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Search results 1601 to 1700 out of 4706 for Coil

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Type Details Score
Publication
18182439 | -
First Author: Latijnhouwers M
Year: 2007
Journal: J Exp Bot
Title: Localization and domain characterization of Arabidopsis golgin candidates.
Volume: 58
Issue: 15-16
Pages: 4373-86
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Publication
22028797 | -
First Author: Garcia-Mayoral MF
Year: 2011
Journal: PLoS One
Title: The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction.
Volume: 6
Issue: 10
Pages: e25912
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Protein Domain
IPR002100 | TF_MADSbox
Type: Domain
Description: Human serum response factor (SRF) is a ubiquitous nuclear protein important for cell proliferation and differentiation. SRF function is essential for transcriptional regulation of numerous growth-factor-inducible genes, such as c-fos oncogene and muscle-specific actin genes. A core domain of around 90 amino acids is sufficient for the activities of DNA-binding, dimerisation and interaction with accessory factors. Within the core is a DNA-binding region, designated the MADS box [], that is highly similar to many eukaryotic regulatory proteins: among these are MCM1, the regulator of cell type-specific genes in fission yeast; DSRF, a Drosophila trachea development factor; the MEF2 family of myocyte-specific enhancer factors; and the Agamous and Deficiens families of plant homeotic proteins.In SRF, the MADS box has been shown to be involved in DNA-binding and dimerisation []. Proteins belonging to the MADS family function as dimers, the primary DNA-binding element of which is an anti-parallel coiled coil of two amphipathic α-helices, one from each subunit. The DNA wraps around the coiled coil allowing the basic N-termini of the helices to fit into the DNA major groove. The chain extending from the helix N-termini reaches over the DNA backbone and penetrates into the minor groove. A 4-stranded, anti-parallel β-sheet packs against the coiled-coil face opposite the DNA and is the central element of the dimerisation interface. The MADS-box domain is commonly found associated with K-box region see ().
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Protein Domain
IPR036879 | TF_MADSbox_sf
Type: Homologous_superfamily
Description: Human serum response factor (SRF) is a ubiquitous nuclear protein important for cell proliferation and differentiation. SRF function is essential for transcriptional regulation of numerous growth-factor-inducible genes, such as c-fos oncogene and muscle-specific actin genes. A core domain of around 90 amino acids is sufficient for the activities of DNA-binding, dimerisation and interaction with accessory factors. Within the core is a DNA-binding region, designated the MADS box [], that is highly similar to many eukaryotic regulatory proteins: among these are MCM1, the regulator of cell type-specific genes in fission yeast; DSRF, a Drosophila trachea development factor; the MEF2 family of myocyte-specific enhancer factors; and the Agamous and Deficiens families of plant homeotic proteins.In SRF, the MADS box has been shown to be involved in DNA-binding and dimerisation []. Proteins belonging to the MADS family function as dimers, the primary DNA-binding element of which is an anti-parallel coiled coil of two amphipathic α-helices, one from each subunit. The DNA wraps around the coiled coil allowing the basic N-termini of the helices to fit into the DNA major groove. The chain extending from the helix N-termini reaches over the DNA backbone and penetrates into the minor groove. A 4-stranded, anti-parallel β-sheet packs against the coiled-coil face opposite the DNA and is the central element of the dimerisation interface. The MADS-box domain is commonly found associated with K-box region see ().
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Protein Domain
IPR010625 | CHCH
Type: Domain
Description: A conserved motif was identified in the LOC118487 protein was called the CHCH motif. Alignment of this protein with related members showed the presence of three subgroups of proteins, which are called the S (Small), N (N-terminal extended) and C (C-terminal extended) subgroups. All three sub-groups of proteins have in common that they contain a predicted conserved [coiled coil 1]-[helix 1]-[coiled coil 2]-[helix 2]domain (CHCH domain). Within each helix of the CHCH domain, there are two cysteines present in a C-X9-C motif. The N-group contains an additional double helix domain, and each helix contains the C-X9-C motif. This family contains a number of characterised proteins: Cox19 protein - a nuclear gene of Saccharomyces cerevisiae, codes for an 11kDa protein (Cox19p) required for expression of cytochrome oxidase. Because cox19 mutants are able to synthesise the mitochondrial and nuclear gene products of cytochrome oxidase, Cox19p probably functions post-translationally during assembly of the enzyme. Cox19p is present in the cytoplasm and mitochondria, where it exists as a soluble intermembrane protein. This dual location is similar to what was previously reported for Cox17p, a low molecular weight copper protein thought to be required for maturation of the CuA centre of subunit 2 of cytochrome oxidase. Cox19p have four conserved potential metal ligands, these are three cysteines and one histidine. Mrp10 - belongs to the class of yeast mitochondrial ribosomal proteins that are essential for translation []. Eukaryotic NADH-ubiquinone oxidoreductase 19kDa (NDUFA8) subunit []. The CHCH domain was previously called DUF657 [].
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Publication
9525888 | J:46846
First Author: Liu YT
Year: 1998
Journal: J Biol Chem
Title: Identification of the binding partners for flightless I, A novel protein bridging the leucine-rich repeat and the gelsolin superfamilies.
Volume: 273
Issue: 14
Pages: 7920-7
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Publication
8450218 | J:4169
First Author: Dierks SE
Year: 1993
Journal: J Immunol
Title: The oligomeric nature of the murine Fc epsilon RII/CD23. Implications for function.
Volume: 150
Issue: 6
Pages: 2372-82
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Publication
16753026 | J:128094
First Author: Fujihara S
Year: 2006
Journal: J Bone Miner Res
Title: Function and regulation of osteopontin in response to mechanical stress.
Volume: 21
Issue: 6
Pages: 956-64
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Publication
- | J:82718
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Download
Title: MGI cDNA Clone Load
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Protein
Q3TRJ4
Organism: Mus musculus/domesticus
Length: 462  
Fragment?: false
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Protein
Q8VCW2
Organism: Mus musculus/domesticus
Length: 446  
Fragment?: false
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Protein
Q6RHW0
Organism: Mus musculus/domesticus
Length: 743  
Fragment?: false
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Protein
Q9Z320
Organism: Mus musculus/domesticus
Length: 448  
Fragment?: false
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Protein
Q6NVD9
Organism: Mus musculus/domesticus
Length: 416  
Fragment?: false
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Protein
A6BLY7
Organism: Mus musculus/domesticus
Length: 462  
Fragment?: false
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Protein
A1L317
Organism: Mus musculus/domesticus
Length: 512  
Fragment?: false
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Protein
Q3UYB8
Organism: Mus musculus/domesticus
Length: 416  
Fragment?: false
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Protein
B2RU72
Organism: Mus musculus/domesticus
Length: 448  
Fragment?: false
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Protein
A2AKJ2
Organism: Mus musculus/domesticus
Length: 134  
Fragment?: true
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Protein
Q9CV17
Organism: Mus musculus/domesticus
Length: 304  
Fragment?: true
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Protein
Q678L1
Organism: Mus musculus/domesticus
Length: 224  
Fragment?: true
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Protein
A0A2R8VHR6
Organism: Mus musculus/domesticus
Length: 399  
Fragment?: false
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Protein
A4IF59
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: true
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Protein
D3Z6N5
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: true
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Protein
Q3V1E5
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: false
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Protein
D3Z6R0
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
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Protein
Q4L0E7
Organism: Mus musculus/domesticus
Length: 222  
Fragment?: true
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Protein
Q9JJY2
Organism: Mus musculus/domesticus
Length: 176  
Fragment?: true
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Protein
D0V735
Organism: Mus musculus/domesticus
Length: 391  
Fragment?: false
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Protein
Q8VDD7
Organism: Mus musculus/domesticus
Length: 118  
Fragment?: true
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Protein
Q60929
Organism: Mus musculus/domesticus
Length: 498  
Fragment?: false
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Protein
O55087
Organism: Mus musculus/domesticus
Length: 349  
Fragment?: false
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Protein
Q8CFN5
Organism: Mus musculus/domesticus
Length: 474  
Fragment?: false
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Protein
Q63943
Organism: Mus musculus/domesticus
Length: 514  
Fragment?: false
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Protein
O70166
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: false
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Protein
P54227
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
Q6NV72
Organism: Mus musculus/domesticus
Length: 663  
Fragment?: false
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Protein
P63042
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
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Publication
19043407 | J:146965
First Author: Cai C
Year: 2009
Journal: Nat Cell Biol
Title: MG53 nucleates assembly of cell membrane repair machinery.
