Search Results

Overview

Uniprot IDP06733
Protein NameAlpha-enolase
Gene NameENO1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
103 EMDGTENKSKFGANA
105 DGTENKSKFGANAIL
126 CKAGAVEKGVPLYRH
193 AEVYHNLKNVIKEKY
202 VIKEKYGKDATNVGD
221 APNILENKEGLELLK
228 KEGLELLKTAIGKAG
233 LLKTAIGKAGYTDKV
256 SEFFRSGKYDLDFKS
262 GKYDLDFKSPDDPSR
281 DQLADLYKSFIKDYP
326 DLTVTNPKRIAKAVN
330 TNPKRIAKAVNEKSC
335 IAKAVNEKSCNCLLL
343 SCNCLLLKVNQIGSV
394 GLCTGQIKTGAPCRS
406 CRSERLAKYNQLLRI
420 IEEELGSKAKFAGRN
422 EELGSKAKFAGRNFR
5 ***MSILKIHAREIF
54 LELRDNDKTRYMGKG
60 DKTRYMGKGVSKAVE
64 YMGKGVSKAVEHINK
71 KAVEHINKTIAPALV
80 IAPALVSKKLNVTEQ
81 APALVSKKLNVTEQE
89 LNVTEQEKIDKLMIE
92 TEQEKIDKLMIEMDG

Function

Enolase that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate in glycolysis and the reverse reaction in gluconeogenesis (PubMed:1369209, PubMed:29775581). Also involved in various processes such as growth control, hypoxia tolerance and allergic responses (PubMed:10802057, PubMed:12666133, PubMed:2005901, PubMed:29775581). May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons (PubMed:12666133). Stimulates immunoglobulin production (PubMed:1369209)

Protein Sequence

10 MSILKIHARE 20 IFDSRGNPTV 30 EVDLFTSKGL 40 FRAAVPSGAS 50 TGIYEALELR 60 DNDKTRYMGK 70 GVSKAVEHIN 80 KTIAPALVSK 90 KLNVTEQEKI 100 DKLMIEMDGT 110 ENKSKFGANA 120 ILGVSLAVCK 130 AGAVEKGVPL 140 YRHIADLAGN 150 SEVILPVPAF 160 NVINGGSHAG 170 NKLAMQEFMI 180 LPVGAANFRE 190 AMRIGAEVYH 200 NLKNVIKEKY 210 GKDATNVGDE 220 GGFAPNILEN 230 KEGLELLKTA 240 IGKAGYTDKV 250 VIGMDVAASE 260 FFRSGKYDLD 270 FKSPDDPSRY 280 ISPDQLADLY 290 KSFIKDYPVV 300 SIEDPFDQDD 310 WGAWQKFTAS 320 AGIQVVGDDL 330 TVTNPKRIAK 340 AVNEKSCNCL 350 LLKVNQIGSV 360 TESLQACKLA 370 QANGWGVMVS 380 HRSGETEDTF 390 IADLVVGLCT 400 GQIKTGAPCR 410 SERLAKYNQL 420 LRIEEELGSK 430 AKFAGRNFRN PLAK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005938 cell cortex
Cellular Component GO:0009986 cell surface
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0031430 M band
Cellular Component GO:0016020 membrane
Cellular Component GO:0005640 nuclear outer membrane
Cellular Component GO:0005634 nucleus
Cellular Component GO:0000015 phosphopyruvate hydratase complex
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0001227 DNA-binding transcription repressor activity, RNA polymerase II-specific
Molecular Function GO:0051020 GTPase binding
Molecular Function GO:0000287 magnesium ion binding
Molecular Function GO:0004634 phosphopyruvate hydratase activity
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0000977 RNA polymerase II transcription regulatory region sequence-specific DNA binding
Molecular Function GO:0003714 transcription corepressor activity
Molecular Function GO:0001222 transcription corepressor binding
Biological Process GO:0061621 canonical glycolysis
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006094 gluconeogenesis
Biological Process GO:0006096 glycolytic process
Biological Process GO:0030308 negative regulation of cell growth
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:1903298 negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:2001171 positive regulation of ATP biosynthetic process
Biological Process GO:0045933 positive regulation of muscle contraction
Biological Process GO:0010756 positive regulation of plasminogen activation
Biological Process GO:0009615 response to virus

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] 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.

[10] 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.

[11] 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.

[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.