| + |
PKC | down-regulates activity 
phosphorylation
|
SUN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263281 |
Ser113 |
HVSRQVTsSGVSHGG |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 28831067 |
The SUN1-NXF1 association is at least partly regulated by a protein kinase C (PKC) which phosphorylates serine 113 (S113) in the N-terminal domain leading to reduced interaction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates activity
phosphorylation
|
SUN1 |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263098 |
Ser138 |
RPPVLDEsWIREQTT |
Homo sapiens |
|
| pmid |
sentence |
| 25482198 |
Here, we show that SUN1, located in the INM, undergoes mitosis-specific phosphorylation on at least 3 sites within its nucleoplasmic N-terminus. We further identify Cdk1 as the kinase responsible for serine 48 and 333 phosphorylation, while serine 138 is phosphorylated by Plk1. Together, these data support a model whereby mitotic phosphorylation of SUN1 disrupts interactions with nucleoplasmic binding partners, promoting disassembly of the nuclear lamina and, potentially, its chromatin interactions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK1 | down-regulates activity
phosphorylation
|
SUN1 |
0.37 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263100 |
Ser334 |
FLLLAGLsLRGQGNF |
Homo sapiens |
|
| pmid |
sentence |
| 25482198 |
Here, we show that SUN1, located in the INM, undergoes mitosis-specific phosphorylation on at least 3 sites within its nucleoplasmic N-terminus. We further identify Cdk1 as the kinase responsible for serine 48 and 333 phosphorylation, while serine 138 is phosphorylated by Plk1. Together, these data support a model whereby mitotic phosphorylation of SUN1 disrupts interactions with nucleoplasmic binding partners, promoting disassembly of the nuclear lamina and, potentially, its chromatin interactions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263099 |
Ser48 |
KLDPVFDsPRMSRRS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25482198 |
Here, we show that SUN1, located in the INM, undergoes mitosis-specific phosphorylation on at least 3 sites within its nucleoplasmic N-terminus. We further identify Cdk1 as the kinase responsible for serine 48 and 333 phosphorylation, while serine 138 is phosphorylated by Plk1. Together, these data support a model whereby mitotic phosphorylation of SUN1 disrupts interactions with nucleoplasmic binding partners, promoting disassembly of the nuclear lamina and, potentially, its chromatin interactions. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SUN1 | up-regulates activity 
binding
|
NUP153 |
0.449 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263294 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 28831067 |
The NXF1:NXT1 complex and NUP153 interact with the amino terminus of SUN1 |In analogy to a proposal made by Chang et al.4, Nesprins could help anchoring SUN1 near the NPC to enable it to fulfill its task in mRNA export. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TP63 | up-regulates quantity by expression
transcriptional regulation
|
SUN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263278 |
|
|
Mus musculus |
Epidermal Stem Cell |
| pmid |
sentence |
| 28595999 |
Here we show that in the developing skin, epidermal progenitor cells of mice lacking p63 transcription factor display alterations in the nuclear shape accompanied by a marked decrease in expression of several nuclear envelope-associated components (Lamin B1, Lamin A/C, Sun1, Nesprin-3, Plectin) compared with controls. Furthermore, chromatin immunoprecipitation-quantitative PCR assay showed enrichment of p63 on Sun1, Syne3, and Plec promoters, suggesting them as p63 targets. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SUN1 | up-regulates activity
binding
|
NXF1 |
0.366 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263296 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 28831067 |
SUN1, a component of the LINC (Linker of Nucleoskeleton and Cytoskeleton) complex, functions in mammalian mRNA export through the NXF1-dependent pathway. It associates with mRNP complexes by direct interaction with NXF1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SUN1 | up-regulates activity
binding
|
SPDYA |
0.251 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263301 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 33015044 |
In this study, we found that SUN1 not only interacted with TERB1 but also interacted with MAJIN, and the interaction of SUN1 with MAJIN is stronger than TERB1. We also found that SUN1 interacted with SPDYA, an activator of CDK2. | Taken together, we speculate that speedy A is likely capable of interacting with both telomeres and the LINC complex and thus might function as the missing linkage between telomeres and the LINC complex during prophase I, stabilizing the telomere–NE connection |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SUN1 | up-regulates activity
binding
|
MAJIN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263300 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 33015044 |
In this study, we found that SUN1 not only interacted with TERB1 but also interacted with MAJIN, and the interaction of SUN1 with MAJIN is stronger than TERB1. We also found that SUN1 interacted with SPDYA, an activator of CDK2. | It will be of great interest to test this hypothesis to fully understand the mechanisms of stable telomere–NE connection and telomere movement along the NE driven by the LINC complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SUN1 | form complex 
binding
|
LINC complex |
0.508 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263282 |
|
|
|
|
| pmid |
sentence |
| 24481844 |
LINC complex couples the nuclear lamina to the cytoskeleton. SUN domain proteins, SUN1 and SUN2, located at the inner nuclear membrane (INM) interact with the nuclear lamins, Lamin A/C, B1, and B2, that line the nucleoplasmic face of the INM. SUN domain proteins interact with Nesprins in the perinuclear space (PNS). Nesprins protrude from the outer nuclear membrane (ONM) and interact with the cytoskeleton, often through an intermediate binding partner. Nesprin 1 giant (g) and Nesprin 2g potentially link the NE directly to the Z-disc (Z), whereas Nesprin 1alpha and 2alpha may connect via an unknown intermediate protein. In addition, the shorter isoforms of Nesprin 1 and Nesprin 2 may localize to the INM. |
|
| Publications: |
1 |
| + |
SUN1 | up-regulates activity
binding
|
TERB1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263299 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 33015044 |
In this study, we found that SUN1 not only interacted with TERB1 but also interacted with MAJIN, and the interaction of SUN1 with MAJIN is stronger than TERB1. We also found that SUN1 interacted with SPDYA, an activator of CDK2. | It will be of great interest to test this hypothesis to fully understand the mechanisms of stable telomere–NE connection and telomere movement along the NE driven by the LINC complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SUN1
- 
- 