Human Gene TPM1 (ENST00000559397.6) from GENCODE V44
Description: Homo sapiens tropomyosin 1 (TPM1), transcript variant Tpm1.3, mRNA. (from RefSeq NM_001018020) RefSeq Summary (NM_001018020): This gene is a member of the tropomyosin family of highly conserved, widely distributed actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosin is composed of two alpha-helical chains arranged as a coiled-coil. It is polymerized end to end along the two grooves of actin filaments and provides stability to the filaments. The encoded protein is one type of alpha helical chain that forms the predominant tropomyosin of striated muscle, where it also functions in association with the troponin complex to regulate the calcium-dependent interaction of actin and myosin during muscle contraction. In smooth muscle and non-muscle cells, alternatively spliced transcript variants encoding a range of isoforms have been described. Mutations in this gene are associated with type 3 familial hypertrophic cardiomyopathy. [provided by RefSeq, Jul 2008]. Gencode Transcript: ENST00000559397.6 Gencode Gene: ENSG00000140416.25 Transcript (Including UTRs) Position: hg38 chr15:63,042,770-63,071,190 Size: 28,421 Total Exon Count: 9 Strand: + Coding Region Position: hg38 chr15:63,042,830-63,071,172 Size: 28,343 Coding Exon Count: 9
ID:TPM1_HUMAN DESCRIPTION: RecName: Full=Tropomyosin alpha-1 chain; AltName: Full=Alpha-tropomyosin; AltName: Full=Tropomyosin-1; FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. SUBUNIT: Heterodimer of an alpha and a beta chain (By similarity). Interacts with HRG (via the HRR domain); the interaction contributes to the antiangiogenic properties of the histidine/proline-rich region (HRR) of HRG (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. TISSUE SPECIFICITY: Detected in primary breast cancer tissues but undetectable in normal breast tissues in Sudanese patients. Isoform 1 is expressed in adult and fetal skeletal muscle and cardiac tissues, with higher expression levels in the cardiac tissues. Isoform 10 is expressed in adult and fetal cardiac tissues, but not in skeletal muscle. DOMAIN: The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven- residues periodicity. PTM: Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells. MASS SPECTROMETRY: Mass=32875.93; Method=MALDI; Range=1-284 (P09493-3); Source=PubMed:11840567; DISEASE: Defects in TPM1 are the cause of familial hypertrophic cardiomyopathy type 3 (CMH3) [MIM:115196]. Familial hypertrophic cardiomyopathy is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. DISEASE: Defects in TPM1 are the cause of cardiomyopathy dilated type 1Y (CMD1Y) [MIM:611878]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. SIMILARITY: Belongs to the tropomyosin family. WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/TPM1";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P09493
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
