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Search results 101 to 146 out of 146 for Hjurp

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Type Details Score
Allele
Name: transgene insertion M8, David McKemy
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
Publication  
First Author: ZasadziƄska E
Year: 2017
Journal: Prog Mol Subcell Biol
Title: Orchestrating the Specific Assembly of Centromeric Nucleosomes.
Volume: 56
Pages: 165-192
Publication
First Author: Hori T
Year: 2020
Journal: Cell Rep
Title: Essentiality of CENP-A Depends on Its Binding Mode to HJURP.
Volume: 33
Issue: 7
Pages: 108388
Publication
First Author: Zhou Z
Year: 2011
Journal: Nature
Title: Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3.
Volume: 472
Issue: 7342
Pages: 234-7
Protein Domain
Type: Domain
Description: This entry represents a central, conserved region found in Holliday junction recognition protein from humans (HJURP) and similar proteins from vertebrates. This domain is not present in Holliday junction recognition proteins from fungi. However, both the N-terminal domain and a repeated domain that appears further downstream, also of unknown function, appear in all both vertebral and fungal Holliday junction recognition proteins. HJURP is a conserved non-histone protein that interact physically with the conventional histone H3 (CENP-A) heterotetramer and is essential for its deposition at centromeres in vivo [, , , , ]. This protein has been implicated in many cancers [].
Publication
First Author: Knowlton WM
Year: 2013
Journal: J Neurosci
Title: A sensory-labeled line for cold: TRPM8-expressing sensory neurons define the cellular basis for cold, cold pain, and cooling-mediated analgesia.
Volume: 33
Issue: 7
Pages: 2837-48
Publication
First Author: Foltz DR
Year: 2009
Journal: Cell
Title: Centromere-specific assembly of CENP-a nucleosomes is mediated by HJURP.
Volume: 137
Issue: 3
Pages: 472-84
Protein
Organism: Mus musculus/domesticus
Length: 401  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 89  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 388  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 70  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 70  
Fragment?: false
Publication
First Author: Stoler S
Year: 2007
Journal: Proc Natl Acad Sci U S A
Title: Scm3, an essential Saccharomyces cerevisiae centromere protein required for G2/M progression and Cse4 localization.
Volume: 104
Issue: 25
Pages: 10571-6
Publication
First Author: Aravind L
Year: 2007
Journal: Cell Cycle
Title: Domain architectures of the Scm3p protein provide insights into centromere function and evolution.
Volume: 6
Issue: 20
Pages: 2511-5
Publication
First Author: Mizuguchi G
Year: 2007
Journal: Cell
Title: Nonhistone Scm3 and histones CenH3-H4 assemble the core of centromere-specific nucleosomes.
Volume: 129
Issue: 6
Pages: 1153-64
Publication
First Author: Camahort R
Year: 2007
Journal: Mol Cell
Title: Scm3 is essential to recruit the histone h3 variant cse4 to centromeres and to maintain a functional kinetochore.
Volume: 26
Issue: 6
Pages: 853-65
Protein Domain
Type: Family
Description: This entry includes human holliday junction recognition protein (HJURP) and its homologue, Scm3 from budding yeasts. HJURP is a histone chaperone that plays a central role in the incorporation and maintenance of histone H3-like variant CENP-A at centromeres []. Scm3 is a non-histone component of centromeric chromatin that binds to CenH3-H4 histones, which are required for kinetochore assembly. Scm3 is required for Cse4 (CENP- homologue) localisation and is required for its centromeric association [, ]. The histone H3 variant Cse4 replaces conventional histone H3 in centromeric chromatin and helps direct the assembly of the kinetochore. In addition, Scm3 has is required for G2/M progression []and is required to maintain kinetochore function throughout the cell cycle. Scm3 contains a nuclear export signal (NES). The N-terminal region of Scm3 is well conserved and functions as the CenH3-interacting domain, while the C-terminal region is variable in size and sometimes consists of DNA binding motifs [].
Protein
Organism: Mus musculus/domesticus
Length: 667  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 667  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: false
Publication
First Author: Stellfox ME
Year: 2013
Journal: Cell Mol Life Sci
Title: Putting CENP-A in its place.
Volume: 70
Issue: 3
Pages: 387-406
Publication
First Author: Tachiwana H
Year: 2011
Journal: Nature
Title: Crystal structure of the human centromeric nucleosome containing CENP-A.
Volume: 476
Issue: 7359
Pages: 232-5
Publication
First Author: Tachiwana H
Year: 2012
Journal: Nucleus
Title: Comparison between the CENP-A and histone H3 structures in nucleosomes.
Volume: 3
Issue: 1
Pages: 6-11
Publication
First Author: Yamagishi Y
Year: 2014
Journal: FEMS Microbiol Rev
Title: Kinetochore composition and its function: lessons from yeasts.
Volume: 38
Issue: 2
Pages: 185-200
Publication
First Author: Hu H
Year: 2011
Journal: Genes Dev
Title: Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP.
Volume: 25
Issue: 9
Pages: 901-6
Publication
First Author: Wiedemann SM
Year: 2010
Journal: J Cell Biol
Title: Identification and characterization of two novel primate-specific histone H3 variants, H3.X and H3.Y.
Volume: 190
Issue: 5
Pages: 777-91
Protein Domain
Type: Family
Description: This entry includes histone H3 and its variant, CENP-A (Cse4 in budding yeast, Cnp1 in fission yeast, and CID/CenH3 in fruit flies). Two primate-specific forms of H3, known as H3.X and H3.Y, are found in the brain [].Histone H3 is one of the five histones, along with H1/H5, H2A, H2B and H4. Two copies of each of the H2A, H2B, H3, and H4 histones ensemble to form the core of the nucleosome []. The nucleosome forms octameric structure that wraps DNA in a left-handed manner. H3 is a highly conserved protein of 135 amino acid residues [, ]. Histones can undergo several different types of post-translational modifications that affect transcription, DNA repair, DNA replication and chromosomal stability.Eukaryotic centromeres consists of an unique nucleosome in which CENP-A can be found []. Human CENP-A nucleosome forms a histone octamer containing two each of histones H2A, H2B, H4 and CENP-A. Similar to the H3-containing nucleosome, the CENP-A nucleosome wraps DNA in a left-handed orientation [, ]. CENP-A nucleosomes function as a scaffold on which other kinetochore proteins assemble. CENP-A may serves as an epigenetic marker for kinetochore assembly []. Deposition of CENP-A to the centromere requires histone chaperone HJURP (Holliday junction recognition protein) [].
Protein
Organism: Mus musculus/domesticus
Length: 136  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 136  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 136  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 134  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 136  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 52  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 136  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 55  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 130  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 136  
Fragment?: false
Publication  
First Author: Wells D
Year: 1991
Journal: Nucleic Acids Res
Title: Histone and histone gene compilation and alignment update.
Volume: 19 Suppl
Pages: 2173-88
Publication
First Author: Thatcher TH
Year: 1994
Journal: Nucleic Acids Res
Title: Phylogenetic analysis of the core histones H2A, H2B, H3, and H4.
Volume: 22
Issue: 2
Pages: 174-9
Publication
First Author: Bhasin M
Year: 2006
Journal: J Comput Biol
Title: Recognition and classification of histones using support vector machine.
Volume: 13
Issue: 1
Pages: 102-12