+ |
CSNK2A1 |
phosphorylation
|
SMC3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178483 |
Ser1067 |
GDVEGSQsQDEGEGS |
Homo sapiens |
|
pmid |
sentence |
18442975 |
Our data provide evidence that phosphorylation of a core cohesin subunit smc3 by atm plays an important role in dna damage response and suggest that a constitutive phosphorylation by ck2 may affect intra-s phase checkpoint by modulating smc3 phosphorylation by atm. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CSNK2A2 |
phosphorylation
|
SMC3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178487 |
Ser1067 |
GDVEGSQsQDEGEGS |
Homo sapiens |
|
pmid |
sentence |
18442975 |
Our data provide evidence that phosphorylation of a core cohesin subunit smc3 by atm plays an important role in dna damage response and suggest that a constitutive phosphorylation by ck2 may affect intra-s phase checkpoint by modulating smc3 phosphorylation by atm. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ATM |
phosphorylation
|
SMC3 |
0.732 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-178479 |
Ser1083 |
ESERGSGsQSSVPSV |
Homo sapiens |
|
pmid |
sentence |
18442975 |
Ser-1083 phosphorylation is ir-inducible, depends on atm and nijmegen breakage syndrome 1 (nbs1), and is required for intra-s phase checkpoint. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SMC3 | form complex
binding
|
Cohesin complex |
0.908 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263312 |
|
|
|
|
pmid |
sentence |
28430577 |
Cohesin is an evolutionarily conserved complex composed of four core proteins (SMC1A, SMC3, RAD21 and either STAG2 or STAG1) that form a ring-shaped structure able to encircle chromatin |
|
Publications: |
1 |
+ |
SMC3 | form complex
binding
|
RAD21L Cohesin complex |
0.814 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264537 |
|
|
Mus musculus |
|
pmid |
sentence |
21242291 |
RAD21L associates with SMC3, STAG3, and either SMC1α or SMC1β. Our results suggest that cohesin complexes containing RAD21L may be involved in synapsis initiation and crossover recombination between homologous chromosomes. In mice, RAD21L is expressed exclusively in early meiosis: it apparently replaces RAD21 in premeiotic S phase, becomes detectable on the axial elements in leptotene, and stays on the axial/lateral elements until mid pachytene. RAD21L then disappears, and is replaced with RAD21. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Gonad |
+ |
SMC3 | down-regulates activity
binding
|
MXD1 |
0.3 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-241278 |
|
|
Chlorocebus aethiops |
CV-1 Cell |
pmid |
sentence |
9528857 |
We identified a novel ZIP-containing protein, Mmip1 (Mad member interacting protein 1) that strongly dimerizes with all four Mad members, but not with c-myc. Mmip1 can inhibit DNA binding by Max-Mad heterodimers and, in vivo, can reverse the suppressive eects of Mad proteins on c-myc functions. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
SMC3 | down-regulates activity
binding
|
MXD3 |
0.3 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-241281 |
|
|
Chlorocebus aethiops |
CV-1 Cell |
pmid |
sentence |
9528857 |
We identified a novel ZIP-containing protein, Mmip1 (Mad member interacting protein 1) that strongly dimerizes with all four Mad members, but not with c-myc. Mmip1 can inhibit DNA binding by Max-Mad heterodimers and, in vivo, can reverse the suppressive eects of Mad proteins on c-myc functions. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
SMC3 | down-regulates activity
binding
|
MXD4 |
0.3 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-241284 |
|
|
Chlorocebus aethiops |
CV-1 Cell |
pmid |
sentence |
9528857 |
We identified a novel ZIP-containing protein, Mmip1 (Mad member interacting protein 1) that strongly dimerizes with all four Mad members, but not with c-myc. Mmip1 can inhibit DNA binding by Max-Mad heterodimers and, in vivo, can reverse the suppressive eects of Mad proteins on c-myc functions. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
SMC3 | down-regulates activity
binding
|
MXI1 |
0.413 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-241223 |
|
|
Chlorocebus aethiops |
CV-1 Cell |
pmid |
sentence |
9528857 |
We identified a novel ZIP-containing protein, Mmip1 (Mad member interacting protein 1) that strongly dimerizes with all four Mad members, but not with c-myc. Mmip1 can inhibit DNA binding by Max-Mad heterodimers and, in vivo, can reverse the suppressive eects of Mad proteins on c-myc functions. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |