Search Results

Overview

Uniprot IDQ9ULV4
Protein NameCoronin-1C
Gene NameCORO1C
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
353 IIMTVPRKSDLFQDD
391 DPILISLKHGYIPGK
398 KHGYIPGKNRDLKVV
407 RDLKVVKKNILDSKP
413 KKNILDSKPTANKKC
419 SKPTANKKCDLISIP
428 DLISIPKKTTDTASV
452 LKEIKSIKDTICNQD

Function

Plays a role in directed cell migration by regulating the activation and subcellular location of RAC1 (PubMed:25074804, PubMed:25925950). Increases the presence of activated RAC1 at the leading edge of migrating cells (PubMed:25074804, PubMed:25925950). Required for normal organization of the cytoskeleton, including the actin cytoskeleton, microtubules and the vimentin intermediate filaments (By similarity). Plays a role in endoplasmic reticulum-associated endosome fission: localizes to endosome membrane tubules and promotes recruitment of TMCC1, leading to recruitment of the endoplasmic reticulum to endosome tubules for fission (PubMed:30220460). Endosome membrane fission of early and late endosomes is essential to separate regions destined for lysosomal degradation from carriers to be recycled to the plasma membrane (PubMed:30220460). Required for normal cell proliferation, cell migration, and normal formation of lamellipodia (By similarity). Required for normal distribution of mitochondria within cells (By similarity). Interacts with GDP-bound RAB44 in bone marrow macrophages to promote osteoclastogenesis (By similarity). Involved in the migration and chemotaxis of macrophages (By similarity)

Protein Sequence

10 MRRVVRQSKF 20 RHVFGQAVKN 30 DQCYDDIRVS 40 RVTWDSSFCA 50 VNPRFVAIII 60 EASGGGAFLV 70 LPLHKTGRID 80 KSYPTVCGHT 90 GPVLDIDWCP 100 HNDQVIASGS 110 EDCTVMVWQI 120 PENGLTLSLT 130 EPVVILEGHS 140 KRVGIVAWHP 150 TARNVLLSAG 160 CDNAIIIWNV 170 GTGEALINLD 180 DMHSDMIYNV 190 SWNRNGSLIC 200 TASKDKKVRV 210 IDPRKQEIVA 220 EKEKAHEGAR 230 PMRAIFLADG 240 NVFTTGFSRM 250 SERQLALWNP 260 KNMQEPIALH 270 EMDTSNGVLL 280 PFYDPDTSII 290 YLCGKGDSSI 300 RYFEITDESP 310 YVHYLNTFSS 320 KEPQRGMGYM 330 PKRGLDVNKC 340 EIARFFKLHE 350 RKCEPIIMTV 360 PRKSDLFQDD 370 LYPDTAGPEA 380 ALEAEEWFEG 390 KNADPILISL 400 KHGYIPGKNR 410 DLKVVKKNIL 420 DSKPTANKKC 430 DLISIPKKTT 440 DTASVQNEAK 450 LDEILKEIKS 460 IKDTICNQDE 470 RISKLEQQMA KIAA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0030017 sarcomere
Biological Process GO:0007015 actin filament organization
Cellular Component GO:0045202 synapse
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0005884 actin filament
Cellular Component GO:0005938 cell cortex
Cellular Component GO:0010008 endosome membrane
Cellular Component GO:0016600 flotillin complex
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0030027 lamellipodium
Cellular Component GO:0016328 lateral plasma membrane
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0032587 ruffle membrane
Cellular Component GO:0042383 sarcolemma
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:0031267 small GTPase binding
Biological Process GO:0090630 activation of GTPase activity
Biological Process GO:0016197 endosomal transport
Biological Process GO:0140285 endosome fission
Biological Process GO:0097750 endosome membrane tubulation
Biological Process GO:0045184 establishment of protein localization
Biological Process GO:0048246 macrophage chemotaxis
Biological Process GO:0090148 membrane fission
Biological Process GO:0010633 negative regulation of epithelial cell migration
Biological Process GO:0051895 negative regulation of focal adhesion assembly
Biological Process GO:0044387 negative regulation of protein kinase activity by regulation of protein phosphorylation
Biological Process GO:0001933 negative regulation of protein phosphorylation
Biological Process GO:1900025 negative regulation of substrate adhesion-dependent cell spreading
Biological Process GO:0001755 neural crest cell migration
Biological Process GO:0006909 phagocytosis
Biological Process GO:2000394 positive regulation of lamellipodium morphogenesis
Biological Process GO:0045672 positive regulation of osteoclast differentiation
Biological Process GO:0010632 regulation of epithelial cell migration
Biological Process GO:0010762 regulation of fibroblast migration
Biological Process GO:0051893 regulation of focal adhesion assembly
Biological Process GO:0001932 regulation of protein phosphorylation
Biological Process GO:1900027 regulation of ruffle assembly
Biological Process GO:1900024 regulation of substrate adhesion-dependent cell spreading
Biological Process GO:0007165 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] 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] 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] Hu J, Jin Z, Gao Y, Liu Q, Yu Y et al.. Global Profiling of Lactylation Proteomics and Specific Lactylated Site Validation in Rheumatoid Arthritis Patients.. J Proteome Res 24(4):1732-1744. 2025 Apr 4. PMID: 40112136.

[8] 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.

[9] 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.

[10] 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.