+ |
Elongator complex | up-regulates activity
acetylation
|
TUBA3C |
0.254 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269716 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19185337 |
Elongator Subunits Interact with the Microtubules and Are Required for Proper Acetylation of α-Tubulin. α-Tubulin Acetylation Promotes Radial Migration and Branching of Cortical Projection Neurons |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ELP2 | form complex
binding
|
Elongator complex |
0.774 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269709 |
|
|
Homo sapiens |
|
pmid |
sentence |
28601220 |
Elongator is a highly conserved eukaryotic protein complex consisting of two sets of six Elp proteins, while homologues of its catalytic subunit Elp3 are found in all the kingdoms of life. Although it was originally described as a transcription elongation factor, cumulating evidence suggests that its primary function is catalyzing tRNA modifications. In humans, defects in Elongator subunits are associated with neurological disorders and cancer. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Elongator complex | up-regulates activity
acetylation
|
TUBA3D |
0.254 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269715 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19185337 |
Elongator Subunits Interact with the Microtubules and Are Required for Proper Acetylation of α-Tubulin. α-Tubulin Acetylation Promotes Radial Migration and Branching of Cortical Projection Neurons |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Elongator complex | up-regulates activity
binding
|
RAB3IL1 |
0.277 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269714 |
|
|
in vitro |
|
pmid |
sentence |
15780940 |
Our results raise the possibility that regulation of polarized exocytosis is an evolutionarily conserved function of the entire Elongator complex and that FD results from a dysregulation of neuronal exocytosis. Our results raise the possibility that regulation of polarized exocytosis is an evolutionarily conserved function of the entire Elongator complex and that FD results from a dysregulation of neuronal exocytosis. We show that elp1Δ suppression of sec2ts is not a result of reduced transcriptional elongation and that Elp1p physically associates with Sec2p. The Sec2p interaction domain of Elp1p is necessary for both Elp1p function and for the polarized localization of Sec2p. Mutations in human Elp1p (IKAP) are a known cause of familial dysautonomia (FD). |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
Elongator complex | up-regulates activity
acetylation
|
TUBA3E |
0.254 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269718 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19185337 |
Elongator Subunits Interact with the Microtubules and Are Required for Proper Acetylation of α-Tubulin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ELP4 | form complex
binding
|
Elongator complex |
0.864 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269711 |
|
|
Homo sapiens |
|
pmid |
sentence |
28601220 |
Elongator is a highly conserved eukaryotic protein complex consisting of two sets of six Elp proteins, while homologues of its catalytic subunit Elp3 are found in all the kingdoms of life. Although it was originally described as a transcription elongation factor, cumulating evidence suggests that its primary function is catalyzing tRNA modifications. In humans, defects in Elongator subunits are associated with neurological disorders and cancer. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Elongator complex | up-regulates activity
acetylation
|
TUBA4A |
0.254 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269722 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19185337 |
Elongator Subunits Interact with the Microtubules and Are Required for Proper Acetylation of α-Tubulin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Elongator complex | up-regulates activity
acetylation
|
TUBA1A |
0.338 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269717 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19185337 |
Elongator Subunits Interact with the Microtubules and Are Required for Proper Acetylation of α-Tubulin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ELP5 | form complex
binding
|
Elongator complex |
0.696 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269712 |
|
|
Homo sapiens |
|
pmid |
sentence |
28601220 |
Elongator is a highly conserved eukaryotic protein complex consisting of two sets of six Elp proteins, while homologues of its catalytic subunit Elp3 are found in all the kingdoms of life. Although it was originally described as a transcription elongation factor, cumulating evidence suggests that its primary function is catalyzing tRNA modifications. In humans, defects in Elongator subunits are associated with neurological disorders and cancer. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ELP3 | form complex
binding
|
Elongator complex |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269710 |
|
|
Homo sapiens |
|
pmid |
sentence |
28601220 |
Elongator is a highly conserved eukaryotic protein complex consisting of two sets of six Elp proteins, while homologues of its catalytic subunit Elp3 are found in all the kingdoms of life. Although it was originally described as a transcription elongation factor, cumulating evidence suggests that its primary function is catalyzing tRNA modifications. In humans, defects in Elongator subunits are associated with neurological disorders and cancer. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ELP1 | form complex
binding
|
Elongator complex |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269708 |
|
|
Homo sapiens |
|
pmid |
sentence |
28601220 |
Elongator is a highly conserved eukaryotic protein complex consisting of two sets of six Elp proteins, while homologues of its catalytic subunit Elp3 are found in all the kingdoms of life. Although it was originally described as a transcription elongation factor, cumulating evidence suggests that its primary function is catalyzing tRNA modifications. In humans, defects in Elongator subunits are associated with neurological disorders and cancer. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Elongator complex | up-regulates activity
acetylation
|
TUBA8 |
0.254 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269721 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19185337 |
Elongator Subunits Interact with the Microtubules and Are Required for Proper Acetylation of α-Tubulin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Elongator complex | up-regulates activity
acetylation
|
TUBA1B |
0.256 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269719 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19185337 |
Elongator Subunits Interact with the Microtubules and Are Required for Proper Acetylation of α-Tubulin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ELP6 | form complex
binding
|
Elongator complex |
0.761 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269713 |
|
|
Homo sapiens |
|
pmid |
sentence |
28601220 |
Elongator is a highly conserved eukaryotic protein complex consisting of two sets of six Elp proteins, while homologues of its catalytic subunit Elp3 are found in all the kingdoms of life. Although it was originally described as a transcription elongation factor, cumulating evidence suggests that its primary function is catalyzing tRNA modifications. In humans, defects in Elongator subunits are associated with neurological disorders and cancer. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Elongator complex | up-regulates activity
acetylation
|
TUBA1C |
0.257 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269720 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19185337 |
Elongator Subunits Interact with the Microtubules and Are Required for Proper Acetylation of α-Tubulin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |