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Search results 301 to 400 out of 401 for Rad21

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Type Details Score
Allele
Rad21<Gt(OST119108)Lex> | MGI:4191546
 
Name: RAD21 cohesin complex component; gene trap OST119108, Lexicon Genetics
Allele Type: Gene trapped
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Publication
21589869 | -
First Author: Nitzsche A
Year: 2011
Journal: PLoS One
Title: RAD21 cooperates with pluripotency transcription factors in the maintenance of embryonic stem cell identity.
Volume: 6
Issue: 5
Pages: e19470
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Allele
Col1a1<tm1(tetO-GFP/RNAi:Rad21)Iaai> | MGI:5911564
Name: collagen, type I, alpha 1; targeted mutation 1, Iannis Aifantis
Allele Type: Targeted
Attribute String: Inducible, Knockdown, Reporter
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Allele
Rad21<Gt(D005E04)Wrst> | MGI:3888117
 
Name: RAD21 cohesin complex component; gene trap D005E04, German Gene Trap Consortium
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST14203H7)Tigm> | MGI:5213402
 
Name: RAD21 cohesin complex component; gene trap IST14203H7, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST13450D11)Tigm> | MGI:5172631
 
Name: RAD21 cohesin complex component; gene trap IST13450D11, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(PST23861)Mfgc> | MGI:3903936
 
Name: RAD21 cohesin complex component; gene trap PST23861, Mammalian Functional Genomics Centre
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST13701D5)Tigm> | MGI:5190375
 
Name: RAD21 cohesin complex component; gene trap IST13701D5, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST14184H9)Tigm> | MGI:5215850
 
Name: RAD21 cohesin complex component; gene trap IST14184H9, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST14393A8)Tigm> | MGI:5230540
 
Name: RAD21 cohesin complex component; gene trap IST14393A8, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(P127D08)Wrst> | MGI:3897951
 
Name: RAD21 cohesin complex component; gene trap P127D08, German Gene Trap Consortium
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST10838G4)Tigm> | MGI:3969950
 
Name: RAD21 cohesin complex component; gene trap IST10838G4, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST13543E5)Tigm> | MGI:5175646
 
Name: RAD21 cohesin complex component; gene trap IST13543E5, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(D045A06)Wrst> | MGI:3889047
 
Name: RAD21 cohesin complex component; gene trap D045A06, German Gene Trap Consortium
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST13611G7)Tigm> | MGI:5175840
 
Name: RAD21 cohesin complex component; gene trap IST13611G7, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(D105H02)Wrst> | MGI:3890796
 
Name: RAD21 cohesin complex component; gene trap D105H02, German Gene Trap Consortium
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST14563D8)Tigm> | MGI:5238464
 
Name: RAD21 cohesin complex component; gene trap IST14563D8, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST14579E11)Tigm> | MGI:5242328
 
Name: RAD21 cohesin complex component; gene trap IST14579E11, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST14664D3)Tigm> | MGI:5249600
 
Name: RAD21 cohesin complex component; gene trap IST14664D3, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST14134E3)Tigm> | MGI:5212822
 
Name: RAD21 cohesin complex component; gene trap IST14134E3, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST14658E3)Tigm> | MGI:5250866
 
Name: RAD21 cohesin complex component; gene trap IST14658E3, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(P048B07)Wrst> | MGI:4352362
 
Name: RAD21 cohesin complex component; gene trap P048B07, German Gene Trap Consortium
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST14631C11)Tigm> | MGI:5245881
 
Name: RAD21 cohesin complex component; gene trap IST14631C11, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST14772C9)Tigm> | MGI:5264304
 
Name: RAD21 cohesin complex component; gene trap IST14772C9, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(D004C08)Wrst> | MGI:3888079
 
Name: RAD21 cohesin complex component; gene trap D004C08, German Gene Trap Consortium
Allele Type: Gene trapped
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Allele
Rad21<Gt(PST2942)Mfgc> | MGI:4332522
 
Name: RAD21 cohesin complex component; gene trap PST2942, Mammalian Functional Genomics Centre
Allele Type: Gene trapped
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Allele
Rad21<Gt(EUCE0091d08)Hmgu> | MGI:4385852
 
