Search Results

Overview

Uniprot IDP26038
Protein NameMoesin
Gene NameMSN
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
139 SKYGDFNKEVHKSGY
143 DFNKEVHKSGYLAGD
151 SGYLAGDKLLPQRVL
162 QRVLEQHKLNKDQWE
165 LEQHKLNKDQWEERI
253 RNISFNDKKFVIKPI
254 NISFNDKKFVIKPID
258 NDKKFVIKPIDKKAP
262 FVIKPIDKKAPDFVF
263 VIKPIDKKAPDFVFY
296 ELYMRRRKPDTIEVQ
3 *****MPKTISVRVT
306 TIEVQQMKAQAREEK
316 AREEKHQKQMERAML
327 RAMLENEKKKREMAE
344 KEKIEREKEELMERL
352 EELMERLKQIEEQTK
360 QIEEQTKKAQQELEE
388 RAQSEAEKLAKERQE
391 SEAEKLAKERQEAEE
400 RQEAEEAKEALLQAS
412 QASRDQKKTQEQLAL
438 LEMARQKKESEAVEW
458 MVQEDLEKTRAELKT
523 ERVQKHLKALTSELA
538 NARDESKKTANDMIH
60 KGFSTWLKLNKKVTA
64 TWLKLNKKVTAQDVR
72 VTAQDVRKESPLLFK
79 KESPLLFKFRAKFYP
83 LLFKFRAKFYPEDVS

Function

Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton (PubMed:10212266). Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement (PubMed:10212266). These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction (PubMed:12387735, PubMed:15039356). The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs (PubMed:9298994, PubMed:9616160). Modulates phagolysosomal biogenesis in macrophages (By similarity). Also participates in immunologic synapse formation (PubMed:27405666)

Protein Sequence

10 MPKTISVRVT 20 TMDAELEFAI 30 QPNTTGKQLF 40 DQVVKTIGLR 50 EVWFFGLQYQ 60 DTKGFSTWLK 70 LNKKVTAQDV 80 RKESPLLFKF 90 RAKFYPEDVS 100 EELIQDITQR 110 LFFLQVKEGI 120 LNDDIYCPPE 130 TAVLLASYAV 140 QSKYGDFNKE 150 VHKSGYLAGD 160 KLLPQRVLEQ 170 HKLNKDQWEE 180 RIQVWHEEHR 190 GMLREDAVLE 200 YLKIAQDLEM 210 YGVNYFSIKN 220 KKGSELWLGV 230 DALGLNIYEQ 240 NDRLTPKIGF 250 PWSEIRNISF 260 NDKKFVIKPI 270 DKKAPDFVFY 280 APRLRINKRI 290 LALCMGNHEL 300 YMRRRKPDTI 310 EVQQMKAQAR 320 EEKHQKQMER 330 AMLENEKKKR 340 EMAEKEKEKI 350 EREKEELMER 360 LKQIEEQTKK 370 AQQELEEQTR 380 RALELEQERK 390 RAQSEAEKLA 400 KERQEAEEAK 410 EALLQASRDQ 420 KKTQEQLALE 430 MAELTARISQ 440 LEMARQKKES 450 EAVEWQQKAQ 460 MVQEDLEKTR 470 AELKTAMSTP 480 HVAEPAENEQ 490 DEQDENGAEA 500 SADLRADAMA 510 KDRSEEERTT 520 EAEKNERVQK 530 HLKALTSELA 540 NARDESKKTA 550 NDMIHAENMR 560 LGRDKYKTLR 570 QIRQGNTKQR IDEFESM

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005912 adherens junction
Cellular Component GO:0045177 apical part of cell
Cellular Component GO:0016324 apical plasma membrane
Cellular Component GO:0016323 basolateral plasma membrane
Cellular Component GO:0072562 blood microparticle
Cellular Component GO:0071944 cell periphery
Cellular Component GO:0009986 cell surface
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005856 cytoskeleton
Cellular Component GO:0005829 cytosol
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:0005902 microvillus
Cellular Component GO:0031528 microvillus membrane
Cellular Component GO:0005634 nucleus
Cellular Component GO:0048471 perinuclear region of cytoplasm
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0031143 pseudopodium
Cellular Component GO:0001931 uropod
Cellular Component GO:0031982 vesicle
Molecular Function GO:0003779 actin binding
Molecular Function GO:0050839 cell adhesion molecule binding
Molecular Function GO:0003725 double-stranded RNA binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0019901 protein kinase binding
Molecular Function GO:0005102 signaling receptor binding
Molecular Function GO:0005200 structural constituent of cytoskeleton
Biological Process GO:0061028 establishment of endothelial barrier
Biological Process GO:0045198 establishment of epithelial cell apical/basal polarity
Biological Process GO:0022612 gland morphogenesis
Biological Process GO:0001771 immunological synapse formation
Biological Process GO:0007159 leukocyte cell-cell adhesion
Biological Process GO:0050900 leukocyte migration
Biological Process GO:0022614 membrane to membrane docking
Biological Process GO:2000643 positive regulation of early endosome to late endosome transport
Biological Process GO:0010628 positive regulation of gene expression
Biological Process GO:0045732 positive regulation of protein catabolic process
Biological Process GO:1902966 positive regulation of protein localization to early endosome
Biological Process GO:0008360 regulation of cell shape
Biological Process GO:0008361 regulation of cell size
Biological Process GO:2000401 regulation of lymphocyte migration
Biological Process GO:1902115 regulation of organelle assembly
Biological Process GO:0070489 T cell aggregation
Biological Process GO:0072678 T cell migration
Biological Process GO:0042098 T cell proliferation

Reference

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[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] 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.

[6] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[7] 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.

[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.