TPM2

TPM2
Identifiers
Aliases	TPM2, AMCD1, DA1, DA2B, HEL-S-273, NEM4, TMSB, tropomyosin 2 (beta), tropomyosin 2
External IDs	HomoloGene: 134045 GeneCards: TPM2
Gene location (Human) Chr. Chromosome 9 (human) Band 9p13.3 Start 35,681,992 bp End 35,691,020 bp
RNA expression pattern More reference expression data
Gene ontology Molecular function • actin binding • structural constituent of muscle • identical protein binding • protein homodimerization activity • protein heterodimerization activity • actin filament binding Cellular component • cytoplasm • muscle thin filament tropomyosin • cytosol • cytoskeleton • actin filament • actin cytoskeleton Biological process • regulation of ATPase activity • muscle filament sliding • muscle contraction • actin filament organization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	7169	n/a
Ensembl	ENSG00000198467	n/a
UniProt	P07951	n/a
RefSeq (mRNA)	NM_001145822 NM_001301226 NM_001301227 NM_003289 NM_213674	n/a
RefSeq (protein)	NP_001288155 NP_001288156 NP_003280 NP_998839	n/a
Location (UCSC)	Chr 9: 35.68 – 35.69 Mb	n/a
PubMed search		n/a

7169

n/a

ENSG00000198467

n/a

P07951

n/a

NM_001145822
NM_001301226
NM_001301227
NM_003289
NM_213674

n/a

NP_001288155
NP_001288156
NP_003280
NP_998839

n/a

β-Tropomyosin, also known as tropomyosin beta chain is a protein that in humans is encoded by the TPM2 gene. β-tropomyosin is striated muscle-specific coiled coil dimer that functions to stabilize actin filaments and regulate muscle contraction.

β-tropomyosin is roughly 32 kDa in molecular weight (284 amino acids), but multiple splice variants exist. Tropomysin is a flexible protein homodimer or heterodimer composed of two alpha-helical chains, which adopt a bent coiled coil conformation to wrap around the seven actin molecules in a functional unit of muscle. It is polymerized end to end along the two grooves of actin filaments and provides stability to the filaments. Tropomyosin dimers are composed of varying combinations of tropomyosin isoforms; human striated muscles express protein from the TPM1 (α-tropoomyosin), TPM2 (β-tropomyosin) and TPM3 (γ-tropomyosin) genes, with α-tropomyosin being the predominant isoform in striated muscle. Fast skeletal muscle and cardiac muscle contain more αα-homodimers, and slow skeletal muscle contains more ββ-homodimers. In human cardiac muscle the ratio of α-tropomyosin to β-tropomyosin is roughly 5:1. It has been shown that different combinations of tropomyosin isoforms bind troponin T with differing affinities, demonstrating that isoform combinations are used to impart a specific functional impact.

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Wikipedia