GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
RAT:TPM1
Contents
Species (Taxon ID) | Rattus norvegicus (Rat). (10116) | |
Gene Name(s) | Tpm1 (synonyms: Alpha-tm, Tpma) | |
Protein Name(s) | Tropomyosin alpha-1 chain
Alpha-tropomyosin Tropomyosin-1 | |
External Links | ||
UniProt | P04692 | |
EMBL | M15474 M15472 M15473 M16432 M16433 M18135 M16432 M15472 M16433 M15473 M18135 M16432 M16433 M18135 M16432 M15472 M16433 X02411 M34135 M34134 M34136 M34137 M34138 M60666 M60668 M60669 X02412 | |
PIR | A34787 A39816 B27407 B34787 C34787 C39816 D39816 | |
RefSeq | NP_001029241.1 NP_001029244.1 NP_001029245.1 NP_001029246.1 NP_001029247.1 NP_001288265.1 NP_001288665.1 NP_062004.1 | |
UniGene | Rn.87540 | |
PDB | 1IHQ 1MV4 1TMZ 2B9C 2G9J 3AZD | |
PDBsum | 1IHQ 1MV4 1TMZ 2B9C 2G9J 3AZD | |
ProteinModelPortal | P04692 | |
SMR | P04692 | |
BioGrid | 246968 | |
DIP | DIP-29020N | |
IntAct | P04692 | |
PhosphoSite | P04692 | |
PaxDb | P04692 | |
PRIDE | P04692 | |
Ensembl | ENSRNOT00000024575 ENSRNOT00000024617 ENSRNOT00000048044 | |
GeneID | 24851 | |
KEGG | rno:24851 | |
CTD | 7168 | |
RGD | 3898 | |
eggNOG | NOG304012 | |
GeneTree | ENSGT00550000074494 | |
HOVERGEN | HBG107404 | |
InParanoid | P04692 | |
KO | K10373 | |
PhylomeDB | P04692 | |
TreeFam | TF351519 | |
Reactome | REACT_224772 REACT_234304 | |
EvolutionaryTrace | P04692 | |
NextBio | 604620 | |
Proteomes | UP000002494 | |
ExpressionAtlas | P04692 | |
Genevestigator | P04692 | |
GO | GO:0005737 GO:0005856 GO:0043234 GO:0003779 GO:0051015 GO:0042803 GO:0047485 GO:0051693 GO:0060048 GO:0006936 GO:0030049 GO:0030336 GO:0032781 GO:0045785 GO:0051496 GO:0043462 GO:0031529 GO:0042060 | |
InterPro | IPR000533 | |
Pfam | PF00261 | |
PRINTS | PR00194 | |
PROSITE | PS00326 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
enables |
GO:0042802 |
identical protein binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0042803 |
protein homodimerization activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0046982 |
protein heterodimerization activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0051015 |
actin filament binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0097718 |
disordered domain specific binding |
ECO:0000353 |
physical interaction evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0015629 |
actin cytoskeleton |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0051015 |
actin filament binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0046982 |
protein heterodimerization activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0042803 |
protein homodimerization activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0042802 |
identical protein binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0051496 |
positive regulation of stress fiber assembly |
ECO:0000316 |
genetic interaction evidence used in manual assertion |
P |
Seeded From UniProt |
Missing: with/from | |||
involved_in |
GO:0045785 |
positive regulation of cell adhesion |
ECO:0000316 |
genetic interaction evidence used in manual assertion |
P |
Seeded From UniProt |
Missing: with/from | |||
involved_in |
GO:0042060 |
wound healing |
ECO:0000316 |
genetic interaction evidence used in manual assertion |
P |
Seeded From UniProt |
Missing: with/from | |||
involved_in |
GO:0032781 |
positive regulation of ATPase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0031529 |
ruffle organization |
ECO:0000316 |
genetic interaction evidence used in manual assertion |
P |
Seeded From UniProt |
Missing: with/from | |||
involved_in |
GO:0030336 |
negative regulation of cell migration |
ECO:0000316 |
genetic interaction evidence used in manual assertion |
P |
Seeded From UniProt |
Missing: with/from | |||
involved_in |
GO:0030049 |
muscle filament sliding |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0060048 |
cardiac muscle contraction |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
involved_in |
GO:0051693 |
actin filament capping |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0051015 |
actin filament binding |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0047485 |
protein N-terminus binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0043462 |
regulation of ATPase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0042803 |
protein homodimerization activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0032991 |
protein-containing complex |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
involved_in |
GO:0032781 |
positive regulation of ATPase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0003779 |
actin binding |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0003779 |
actin binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0060048 |
cardiac muscle contraction |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
MGI:MGI:98809 |
P |
Seeded From UniProt |
complete | ||
enables |
GO:0051015 |
actin filament binding |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
FB:FBgn0003721 |
F |
Seeded From UniProt |
complete | ||
involved_in |
GO:0007015 |
actin filament organization |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000443979 |
P |
Seeded From UniProt |
complete | ||
part_of |
GO:0005884 |
actin filament |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000443979 |
C |
Seeded From UniProt |
complete | ||
involved_in |
GO:0006936 |
muscle contraction |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0003779 |
actin binding |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0005856 |
cytoskeleton |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0005737 |
cytoplasm |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0003779 |
actin binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 1.3 Kalyva, A et al. (2012) In vitro formation and characterization of the skeletal muscle α·β tropomyosin heterodimers. Biochemistry 51 6388-99 PubMed GONUTS page
- ↑ Greenfield, NJ et al. (2005) Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1. Biophys. J. 88 372-83 PubMed GONUTS page
- ↑ 3.0 3.1 3.2 3.3 3.4 Gimona, M et al. (1995) Specificity of dimer formation in tropomyosins: influence of alternatively spliced exons on homodimer and heterodimer assembly. Proc. Natl. Acad. Sci. U.S.A. 92 9776-80 PubMed GONUTS page
- ↑ 4.0 4.1 4.2 Varga, AE et al. (2005) Silencing of the Tropomyosin-1 gene by DNA methylation alters tumor suppressor function of TGF-beta. Oncogene 24 5043-52 PubMed GONUTS page
- ↑ 5.0 5.1 Zheng, Q et al. (2008) Role of high-molecular weight tropomyosins in TGF-beta-mediated control of cell motility. Int. J. Cancer 122 78-90 PubMed GONUTS page
- ↑ 6.0 6.1 Karibe, A et al. (2001) Hypertrophic cardiomyopathy caused by a novel alpha-tropomyosin mutation (V95A) is associated with mild cardiac phenotype, abnormal calcium binding to troponin, abnormal myosin cycling, and poor prognosis. Circulation 103 65-71 PubMed GONUTS page
- ↑ Radisic, M et al. (2004) Medium perfusion enables engineering of compact and contractile cardiac tissue. Am. J. Physiol. Heart Circ. Physiol. 286 H507-16 PubMed GONUTS page
- ↑ 8.0 8.1 Kostyukova, AS et al. (2005) Structural requirements of tropomodulin for tropomyosin binding and actin filament capping. Biochemistry 44 4905-10 PubMed GONUTS page
- ↑ 9.0 9.1 Hitchcock-DeGregori, SE et al. (2001) Importance of internal regions and the overall length of tropomyosin for actin binding and regulatory function. Biochemistry 40 2104-12 PubMed GONUTS page
- ↑ 10.0 10.1 Skórzewski, R et al. (2009) Effect of actin C-terminal modification on tropomyosin isoforms binding and thin filament regulation. Biochim. Biophys. Acta 1794 237-43 PubMed GONUTS page
- ↑ Kremneva, E et al. (2006) Thermal unfolding of smooth muscle and nonmuscle tropomyosin alpha-homodimers with alternatively spliced exons. FEBS J. 273 588-600 PubMed GONUTS page
- ↑ Noda, Y et al. (2005) Identification of a multiprotein "motor" complex binding to water channel aquaporin-2. Biochem. Biophys. Res. Commun. 330 1041-7 PubMed GONUTS page
- ↑ Singh, A & Hitchcock-DeGregori, SE (2003) Local destabilization of the tropomyosin coiled coil gives the molecular flexibility required for actin binding. Biochemistry 42 14114-21 PubMed GONUTS page
- ↑ 14.0 14.1 14.2 14.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ 15.0 15.1 Goodwin, LO et al. (1991) Four fibroblast tropomyosin isoforms are expressed from the rat alpha-tropomyosin gene via alternative RNA splicing and the use of two promoters. J. Biol. Chem. 266 8408-15 PubMed GONUTS page
a
c
g
m
p
- GO:0032781 ! positive regulation of ATP-dependent activity
- GO:0045785 ! positive regulation of cell adhesion
- GO:0051496 ! positive regulation of stress fiber assembly
- GO:0032991 ! protein-containing complex
- GO:0046982 ! protein heterodimerization activity
- GO:0042803 ! protein homodimerization activity
r