Type |
Details |
Score |
Protein Domain |
Type: |
Family |
Description: |
This entry consists of the E3 SUMO-protein ligase Nse2 (also known as Mms21). Nse2 is an E3 SUMO-protein ligase component of the SMC5-SMC6 complex [, ]. Nse2 acts as an E3 ligase targeting several proteins for sumoylation and is required for efficient DNA repair and maintenance of genome stability [, , , ]. Nse2 and SMC5 may also be required for sister chromatid cohesion during prometaphase and mitotic progression; this role is apparently independent of SMC6 []. Nse2 is necessary for normal cell cycle progression in Arabidopsis, where Nse2 mutation results in abnormal root development []. |
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•
•
•
•
•
|
Publication |
First Author: |
Pebernard S |
Year: |
2004 |
Journal: |
Mol Biol Cell |
Title: |
Nse1, Nse2, and a novel subunit of the Smc5-Smc6 complex, Nse3, play a crucial role in meiosis. |
Volume: |
15 |
Issue: |
11 |
Pages: |
4866-76 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gómez R |
Year: |
2013 |
Journal: |
J Cell Sci |
Title: |
Dynamic localization of SMC5/6 complex proteins during mammalian meiosis and mitosis suggests functions in distinct chromosome processes. |
Volume: |
126 |
Issue: |
Pt 18 |
Pages: |
4239-52 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
451
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
353
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
284
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
171
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
337
|
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Hu B |
Year: |
2005 |
Journal: |
Mol Microbiol |
Title: |
Qri2/Nse4, a component of the essential Smc5/6 DNA repair complex. |
Volume: |
55 |
Issue: |
6 |
Pages: |
1735-50 |
|
•
•
•
•
•
|
Publication |
First Author: |
Bermúdez-López M |
Year: |
2010 |
Journal: |
Nucleic Acids Res |
Title: |
The Smc5/6 complex is required for dissolution of DNA-mediated sister chromatid linkages. |
Volume: |
38 |
Issue: |
19 |
Pages: |
6502-12 |
|
•
•
•
•
•
|
Publication |
First Author: |
Vondrova L |
Year: |
2020 |
Journal: |
Sci Rep |
Title: |
A role of the Nse4 kleisin and Nse1/Nse3 KITE subunits in the ATPase cycle of SMC5/6. |
Volume: |
10 |
Issue: |
1 |
Pages: |
9694 |
|
•
•
•
•
•
|
Publication |
First Author: |
McDonald WH |
Year: |
2003 |
Journal: |
J Biol Chem |
Title: |
Novel essential DNA repair proteins Nse1 and Nse2 are subunits of the fission yeast Smc5-Smc6 complex. |
Volume: |
278 |
Issue: |
46 |
Pages: |
45460-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Harvey SH |
Year: |
2002 |
Journal: |
Genome Biol |
Title: |
Structural maintenance of chromosomes (SMC) proteins, a family of conserved ATPases. |
Volume: |
3 |
Issue: |
2 |
Pages: |
REVIEWS3003 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This entry represents the Nse3/MAGE () binding domain found in NSE4/EID family proteins [, ]. Proteins in the NSE4/EID (Non-structural maintenance of chromosomes element 4/EP300-interacting inhibitor of differentiation 3) family are components of the Smc5/6 complex that is involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination and mediates sumoylation of shelterin complex (telosome) components [, , ]. In human, it acts as a repressor of nuclear receptor-dependent transcription possibly by interfering with CREBBP-dependent coactivation. It may function as a coinhibitor of other CREBBP/EP300-dependent transcription factors []. Interestingly, there is a single NSE4 gene in most eukaryotes up to non-placental mammals while there are several NSE4/EID copies in placental mammals []. In humans, there are two NSE4 proteins, NSE4a and NSE4b/EID3. They contain both N and C-terminal kleisin domains. Their N-terminal domain binds to SMC6 neck and bridges it to the SMC5 head []and to the Nse3 (another SMC5-6 complex subunit) pocket [], which seems to increased the stability of the ATP-free SMC5/6 complex. |
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•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Proteins in the NSE4/EID (Non-structural maintenance of chromosomes element 4/EP300-interacting inhibitor of differentiation 3) family are components of the Smc5/6 complex that is involved in repair of DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination and mediates sumoylation of shelterin complex (telosome) components [, , ]. In human, it acts as a repressor of nuclear receptor-dependent transcription possibly by interfering with CREBBP-dependent coactivation. It may function as a coinhibitor of other CREBBP/EP300-dependent transcription factors []. Interestingly, there is a single NSE4 gene in most eukaryotes up to non-placental mammals while there are several NSE4/EID copies in placental mammals []. In humans, there are two NSE4 proteins, NSE4a and NSE4b/EID3. They contain both N and C-terminal kleisin domains. Their N-terminal domain binds to SMC6 neck and bridges it to the SMC5 head []and to the Nse3 (another SMC5-6 complex subunit) pocket [], which seems to increased the stability of the ATP-free SMC5/6 complex. |
|
•
•
•
•
•
|
Publication |
First Author: |
Hudson JJ |
Year: |
2011 |
Journal: |
PLoS One |
Title: |
Interactions between the Nse3 and Nse4 components of the SMC5-6 complex identify evolutionarily conserved interactions between MAGE and EID Families. |
Volume: |
6 |
Issue: |
2 |
Pages: |
e17270 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
723
|
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Båvner A |
Year: |
2005 |
Journal: |
Nucleic Acids Res |
Title: |
EID3 is a novel EID family member and an inhibitor of CBP-dependent co-activation. |
Volume: |
33 |
Issue: |
11 |
Pages: |
3561-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Guerineau M |
Year: |
2012 |
Journal: |
PLoS One |
Title: |
Analysis of the Nse3/MAGE-binding domain of the Nse4/EID family proteins. |
Volume: |
7 |
Issue: |
4 |
Pages: |
e35813 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1217
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1286
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1216
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1216
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1261
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1217
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
247
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
273
|
Fragment?: |
false |
|
•
•
•
•
•
|