Search Results

Overview

Uniprot IDQ99439
Protein NameCalponin-2
Gene NameCNN2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
134 LAGKAKTKGLQSGVD
19 YGLSAEVKNRLLSKY
234 RRHIYDTKLGTDKCD
25 VKNRLLSKYDPQKEA
74 LQPGSVPKINRSMQN
8 MSSTQFNKGPSYGLS

Function

Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity

Protein Sequence

10 MSSTQFNKGP 20 SYGLSAEVKN 30 RLLSKYDPQK 40 EAELRTWIEG 50 LTGLSIGPDF 60 QKGLKDGTIL 70 CTLMNKLQPG 80 SVPKINRSMQ 90 NWHQLENLSN 100 FIKAMVSYGM 110 NPVDLFEAND 120 LFESGNMTQV 130 QVSLLALAGK 140 AKTKGLQSGV 150 DIGVKYSEKQ 160 ERNFDDATMK 170 AGQCVIGLQM 180 GTNKCASQSG 190 MTAYGTRRHL 200 YDPKNHILPP 210 MDHSTISLQM 220 GTNKCASQVG 230 MTAPGTRRHI 240 YDTKLGTDKC 250 DNSSMSLQMG 260 YTQGANQSGQ 270 VFGLGRQIYD 280 PKYCPQGTVA 290 DGAPSGTGDC 300 PDPGEVPEYP PYYQEEAGY

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0005911 cell-cell junction
Cellular Component GO:0005856 cytoskeleton
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0016020 membrane
Cellular Component GO:0035580 specific granule lumen
Cellular Component GO:0001725 stress fiber
Cellular Component GO:1904724 tertiary granule lumen
Molecular Function GO:0003779 actin binding
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0005516 calmodulin binding
Biological Process GO:0007015 actin filament organization
Biological Process GO:0031032 actomyosin structure organization
Biological Process GO:0071260 cellular response to mechanical stimulus
Biological Process GO:0007010 cytoskeleton organization
Biological Process GO:0032970 regulation of actin filament-based process

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] 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.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] 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.

[6] 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.

[7] 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.

[8] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.