| + |
TAGLN2 | down-regulates activity 
binding
|
ACTB |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265104 |
|
|
|
|
| pmid |
sentence |
| 21577206 |
Taken together, our data propose a novel, oncogene-tumor suppressor interplay, where oncogenic PFTK1 confers HCC cell motility through inactivating the actin-binding motile suppressing function of TAGLN2 via phosphorylation. |
|
| Publications: |
1 |
| + |
ACTB | up-regulates 
|
Early Endosome |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260610 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19121306 |
However, we did detect WAFL binding to bothWIP and actin by immunoprecipitation (Fig. 4). In conclusion, we propose a model whereby WAFL associates toendocytic vesicles by its coiled-coil domain and is involved in actin-based movement of early endosomes via WIP and binding to actin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYN1 | up-regulates activity 
binding
|
ACTB |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269184 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15265865 |
Synapsins, a family of neuron-specific phosphoproteins, have been demonstrated to regulate the availability of synaptic vesicles for exocytosis by binding to both synaptic vesicles and the actin cytoskeleton in a phosphorylation-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACTB | form complex 
binding
|
NuA4 complex |
0.481 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269293 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14966270 |
NuA4 (for nucleosome acetyltransferase of H4) is a 12-subunit HAT complex responsible for acetylation of histone H4 and H2A N-terminal tails. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MYO5A | up-regulates activity
binding
|
ACTB |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269280 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21077886 |
Myosin Va regulates exocytosis of large dense-core vesicles (LDCVs). interestingly, inhibition of myosin Va potentiates LDCV exocytosis to the same extent as F-actin depolymerization does, suggesting that myosin Va cooperates with the actin cytoskeleton to impede or control LDCV exocytosis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IPP complex | up-regulates activity
relocalization
|
ACTB |
0.355 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265768 |
|
|
|
|
| pmid |
sentence |
| 27590440 |
Apart from binding with integrins on the membrane, IPP complex can interact with the cytoskeleton as well as many signaling proteins inside the cell. Up to now, dozens of IPP complex-related proteins have been identified. One of these proteins is parvin that binds to F-actin, thus connecting ECM with cytoskeleton.17 In the following, we will discuss PINCH-interacting proteins and their roles. |
|
| Publications: |
1 |
| + |
ACTB | form complex
binding
|
Muscle cell-specific SWI/SNF ARID1B variant |
0.476 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270711 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11073988 |
The SWI/SNF family of chromatin-remodeling complexes facilitates gene activation by assisting transcription machinery to gain access to targets in chromatin. Our data suggest that BAF250 confers specificity to the human BAF complex and may recruit the complex to its targets through either protein-DNA or protein-protein interactions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
ACTB | form complex
binding
|
Brain-specific SWI/SNF SMARCA4 variant |
0.503 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270757 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11790558 |
Whereas chromatin-remodeling complexes are generally thought to promote gene expression, recent genetic and biochemical studies suggest that the SWI/SNF complex may also be involved in transcriptional repression . The subunit composition of the different human complexes that belong to this family is listed in Table 1. Several of the subunits, including SNF5/INI1, are common to all complexes and may constitute its core. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
IGF2BP1 | up-regulates quantity
post transcriptional regulation
|
ACTB |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268160 |
|
|
Rattus norvegicus |
Cerebral Cortical Neuron |
| pmid |
sentence |
| 21734271 |
We found that ZBP1 is necessary for netrin-1 stimulated local translation of β-actin mRNA in axonal growth cones. ZBP1 binds to β-actin mRNA in the soma and transports it to the growth cone on microtubules. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
ACTB | form complex
binding
|
Embryonic stem cell-specific SWI/SNF |
0.472 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270717 |
|
|
Mus musculus |
Embryonic Stem Cell |
| pmid |
sentence |
| 19279220 |
An embryonic stem cell chromatin remodeling complex, esBAF, is essential for embryonic stem cell self-renewal and pluripotency |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
