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Search results 601 to 686 out of 686 for Sumo1

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Type Details Score
Publication
14596924 | J:86405
First Author: Duval D
Year: 2003
Journal: FEBS Lett
Title: The 'PINIT' motif, of a newly identified conserved domain of the PIAS protein family, is essential for nuclear retention of PIAS3L.
Volume: 554
Issue: 1-2
Pages: 111-8
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Protein Domain
IPR019956 | Ubiquitin_dom
Type: Domain
Description: Ubiquitinylation is an ATP-dependent process that involves the action of at least three enzymes: a ubiquitin-activating enzyme (E1, ), a ubiquitin-conjugating enzyme (E2, ), and a ubiquitin ligase (E3, , ), which work sequentially in a cascade. There are many different E3 ligases, which are responsible for the type of ubiquitin chain formed, the specificity of the target protein, and the regulation of the ubiquitinylation process []. Ubiquitinylation is an important regulatory tool that controls the concentration of key signalling proteins, such as those involved in cell cycle control, as well as removing misfolded, damaged or mutant proteins that could be harmful to the cell. Several ubiquitin-like molecules have been discovered, such as Ufm1 (), SUMO1 (), NEDD8, Rad23 (), Elongin B and Parkin (), the latter being involved in Parkinson's disease [].Ubiquitin is a protein of 76 amino acid residues, found in all eukaryotic cells and whose sequence is extremely well conserved from protozoan to vertebrates. Ubiquitin acts through its post-translational attachment (ubiquitinylation) to other proteins, where these modifications alter the function, location or trafficking of the protein, or targets it for destruction by the 26S proteasome []. The terminal glycine in the C-terminal 4-residue tail of ubiquitin can form an isopeptide bond with a lysine residue in the target protein, or with a lysine in another ubiquitin molecule to form a ubiquitin chain that attaches itself to a target protein. Ubiquitin has seven lysine residues, any one of which can be used to link ubiquitin molecules together, resulting in different structures that alter the target protein in different ways. It appears that Lys(11)-, Lys(29) and Lys(48)-linked poly-ubiquitin chains target the protein to the proteasome for degradation, while mono-ubiquitinylatedand Lys(6)- or Lys(63)-linked poly-ubiquitin chains signal reversible modifications in protein activity, location or trafficking []. For example, Lys(63)-linked poly-ubiquitinylation is known to be involved in DNA damage tolerance, inflammatory response, protein trafficking and signal transduction through kinase activation []. In addition, the length of the ubiquitin chain alters the fate of the target protein. Regulatory proteins such as transcription factors and histones are frequent targets of ubquitinylation [].
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Protein Domain
IPR019954 | Ubiquitin_CS
Type: Conserved_site
Description: Ubiquitinylation is an ATP-dependent process that involves the action of at least three enzymes: a ubiquitin-activating enzyme (E1, ), a ubiquitin-conjugating enzyme (E2, ), and a ubiquitin ligase (E3, , ), which work sequentially in a cascade. There are many different E3 ligases, which are responsible for the type of ubiquitin chain formed, the specificity of the target protein, and the regulation of the ubiquitinylation process []. Ubiquitinylation is an important regulatory tool that controls the concentration of key signalling proteins, such as those involved in cell cycle control, as well as removing misfolded, damaged or mutant proteins that could be harmful to the cell. Several ubiquitin-like molecules have been discovered, such as Ufm1 (), SUMO1 (), NEDD8, Rad23 (), Elongin B and Parkin (), the latter being involved in Parkinson's disease [].Ubiquitin is a protein of 76 amino acid residues, found in all eukaryotic cells and whose sequence is extremely well conserved from protozoan to vertebrates. Ubiquitin acts through its post-translational attachment (ubiquitinylation) to other proteins, where these modifications alter the function, location or trafficking of the protein, or targets it for destruction by the 26S proteasome []. The terminal glycine in the C-terminal 4-residue tail of ubiquitin can form an isopeptide bond with a lysine residue in the target protein, or with a lysine in another ubiquitin molecule to form a ubiquitin chain that attaches itself to a target protein. Ubiquitin has seven lysine residues, any one of which can be used to link ubiquitin molecules together, resulting in different structures that alter the target protein in different ways. It appears that Lys(11)-, Lys(29) and Lys(48)-linked poly-ubiquitin chains target the protein to the proteasome for degradation, while mono-ubiquitinylated and Lys(6)- or Lys(63)-linked poly-ubiquitin chains signal reversible modifications in protein activity, location or trafficking []. For example, Lys(63)-linked poly-ubiquitinylation is known to be involved in DNA damage tolerance, inflammatory response, protein trafficking and signal transduction through kinase activation []. In addition, the length of the ubiquitin chain alters the fate of the target protein. Regulatory proteins such as transcription factors and histones are frequent targets of ubquitinylation [].This entry represents the conserved region at the centre of the Ubiquitin sequence.
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Publication
15525528 | J:94519
First Author: de Napoles M
Year: 2004
Journal: Dev Cell
Title: Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation.
Volume: 7
Issue: 5
Pages: 663-76
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Protein
P0CG50
Organism: Mus musculus/domesticus
Length: 734  
Fragment?: false
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Protein
P0CG49
Organism: Mus musculus/domesticus
Length: 305  
Fragment?: false
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Protein
Q8R0Z9
Organism: Mus musculus/domesticus
Length: 354  
Fragment?: false
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Protein
Q78XY9
Organism: Mus musculus/domesticus
Length: 305  
Fragment?: false
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Protein
Q3TH47
Organism: Mus musculus/domesticus
Length: 278  
Fragment?: false
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Protein
A0A0A6YW67
Organism: Mus musculus/domesticus
Length: 77  
Fragment?: false
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Protein
Q922Z8
Organism: Mus musculus/domesticus
Length: 582  
Fragment?: false
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Protein
E9Q5F6
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: true
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Protein
Q922B0
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: false
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Protein
Q8C2K3
Organism: Mus musculus/domesticus
Length: 153  
Fragment?: false
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Protein
B0LAC2
Organism: Mus musculus/domesticus
Length: 71  
Fragment?: true
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Protein
Q8VC46
Organism: Mus musculus/domesticus
Length: 658  
Fragment?: false
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Protein
A5JUZ1
Organism: Mus musculus/domesticus
Length: 76  
Fragment?: true
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Protein
Q5SX22
Organism: Mus musculus/domesticus
Length: 236  
Fragment?: true
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Protein
E9Q4P0
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: true
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Protein
P63166
Organism: Mus musculus/domesticus
Length: 101  
Fragment?: false
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Protein
Q78JW9
Organism: Mus musculus/domesticus
Length: 368  
Fragment?: false
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Protein
A0A1Y7VIN5
Organism: Mus musculus/domesticus
Length: 232  
Fragment?: false
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Protein
Q9CYA9
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
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Protein
G3UYZ0
Organism: Mus musculus/domesticus
Length: 209  
Fragment?: true
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Protein
S4R183
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: true
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Protein
G3V013
Organism: Mus musculus/domesticus
Length: 253  
Fragment?: true
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Publication
15660128 | -
First Author: Lois LM
Year: 2005
Journal: EMBO J
Title: Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1.
Volume: 24
Issue: 3
Pages: 439-51
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Protein
P29595
Organism: Mus musculus/domesticus
Length: 81  
Fragment?: false
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Protein
P35545
Organism: Mus musculus/domesticus
Length: 74  
Fragment?: false
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Protein
P21126
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: false
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Protein
B2M0S0
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: false
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Protein
Q3UI46
Organism: Mus musculus/domesticus
Length: 81  
Fragment?: false
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Protein
B2M0R9
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: false
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Protein
Q3TY05
Organism: Mus musculus/domesticus
Length: 68  
Fragment?: true
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Protein
Q684Q9
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: true
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Protein
Q91V47
Organism: Mus musculus/domesticus
Length: 152  
Fragment?: true
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Protein
Q3UK94
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: false
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Publication
15556404 | -
First Author: Pickart CM
Year: 2004
Journal: Curr Opin Chem Biol
Title: Polyubiquitin chains: polymeric protein signals.
Volume: 8
Issue: 6
Pages: 610-6
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Protein
P62984
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: false
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Protein
E9QNP0
Organism: Mus musculus/domesticus
Length: 232  
Fragment?: false
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Protein
Q642K5
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: false
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Protein
Q5M9K3
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: false
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Protein
E9Q9J0
Organism: Mus musculus/domesticus
Length: 96  
Fragment?: true
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Protein
Q920W8
Organism: Mus musculus/domesticus
Length: 137  
Fragment?: true
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Protein
Q91V99
Organism: Mus musculus/domesticus
Length: 137  
Fragment?: true
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Publication
15454246 | -
First Author: Burger AM
Year: 2004
Journal: Eur J Cancer
Title: The ubiquitin-mediated protein degradation pathway in cancer: therapeutic implications.
Volume: 40
Issue: 15
Pages: 2217-29
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Publication
14998368 | -
First Author: Passmore LA
Year: 2004
Journal: Biochem J
Title: Getting into position: the catalytic mechanisms of protein ubiquitylation.
Volume: 379
Issue: Pt 3
Pages: 513-25
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Protein
Q9Z1R2
Organism: Mus musculus/domesticus
Length: 1154  
Fragment?: false
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Protein
Q91WB7
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
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Protein
P63072
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
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Protein
Q9CQ84
Organism: Mus musculus/domesticus
Length: 188  
Fragment?: false
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Protein
E9Q5Y5
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: true
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Protein
H3BJ41
Organism: Mus musculus/domesticus
Length: 52  
Fragment?: false
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Protein
E0CZH5
Organism: Mus musculus/domesticus
Length: 90  
Fragment?: true
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Protein
Q3UYT2
Organism: Mus musculus/domesticus
Length: 385  
Fragment?: true
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Protein
G3UYQ2
Organism: Mus musculus/domesticus
Length: 1082  
Fragment?: false
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Protein
G3UXT8
Organism: Mus musculus/domesticus
Length: 563  
Fragment?: true
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Protein
Q8HWH4
Organism: Mus musculus/domesticus
Length: 522  
Fragment?: true
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Protein
A0A1B0GX81
Organism: Mus musculus/domesticus
Length: 1107  
Fragment?: true
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Protein
Q3THB2
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: false
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Protein
G3UZT6
Organism: Mus musculus/domesticus
Length: 1122  
Fragment?: false
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Protein
Q3TDL4
Organism: Mus musculus/domesticus
Length: 1108  
Fragment?: true
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Protein
Q3UF95
Organism: Mus musculus/domesticus
Length: 1136  
Fragment?: false
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Publication
19334288 | J:148410
First Author: Combes AN
Year: 2009
Journal: Dev Dyn
Title: Three-dimensional visualization of testis cord morphogenesis, a novel tubulogenic mechanism in development.
Volume: 238
Issue: 5
Pages: 1033-41
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Protein
P62983
Organism: Mus musculus/domesticus
Length: 156  
Fragment?: false
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Protein
Q642L7
Organism: Mus musculus/domesticus
Length: 156  
Fragment?: false
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Protein
O54714
Organism: Mus musculus/domesticus
Length: 628  
Fragment?: false
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Protein
D3Z3C6
Organism: Mus musculus/domesticus
Length: 739  
Fragment?: false
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Protein
E0CZ31
Organism: Mus musculus/domesticus
Length: 430  
Fragment?: false
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Protein
K3W4R9
Organism: Mus musculus/domesticus
Length: 758  
Fragment?: false
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Protein
Q8VC56
Organism: Mus musculus/domesticus
Length: 488  
Fragment?: false
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Protein
Q9JMA1
Organism: Mus musculus/domesticus
Length: 493  
Fragment?: false
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Protein
Q6A027
Organism: Mus musculus/domesticus
Length: 749  
Fragment?: true
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Protein
E9PYI8
Organism: Mus musculus/domesticus
Length: 458  
Fragment?: false
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Protein
E0CXC2
Organism: Mus musculus/domesticus
Length: 719  
Fragment?: false
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Protein
Q80UN0
Organism: Mus musculus/domesticus
Length: 458  
Fragment?: false
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Publication
- | J:188991
     
First Author: The Jackson Laboratory
Year: 2012
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by The Jackson Laboratory
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Publication
- | J:24194
     
First Author: The Jackson Laboratory Backcross DNA Panel Mapping Resource
Year: 1999
Journal: Database Release
Title: JAX BSS Panel Mapping Data
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Publication
- | J:342601
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniPathway vocabulary mapping
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Publication
- | J:342607
       
First Author: Birgit Meldal and Sandra Orchard (1). (1) European Bioinformatics Institute (EBI), Hinxton, Cambridgeshire, United Kingdom
Year: 2023
Title: Manual transfer of experimentally-verified manual GO annotation data to homologous complexes by curator judgment of sequence, composition and function similarity
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Publication
- | J:66660
       
First Author: Mouse Genome Database and National Center for Biotechnology Information Editorial Staff Collaboration
Year: 2001
Title: LocusLink Collaboration
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Publication
- | J:68100
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: RIKEN Data Curation in Mouse Genome Informatics
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Publication
10725249 | J:60984
First Author: Ko MS
Year: 2000
Journal: Development
Title: Large-scale cDNA analysis reveals phased gene expression patterns during preimplantation mouse development.
Volume: 127
Issue: 8
Pages: 1737-49
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Publication
- | J:171409
     
First Author: GUDMAP Consortium
Year: 2004
Journal: www.gudmap.org
Title: GUDMAP: the GenitoUrinary Development Molecular Anatomy Project
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Publication
- | J:85000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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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

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Cambridge CB2 3EH, United Kingdom