Volume: 11
Issue: 1
Pages: 56-64
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Protein
Q9CZA6
Organism: Mus musculus/domesticus
Length: 344  
Fragment?: false
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Protein
Q3V1B5
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
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Protein
A0A0G2JDQ1
Organism: Mus musculus/domesticus
Length: 400  
Fragment?: false
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Protein
Q921S6
Organism: Mus musculus/domesticus
Length: 507  
Fragment?: false
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Protein
Q8CC29
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: false
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Protein
Q3URR2
Organism: Mus musculus/domesticus
Length: 506  
Fragment?: false
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Protein
A0A0G2JEC2
Organism: Mus musculus/domesticus
Length: 434  
Fragment?: false
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Protein
Q9CXQ8
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
A0A0G2JFM7
Organism: Mus musculus/domesticus
Length: 29  
Fragment?: true
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Protein
A0A0G2JEM8
Organism: Mus musculus/domesticus
Length: 23  
Fragment?: true
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Protein
D3Z4C2
Organism: Mus musculus/domesticus
Length: 203  
Fragment?: false
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Protein
E9QKT0
Organism: Mus musculus/domesticus
Length: 506  
Fragment?: false
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Protein
D3Z6M5
Organism: Mus musculus/domesticus
Length: 235  
Fragment?: true
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Protein
A0A0H2UH28
Organism: Mus musculus/domesticus
Length: 484  
Fragment?: false
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Protein
A0A0G2JFS4
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: true
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Protein
E9Q5E0
Organism: Mus musculus/domesticus
Length: 506  
Fragment?: false
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Protein
A0A0G2JFX1
Organism: Mus musculus/domesticus
Length: 205  
Fragment?: true
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Protein
Q8C895
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: false
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Protein
Q8C2H3
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
A0A1W2P880
Organism: Mus musculus/domesticus
Length: 540  
Fragment?: true
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Protein
Q9DCP3
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
A0A0G2JDT0
Organism: Mus musculus/domesticus
Length: 418  
Fragment?: false
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Protein
A0A0G2JES4
Organism: Mus musculus/domesticus
Length: 227  
Fragment?: true
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Protein
A0A0G2JGL3
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: true
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Protein
G3X9Z6
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
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Protein
F6Q325
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: true
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Protein
K7N7F1
Organism: Mus musculus/domesticus
Length: 349  
Fragment?: false
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Protein
D3Z1Z8
Organism: Mus musculus/domesticus
Length: 102  
Fragment?: true
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Protein
A0A0G2JDK0
Organism: Mus musculus/domesticus
Length: 126  
Fragment?: true
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Protein
A0A0G2JET3
Organism: Mus musculus/domesticus
Length: 129  
Fragment?: true
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Protein
S4R2H4
Organism: Mus musculus/domesticus
Length: 100  
Fragment?: false
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Protein
A0A0G2JE18
Organism: Mus musculus/domesticus
Length: 394  
Fragment?: false
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Protein
A0A0G2JFI7
Organism: Mus musculus/domesticus
Length: 242  
Fragment?: true
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Protein
A0A0G2JFL7
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
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Protein
A0A1B0GRG0
Organism: Mus musculus/domesticus
Length: 196  
Fragment?: false
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Protein
D3Z372
Organism: Mus musculus/domesticus
Length: 232  
Fragment?: false
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Protein
A0A0H2UKB6
Organism: Mus musculus/domesticus
Length: 464  
Fragment?: false
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Protein
A0A0G2JFX2
Organism: Mus musculus/domesticus
Length: 169  
Fragment?: true
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Protein
Q91XT3
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
Q9CYU5
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
A0A1Y7VJP4
Organism: Mus musculus/domesticus
Length: 710  
Fragment?: false
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Protein
D3Z5N2
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: false
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Protein
Q9D1K5
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: false
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Protein
E9Q2M6
Organism: Mus musculus/domesticus
Length: 242  
Fragment?: false
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Protein
A0A0G2JGK3
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: true
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Protein
Q545B6
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: false
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Protein
Q80VR4
Organism: Mus musculus/domesticus
Length: 339  
Fragment?: false
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Protein
Q05DI3
Organism: Mus musculus/domesticus
Length: 176  
Fragment?: false
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Protein
Q545T6
Organism: Mus musculus/domesticus
Length: 180  
Fragment?: false
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Publication
15014504 | -
First Author: Ravelli RB
Year: 2004
Journal: Nature
Title: Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain.
Volume: 428
Issue: 6979
Pages: 198-202
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Publication
12077354 | -
First Author: Whyte JR
Year: 2002
Journal: J Cell Sci
Title: Vesicle tethering complexes in membrane traffic.
Volume: 115
Issue: Pt 13
Pages: 2627-37
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Publication
22114354 | -
First Author: Alkhaja AK
Year: 2012
Journal: Mol Biol Cell
Title: MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization.
Volume: 23
Issue: 2
Pages: 247-57
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Publication
12949583 | -
First Author: van den Bosch M
Year: 2003
Journal: EMBO Rep
Title: The MRN complex: coordinating and mediating the response to broken chromosomes.
Volume: 4
Issue: 9
Pages: 844-9
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Publication
11741547 | -
First Author: de Jager M
Year: 2001
Journal: Mol Cell
Title: Human Rad50/Mre11 is a flexible complex that can tether DNA ends.
Volume: 8
Issue: 5
Pages: 1129-35
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Publication
12152085 | -
First Author: Hopfner KP
Year: 2002
Journal: Nature
Title: The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair.
Volume: 418
Issue: 6897
Pages: 562-6
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Publication
18701350 | -
First Author: Barea F
Year: 2008
Journal: Comput Biol Chem
Title: In silico analyses of a new group of fungal and plant RecQ4-homologous proteins.
Volume: 32
Issue: 5
Pages: 349-58
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Publication
33300032 | -
First Author: Roske JJ
Year: 2021
Journal: Nucleic Acids Res
Title: A skipping rope translocation mechanism in a widespread family of DNA repair helicases.
Volume: 49
Issue: 1
Pages: 504-518
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Publication
19632184 | -
First Author: Honnappa S
Year: 2009
Journal: Cell
Title: An EB1-binding motif acts as a microtubule tip localization signal.
Volume: 138
Issue: 2
Pages: 366-76
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Publication
25469238 | -
First Author: Yokoyama N
Year: 2015
Journal: Biomed Rep
Title: Molecular characterization of WDCP, a novel fusion partner for the anaplastic lymphoma tyrosine kinase ALK.
Volume: 3
Issue: 1
Pages: 9-13
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Publication
18836477 | -
First Author: Ozato K
Year: 2008
Journal: Nat Rev Immunol
Title: TRIM family proteins and their emerging roles in innate immunity.
Volume: 8
Issue: 11
Pages: 849-60
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Publication
20466981 | J:175051
First Author: Wang X
Year: 2010
Journal: Circ Res
Title: Cardioprotection of ischemia/reperfusion injury by cholesterol-dependent MG53-mediated membrane repair.
Volume: 107
Issue: 1
Pages: 76-83
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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