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Search results 2501 to 2600 out of 3345 for Myb

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Type Details Score
Protein
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 396  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 127  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 90  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 674  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 305  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 205  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 35  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 242  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 71  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 281  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 74  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 252  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 91  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 113  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 63  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 433  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 281  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 242  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 84  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 50  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 380  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 57  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 321  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 167  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 137  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 58  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 114  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 112  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 196  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 237  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 246  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 198  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 206  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 182  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
Publication
First Author: Boyer LA
Year: 2004
Journal: Nat Rev Mol Cell Biol
Title: The SANT domain: a unique histone-tail-binding module?
Volume: 5
Issue: 2
Pages: 158-63
Publication
First Author: Cutler G
Year: 1998
Journal: Mol Cell Biol
Title: Adf-1 is a nonmodular transcription factor that contains a TAF-binding Myb-like motif.
Volume: 18
Issue: 4
Pages: 2252-61
Publication
First Author: Bhaskar V
Year: 2002
Journal: Gene
Title: The MADF-BESS domain factor Dip3 potentiates synergistic activation by Dorsal and Twist.
Volume: 299
Issue: 1-2
Pages: 173-84
Protein Domain
Type: Homologous_superfamily
Description: Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. Pirh2 is an eukaryotic ubiquitin protein ligase, which has been shown to promote p53 degradation in mammals. Pirh2 physically interacts with p53 and promotes ubiquitination of p53 independently of MDM2. Like MDM2, Pirh2 is thought to participate in an autoregulatory feedback loop that controls p53 function. Pirh2 proteins contain three distinct zinc fingers, the CHY-type, the CTCHY-type which is C-terminal to the CHY-type zinc finger and a RING finger. The CHY-type zinc finger has no currently known function [].As well as Pirh2, the CHY-type zinc finger is also found in the following proteins:Yeast helper of Tim protein 13. Hot13 may have a role in the assembly and recycling of the small Tims, a complex of the mitochondrial intermembrane space that participates in the TIM22 import pathway for assembly of the inner membrane []Several plant hypothetical proteins that also contain haemerythrin cation binding domainsSeveral protozoan hypothetical proteins that also contain a Myb domainThe solution structure of this zinc finger has been solved and binds three zinc atoms as shown in the following schematic representation:++---------+-----+|| | |CXHYxxxxxxxxxCCxxxxxCxxCHxxxxxHxxxxxxxxxxxCxxCxxxxxxxxxCxxC| | | | | | | |+-+-----------------+--+ +--+---------+--+'C': conserved cysteine involved in the binding of one zinc atom.'H': conserved histidine involved in the binding of one zinc atom.
Protein Domain
Type: Domain
Description: Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. Pirh2 is an eukaryotic ubiquitin protein ligase, which has been shown to promote p53 degradation in mammals. Pirh2 physically interacts with p53 and promotes ubiquitination of p53 independently of MDM2. Like MDM2, Pirh2 is thought to participate in an autoregulatory feedback loop that controls p53 function. Pirh2 proteins contain three distinct zinc fingers, the CHY-type, the CTCHY-type which is C-terminal to the CHY-type zinc finger and a RING finger. The CHY-type zinc finger has no currently known function [].As well as Pirh2, the CHY-type zinc finger is also found in the following proteins:Yeast helper of Tim protein 13. Hot13 may have a role in the assembly and recycling of the small Tims, a complex of the mitochondrial intermembrane space that participates in the TIM22 import pathway for assembly of the inner membrane []Several plant hypothetical proteins that also contain haemerythrin cation binding domainsSeveral protozoan hypothetical proteins that also contain a Myb domainThe solution structure of this zinc finger has been solved and binds three zinc atoms as shown in the following schematic representation:++---------+-----+|| | |CXHYxxxxxxxxxCCxxxxxCxxCHxxxxxHxxxxxxxxxxxCxxCxxxxxxxxxCxxC| | | | | | | |+-+-----------------+--+ +--+---------+--+'C': conserved cysteine involved in the binding of one zinc atom.'H': conserved histidine involved in the binding of one zinc atom.
Publication
First Author: Tasic B
Year: 2012
Journal: PLoS One
Title: Extensions of MADM (mosaic analysis with double markers) in mice.
Volume: 7
Issue: 3
Pages: e33332
Protein
Organism: Mus musculus/domesticus
Length: 480  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 523  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 451  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 541  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2260  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 511  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 551  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 768  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 485  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2242  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 395  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 479  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 351  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 430  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 534  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 551  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 2036  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 511  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 524  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 541  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 443  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 382  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 584  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 447  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 322  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 767  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 271  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1010  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 257  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 549  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1011  
Fragment?: true
Publication
First Author: Curran SP
Year: 2004
Journal: J Biol Chem
Title: The role of Hot13p and redox chemistry in the mitochondrial TIM22 import pathway.
Volume: 279
Issue: 42
Pages: 43744-51
Publication
First Author: Noben-Trauth K
Year: 1996
Journal: Genomics
Title: Mybl2 (Bmyb) maps to mouse chromosome 2 and human chromosome 20q 13.1.
Volume: 35
Issue: 3
Pages: 610-2
Publication
First Author: Hofmann CS
Year: 2005
Journal: J Biol Chem
Title: B-Myb represses elastin gene expression in aortic smooth muscle cells.
Volume: 280
Issue: 9
Pages: 7694-701
Publication
First Author: Tarasov KV
Year: 2008
Journal: PLoS One
Title: B-MYB is essential for normal cell cycle progression and chromosomal stability of embryonic stem cells.
Volume: 3
Issue: 6
Pages: e2478
Publication
First Author: Brahim S
Year: 2023
Journal: Cell Death Dis
Title: Notch3 regulates Mybl2 via HeyL to limit proliferation and tumor initiation in breast cancer.
Volume: 14
Issue: 2
Pages: 171
Protein
Organism: Mus musculus/domesticus
Length: 1213  
Fragment?: false