Type |
Details |
Score |
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
476
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Thom CS |
Year: |
2014 |
Journal: |
Dev Cell |
Title: |
Trim58 degrades Dynein and regulates terminal erythropoiesis. |
Volume: |
30 |
Issue: |
6 |
Pages: |
688-700 |
|
•
•
•
•
•
|
Publication |
First Author: |
Koyama S |
Year: |
2008 |
Journal: |
J Mol Biol |
Title: |
Muscle RING-finger protein-1 (MuRF1) as a connector of muscle energy metabolism and protein synthesis. |
Volume: |
376 |
Issue: |
5 |
Pages: |
1224-36 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
462
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
249
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
75
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
319
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
289
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
221
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
236
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
52
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
82
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
117
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
117
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
213
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
92
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
130
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
191
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
55
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
102
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
209
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
129
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
97
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
81
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
172
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
154
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
553
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
77
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
114
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
58
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
126
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
95
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
91
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
102
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
180
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
139
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
219
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Darsow T |
Year: |
2001 |
Journal: |
Mol Biol Cell |
Title: |
Vps41p function in the alkaline phosphatase pathway requires homo-oligomerization and interaction with AP-3 through two distinct domains. |
Volume: |
12 |
Issue: |
1 |
Pages: |
37-51 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kodama T |
Year: |
1990 |
Journal: |
Nature |
Title: |
Type I macrophage scavenger receptor contains alpha-helical and collagen-like coiled coils. |
Volume: |
343 |
Issue: |
6258 |
Pages: |
531-5 |
|
•
•
•
•
•
|
Publication |
First Author: |
Matsumoto A |
Year: |
1990 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Human macrophage scavenger receptors: primary structure, expression, and localization in atherosclerotic lesions. |
Volume: |
87 |
Issue: |
23 |
Pages: |
9133-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Prabhudas M |
Year: |
2014 |
Journal: |
J Immunol |
Title: |
Standardizing scavenger receptor nomenclature. |
Volume: |
192 |
Issue: |
5 |
Pages: |
1997-2006 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yu XH |
Year: |
2013 |
Journal: |
Clin Chim Acta |
Title: |
Foam cells in atherosclerosis. |
Volume: |
424 |
|
Pages: |
245-52 |
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•
•
•
•
|
Publication |
First Author: |
Borden KL |
Year: |
1995 |
Journal: |
EMBO J |
Title: |
Novel topology of a zinc-binding domain from a protein involved in regulating early Xenopus development. |
Volume: |
14 |
Issue: |
23 |
Pages: |
5947-56 |
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•
•
•
•
|
Publication |
First Author: |
Borden KL |
Year: |
1998 |
Journal: |
Biochem Cell Biol |
Title: |
RING fingers and B-boxes: zinc-binding protein-protein interaction domains. |
Volume: |
76 |
Issue: |
2-3 |
Pages: |
351-8 |
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•
•
•
•
|
Publication |
First Author: |
Catalano-Sherman J |
Year: |
1994 |
Journal: |
Calcif Tissue Int |
Title: |
Production of a monoclonal antibody against human amelogenin. |
Volume: |
54 |
Issue: |
1 |
Pages: |
76-80 |
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•
•
•
•
|
Publication |
First Author: |
Goto Y |
Year: |
1993 |
Journal: |
J Biochem |
Title: |
Molecular conformation of porcine amelogenin in solution: three folding units at the N-terminal, central, and C-terminal regions. |
Volume: |
113 |
Issue: |
1 |
Pages: |
55-60 |
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•
•
•
•
|
Publication |
First Author: |
Renugopalakrishnan V |
Year: |
1989 |
Journal: |
Connect Tissue Res |
Title: |
Secondary structure and limited three-dimensional structure of bovine amelogenin. |
Volume: |
22 |
Issue: |
1-4 |
Pages: |
131-8 |
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•
•
•
•
|
Publication |
First Author: |
Lagerström-Fermér M |
Year: |
1995 |
Journal: |
Genomics |
Title: |
Amelogenin signal peptide mutation: correlation between mutations in the amelogenin gene (AMGX) and manifestations of X-linked amelogenesis imperfecta. |
Volume: |
26 |
Issue: |
1 |
Pages: |
159-62 |
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•
•
•
•
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Publication |
First Author: |
Yeats C |
Year: |
2004 |
Journal: |
Trends Biochem Sci |
Title: |
The PepSY domain: a regulator of peptidase activity in the microbial environment? |
Volume: |
29 |
Issue: |
4 |
Pages: |
169-72 |
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•
•
•
•
|
Publication |
First Author: |
Krzywda S |
Year: |
2002 |
Journal: |
Acta Crystallogr D Biol Crystallogr |
Title: |
Crystallization of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli. |
Volume: |
58 |
Issue: |
Pt 6 Pt 2 |
Pages: |
1066-7 |
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•
•
•
•
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Publication |
First Author: |
Janska H |
Year: |
2013 |
Journal: |
Biochim Biophys Acta |
Title: |
Protein quality control in organelles - AAA/FtsH story. |
Volume: |
1833 |
Issue: |
2 |
Pages: |
381-7 |
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•
•
•
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Publication |
First Author: |
Rainey RN |
Year: |
2006 |
Journal: |
Mol Cell Biol |
Title: |
A new function in translocation for the mitochondrial i-AAA protease Yme1: import of polynucleotide phosphorylase into the intermembrane space. |
Volume: |
26 |
Issue: |
22 |
Pages: |
8488-97 |
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•
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•
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Publication |
First Author: |
Potting C |
Year: |
2010 |
Journal: |
EMBO J |
Title: |
Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35. |
Volume: |
29 |
Issue: |
17 |
Pages: |
2888-98 |
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•
•
•
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Publication |
First Author: |
Tailleux A |
Year: |
2002 |
Journal: |
Atherosclerosis |
Title: |
Apolipoprotein A-II, HDL metabolism and atherosclerosis. |
Volume: |
164 |
Issue: |
1 |
Pages: |
1-13 |
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•
•
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Publication |
First Author: |
Motizuki M |
Year: |
1998 |
Journal: |
J Biochem |
Title: |
Purification, primary structure, and antimicrobial activities of bovine apolipoprotein A-II. |
Volume: |
123 |
Issue: |
4 |
Pages: |
675-9 |
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•
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Publication |
First Author: |
Schluchter WM |
Year: |
1992 |
Journal: |
Biochemistry |
Title: |
Molecular characterization of ferredoxin-NADP+ oxidoreductase in cyanobacteria: cloning and sequence of the petH gene of Synechococcus sp. PCC 7002 and studies on the gene product. |
Volume: |
31 |
Issue: |
12 |
Pages: |
3092-102 |
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•
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Publication |
First Author: |
Fischer PW |
Year: |
1991 |
Journal: |
Clin Biochem |
Title: |
An evaluation of plasma and erythrocyte magnesium concentration and the activities of alkaline phosphatase and creatine kinase as indicators of magnesium status. |
Volume: |
24 |
Issue: |
2 |
Pages: |
215-8 |
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•
•
•
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Publication |
First Author: |
Bradham GB |
Year: |
1972 |
Journal: |
Med Biol Eng |
Title: |
An automatically compensating gradient-layer calorimeter for animal metabolic studies. |
Volume: |
10 |
Issue: |
6 |
Pages: |
793-5 |
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Publication |
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Suarez DL |
Year: |
1997 |
Journal: |
J Virol |
Title: |
Size variation within the second hypervariable region of the surface envelope gene of the bovine lentivirus BIV in experimentally and naturally infected cattle. |
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71 |
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3 |
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Meas S |
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2001 |
Journal: |
Arch Virol |
Title: |
Phylogenetic relationships of bovine immunodeficiency virus in cattle and buffaloes based on surface envelope gene sequences. Brief report. |
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2008 |
Journal: |
Nat Struct Mol Biol |
Title: |
Fission yeast SWI/SNF and RSC complexes show compositional and functional differences from budding yeast. |
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15 |
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8 |
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Newman J |
Year: |
2020 |
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Acta Crystallogr F Struct Biol Commun |
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The X-ray crystal structure of the N-terminal domain of Ssr4, a Schizosaccharomyces pombe chromatin-remodelling protein. |
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76 |
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Pt 12 |
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Publication |
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Nat Struct Biol |
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Three-dimensional structure of bacteriophage T4 baseplate. |
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10 |
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9 |
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Publication |
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2000 |
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J Mol Biol |
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Structure of bacteriophage T4 gene product 11, the interface between the baseplate and short tail fibers. |
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301 |
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J Exp Bot |
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Regulated expression of a novel TCP domain transcription factor indicates an involvement in the control of meristem activation processes in Solanum tuberosum. |
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An essential quality control mechanism at the eukaryotic basal body prior to intraflagellar transport. |
