+ |
CSNK2A2 | up-regulates activity
phosphorylation
|
GTF2A1 |
0.382 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250995 |
Ser280 |
VDGTGDTsSEEDEDE |
in vitro |
|
pmid |
sentence |
11278496 |
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 |
11278496 |
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 |
11278496 |
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 |
11278496 |
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 |
+ |
TAF1 | up-regulates activity
phosphorylation
|
GTF2A1 |
0.662 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-246630 |
Ser280 |
VDGTGDTsSEEDEDE |
Homo sapiens |
|
pmid |
sentence |
11278496 |
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 |
11278496 |
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 |
11278496 |
Taf(ii) 250 phosphorylates human transcription factor iia on serine residues important for tbp binding and transcription activity. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
CSNK2A1 | up-regulates activity
phosphorylation
|
GTF2A1 |
0.388 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250874 |
Ser280 |
VDGTGDTsSEEDEDE |
in vitro |
|
pmid |
sentence |
11278496 |
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 |
11278496 |
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 |
11278496 |
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 |
11278496 |
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 |
+ |
TAF1 | up-regulates
phosphorylation
|
GTF2A1 |
0.662 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-105745 |
Ser321 |
LNSEDDVsDEEGQEL |
Homo sapiens |
|
pmid |
sentence |
11278496 |
Taf(ii) 250 phosphorylates human transcription factor iia on serine residues important for tbp binding and transcription activity. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GTF2A1 | form complex
binding
|
TFIIA |
0.938 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266197 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
7724559 |
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 |