Name: RAD21 cohesin complex component; gene trap EUCE0091d08, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
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Allele
Rad21<Gt(PST16636)Mfgc> | MGI:3901050
 
Name: RAD21 cohesin complex component; gene trap PST16636, Mammalian Functional Genomics Centre
Allele Type: Gene trapped
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Allele
Rad21<Gt(XT0787)Wtsi> | MGI:3864637
 
Name: RAD21 cohesin complex component; gene trap XT0787, Wellcome Trust Sanger Institute
Allele Type: Gene trapped
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Allele
Rad21<Gt(EUCE0274b05)Hmgu> | MGI:4381755
 
Name: RAD21 cohesin complex component; gene trap EUCE0274b05, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
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Allele
Rad21<Gt(D018C07)Wrst> | MGI:3888369
 
Name: RAD21 cohesin complex component; gene trap D018C07, German Gene Trap Consortium
Allele Type: Gene trapped
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Allele
Rad21<Gt(EUCE0073e09)Hmgu> | MGI:4378838
 
Name: RAD21 cohesin complex component; gene trap EUCE0073e09, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST13350B4)Tigm> | MGI:5160774
 
Name: RAD21 cohesin complex component; gene trap IST13350B4, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Strain
MGI:7588885 | C57BL/6J-Rad21<em2Cya>/Cya
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
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Allele
Rad21<Gt(IST10897F5)Tigm> | MGI:5145670
 
Name: RAD21 cohesin complex component; gene trap IST10897F5, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST14483A5)Tigm> | MGI:5236076
 
Name: RAD21 cohesin complex component; gene trap IST14483A5, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST13613D9)Tigm> | MGI:5175926
 
Name: RAD21 cohesin complex component; gene trap IST13613D9, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST14116G7)Tigm> | MGI:5203708
 
Name: RAD21 cohesin complex component; gene trap IST14116G7, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Allele
Rad21<Gt(IST14159G3)Tigm> | MGI:5210204
 
Name: RAD21 cohesin complex component; gene trap IST14159G3, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
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Genotype
Genotype
Symbol: Rad21/Rad21
Background: involves: 129P2/OlaHsd * C57BL/6 * CBA
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Rad21/Rad21
Background: involves: 129P2/OlaHsd * C57BL/6 * CBA
Zygosity: hm
Has Mutant Allele: true
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DO Term
DOID:0080508 | Cornelia de Lange syndrome 4
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Publication
12130806 | -
First Author: Lee J
Year: 2002
Journal: Zoolog Sci
Title: Analyses of mRNA expression patterns of cohesin subunits Rad21 and Rec8 in mice: germ cell-specific expression of rec8 mRNA in both male and female mice.
Volume: 19
Issue: 5
Pages: 539-44
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Genotype
Genotype
Symbol: Rad21/Rad21 Tg(Cd4-cre)1Cwi/?
Background: involves: 129 * C57BL/6
Zygosity: cn
Has Mutant Allele: true
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Protein Domain
IPR023093 | ScpA-like_C
Type: Homologous_superfamily
Description: This superfamily represents a conserved C-terminal region found in bacterial segregation and condensation protein A (ScpA) as well as in eukaryotic cohesins of the Rad21 and Scc1 families. ScpA participates in chromosomal partition during cell division. It may act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves.
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Genotype
Genotype
Symbol: Col1a1/Col1a1<+> Gt(ROSA)26Sor/Gt(ROSA)26Sor<+>
Background: involves: 129S4/SvJae * C57BL/6
Zygosity: cx
Has Mutant Allele: true
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HT Experiment
E-GEOD-59119 | The contribution of cohesin-SA1 to chromatin architecture and gene expression in two murine tissues [RNA-seq]
Series Id: GSE59119
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: ArrayExpress
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Publication
17205076 | J:159144
First Author: Gómez R
Year: 2007
Journal: EMBO Rep
Title: Mammalian SGO2 appears at the inner centromere domain and redistributes depending on tension across centromeres during meiosis II and mitosis.
Volume: 8
Issue: 2
Pages: 173-80
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Publication
28116354 | J:258185
First Author: Li Z
Year: 2017
Journal: Sci Adv
Title: ASXL1 interacts with the cohesin complex to maintain chromatid separation and gene expression for normal hematopoiesis.
Volume: 3
Issue: 1
Pages: e1601602
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Publication
33863876 | J:306058
First Author: Ushiki A
Year: 2021
Journal: Nat Commun
Title: Deletion of CTCF sites in the SHH locus alters enhancer-promoter interactions and leads to acheiropodia.
Volume: 12
Issue: 1
Pages: 2282
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Publication
26438359 | J:229031
First Author: Mullenders J
Year: 2015
Journal: J Exp Med
Title: Cohesin loss alters adult hematopoietic stem cell homeostasis, leading to myeloproliferative neoplasms.
Volume: 212
Issue: 11
Pages: 1833-50
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Publication
25735743 | J:231644
First Author: Cuadrado A
Year: 2015
Journal: Nucleic Acids Res
Title: The contribution of cohesin-SA1 to gene expression and chromatin architecture in two murine tissues.
Volume: 43
Issue: 6
Pages: 3056-67
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Publication
24013524 | J:344797
First Author: Gómez R
Year: 2014
Journal: Chromosoma
Title: Cohesin removal precedes topoisomerase IIα-dependent decatenation at centromeres in male mammalian meiosis II.
Volume: 123
Issue: 1-2
Pages: 129-46
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Publication
18728194 | J:139128
First Author: Zhang N
Year: 2008
Journal: Proc Natl Acad Sci U S A
Title: Overexpression of Separase induces aneuploidy and mammary tumorigenesis.
Volume: 105
Issue: 35
Pages: 13033-8
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Publication
25895170 | J:243254
First Author: Rankin S
Year: 2015
Journal: FEBS J
Title: Complex elaboration: making sense of meiotic cohesin dynamics.
Volume: 282
Issue: 13
Pages: 2426-43
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Publication
32717742 | J:297408
First Author: Ba Z
Year: 2020
Journal: Nature
Title: CTCF orchestrates long-range cohesin-driven V(D)J recombinational scanning.
Volume: 586
Issue: 7828
Pages: 305-310
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Publication
31533351 | J:303395
 
