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Overview

Uniprot IDQ05682
Protein NameCaldesmon
Gene NameCALD1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
119 QEALERQKEFDPTIT
170 EETETVTKSYQKNDW
174 TVTKSYQKNDWRDAE
416 VEQKIEGKWVNEKKA
475 IKKDKEPKEEVKSFM
504 EFMTHKLKHTENTFS
522 GRASVDTKEAEGAPQ
534 APQVEAGKRLEELRR
557 EFEKLKQKQQEAALE
577 KKREERRKVLEEEEQ
621 EAAEKRQKMPEDGLS
640 PFKCFTPKGSSLKIE
645 TPKGSSLKIEERAEF
655 ERAEFLNKSVQKSSG
659 FLNKSVQKSSGVKST
664 VQKSSGVKSTHQAAI
674 HQAAIVSKIDSRLEQ
690 TSAIEGTKSAKPTKP
696 TKSAKPTKPAASDLP
718 NIKSMWEKGNVFSSP
733 TAAGTPNKETAGLKV
739 NKETAGLKVGVSSRI
752 RINEWLTKTPDGNKS
758 TKTPDGNKSPAPKPS
775 RPGDVSSKRNLWEKQ
781 SKRNLWEKQSVDKVT
786 WEKQSVDKVTSPTKV

Function

Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also plays an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity)

Protein Sequence

10 MDDFERRREL 20 RRQKREEMRL 30 EAERIAYQRN 40 DDDEEEAARE 50 RRRRARQERL 60 RQKQEEESLG 70 QVTDQVEVNA 80 QNSVPDEEAK 90 TTTTNTQVEG 100 DDEAAFLERL 110 ARREERRQKR 120 LQEALERQKE 130 FDPTITDASL 140 SLPSRRMQND 150 TAENETTEKE 160 EKSESRQERY 170 EIEETETVTK 180 SYQKNDWRDA 190 EENKKEDKEK 200 EEEEEEKPKR 210 GSIGENQVEV 220 MVEEKTTESQ 230 EETVVMSLKN 240 GQISSEEPKQ 250 EEEREQGSDE 260 ISHHEKMEEE 270 DKERAEAERA 280 RLEAEERERI 290 KAEQDKKIAD 300 ERARIEAEEK 310 AAAQERERRE 320 AEERERMREE 330 EKRAAEERQR 340 IKEEEKRAAE 350 ERQRIKEEEK 360 RAAEERQRIK 370 EEEKRAAEER 380 QRARAEEEEK 390 AKVEEQKRNK 400 QLEEKKHAMQ 410 ETKIKGEKVE 420 QKIEGKWVNE 430 KKAQEDKLQT 440 AVLKKQGEEK 450 GTKVQAKREK 460 LQEDKPTFKK 470 EEIKDEKIKK 480 DKEPKEEVKS 490 FMDRKKGFTE 500 VKSQNGEFMT 510 HKLKHTENTF 520 SRPGGRASVD 530 TKEAEGAPQV 540 EAGKRLEELR 550 RRRGETESEE 560 FEKLKQKQQE 570 AALELEELKK 580 KREERRKVLE 590 EEEQRRKQEE 600 ADRKLREEEE 610 KRRLKEEIER 620 RRAEAAEKRQ 630 KMPEDGLSDD 640 KKPFKCFTPK 650 GSSLKIEERA 660 EFLNKSVQKS 670 SGVKSTHQAA 680 IVSKIDSRLE 690 QYTSAIEGTK 700 SAKPTKPAAS 710 DLPVPAEGVR 720 NIKSMWEKGN 730 VFSSPTAAGT 740 PNKETAGLKV 750 GVSSRINEWL 760 TKTPDGNKSP 770 APKPSDLRPG 780 DVSSKRNLWE 790 KQSVDKVTSP TKV

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0005856 cytoskeleton
Cellular Component GO:0005829 cytosol
Cellular Component GO:0030016 myofibril
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0001725 stress fiber
Molecular Function GO:0003779 actin binding
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0005516 calmodulin binding
Molecular Function GO:0017022 myosin binding
Molecular Function GO:0005523 tropomyosin binding
Biological Process GO:0051017 actin filament bundle assembly
Biological Process GO:0006936 muscle contraction

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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] 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.

[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] 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.

[7] 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.