NTN1 | up-regulates quantity
post transcriptional regulation
|
ACTB |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268161 |
|
|
Xenopus laevis laevis |
Retinal Cone |
| pmid |
sentence |
| 16980963 |
Netrin-1 induces β-actin translation driven by its 3’UTR. |
|
| Publications: |
1 |
Organism: |
Xenopus Laevis Laevis |
| Pathways: | Axon guidance |
| + |
ACTB | form complex
binding
|
Brain-specific SWI/SNF SMARCA2 variant |
0.479 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270748 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11790558 |
Whereas chromatin-remodeling complexes are generally thought to promote gene expression, recent genetic and biochemical studies suggest that the SWI/SNF complex may also be involved in transcriptional repression . The subunit composition of the different human complexes that belong to this family is listed in Table 1. Several of the subunits, including SNF5/INI1, are common to all complexes and may constitute its core. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
CKB | up-regulates quantity
relocalization
|
ACTB |
0.298 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265791 |
|
|
Homo sapiens |
Astrocyte |
| pmid |
sentence |
| 19333390 |
In summary, data presented here strongly suggest that locally generated ATP is an important regulator for actin-based cytoskeletal dynamics involved in cell extension and motility and that CK-B is a controlling enzyme in the compartmentalization of ATP availability. CK-B co-localizes with cortical actin and facilitates spreading of astrocytes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYN2 | up-regulates activity
binding
|
ACTB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269182 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15265865 |
Synapsins, a family of neuron-specific phosphoproteins, have been demonstrated to regulate the availability of synaptic vesicles for exocytosis by binding to both synaptic vesicles and the actin cytoskeleton in a phosphorylation-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FKBP15 | up-regulates activity
binding
|
ACTB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260595 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19121306 |
However, we did detect WAFL binding to bothWIP and actin by immunoprecipitation (Fig. 4). In conclusion, we propose a model whereby WAFL associates toendocytic vesicles by its coiled-coil domain and is involved in actin-based movement of early endosomes via WIP and binding to actin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACTB | form complex
binding
|
Muscle cell-specific SWI/SNF ARID1A variant |
0.478 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270698 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11073988 |
The SWI/SNF family of chromatin-remodeling complexes facilitates gene activation by assisting transcription machinery to gain access to targets in chromatin. Our data suggest that BAF250 confers specificity to the human BAF complex and may recruit the complex to its targets through either protein-DNA or protein-protein interactions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
ACTB | up-regulates
|
Endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260608 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19121306 |
However, we did detect WAFL binding to bothWIP and actin by immunoprecipitation (Fig. 4). In conclusion, we propose a model whereby WAFL associates toendocytic vesicles by its coiled-coil domain and is involved in actin-based movement of early endosomes via WIP and binding to actin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACTB | up-regulates quantity
binding
|
F-actin_assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261879 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28233384 |
Here, we report the highest resolution, cryo-EM structures of actin filaments with bound ATP analog β,γ-imidoadenosine 5′-triphosphate (AMPPNP) (3.1 Å) and ADP with inorganic phosphate (ADP-Pi) (3.1 Å) as well as a 3.6-Å resolution structure of the ADP filament. These structures of the three well-characterized nucleotide states of actin monomers and filaments |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Axon guidance |
| + |
ACTB | form complex
binding
|
SWI/SNF ACTL6B varian |
0.481 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270599 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30397315 |
Mammalian SWI/SNF (mSWI/SNF) complexes are ATP-dependent chromatin remodelers that modulate genomic architecture and DNA accessibility, enabling timely and appropriate control of gene expression. They are combinatorially assembled from the products of 29 total genes into three final-form complexes: canonical BAF, PBAF (polybromo-associated BAF complexes), and a newly-defined non-canonical BAF (ncBAF), with specific subunits specifying distinct complexes, such as PBRM1, ARID2, and BRD7 in PBAF complexes, ARID1A/ARID1B and DPF2 in canonical BAF (cBAF) complexes, and GLTSCR1/GLTSCR1L and BRD9 in ncBAF complexes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACTB | form complex
