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Search results 101 to 156 out of 156 for Smc6

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0.019s

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Type Details Score
Protein
Q3TST9
Organism: Mus musculus/domesticus
Length: 681  
Fragment?: true
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Protein
E9Q839
Organism: Mus musculus/domesticus
Length: 1163  
Fragment?: false
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Protein
E9PXB2
Organism: Mus musculus/domesticus
Length: 523  
Fragment?: false
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Protein
A0A494BB77
Organism: Mus musculus/domesticus
Length: 546  
Fragment?: false
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Protein
B7ZWK5
Organism: Mus musculus/domesticus
Length: 1140  
Fragment?: false
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Protein
A0A0A6YWQ3
Organism: Mus musculus/domesticus
Length: 140  
Fragment?: true
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Protein
A0A494BB73
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: false
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Protein
A0A0A6YWE8
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: true
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Protein
E9PUL8
Organism: Mus musculus/domesticus
Length: 379  
Fragment?: false
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Protein
B2RXQ3
Organism: Mus musculus/domesticus
Length: 1163  
Fragment?: false
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Publication
32389690 | -
First Author: Adamus M
Year: 2020
Journal: J Mol Biol
Title: Molecular Insights into the Architecture of the Human SMC5/6 Complex.
Volume: 432
Issue: 13
Pages: 3820-3837
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Publication
24207055 | -
First Author: Yan S
Year: 2013
Journal: Mol Cell
Title: Salicylic acid activates DNA damage responses to potentiate plant immunity.
Volume: 52
Issue: 4
Pages: 602-10
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Publication
17005570 | -
First Author: Palecek J
Year: 2006
Journal: J Biol Chem
Title: The Smc5-Smc6 DNA repair complex. bridging of the Smc5-Smc6 heads by the KLEISIN, Nse4, and non-Kleisin subunits.
Volume: 281
Issue: 48
Pages: 36952-9
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Protein Domain
IPR014854 | Nse4_C
Type: Domain
Description: Nse4 is the kleisin component of the Smc5/6 DNA repair complex. It bridges the heads of Smc5 and Smc6 []. This entry represents the highly conserved C-terminal domain which interacts with the head domain of Smc5 [].
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Protein Domain
IPR041741 | SMC3_ABC_euk
Type: Domain
Description: The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'WalkerA' nucleotide-binding domain (GxxGxGKS/T), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 [].This entry represents the ATP-binding cassette domain of eukaryotic SMC3 proteins, which is found at the N terminus.
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Protein Domain
IPR041738 | SMC4_ABC_euk
Type: Domain
Description: The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 [].This entry represents the ATP-binding cassette domain of eukaryotic SMC4 proteins.
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Publication
23843628 | J:210407
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
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Publication
15601841 | -
First Author: Andrews EA
Year: 2005
Journal: Mol Cell Biol
Title: Nse2, a component of the Smc5-6 complex, is a SUMO ligase required for the response to DNA damage.
Volume: 25
Issue: 1
Pages: 185-96
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Publication
16055714 | -
First Author: Potts PR
Year: 2005
Journal: Mol Cell Biol
Title: Human MMS21/NSE2 is a SUMO ligase required for DNA repair.
Volume: 25
Issue: 16
Pages: 7021-32
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Publication
19682286 | -
First Author: Huang L
Year: 2009
Journal: Plant J
Title: The Arabidopsis SUMO E3 ligase AtMMS21, a homologue of NSE2/MMS21, regulates cell proliferation in the root.
Volume: 60
Issue: 4
Pages: 666-78
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Publication
22921571 | -
First Author: Kliszczak M
Year: 2012
Journal: DNA Repair (Amst)
Title: SUMO ligase activity of vertebrate Mms21/Nse2 is required for efficient DNA repair but not for Smc5/6 complex stability.
Volume: 11
Issue: 10
Pages: 799-810
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Publication
21550342 | -
First Author: Stephan AK
Year: 2011
Journal: FEBS Lett
Title: The Nse2/Mms21 SUMO ligase of the Smc5/6 complex in the maintenance of genome stability.
Volume: 585
Issue: 18
Pages: 2907-13
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Publication
10747036 | -
First Author: Fousteri MI
Year: 2000
Journal: EMBO J
Title: A novel SMC protein complex in Schizosaccharomyces pombe contains the Rad18 DNA repair protein.
Volume: 19
Issue: 7
Pages: 1691-702
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Protein Domain
IPR026846 | Nse2(Mms21)
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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Protein Domain
IPR027131 | SMC5
Type: Family
Description: SMC5 is a core component of the SMC5-SMC6 complex [, ], a complex involved in repair of DNA double-strand breaks by homologous recombination [, ]. In humans, the SMC5-SMC6 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 in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs) []. SMC5 is required for sister chromatid cohesion during prometaphase and mitotic progression; the function seems to be independent of SMC6 [].
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Protein
Q5EBG4
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: true
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Publication
19502785 | -
First Author: Behlke-Steinert S
Year: 2009
Journal: Cell Cycle
Title: SMC5 and MMS21 are required for chromosome cohesion and mitotic progression.
Volume: 8
Issue: 14
Pages: 2211-8
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Protein
Q3V124
Organism: Mus musculus/domesticus
Length: 375  
Fragment?: false
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Protein
G3XA30
Organism: Mus musculus/domesticus
Length: 381  
Fragment?: false
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Protein
Q3UZJ7
Organism: Mus musculus/domesticus
Length: 451  
Fragment?: true
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Protein
Q3TPG9
Organism: Mus musculus/domesticus
Length: 353  
Fragment?: true
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Protein
Q3US85
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: true
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Protein
Q3TMK9
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: true
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Protein
Q3U763
Organism: Mus musculus/domesticus
Length: 337  
Fragment?: true
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Publication
15752197 | -
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
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Publication
20571088 | -
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
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Publication
32546830 | -
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
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Publication
12966087 | -
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
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Publication
15331764 | -
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
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Publication
11864377 | -
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
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Protein Domain
IPR029225 | Nse4_Nse3-bd
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
IPR027786 | Nse4/EID
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.
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Publication
21364888 | -
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
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Protein
Q3UNU2
Organism: Mus musculus/domesticus
Length: 723  
Fragment?: true
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Publication
15987788 | -
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
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Publication
22536443 | -
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
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Protein
Q8CG46
Organism: Mus musculus/domesticus
Length: 1101  
Fragment?: false
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Protein
A0A286YDG5
Organism: Mus musculus/domesticus
Length: 1011  
Fragment?: false
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Protein
Q9CW03
Organism: Mus musculus/domesticus
Length: 1217  
Fragment?: false
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Protein
Q8CG47
Organism: Mus musculus/domesticus
Length: 1286  
Fragment?: false
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Protein
Q6P5E5
Organism: Mus musculus/domesticus
Length: 1216  
Fragment?: false
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Protein
Q6P7V9
Organism: Mus musculus/domesticus
Length: 1216  
Fragment?: false
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Protein
E9Q2X6
Organism: Mus musculus/domesticus
Length: 1261  
Fragment?: false
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Protein
Q1HL32
Organism: Mus musculus/domesticus
Length: 1217  
Fragment?: false
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Protein
Q91VT1
Organism: Mus musculus/domesticus
Length: 247  
Fragment?: false
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Protein
A0A2I3BS18
Organism: Mus musculus/domesticus
Length: 273  
Fragment?: false
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom