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Search results 201 to 257 out of 257 for Tpm2

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Type Details Score
Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
7844152 | -
First Author: Drees B
Year: 1995
Journal: J Cell Biol
Title: Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform distinct functions.
Volume: 128
Issue: 3
Pages: 383-92
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DO Term
DOID:0110932 | nemaline myopathy 4
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DO Term
DOID:0111597 | distal arthrogryposis type 1A
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Allele
Tg(Myh6-Tpm2)1Dfw | MGI:2387933
Name: transgene insertion 1, David F Wieczorek
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
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Publication
17951248 | J:130053
First Author: Schevzov G
Year: 2008
Journal: J Biol Chem
Title: Divergent regulation of the sarcomere and the cytoskeleton.
Volume: 283
Issue: 1
Pages: 275-83
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Publication
23207592 | J:207956
First Author: Mamidi R
Year: 2013
Journal: J Physiol
Title: Identification of two new regions in the N-terminus of cardiac troponin T that have divergent effects on cardiac contractile function.
Volume: 591
Issue: 5
Pages: 1217-34
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Publication
11709421 | J:134703
First Author: MacGowan GA
Year: 2001
Journal: Am J Physiol Heart Circ Physiol
Title: Compensatory changes in Ca(2+) and myocardial O(2) consumption in beta-tropomyosin transgenic hearts.
Volume: 281
Issue: 6
Pages: H2539-48
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Publication
9737941 | J:127513
First Author: Muthuchamy M
Year: 1998
Journal: J Mol Cell Cardiol
Title: Beta-tropomyosin overexpression induces severe cardiac abnormalities.
Volume: 30
Issue: 8
Pages: 1545-57
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Publication
9733519 | J:49872
First Author: Sussman MA
Year: 1998
Journal: Science
Title: Prevention of cardiac hypertrophy in mice by calcineurin inhibition.
Volume: 281
Issue: 5383
Pages: 1690-3
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Protein
P21107
Organism: Mus musculus/domesticus
Length: 285  
Fragment?: false
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Protein
P58771
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
P58774
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
Q8BP43
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
Q545Y3
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
G5E8R0
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: false
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Protein
E9Q454
Organism: Mus musculus/domesticus
Length: 287  
Fragment?: false
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Protein
E9Q456
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: false
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Protein
Q9D1R6
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
A2AIM5
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: true
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Protein
E9Q455
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: false
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Protein
A0A0R4J1P2
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
E9Q452
Organism: Mus musculus/domesticus
Length: 281  
Fragment?: false
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Protein
D3Z6I8
Organism: Mus musculus/domesticus
Length: 247  
Fragment?: false
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Protein
Q8C7C3
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: false
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Protein
A2RRI1
Organism: Mus musculus/domesticus
Length: 52  
Fragment?: false
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Protein
E9Q453
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: false
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Protein
S4R2U0
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: false
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Protein
E9Q7Q3
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: false
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Protein
A2AIM4
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
A0A2R2Y2P8
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
D3YVR0
Organism: Mus musculus/domesticus
Length: 71  
Fragment?: true
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Protein
Q8BSH3
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Publication
3606587 | -
First Author: MacLeod AR
Year: 1987
Journal: Bioessays
Title: Genetic origin of diversity of human cytoskeletal tropomyosins.
Volume: 6
Issue: 5
Pages: 208-12
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Publication
6993480 | -
First Author: Lewis WG
Year: 1980
Journal: J Biol Chem
Title: The amino acid sequence of rabbit cardiac tropomyosin.
Volume: 255
Issue: 14
Pages: 6854-9
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Publication
12690456 | -
First Author: Wolska BM
Year: 2003
Journal: Pflugers Arch
Title: The role of tropomyosin in the regulation of myocardial contraction and relaxation.
Volume: 446
Issue: 1
Pages: 1-8
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Protein Domain
IPR000533 | Tropomyosin
Type: Family
Description: Tropomyosins [], are a family of closely related proteins present in muscle and non-muscle cells. In striated muscle, tropomyosin mediate the interactions between the troponin complex and actin so as to regulate muscle contraction []. The role of tropomyosin in smooth muscle and non-muscle tissues is not clear. Tropomyosin is an α-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites []. There are multiple cell-specific isoforms, created by differential splicing of the messenger RNA from one gene, but the proportions of the isoforms vary between different cell types. Muscle isoforms of tropomyosin are characterised by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.This entry represents tropomyosin (Tmp) 1, 2 and 3. Within the yeast Tmp1 and Tmp2, biochemical and sequence analyses indicate that Tpm2 spans four actin monomers along a filament, whereas Tpm1 spans five. Despite its shorter length, Tpm2 can compete with Tpm1 for binding to F-actin. Over-expression of Tpm2 in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis [].
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Protein
Q6IRU2
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: false
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Protein
B7ZNL3
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
Q564G1
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
F8WID5
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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Protein
G5E8R2
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: false
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Protein
E9Q5J9
Organism: Mus musculus/domesticus
Length: 285  
Fragment?: false
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Protein
E9Q450
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
D3Z2H9
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: false
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Protein
A0A571BEU1
Organism: Mus musculus/domesticus
Length: 158  
Fragment?: false
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Protein
Q3TJ53
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: false
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Protein
E9Q448
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
G5E8R1
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: false
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Protein
Q61344
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
Q8K0Z5
Organism: Mus musculus/domesticus
Length: 284  
Fragment?: false
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Protein
Q58E70
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: false
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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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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.

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Cambridge CB2 3EH, United Kingdom