Search Results

Overview

Uniprot IDP08670
Protein NameVimentin
Gene NameVIM
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
104 KNTRTNEKVELQELN
120 RFANYIDKVRFLEQQ
129 RFLEQQNKILLAELE
139 LAELEQLKGQGKSRL
143 EQLKGQGKSRLGDLY
168 VDQLTNDKARVEVER
188 DIMRLREKLQEEMLQ
223 ARLDLERKVESLQEE
235 QEEIAFLKKLHEEEI
282 QYESVAAKNLQEAEE
292 QEAEEWYKSKFADLS
294 AEEWYKSKFADLSEA
313 NDALRQAKQESTEYR
334 TCEVDALKGTNESLE
373 QDEIQNMKEEMARHL
402 IEIATYRKLLEGEES
439 PLVDTHSKRTLLIKT
445 SKRTLLIKTVETRDG
97 DAINTEFKNTRTNEK

Function

Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Plays a role in cell directional movement, orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity). May promote axon outgrowth and motor fiber repair via DSP-mediated recruitment to outgrowth tips (By similarity)

Protein Sequence

10 MSTRSVSSSS 20 YRRMFGGPGT 30 ASRPSSSRSY 40 VTTSTRTYSL 50 GSALRPSTSR 60 SLYASSPGGV 70 YATRSSAVRL 80 RSSVPGVRLL 90 QDSVDFSLAD 100 AINTEFKNTR 110 TNEKVELQEL 120 NDRFANYIDK 130 VRFLEQQNKI 140 LLAELEQLKG 150 QGKSRLGDLY 160 EEEMRELRRQ 170 VDQLTNDKAR 180 VEVERDNLAE 190 DIMRLREKLQ 200 EEMLQREEAE 210 NTLQSFRQDV 220 DNASLARLDL 230 ERKVESLQEE 240 IAFLKKLHEE 250 EIQELQAQIQ 260 EQHVQIDVDV 270 SKPDLTAALR 280 DVRQQYESVA 290 AKNLQEAEEW 300 YKSKFADLSE 310 AANRNNDALR 320 QAKQESTEYR 330 RQVQSLTCEV 340 DALKGTNESL 350 ERQMREMEEN 360 FAVEAANYQD 370 TIGRLQDEIQ 380 NMKEEMARHL 390 REYQDLLNVK 400 MALDIEIATY 410 RKLLEGEESR 420 ISLPLPNFSS 430 LNLRETNLDS 440 LPLVDTHSKR 450 TLLIKTVETR 460 DGQVINETSQ HHDDLE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0030424 axon
Cellular Component GO:0031252 cell leading edge
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005856 cytoskeleton
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0005882 intermediate filament
Cellular Component GO:0045111 intermediate filament cytoskeleton
Cellular Component GO:0005815 microtubule organizing center
Cellular Component GO:0016363 nuclear matrix
Cellular Component GO:0005777 peroxisome
Cellular Component GO:0045335 phagocytic vesicle
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0003725 double-stranded RNA binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:1990254 keratin filament binding
Molecular Function GO:0060090 molecular adaptor activity
Molecular Function GO:0019904 protein domain specific binding
Molecular Function GO:0097110 scaffold protein binding
Molecular Function GO:0005200 structural constituent of cytoskeleton
Molecular Function GO:0005212 structural constituent of eye lens
Biological Process GO:0071222 cellular response to lipopolysaccharide
Biological Process GO:0071225 cellular response to muramyl dipeptide
Biological Process GO:0045109 intermediate filament organization
Biological Process GO:0032967 positive regulation of collagen biosynthetic process
Biological Process GO:0010628 positive regulation of gene expression
Biological Process GO:0043488 regulation of mRNA stability

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] 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] 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.

[8] 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.

[9] 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.

[10] 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.

[11] 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.

[12] 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.