Search Results

Overview

Uniprot IDP23528
Protein NameCofilin-1
Gene NameCFL1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
114 ESAPLKSKMIYASSK
121 KMIYASSKDAIKKKL
13 AVSDGVIKVFNDMKV
132 KKKLTGIKHELQANC
144 ANCYEEVKDRCTLAE
19 IKVFNDMKVRKSSTP
22 FNDMKVRKSSTPEEV
30 SSTPEEVKKRKKAVL
31 STPEEVKKRKKAVLF
34 EEVKKRKKAVLFCLS
44 LFCLSEDKKNIILEE
45 FCLSEDKKNIILEEG
53 NIILEEGKEILVGDV
73 DPYATFVKMLPDKDC
78 FVKMLPDKDCRYALY
92 YDATYETKESKKEDL

Function

Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (PubMed:11812157, PubMed:33670794). In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (PubMed:15580268). Required for the centralization of the mitotic spindle and symmetric division of zygotes (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells (PubMed:21834987). Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (PubMed:23633677). Required for neural tube morphogenesis and neural crest cell migration (By similarity)

Protein Sequence

10 MASGVAVSDG 20 VIKVFNDMKV 30 RKSSTPEEVK 40 KRKKAVLFCL 50 SEDKKNIILE 60 EGKEILVGDV 70 GQTVDDPYAT 80 FVKMLPDKDC 90 RYALYDATYE 100 TKESKKEDLV 110 FIFWAPESAP 120 LKSKMIYASS 130 KDAIKKKLTG 140 IKHELQANCY 150 EEVKDRCTLA 160 EKLGGSAVIS LEGKPL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0031982 vesicle
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0005911 cell-cell junction
Cellular Component GO:0090732 cofilin-actin rod
Cellular Component GO:0030864 cortical actin cytoskeleton
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0043197 dendritic spine
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0030175 filopodium
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0030426 growth cone
Cellular Component GO:0030027 lamellipodium
Cellular Component GO:0031258 lamellipodium membrane
Cellular Component GO:0016020 membrane
Cellular Component GO:0031966 mitochondrial membrane
Cellular Component GO:0043025 neuronal cell body
Cellular Component GO:0016363 nuclear matrix
Cellular Component GO:0005634 nucleus
Cellular Component GO:0099092 postsynaptic density, intracellular component
Cellular Component GO:0032587 ruffle membrane
Cellular Component GO:0097060 synaptic membrane
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:1902936 phosphatidylinositol bisphosphate binding
Molecular Function GO:0019903 protein phosphatase binding
Molecular Function GO:0005102 signaling receptor binding
Biological Process GO:0030036 actin cytoskeleton organization
Biological Process GO:0030042 actin filament depolymerization
Biological Process GO:0030043 actin filament fragmentation
Biological Process GO:0051014 actin filament severing
Biological Process GO:0071364 cellular response to epidermal growth factor stimulus
Biological Process GO:0071362 cellular response to ether
Biological Process GO:0070301 cellular response to hydrogen peroxide
Biological Process GO:1990314 cellular response to insulin-like growth factor stimulus
Biological Process GO:0071347 cellular response to interleukin-1
Biological Process GO:0071354 cellular response to interleukin-6
Biological Process GO:0071356 cellular response to tumor necrosis factor
Biological Process GO:0051293 establishment of spindle localization
Biological Process GO:0021766 hippocampus development
Biological Process GO:0044794 host-mediated activation of viral process
Biological Process GO:0000281 mitotic cytokinesis
Biological Process GO:0098885 modification of postsynaptic actin cytoskeleton
Biological Process GO:0032232 negative regulation of actin filament bundle assembly
Biological Process GO:0030835 negative regulation of actin filament depolymerization
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:0007162 negative regulation of cell adhesion
Biological Process GO:2000146 negative regulation of cell motility
Biological Process GO:1902951 negative regulation of dendritic spine maintenance
Biological Process GO:0010593 negative regulation of lamellipodium assembly
Biological Process GO:1905875 negative regulation of postsynaptic density organization
Biological Process GO:0051511 negative regulation of unidimensional cell growth
Biological Process GO:0030836 positive regulation of actin filament depolymerization
Biological Process GO:2000814 positive regulation of barbed-end actin filament capping
Biological Process GO:0030307 positive regulation of cell growth
Biological Process GO:2000147 positive regulation of cell motility
Biological Process GO:0060999 positive regulation of dendritic spine development
Biological Process GO:0040019 positive regulation of embryonic development
Biological Process GO:2000784 positive regulation of establishment of cell polarity regulating cell shape
Biological Process GO:0051894 positive regulation of focal adhesion assembly
Biological Process GO:0010592 positive regulation of lamellipodium assembly
Biological Process GO:1905873 positive regulation of protein localization to cell leading edge
Biological Process GO:0045862 positive regulation of proteolysis
Biological Process GO:0031915 positive regulation of synaptic plasticity
Biological Process GO:0006606 protein import into nucleus
Biological Process GO:0061001 regulation of dendritic spine morphogenesis
Biological Process GO:0014823 response to activity
Biological Process GO:0009615 response to virus
Biological Process GO:0007266 Rho protein signal transduction

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] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[7] 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.

[8] 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.

[9] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[10] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[11] 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.