First Author: Ohneda K
Year: 2019
Journal: Int J Mol Sci
Title: Mouse Tryptase Gene Expression is Coordinately Regulated by GATA1 and GATA2 in Bone Marrow-Derived Mast Cells.
Volume: 20
Issue: 18
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HT Experiment
GSE47885 | Deep sequencing of the murine Igh repertoire reveals complex regulation of non-random V gene rearrangement frequencies (RNA-seq)
Series Id: E-GEOD-47885
Experiment Type: RNA-Seq
Study Type: WT vs. Mutant
Source: GEO
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Publication
14730319 | J:88148
First Author: Kitajima TS
Year: 2004
Journal: Nature
Title: The conserved kinetochore protein shugoshin protects centromeric cohesion during meiosis.
Volume: 427
Issue: 6974
Pages: 510-7
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Publication
18987869 | -
First Author: Rivera T
Year: 2009
Journal: Chromosoma
Title: Shugoshin regulates cohesion by driving relocalization of PP2A in Xenopus extracts.
Volume: 118
Issue: 2
Pages: 223-33
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Publication
16687935 | -
First Author: Suzuki H
Year: 2006
Journal: Cell Cycle
Title: Human Shugoshin mediates kinetochore-driven formation of kinetochore microtubules.
Volume: 5
Issue: 10
Pages: 1094-101
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Publication
17322402 | -
First Author: Kawashima SA
Year: 2007
Journal: Genes Dev
Title: Shugoshin enables tension-generating attachment of kinetochores by loading Aurora to centromeres.
Volume: 21
Issue: 4
Pages: 420-35
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Publication
11877377 | -
First Author: Yazdi PT
Year: 2002
Journal: Genes Dev
Title: SMC1 is a downstream effector in the ATM/NBS1 branch of the human S-phase checkpoint.
Volume: 16
Issue: 5
Pages: 571-82
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Publication
24756084 | -
First Author: Parenti I
Year: 2014
Journal: Epigenetics
Title: Overall and allele-specific expression of the SMC1A gene in female Cornelia de Lange syndrome patients and healthy controls.
Volume: 9
Issue: 7
Pages: 973-9
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Publication
18996922 | -
First Author: Revenkova E
Year: 2009
Journal: Hum Mol Genet
Title: Cornelia de Lange syndrome mutations in SMC1A or SMC3 affect binding to DNA.
Volume: 18
Issue: 3
Pages: 418-27
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Publication
22885700 | -
First Author: Deardorff MA
Year: 2012
Journal: Nature
Title: HDAC8 mutations in Cornelia de Lange syndrome affect the cohesin acetylation cycle.
Volume: 489
Issue: 7415
Pages: 313-7
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Publication
23106691 | -
First Author: Gimigliano A
Year: 2012
Journal: J Proteome Res
Title: Proteomic profile identifies dysregulated pathways in Cornelia de Lange syndrome cells with distinct mutations in SMC1A and SMC3 genes.
Volume: 11
Issue: 12
Pages: 6111-23
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Publication
8392064 | -
First Author: Jessberger R
Year: 1993
Journal: J Biol Chem
Title: A mammalian protein complex that repairs double-strand breaks and deletions by recombination.
Volume: 268
Issue: 20
Pages: 15070-9
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Publication
28301465 | -
First Author: Chao LF
Year: 2017
Journal: PLoS Genet
Title: An SMC-like protein binds and regulates Caenorhabditis elegans condensins.
Volume: 13
Issue: 3
Pages: e1006614
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Protein Domain
IPR029683 | SMC1A_metazoan
Type: Family
Description: Structural maintenance of chromosomes protein 1A (SMC1A) is a homologue of the yeast Smc1 protein, which is a component of the cohesin complex required for sister chromatid cohesion []. In human, it is part of the core cohesion complex composed of SMC1A, SMC3, RAD21 and STAG proteins []. These proteins form a ring structure that encircles sister chromatids to mediate sister chromatid cohesion []. SMC1A binds to SMC3 through its hinge domain []. Besides sister chromatid cohesion function, SMC1A-SMC3 heterodimer can also found in the RC-1 complex, a mammalian protein complex that promotes repair of DNA gaps and deletions through recombination [, ]. This entry also includes Smc1 homologue from Caenorhabditis elegans, SMCL-1. Unlike canonical SMC proteins, SMCL-1 lacks hinge and coil domains, and its ATPase domain lacks conserved amino acids required for ATP hydrolysis []. Mutations in SMC1A gene cause Cornelia de Lange syndrome 2 (CDLS2), which is a form of Cornelia de Lange syndrome, a clinically heterogeneous developmental disorder associated with malformations affecting multiple systems [, ].