binding
|
GBAF |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269788 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30397315 |
Mammalian SWI/SNF (mSWI/SNF) complexes are ATP-dependent chromatin remodelers that modulate genomic architecture and DNA accessibility, enabling timely and appropriate control of gene expression. They are combinatorially assembled from the products of 29 total genes into three final-form complexes: canonical BAF, PBAF (polybromo-associated BAF complexes), and a newly-defined non-canonical BAF (ncBAF), with specific subunits specifying distinct complexes, such as PBRM1, ARID2, and BRD7 in PBAF complexes, ARID1A/ARID1B and DPF2 in canonical BAF (cBAF) complexes, and GLTSCR1/GLTSCR1L and BRD9 in ncBAF complexes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACTB | form complex
binding
|
SWI/SNF ACTL6A-ARID1A-SMARCA2 variant |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269826 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30397315 |
Mammalian SWI/SNF (mSWI/SNF) complexes are ATP-dependent chromatin remodelers that modulate genomic architecture and DNA accessibility, enabling timely and appropriate control of gene expression. They are combinatorially assembled from the products of 29 total genes into three final-form complexes: canonical BAF, PBAF (polybromo-associated BAF complexes), and a newly-defined non-canonical BAF (ncBAF), with specific subunits specifying distinct complexes, such as PBRM1, ARID2, and BRD7 in PBAF complexes, ARID1A/ARID1B and DPF2 in canonical BAF (cBAF) complexes, and GLTSCR1/GLTSCR1L and BRD9 in ncBAF complexes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GFAP | up-regulates quantity
binding
|
ACTB |
0.388 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269271 |
|
|
Homo sapiens |
Astrocyte |
| pmid |
sentence |
| 31626364 |
GFAP is the major cytoskeletal element and scaffold of astrocytes In astrocytes, GFAP has close interaction with F-actin molecularly and functionally. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CD2AP | up-regulates activity
binding
|
ACTB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264770 |
|
|
Homo sapiens |
HEK-293 Cell, U2-OS Cell |
| pmid |
sentence |
| 29175910 |
One such regulator is the adaptor protein CD2AP, which delivers capping proteins to the barbed ends of polymerizing F-actin. Capping growing filaments can promote the formation of actin branches by increasing the G-actin pool available to form branches |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYN3 | up-regulates activity
binding
|
ACTB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269183 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15265865 |
Synapsins, a family of neuron-specific phosphoproteins, have been demonstrated to regulate the availability of synaptic vesicles for exocytosis by binding to both synaptic vesicles and the actin cytoskeleton in a phosphorylation-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACTB | form complex
binding
|
Muscle cell-specific SWI/SNF SMARCA4 variant |
0.491 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270739 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11073988 |
We have also found that, of the two human SWI/2/SNF2 family-related ATPases, the PBAF complex contains only BRG1 but not hbrm (Xue et al., submitted). In contrast, the BAF complex isolated by BAF250 can include either BRG1 or hbrm (Fig. (Fig.4b).4b). These data underscore the distinctness of the two human complexes and suggest that BAF250 is a signature subunit that may confer specificity to the BAF complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
ACTB | form complex
binding
|
Neural progenitor-specific SWI/SNF |
0.484 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270619 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25195934 |
The BAF (mammalian SWI/SNF) complexes are a family of multi-subunit ATP-dependent chromatin remodelers that use ATP hydrolysis to alter chromatin structure. Distinct BAF complex compositions are possible through combinatorial assembly of homologous subunit families and can serve non-redundant functions. In mammalian neural development, developmental stage-specific BAF assemblies are found in embryonic stem cells, neural progenitors and postmitotic neurons. In particular, the neural progenitor-specific BAF complexes are essential for controlling the kinetics and mode of neural progenitor cell division, while neuronal BAF function is necessary for the maturation of postmitotic neuronal phenotypes as well as long-term memory formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ACTB
- 
- 