Search Results

Overview

Uniprot IDP32455
Protein NameGuanylate-binding protein 1
Gene NameGBP1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
215 LKKGTSQKDETFNLP
246 DRPVHRRKLAQLEKL
280 IFSNSKTKTLSGGIQ
439 GYRLFVQKLQDLKKK
446 KLQDLKKKYYEEPRK
468 LQTYLKSKESMTDAI
485 TDQTLTEKEKEIEVE
573 QKESRIMKNEIQDLQ
582 EIQDLQTKMRRRKAC
63 NKLAGKKKGFSLGST

Function

Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens (PubMed:16511497, PubMed:22106366, PubMed:29144452, PubMed:31268602, PubMed:32510692, PubMed:32581219, PubMed:37797010, PubMed:7512561). Hydrolyzes GTP to GMP in two consecutive cleavage reactions: GTP is first hydrolyzed to GDP and then to GMP in a processive manner (PubMed:16511497, PubMed:32510692, PubMed:7512561, PubMed:39394410). Following infection, recruited to the pathogen-containing vacuoles or vacuole-escaped bacteria and promotes both inflammasome assembly and autophagy (PubMed:29144452, PubMed:31268602). Acts as a positive regulator of inflammasome assembly by facilitating the detection of inflammasome ligands from pathogens (PubMed:31268602, PubMed:32510692, PubMed:32581219). Involved in the lysis of pathogen-containing vacuoles, releasing pathogens into the cytosol (By similarity). Following pathogen release in the cytosol, forms a protein coat in a GTPase-dependent manner that encapsulates pathogens and promotes the detection of ligands by pattern recognition receptors (PubMed:32510692, PubMed:32581219). Plays a key role in inflammasome assembly in response to infection by Gram-negative bacteria: following pathogen release in the cytosol, forms a protein coat that encapsulates Gram-negative bacteria and directly binds to lipopolysaccharide (LPS), disrupting the O-antigen barrier and unmasking lipid A that is that detected by the non-canonical inflammasome effector CASP4/CASP11 (PubMed:32510692, PubMed:32581219). Also promotes recruitment of proteins that mediate bacterial cytolysis, leading to release double-stranded DNA (dsDNA) that activates the AIM2 inflammasome (PubMed:31268602). Involved in autophagy by regulating bacteriolytic peptide generation via its interaction with ubiquitin-binding protein SQSTM1, which delivers monoubiquitinated proteins to autolysosomes for the generation of bacteriolytic peptides (By similarity). Confers protection to several pathogens, including the bacterial pathogens L.monocytogenes and M.bovis BCG as well as the protozoan pathogen T.gondii (PubMed:31268602). Exhibits antiviral activity against influenza virus (PubMed:22106366)

Protein Sequence

10 MASEIHMTGP 20 MCLIENTNGR 30 LMANPEALKI 40 LSAITQPMVV 50 VAIVGLYRTG 60 KSYLMNKLAG 70 KKKGFSLGST 80 VQSHTKGIWM 90 WCVPHPKKPG 100 HILVLLDTEG 110 LGDVEKGDNQ 120 NDSWIFALAV 130 LLSSTFVYNS 140 IGTINQQAMD 150 QLYYVTELTH 160 RIRSKSSPDE 170 NENEVEDSAD 180 FVSFFPDFVW 190 TLRDFSLDLE 200 ADGQPLTPDE 210 YLTYSLKLKK 220 GTSQKDETFN 230 LPRLCIRKFF 240 PKKKCFVFDR 250 PVHRRKLAQL 260 EKLQDEELDP 270 EFVQQVADFC 280 SYIFSNSKTK 290 TLSGGIQVNG 300 PRLESLVLTY 310 VNAISSGDLP 320 CMENAVLALA 330 QIENSAAVQK 340 AIAHYEQQMG 350 QKVQLPTETL 360 QELLDLHRDS 370 EREAIEVFIR 380 SSFKDVDHLF 390 QKELAAQLEK 400 KRDDFCKQNQ 410 EASSDRCSAL 420 LQVIFSPLEE 430 EVKAGIYSKP 440 GGYRLFVQKL 450 QDLKKKYYEE 460 PRKGIQAEEI 470 LQTYLKSKES 480 MTDAILQTDQ 490 TLTEKEKEIE 500 VERVKAESAQ 510 ASAKMLQEMQ 520 RKNEQMMEQK 530 ERSYQEHLKQ 540 LTEKMENDRV 550 QLLKEQERTL 560 ALKLQEQEQL 570 LKEGFQKESR 580 IMKNEIQDLQ 590 TKMRRRKACT IS

Gene Ontology

Classification GO ID Description
Biological Process GO:0071347 cellular response to interleukin-1
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0031410 cytoplasmic vesicle
Cellular Component GO:0030659 cytoplasmic vesicle membrane
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005794 Golgi apparatus
Cellular Component GO:0000139 Golgi membrane
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0106139 symbiont cell surface
Cellular Component GO:0012506 vesicle membrane
Molecular Function GO:0003779 actin binding
Molecular Function GO:0019955 cytokine binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0003925 G protein activity
Molecular Function GO:0019003 GDP binding
Molecular Function GO:0004382 GDP phosphatase activity
Molecular Function GO:0005525 GTP binding
Molecular Function GO:0003924 GTPase activity
Molecular Function GO:0051879 Hsp90 protein binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0001530 lipopolysaccharide binding
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0030507 spectrin binding
Biological Process GO:0071356 cellular response to tumor necrosis factor
Biological Process GO:0071346 cellular response to type II interferon
Biological Process GO:0051715 cytolysis in another organism
Biological Process GO:0042742 defense response to bacterium
Biological Process GO:0042832 defense response to protozoan
Biological Process GO:0051607 defense response to virus
Biological Process GO:0045087 innate immune response
Biological Process GO:0070373 negative regulation of ERK1 and ERK2 cascade
Biological Process GO:0032703 negative regulation of interleukin-2 production
Biological Process GO:1903077 negative regulation of protein localization to plasma membrane
Biological Process GO:1900025 negative regulation of substrate adhesion-dependent cell spreading
Biological Process GO:0050860 negative regulation of T cell receptor signaling pathway
Biological Process GO:0160075 non-canonical inflammasome complex assembly
Biological Process GO:0140639 positive regulation of pyroptotic inflammatory response
Biological Process GO:0072665 protein localization to vacuole
Biological Process GO:0050848 regulation of calcium-mediated signaling
Biological Process GO:1903076 regulation of protein localization to plasma membrane

Reference

[1] 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.

[2] 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.

[3] 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.

[4] 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.

[5] 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.

[6] 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.