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Protein Domain
IPR011515 | Shugoshin_C
Type: Domain
Description: This entry represents the C-terminal domain of Shugoshin (Sgo1) kinetochore-attachment proteins. Shugoshin has a conserved coiled-coil N-terminal domain and a highly conserved C-terminal basic region (). Shugoshin is a crucial target of Bub1 kinase that plays a central role in chromosome cohesion during mitosis and meiosis divisions by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms [, ]. Shugoshin is thought to act by protecting Rec8 and Rad21 at the centromeres from separase degradation during anaphase I (during meiosis) so that sister chromatids remain tethered []. Shugoshin also acts as a spindle checkpoint component required for sensing tension between sister chromatids during mitosis, its degradation when they separate preventing cell cycle arrest and chromosome loss in anaphase, a time when sister chromatids are no longer under tension. Human shugoshin is diffusible and mediates kinetochore-driven formation of kinetochore-microtubules during bipolar spindle assembly []. Further, the primary role of shugoshin is to ensure bipolar attachment of kinetochores, and its role in protecting cohesion has co-developed to facilitate this process [].
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Protein Domain
IPR011516 | Shugoshin_N
Type: Domain
Description: This entry represents the N-terminal domain of Shugoshin (Sgo1) kinetochore-attachment proteins. Shugoshin has this conserved coiled-coil N-terminal domain and a highly conserved C-terminal basic region ().Shugoshin is a crucial target of Bub1 kinase that plays a central role in chromosome cohesion during mitosis and meiosis divisions by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms [, ]. Shugoshin is thought to act by protecting Rec8 and Rad21 at the centromeres from separase degradation during anaphase I (during meiosis) so that sister chromatids remain tethered []. Shugoshin also acts as a spindle checkpoint component required for sensing tension between sister chromatids during mitosis, its degradation when they separate preventing cell cycle arrest and chromosome loss in anaphase, a time when sister chromatids are no longer under tension. Human shugoshin is diffusible and mediates kinetochore-driven formation of kinetochore-microtubules during bipolar spindle assembly []. Further, the primary role of shugoshin is to ensure bipolar attachment of kinetochores, and its role in protecting cohesion has co-developed to facilitate this process [].
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Publication
12759374 | J:84400
First Author: Lee J
Year: 2003
Journal: J Cell Sci
Title: Temporally and spatially selective loss of Rec8 protein from meiotic chromosomes during mammalian meiosis.
Volume: 116
Issue: Pt 13
Pages: 2781-90
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Publication
21606361 | J:173337
First Author: Degner SC
Year: 2011
Journal: Proc Natl Acad Sci U S A
Title: CCCTC-binding factor (CTCF) and cohesin influence the genomic architecture of the Igh locus and antisense transcription in pro-B cells.
Volume: 108
Issue: 23
Pages: 9566-71
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Protein
Q9CXH7
Organism: Mus musculus/domesticus
Length: 517  
Fragment?: false
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Protein
Q6ZQJ6
Organism: Mus musculus/domesticus
Length: 426  
Fragment?: true
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Publication
11471062 | J:70827
First Author: Ehringer MA
Year: 2001
Journal: Mamm Genome
Title: High-throughput sequence identification of gene coding variants within alcohol-related QTLs.
Volume: 12
Issue: 8
Pages: 657-63
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Protein
A2AU37
Organism: Mus musculus/domesticus
Length: 552  
Fragment?: false
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Protein
Q8C5S7
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
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Protein
Q3TG35
Organism: Mus musculus/domesticus
Length: 635  
Fragment?: false
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Protein
Q3UTE4
Organism: Mus musculus/domesticus
Length: 601  
Fragment?: true
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Protein
R4GML2
Organism: Mus musculus/domesticus
Length: 549  
Fragment?: false
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Protein
Q6A0B0
Organism: Mus musculus/domesticus
Length: 236  
Fragment?: true
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Protein
Q7TNG4
Organism: Mus musculus/domesticus
Length: 362  
Fragment?: true
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Protein
Q6PIE1
Organism: Mus musculus/domesticus
Length: 831  
Fragment?: true
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Protein
A0JLM6
Organism: Mus musculus/domesticus
Length: 679  
Fragment?: true
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Protein
P60330
Organism: Mus musculus/domesticus
Length: 2118  
Fragment?: false
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Protein
Q9CU62
Organism: Mus musculus/domesticus
Length: 1233  
Fragment?: false
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Protein
A6H6E1
Organism: Mus musculus/domesticus
Length: 2118  
Fragment?: false
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Protein
Q0VGV2
Organism: Mus musculus/domesticus
Length: 2118  
Fragment?: false
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Protein
Q56TS3
Organism: Mus musculus/domesticus
Length: 2118  
Fragment?: false
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Protein
A0A2R8VI27
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: true
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Protein Domain
IPR005314 | Peptidase_C50
Type: Family
Description: This group of cysteine peptidases belong to MEROPS peptidase family C50 (separase family, clan CD). The active site residues for members of this family and family C14 occur in the same order in the sequence: H,C.The separases are caspase-like proteases, which plays a central role in the chromosome segregation. In yeast they cleave the rad21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, separase is inactivated by the securin/cut2 protein, which probably covers its active site. A cysteine peptidase is a proteolytic enzyme that hydrolyses a peptide bond using the thiol group of a cysteine residue as a nucleophile. Hydrolysis involves usually a catalytic triad consisting of the thiol group of the cysteine, the imidazolium ring of a histidine, and a third residue, usually asparagine or aspartic acid, to orientate and activate the imidazolium ring. In only one family of cysteine peptidases, is the role of the general base assigned to a residue other than a histidine: in peptidases from family C89 (acid ceramidase) an arginine is the general base. Cysteine peptidases can be grouped into fourteen different clans, with members of each clan possessing a tertiary fold unique to the clan. Four clans of cysteine peptidases share structural similarities with serine and threonine peptidases and asparagine lyases. From sequence similarities, cysteine peptidases can be clustered into over 80 different families []. Clans CF, CM, CN, CO, CP and PD contain only one family.Cysteine peptidases are often active at acidic pH and are therefore confined to acidic environments, such as the animal lysosome or plant vacuole. Cysteine peptidases can be endopeptidases, aminopeptidases, carboxypeptidases, dipeptidyl-peptidases or omega-peptidases. They are inhibited by thiol chelators such as iodoacetate, iodoacetic acid, N-ethylmaleimide or p-chloromercuribenzoate.Clan CA includes proteins with a papain-like fold. There is a catalytic triad which occurs in the order: Cys/His/Asn (or Asp). A fourth residue, usually Gln, is important for stabilising the acyl intermediate that forms during catalysis, and this precedes the active site Cys. The fold consists of two subdomains with the active site between them. One subdomain consists of a bundle of helices, with the catalytic Cys at the end of one of them, and the other subdomain is a β-barrel with the active site His and Asn (or Asp). There are over thirty families in the clan, and tertiary structures have been solved for members of most of these. Peptidases in clan CA are usually sensitive to the small molecule inhibitor E64, which is ineffective against peptidases from other clans of cysteine peptidases [].Clan CD includes proteins with a caspase-like fold. Proteins in the clan have an α/β/α sandwich structure. There is a catalytic dyad which occurs in the order His/Cys. The active site His occurs in a His-Gly motif and the active site Cys occurs in an Ala-Cys motif; both motifs are preceded by a block of hydrophobic residues []. Specificity is predominantly directed towards residues that occupy the S1 binding pocket, so that caspases cleave aspartyl bonds, legumains cleave asparaginyl bonds, and gingipains cleave lysyl or arginyl bonds.Clan CE includes proteins with an adenain-like fold. The fold consists of two subdomains with the active site between them. One domain is a bundle of helices, and the other a β-barrell. The subdomains are in the opposite order to those found in peptidases from clan CA, and this is reflected in the order of active site residues: His/Asn/Gln/Cys. This has prompted speculation that proteins in clans CA and CE are related, and that members of one clan are derived from a circular permutation of the structure of the other.Clan CL includes proteins with a sortase B-like fold. Peptidases in the clan hydrolyse and transfer bacterial cell wall peptides. The fold shows a closed β-barrel decorated with helices with the active site at one end of the barrel []. The active site consists of a His/Cys catalytic dyad.Cysteine peptidases with a chymotrypsin-like fold are included in clan PA, which also includes serine peptidases. Cysteine peptidases that are N-terminal nucleophile hydrolases are included in clan PB. Cysteine peptidases with a tertiary structure similar to that of the serine-type aspartyl dipeptidase are included in clan PC. Cysteine peptidases with an intein-like fold are included in clan PD, which also includes asparagine lyases.
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Publication
16452087 | J:263376
First Author: Trinidad JC
Year: 2006
Journal: Mol Cell Proteomics
Title: Comprehensive identification of phosphorylation sites in postsynaptic density preparations.
Volume: 5
Issue: 5
Pages: 914-22
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Publication
9891971 | -
First Author: Chen JM
Year: 1998
Journal: FEBS Lett
Title: Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases.
Volume: 441
Issue: 3
Pages: 361-5
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Publication
14725770 | -
First Author: Zong Y
Year: 2004
Journal: Structure
Title: The structure of sortase B, a cysteine transpeptidase that tethers surface protein to the Staphylococcus aureus cell wall.
Volume: 12
Issue: 1
Pages: 105-12
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Publication
7044372 | -
First Author: Barrett AJ
Year: 1982
Journal: Biochem J
Title: L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L.
Volume: 201
Issue: 1
Pages: 189-98
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Publication
11517925 | -
First Author: Barrett AJ
Year: 2001
Journal: Biol Chem
Title: Evolutionary lines of cysteine peptidases.
Volume: 382
Issue: 5
Pages: 727-33
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Publication
15489334 | -
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
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Publication
21183079 | J:292518
First Author: Huttlin EL
Year: 2010
Journal: Cell
Title: A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume: 143
Issue: 7
Pages: 1174-89
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