, TFIIAL, Transcription initiation factor TFIIA 42 kDa subunit, TFIIA-42 | TF2A1
Primary ID P52655
Links - -
Type protein
Relations 13
Function TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex ...
View More

Viewer

Type: Score: Layout: SPV 
0.3840.3790.6680.939CSNK2A1GTF2A1CSNK2A2TAF1TFIIA

Search Tools

Refine search:

  • by mechanism


  • by effect
  • by organism:


  • by tissue:


  • by cell-line

▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ CSNK2A1up-regulates activity img/direct-activation.png phosphorylation GTF2A1 0.384
Identifier Residue Sequence Organism Cell Line
SIGNOR-250874 Ser280 VDGTGDTsSEEDEDE in vitro
pmid sentence
We now show that human TFIIA is phosphorylated in vivo on serine residues that are partially conserved between yeast and human TFIIA large subunits. Alanine substitution mutation of serine residues 316 and 321 in TFIIA alphabeta reduced TFIIA phosphorylation significantly in vivo. Additional alanine substitutions at serines 280 and 281 reduced phosphorylation to undetectable levels. Mutation of all four serine residues reduced the ability of TFIIA to stimulate transcription in transient transfection assays with various activators and promoters, indicating that TFIIA phosphorylation is required globally for optimal function.
Identifier Residue Sequence Organism Cell Line
SIGNOR-250875 Ser281 DGTGDTSsEEDEDEE in vitro
pmid sentence
We now show that human TFIIA is phosphorylated in vivo on serine residues that are partially conserved between yeast and human TFIIA large subunits. Alanine substitution mutation of serine residues 316 and 321 in TFIIA alphabeta reduced TFIIA phosphorylation significantly in vivo. Additional alanine substitutions at serines 280 and 281 reduced phosphorylation to undetectable levels. Mutation of all four serine residues reduced the ability of TFIIA to stimulate transcription in transient transfection assays with various activators and promoters, indicating that TFIIA phosphorylation is required globally for optimal function.
Identifier Residue Sequence Organism Cell Line
SIGNOR-250876 Ser316 VEEEPLNsEDDVSDE in vitro
pmid sentence
We now show that human TFIIA is phosphorylated in vivo on serine residues that are partially conserved between yeast and human TFIIA large subunits. Alanine substitution mutation of serine residues 316 and 321 in TFIIA alphabeta reduced TFIIA phosphorylation significantly in vivo. Additional alanine substitutions at serines 280 and 281 reduced phosphorylation to undetectable levels. Mutation of all four serine residues reduced the ability of TFIIA to stimulate transcription in transient transfection assays with various activators and promoters, indicating that TFIIA phosphorylation is required globally for optimal function.
Identifier Residue Sequence Organism Cell Line
SIGNOR-250877 Ser321 LNSEDDVsDEEGQEL in vitro
pmid sentence
We now show that human TFIIA is phosphorylated in vivo on serine residues that are partially conserved between yeast and human TFIIA large subunits. Alanine substitution mutation of serine residues 316 and 321 in TFIIA alphabeta reduced TFIIA phosphorylation significantly in vivo. Additional alanine substitutions at serines 280 and 281 reduced phosphorylation to undetectable levels. Mutation of all four serine residues reduced the ability of TFIIA to stimulate transcription in transient transfection assays with various activators and promoters, indicating that TFIIA phosphorylation is required globally for optimal function.
Publications: 4 Organism: In Vitro
+ CSNK2A2up-regulates activity img/direct-activation.png phosphorylation GTF2A1 0.379
Identifier Residue Sequence Organism Cell Line
SIGNOR-250995 Ser280 VDGTGDTsSEEDEDE in vitro
pmid sentence
We now show that human TFIIA is phosphorylated in vivo on serine residues that are partially conserved between yeast and human TFIIA large subunits. Alanine substitution mutation of serine residues 316 and 321 in TFIIA alphabeta reduced TFIIA phosphorylation significantly in vivo. Additional alanine substitutions at serines 280 and 281 reduced phosphorylation to undetectable levels. Mutation of all four serine residues reduced the ability of TFIIA to stimulate transcription in transient transfection assays with various activators and promoters, indicating that TFIIA phosphorylation is required globally for optimal function.
Identifier Residue Sequence Organism Cell Line
SIGNOR-250996 Ser281 DGTGDTSsEEDEDEE in vitro
pmid sentence
We now show that human TFIIA is phosphorylated in vivo on serine residues that are partially conserved between yeast and human TFIIA large subunits. Alanine substitution mutation of serine residues 316 and 321 in TFIIA alphabeta reduced TFIIA phosphorylation significantly in vivo. Additional alanine substitutions at serines 280 and 281 reduced phosphorylation to undetectable levels. Mutation of all four serine residues reduced the ability of TFIIA to stimulate transcription in transient transfection assays with various activators and promoters, indicating that TFIIA phosphorylation is required globally for optimal function.
Identifier Residue Sequence Organism Cell Line
SIGNOR-250997 Ser316 VEEEPLNsEDDVSDE in vitro
pmid sentence
We now show that human TFIIA is phosphorylated in vivo on serine residues that are partially conserved between yeast and human TFIIA large subunits. Alanine substitution mutation of serine residues 316 and 321 in TFIIA alphabeta reduced TFIIA phosphorylation significantly in vivo. Additional alanine substitutions at serines 280 and 281 reduced phosphorylation to undetectable levels. Mutation of all four serine residues reduced the ability of TFIIA to stimulate transcription in transient transfection assays with various activators and promoters, indicating that TFIIA phosphorylation is required globally for optimal function.
Identifier Residue Sequence Organism Cell Line
SIGNOR-250998 Ser321 LNSEDDVsDEEGQEL in vitro
pmid sentence
We now show that human TFIIA is phosphorylated in vivo on serine residues that are partially conserved between yeast and human TFIIA large subunits. Alanine substitution mutation of serine residues 316 and 321 in TFIIA alphabeta reduced TFIIA phosphorylation significantly in vivo. Additional alanine substitutions at serines 280 and 281 reduced phosphorylation to undetectable levels. Mutation of all four serine residues reduced the ability of TFIIA to stimulate transcription in transient transfection assays with various activators and promoters, indicating that TFIIA phosphorylation is required globally for optimal function.
Publications: 4 Organism: In Vitro
+ TAF1up-regulates activity img/direct-activation.png phosphorylation GTF2A1 0.668
Identifier Residue Sequence Organism Cell Line
SIGNOR-246630 Ser280 VDGTGDTsSEEDEDE Homo sapiens
pmid sentence
TAFII 250 Phosphorylates Human Transcription Factor IIA on Serine Residues Important for TBP Binding and Transcription ActivityAdditional alanine substitutions at serines 280 and 281 reduced phosphorylation to undetectable levels
Identifier Residue Sequence Organism Cell Line
SIGNOR-246634 Ser281 DGTGDTSsEEDEDEE Homo sapiens
pmid sentence
TAFII 250 Phosphorylates Human Transcription Factor IIA on Serine Residues Important for TBP Binding and Transcription ActivityAdditional alanine substitutions at serines 280 and 281 reduced phosphorylation to undetectable levels
Identifier Residue Sequence Organism Cell Line
SIGNOR-105688 Ser316 VEEEPLNsEDDVSDE Homo sapiens
pmid sentence
Taf(ii) 250 phosphorylates human transcription factor iia on serine residues important for tbp binding and transcription activity.
Publications: 3 Organism: Homo Sapiens
+ TAF1up-regulates img/direct-activation.png phosphorylation GTF2A1 0.668
Identifier Residue Sequence Organism Cell Line
SIGNOR-105745 Ser321 LNSEDDVsDEEGQEL Homo sapiens
pmid sentence
Taf(ii) 250 phosphorylates human transcription factor iia on serine residues important for tbp binding and transcription activity.
Publications: 1 Organism: Homo Sapiens
+ GTF2A1form complex img/form-complex.png binding TFIIA 0.939
Identifier Residue Sequence Organism Cell Line
SIGNOR-266197 Homo sapiens HeLa Cell
pmid sentence
TFIIA purified from HeLa extracts consists of 35-, 19-, and 12-kDa subunits. Here we describe the isolation of a cDNA clone (hTFIIA gamma) encoding the 12-kDa subunit.
Publications: 1 Organism: Homo Sapiens
a simple tooltip