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10 |
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BMC Bioinformatics |
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Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization. |
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2008 |
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J Biol Chem |
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Proteomic analysis of a nutritional shift-up in Saccharomyces cerevisiae identifies Gvp36 as a BAR-containing protein involved in vesicular traffic and nutritional adaptation. |
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Cell |
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Boca, an endoplasmic reticulum protein required for wingless signaling and trafficking of LDL receptor family members in Drosophila. |
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Biochemistry |
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Requirement for natively unstructured regions of mesoderm development candidate 2 in promoting low-density lipoprotein receptor-related protein 6 maturation. |
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J Biol Chem |
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Molecular insights into mammalian end-binding protein heterodimerization. |
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Mol Microbiol |
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Aspergillus fumigatus AcuM regulates both iron acquisition and gluconeogenesis. |
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Genes Dev |
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SMC1 is a downstream effector in the ATM/NBS1 branch of the human S-phase checkpoint. |
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Overall and allele-specific expression of the SMC1A gene in female Cornelia de Lange syndrome patients and healthy controls. |
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The F-BAR protein PSTPIP1 controls extracellular matrix degradation and filopodia formation in macrophages. |
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Proc Natl Acad Sci U S A |
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Nat Genet |
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Hum Mol Genet |
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Issue: |
15 |
Pages: |
1847-63 |
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Publication |
First Author: |
Coene KL |
Year: |
2011 |
Journal: |
Hum Mol Genet |
Title: |
The ciliopathy-associated protein homologs RPGRIP1 and RPGRIP1L are linked to cilium integrity through interaction with Nek4 serine/threonine kinase. |
Volume: |
20 |
Issue: |
18 |
Pages: |
3592-605 |
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Publication |
First Author: |
Devuyst O |
Year: |
2008 |
Journal: |
Nephrol Dial Transplant |
Title: |
Mutations in RPGRIP1L: extending the clinical spectrum of ciliopathies. |
Volume: |
23 |
Issue: |
5 |
Pages: |
1500-3 |
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Publication |
First Author: |
Song D |
Year: |
2008 |
Journal: |
J Biol Chem |
Title: |
A role for IOP1 in mammalian cytosolic iron-sulfur protein biogenesis. |
Volume: |
283 |
Issue: |
14 |
Pages: |
9231-8 |
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Publication |
First Author: |
Park YJ |
Year: |
2006 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
The structure of nucleosome assembly protein 1. |
Volume: |
103 |
Issue: |
5 |
Pages: |
1248-53 |
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Publication |
First Author: |
Mrosek M |
Year: |
2008 |
Journal: |
Biochemistry |
Title: |
Structural analysis of B-Box 2 from MuRF1: identification of a novel self-association pattern in a RING-like fold. |
Volume: |
47 |
Issue: |
40 |
Pages: |
10722-30 |
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Publication |
First Author: |
Bodine SC |
Year: |
2001 |
Journal: |
Science |
Title: |
Identification of ubiquitin ligases required for skeletal muscle atrophy. |
Volume: |
294 |
Issue: |
5547 |
Pages: |
1704-8 |
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Publication |
First Author: |
McElhinny AS |
Year: |
2002 |
Journal: |
J Cell Biol |
Title: |
Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1. |
Volume: |
157 |
Issue: |
1 |
Pages: |
125-36 |
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Publication |
First Author: |
Hirner S |
Year: |
2008 |
Journal: |
J Mol Biol |
Title: |
MuRF1-dependent regulation of systemic carbohydrate metabolism as revealed from transgenic mouse studies. |
Volume: |
379 |
Issue: |
4 |
Pages: |
666-77 |
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Publication |
First Author: |
Fielitz J |
Year: |
2007 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Loss of muscle-specific RING-finger 3 predisposes the heart to cardiac rupture after myocardial infarction. |
Volume: |
104 |
Issue: |
11 |
Pages: |
4377-82 |
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Protein Domain |
Type: |
Family |
Description: |
The NRL (for NPH3/RPT2-Like) family is formed by signaling molecules specificto higher plants. Several regions of sequence and predicted structuralconservation define members of the NRL family, with three domains being mostnotable: an N-terminal BTB domain, a centrally located NPH3domain, and a C-terminal coiled coil domain. The function of the NPH3 domainis not yet known [, , , , , , , ].Root phototropism protein 3 (RPT3), also known as nonphototropic hypocotyl 3 (NPH3), and root phototropism 2 (RPT2) () represent the founding members of a novel plant-specific family []. Three domains define the members of this family: an N-terminal BTB (broad complex, tramtrack, bric a brac) domain (), a centrally located NPH3 domain (), and a C-terminal coiled-coil domain.NPH3 assembles with CUL3 to form a E3 complex that ubiquitinates phototropin 1 (phot1) and modulates phototropic responsiveness [, ]. NPH3 is necessary for root and hypocotyl phototropisms, but not for the regulation of stomata opening or chloroplast relocation []. Coleoptile phototropism protein 1 (CPT1) is a rice orthologue of Arabidopsis NPH3 also required for phototropism []. This entry also includes DOT3 (AT5G10250) that is involved in shoot and primary root growth; DOT3 mutants produce an aberrant parallel venation pattern in juvenile leaves []. |
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Protein Domain |
Type: |
Family |
Description: |
Amelogenins, cell adhesion proteins, play a role in the biomineralisation ofteeth. They seem to regulate formation of crystallites during the secretorystage of tooth enamel development and are thought to play a major role inthe structural organisation and mineralisation of developing enamel. Theextracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins [].Circulardichroism studies of porcine amelogenin have shown that the proteinconsists of 3 discrete folding units []: the N-terminal region appears tocontain β-strand structures, while the C-terminal region displayscharacteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain arepetitive β-turn segment and a "β-spiral"between Gln112 and Leu138,which sequester a (Pro, Leu, Gln) rich region []. The β-spiraloffers a probable site for interactions with Ca2+ ions.Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplasticamelogenesis imperfecta, a disease characterised by defective enamel. A 9bpdeletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disruptingthe 16-residue (Met1-Ala16) amelogenin signal peptide []. |
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Protein Domain |
Type: |
Domain |
Description: |
Endocytosis and intracellular transport involve several mechanistic steps: (1) for the internalisation of cargo molecules, the membrane needs to bend to form a vesicular structure, which requires membrane curvature and a rearrangement of the cytoskeleton; (2) following its formation, the vesicle has to be pinched off the membrane; (3) the cargo has to be subsequently transported through the cell and the vesicle must fuse with the correct cellular compartment.Members of the Amphiphysin protein family are key regulators in the early steps of endocytosis, involved in the formation of clathrin-coated vesicles by promoting the assembly of a protein complex at the plasma membrane and directly assist in the induction of the high curvature of the membrane at the neck of the vesicle. Amphiphysins contain a characteristic domain, known as the BAR (Bin-Amphiphysin-Rvs)-domain, which is required for their in vivofunction and their ability to tubulate membranes []. The crystal structure of these proteins suggest the domain forms a crescent-shaped dimer of a three-helix coiled coil with a characteristic set of conserved hydrophobic, aromatic and hydrophilic amino acids. Proteins containing this domain have been shown to homodimerise, heterodimerise or, in a few cases, interact with small GTPases. |
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Protein Domain |
Type: |
Family |
Description: |
Endocytosis and intracellular transport involve several mechanistic steps: (1) for the internalisation of cargo molecules, the membrane needs to bend to form a vesicular structure, which requires membrane curvature and a rearrangement of the cytoskeleton; (2) following its formation, the vesicle has to be pinched off the membrane; (3) the cargo has to be subsequently transported through the cell and the vesicle must fuse with the correct cellular compartment.Members of the Amphiphysin protein family are key regulators in the early steps of endocytosis, involved in the formation of clathrin-coated vesicles by promoting the assembly of a protein complex at the plasma membrane and directly assist in the induction of the high curvature of the membrane at the neck of the vesicle. Amphiphysins contain a characteristic domain, known as the BAR (Bin-Amphiphysin-Rvs)-domain, which is required for their in vivofunction and their ability to tubulate membranes []. The crystal structure of these proteins suggest the domain forms a crescent-shaped dimer of a three-helix coiled coil with a characteristic set of conserved hydrophobic, aromatic and hydrophilic amino acids. Proteins containing this domain have been shown to homodimerise, heterodimerise or, in a few cases, interact with small GTPases. This entry identifies several fungal BAR domain-containing proteins, such as Gvp36, that are not detected by []. |
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Protein Domain |
Type: |
Family |
Description: |
It is thought that NAPs act as histone chaperones, shuttling both core and linker histones from their site of synthesis in the cytoplasm to the nucleus. The proteins may be involved in regulating gene expression and therefore cellular differentiation [, ].The centrosomal protein c-Nap1, also known as Cep250, has been implicated in the cell-cycle-regulated cohesion of microtubule-organizing centres. This 281kDa protein consists mainly of domains predicted to form coiled coil structures. The C-terminal region defines a novel histone-binding domain that is responsible for targeting CNAP1, and possibly condensin, to mitotic chromosomes []. During interphase, C-Nap1 localizes to the proximal ends of both parental centrioles, but it dissociates from these structures at the onset of mitosis. Re-association with centrioles then occurs in late telophase or at the very beginning of G1 phase, when daughter cells are still connected by post-mitotic bridges. Electron microscopic studies performed on isolated centrosomes suggest that a proteinaceous linker connects parental centrioles and C-Nap1 may be part of a linker structure that assures the cohesion of duplicated centrosomes during interphase, but that is dismantled upon centrosome separation at the onset of mitosis []. |
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