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Overview

Uniprot IDQ8NC51
Protein NameSERPINE1 mRNA-binding protein 1
Gene NameSERBP1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
102 TQPPVALKKEGIRRV
103 QPPVALKKEGIRRVG
122 QQLQGEGKIIDRRPE
211 FSHYSGLKHEDKRGG
215 SGLKHEDKRGGSGSH
236 DELTESPKYIQKQIS
303 IQNKDRAKVEFNIRK
320 EGADGQWKKGFVLHK
321 GADGQWKKGFVLHKS
327 KKGFVLHKSKSEEAH
329 GFVLHKSKSEEAHAE
39 KAAENKKKEAGGGGV
390 NRGSRTDKSSASAPD
52 GVGGPGAKSAAQAAA
68 TNSNAAGKQLRKESQ
79 KESQKDRKNPLPPSV
92 SVGVVDKKEETQPPV

Function

Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (PubMed:36691768). Acts via its association with EEF2/eEF2 factor, sequestering EEF2/eEF2 at the A-site of the ribosome and promoting ribosome stabilization and storage in an inactive state (By similarity). May also play a role in the regulation of mRNA stability: binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay (PubMed:11001948). Seems to play a role in PML-nuclear bodies formation (PubMed:28695742)

Protein Sequence

10 MPGHLQEGFG 20 CVVTNRFDQL 30 FDDESDPFEV 40 LKAAENKKKE 50 AGGGGVGGPG 60 AKSAAQAAAQ 70 TNSNAAGKQL 80 RKESQKDRKN 90 PLPPSVGVVD 100 KKEETQPPVA 110 LKKEGIRRVG 120 RRPDQQLQGE 130 GKIIDRRPER 140 RPPRERRFEK 150 PLEEKGEGGE 160 FSVDRPIIDR 170 PIRGRGGLGR 180 GRGGRGRGMG 190 RGDGFDSRGK 200 REFDRHSGSD 210 RSSFSHYSGL 220 KHEDKRGGSG 230 SHNWGTVKDE 240 LTESPKYIQK 250 QISYNYSDLD 260 QSNVTEETPE 270 GEEHHPVADT 280 ENKENEVEEV 290 KEEGPKEMTL 300 DEWKAIQNKD 310 RAKVEFNIRK 320 PNEGADGQWK 330 KGFVLHKSKS 340 EEAHAEDSVM 350 DHHFRKPAND 360 ITSQLEINFG 370 DLGRPGRGGR 380 GGRGGRGRGG 390 RPNRGSRTDK 400 SSASAPDVDD PEAFPALA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0005634 nucleus
Cellular Component GO:0048471 perinuclear region of cytoplasm
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0003730 mRNA 3'-UTR binding
Molecular Function GO:0043022 ribosome binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0032183 SUMO binding
Molecular Function GO:0061770 translation elongation factor binding
Molecular Function GO:0030371 translation repressor activity
Biological Process GO:0017148 negative regulation of translation
Biological Process GO:0030578 PML body organization
Biological Process GO:0043488 regulation of mRNA stability
Biological Process GO:0141014 ribosome hibernation

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] 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] 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.

[7] 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.

[8] 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.