| + |
AEP complex | up-regulates quantity by expression 
|
MEIS1 |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256144 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20854876 |
Inhibition of EAP components pTEFb and Dot1l show that both contribute significantly to activation of Hoxa9 and Meis1 expression. EAP is dynamically associated with the Hoxa9 and Meis1 loci in hematopoietic cells and rapidly dissociates during induction of differentiation. In the presence of MLL fusion proteins, its dissociation is prevented. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, MLL fusion protein in AML |
| + |
MLL-AF4 | up-regulates activity 
binding
|
AEP complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255877 |
|
|
Homo sapiens |
B-lymphoblast Cell Line |
| pmid |
sentence |
| 19956800 |
Although the complex was initially termed ENL associated proteins (EAP), we now propose to redefine EAP as ‘‘elongation assisting proteins’’ to better reflect the function of this protein complex. In this report, we present evidence that the most frequently occurring MLL fusion proteins exploit molecular control mechanisms of transcriptional elongation to transform hematopoietic cells. MLL fusions become incorporated into an ‘‘elongation assisting protein’’ complex, recruit it to their respective target genes, and enforce ectopic transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, MLL fusion protein in AML |
| + |
MLL-AF9 | up-regulates activity
binding
|
AEP complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255876 |
|
|
Homo sapiens |
B-lymphoblast Cell Line |
| pmid |
sentence |
| 19956800 |
Although the complex was initially termed ENL associated proteins (EAP), we now propose to redefine EAP as ‘‘elongation assisting proteins’’ to better reflect the function of this protein complex. In this report, we present evidence that the most frequently occurring MLL fusion proteins exploit molecular control mechanisms of transcriptional elongation to transform hematopoietic cells. MLL fusions become incorporated into an ‘‘elongation assisting protein’’ complex, recruit it to their respective target genes, and enforce ectopic transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, MLL fusion protein in AML |
| + |
AFF1 | form complex 
binding
|
AEP complex |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-239231 |
|
|
Homo sapiens |
K-562 Cell |
| pmid |
sentence |
| 20153263 |
These data demonstrate that AF4, AF5q31 and ENL associate in an endogenous higher-order complex (hereafter referred to as AEP for the AF4 family/ENL family/P-TEFb complex) containing P-TEFb in hematopoietic lineage cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MLL Fusion | up-regulates activity
binding
|
AEP complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260131 |
|
|
Homo sapiens |
B-lymphoblast Cell Line |
| pmid |
sentence |
| 19956800 |
Although the complex was initially termed ENL associated proteins (EAP), we now propose to redefine EAP as ‘‘elongation assisting proteins’’ to better reflect the function of this protein complex. In this report, we present evidence that the most frequently occurring MLL fusion proteins exploit molecular control mechanisms of transcriptional elongation to transform hematopoietic cells. MLL fusions become incorporated into an ‘‘elongation assisting protein’’ complex, recruit it to their respective target genes, and enforce ectopic transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, MLL fusion protein in AML |
| + |
MLLT1 | form complex
binding
|
AEP complex |
0.68 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-239228 |
|
|
Homo sapiens |
K-562 Cell |
| pmid |
sentence |
| 20153263 |
These data demonstrate that AF4, AF5q31 and ENL associate in an endogenous higher-order complex (hereafter referred to as AEP for the AF4 family/ENL family/P-TEFb complex) containing P-TEFb in hematopoietic lineage cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AFF4 | form complex
binding
|
AEP complex |
0.547 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-239224 |
|
|
Homo sapiens |
K-562 Cell |
| pmid |
sentence |
| 20153263 |
These data demonstrate that AF4, AF5q31 and ENL associate in an endogenous higher-order complex (hereafter referred to as AEP for the AF4 family/ENL family/P-TEFb complex) containing P-TEFb in hematopoietic lineage cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MLL-ENL | up-regulates activity
binding
|
AEP complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255878 |
|
|
Homo sapiens |
B-lymphoblast Cell Line |
| pmid |
sentence |
| 19956800 |
Although the complex was initially termed ENL associated proteins (EAP), we now propose to redefine EAP as ‘‘elongation assisting proteins’’ to better reflect the function of this protein complex. In this report, we present evidence that the most frequently occurring MLL fusion proteins exploit molecular control mechanisms of transcriptional elongation to transform hematopoietic cells. MLL fusions become incorporated into an ‘‘elongation assisting protein’’ complex, recruit it to their respective target genes, and enforce ectopic transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, MLL fusion protein in AML |
| + |
AEP complex | up-regulates quantity by expression
|
HOXA9 |
0.418 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255879 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20854876 |
Inhibition of EAP components pTEFb and Dot1l show that both contribute significantly to activation of Hoxa9 and Meis1 expression. EAP is dynamically associated with the Hoxa9 and Meis1 loci in hematopoietic cells and rapidly dissociates during induction of differentiation. In the presence of MLL fusion proteins, its dissociation is prevented. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, MLL fusion protein in AML |
| + |
P-TEFb | form complex
binding
|
AEP complex |
0.755 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-239237 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20153263 |
These data demonstrate that AF4, AF5q31 and ENL associate in an endogenous higher-order complex (hereafter referred to as AEP for the AF4 family/ENL family/P-TEFb complex) containing P-TEFb in hematopoietic lineage cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
AEP complex