Search Results

Overview

Uniprot IDP67936
Protein NameTropomyosin alpha-4 chain
Gene NameTPM4
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
11 LNSLEAVKRKIQALQ
113 EIQEMQLKEAKHIAE
13 SLEAVKRKIQALQQQ
132 KYEEVARKLVILEGE
169 KNVTNNLKSLEAASE
177 SLEAASEKYSEKEDK
44 GERERREKAEGDVAA

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 (By similarity). Binds calcium (PubMed:1836432). Plays a role in platelet biogenesis

Protein Sequence

10 MAGLNSLEAV 20 KRKIQALQQQ 30 ADEAEDRAQG 40 LQRELDGERE 50 RREKAEGDVA 60 ALNRRIQLVE 70 EELDRAQERL 80 ATALQKLEEA 90 EKAADESERG 100 MKVIENRAMK 110 DEEKMEIQEM 120 QLKEAKHIAE 130 EADRKYEEVA 140 RKLVILEGEL 150 ERAEERAEVS 160 ELKCGDLEEE 170 LKNVTNNLKS 180 LEAASEKYSE 190 KEDKYEEEIK 200 LLSDKLKEAE 210 TRAEFAERTV 220 AKLEKTIDDL 230 EEKLAQAKEE 240 NVGLHQTLDQ TLNELNCI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005884 actin filament
Cellular Component GO:0030863 cortical cytoskeleton
Cellular Component GO:0005856 cytoskeleton
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0016020 membrane
Cellular Component GO:0005862 muscle thin filament tropomyosin
Cellular Component GO:0002102 podosome
Cellular Component GO:0001725 stress fiber
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:0005509 calcium ion binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0046982 protein heterodimerization activity
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0008307 structural constituent of muscle
Biological Process GO:0007015 actin filament organization
Biological Process GO:0006936 muscle contraction
Biological Process GO:0001649 osteoblast differentiation
Biological Process GO:0030220 platelet formation

Reference

[1] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.