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Overview

Uniprot ID	Q9NVN8
Protein Name	Guanine nucleotide-binding protein-like 3-like protein
Gene Name	GNL3L
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
375	HRLGKKKKGGLYSQE
482	ENKTTVYKIGDLTGY

Function

Stabilizes TERF1 telomeric association by preventing TERF1 recruitment by PML. Stabilizes TERF1 protein by preventing its ubiquitination and hence proteasomal degradation. Does so by interfering with TERF1-binding to FBXO4 E3 ubiquitin-protein ligase. Required for cell proliferation. By stabilizing TRF1 protein during mitosis, promotes metaphase-to-anaphase transition. Stabilizes MDM2 protein by preventing its ubiquitination, and hence proteasomal degradation. By acting on MDM2, may affect TP53 activity. Required for normal processing of ribosomal pre-rRNA. Binds GTP

Protein Sequence

10 MMKLRHKNKK 20 PGEGSKGHKK 30 ISWPYPQPAK 40 QNGKKATSKV 50 PSAPHFVHPN 60 DHANREAELK 70 KKWVEEMREK 80 QQAAREQERQ 90 KRRTIESYCQ 100 DVLRRQEEFE 110 HKEEVLQELN 120 MFPQLDDEAT 130 RKAYYKEFRK 140 VVEYSDVILE 150 VLDARDPLGC 160 RCFQMEEAVL 170 RAQGNKKLVL 180 VLNKIDLVPK 190 EVVEKWLDYL 200 RNELPTVAFK 210 ASTQHQVKNL 220 NRCSVPVDQA 230 SESLLKSKAC 240 FGAENLMRVL 250 GNYCRLGEVR 260 THIRVGVVGL 270 PNVGKSSLIN 280 SLKRSRACSV 290 GAVPGITKFM 300 QEVYLDKFIR 310 LLDAPGIVPG 320 PNSEVGTILR 330 NCVHVQKLAD 340 PVTPVETILQ 350 RCNLEEISNY 360 YGVSGFQTTE 370 HFLTAVAHRL 380 GKKKKGGLYS 390 QEQAAKAVLA 400 DWVSGKISFY 410 IPPPATHTLP 420 THLSAEIVKE 430 MTEVFDIEDT 440 EQANEDTMEC 450 LATGESDELL 460 GDTDPLEMEI 470 KLLHSPMTKI 480 ADAIENKTTV 490 YKIGDLTGYC 500 TNPNRHQMGW 510 AKRNVDHRPK 520 SNSMVDVCSV 530 DRRSVLQRIM 540 ETDPLQQGQA 550 LASALKNKKK 560 MQKRADKIAS 570 KLSDSMMSAL 580 DLSGNADDGV GD

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0016020	membrane
Cellular Component	GO:0005730	nucleolus
Cellular Component	GO:0005697	telomerase holoenzyme complex
Molecular Function	GO:0005525	GTP binding
Molecular Function	GO:0003723	RNA binding
Biological Process	GO:0033234	negative regulation of protein sumoylation
Biological Process	GO:0031397	negative regulation of protein ubiquitination
Biological Process	GO:0032211	negative regulation of telomere maintenance via telomerase
Biological Process	GO:1904816	positive regulation of protein localization to chromosome, telomeric region
Biological Process	GO:0031334	positive regulation of protein-containing complex assembly
Biological Process	GO:0031647	regulation of protein stability
Biological Process	GO:0042254	ribosome biogenesis

Reference

[1] 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.

[2] 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.