Search Results

Overview

Uniprot ID	Q8IZL8
Protein Name	Proline-, glutamic acid- and leucine-rich protein 1
Gene Name	PELP1
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
495	TGKPSAPKKLKLDVG
496	GKPSAPKKLKLDVGE
498	PSAPKKLKLDVGEAM

Function

Coactivator of estrogen receptor-mediated transcription and a corepressor of other nuclear hormone receptors and sequence-specific transcription factors (PubMed:14963108). Plays a role in estrogen receptor (ER) genomic activity when present in the nuclear compartment by activating the ER target genes in a hormonal stimulation dependent manner. Can facilitate ER non-genomic signaling via SRC and PI3K interaction in the cytosol. Plays a role in E2-mediated cell cycle progression by interacting with RB1. May have important functional implications in ER/growth factor cross-talk. Interacts with several growth factor signaling components including EGFR and HRS. Functions as the key stabilizing component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes. Component of the PELP1 complex involved in the nucleolar steps of 28S rRNA maturation and the subsequent nucleoplasmic transit of the pre-60S ribosomal subunit. Regulates pre-60S association of the critical remodeling factor MDN1 (PubMed:21326211). May promote tumorigenesis via its interaction with and modulation of several oncogenes including SRC, PI3K, STAT3 and EGFR. Plays a role in cancer cell metastasis via its ability to modulate E2-mediated cytoskeleton changes and cell migration via its interaction with SRC and PI3K

Protein Sequence

10 MAAAVLSGPS 20 AGSAAGVPGG 30 TGGLSAVSSG 40 PRLRLLLLES 50 VSGLLQPRTG 60 SAVAPVHPPN 70 RSAPHLPGLM 80 CLLRLHGSVG 90 GAQNLSALGA 100 LVSLSNARLS 110 SIKTRFEGLC 120 LLSLLVGESP 130 TELFQQHCVS 140 WLRSIQQVLQ 150 TQDPPATMEL 160 AVAVLRDLLR 170 YAAQLPALFR 180 DISMNHLPGL 190 LTSLLGLRPE 200 CEQSALEGMK 210 ACMTYFPRAC 220 GSLKGKLASF 230 FLSRVDALSP 240 QLQQLACECY 250 SRLPSLGAGF 260 SQGLKHTESW 270 EQELHSLLAS 280 LHTLLGALYE 290 GAETAPVQNE 300 GPGVEMLLSS 310 EDGDAHVLLQ 320 LRQRFSGLAR 330 CLGLMLSSEF 340 GAPVSVPVQE 350 ILDFICRTLS 360 VSSKNISLHG 370 DGPLRLLLLP 380 SIHLEALDLL 390 SALILACGSR 400 LLRFGILIGR 410 LLPQVLNSWS 420 IGRDSLSPGQ 430 ERPYSTVRTK 440 VYAILELWVQ 450 VCGASAGMLQ 460 GGASGEALLT 470 HLLSDISPPA 480 DALKLRSPRG 490 SPDGSLQTGK 500 PSAPKKLKLD 510 VGEAMAPPSH 520 RKGDSNANSD 530 VCAAALRGLS 540 RTILMCGPLI 550 KEETHRRLHD 560 LVLPLVMGVQ 570 QGEVLGSSPY 580 TSSRCRRELY 590 CLLLALLLAP 600 SPRCPPPLAC 610 ALQAFSLGQR 620 EDSLEVSSFC 630 SEALVTCAAL 640 THPRVPPLQP 650 MGPTCPTPAP 660 VPPPEAPSPF 670 RAPPFHPPGP 680 MPSVGSMPSA 690 GPMPSAGPMP 700 SAGPVPSARP 710 GPPTTANHLG 720 LSVPGLVSVP 730 PRLLPGPENH 740 RAGSNEDPIL 750 APSGTPPPTI 760 PPDETFGGRV 770 PRPAFVHYDK 780 EEASDVEISL 790 ESDSDDSVVI 800 VPEGLPPLPP 810 PPPSGATPPP 820 IAPTGPPTAS 830 PPVPAKEEPE 840 ELPAAPGPLP 850 PPPPPPPPVP 860 GPVTLPPPQL 870 VPEGTPGGGG 880 PPALEEDLTV 890 ININSSDEEE 900 EEEEEEEEEE 910 EEEEEEEEDF 920 EEEEEDEEEY 930 FEEEEEEEEE 940 FEEEFEEEEG 950 ELEEEEEEED 960 EEEEEELEEV 970 EDLEFGTAGG 980 EVEEGAPPPP 990 TLPPALPPPE 1000 SPPKVQPEPE 1010 PEPGLLLEVE 1020 EPGTEEERGA 1030 DTAPTLAPEA 1040 LPSQGEVERE 1050 GESPAAGPPP 1060 QELVEEEPSA 1070 PPTLLEEETE 1080 DGSDKVQPPP 1090 ETPAEEEMET 1100 ETEAEALQEK 1110 EQDDTAAMLA 1120 DFIDCPPDDE 1130 KPPPPTEPDS

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0000791	euchromatin
Cellular Component	GO:0016020	membrane
Cellular Component	GO:0071339	MLL1 complex
Cellular Component	GO:0005730	nucleolus
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Molecular Function	GO:0003682	chromatin binding
Molecular Function	GO:0003723	RNA binding
Molecular Function	GO:0032183	SUMO binding
Biological Process	GO:0071391	cellular response to estrogen stimulus
Biological Process	GO:0000448	cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
Biological Process	GO:0006351	DNA-templated transcription
Biological Process	GO:0045944	positive regulation of transcription by RNA polymerase II
Biological Process	GO:0006364	rRNA processing

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] 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.

[4] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[5] 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.

[6] 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.

[7] 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.