Search Results

Overview

Uniprot IDQ8N3X1
Protein NameFormin-binding protein 4
Gene NameFNBP4
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
290 TISVSSSKSGPVIAK
297 KSGPVIAKREVKKEV
348 WRRKVICKEEPVSEV
792 STKGIKRKATEISTA
942 KAKKSKTKMPSLVKK
948 TKMPSLVKKWQSIQR
949 KMPSLVKKWQSIQRE

Function

No function data available.

Protein Sequence

10 MGKKSRAVPG 20 RRPILQLSPP 30 GPRGSTPGRD 40 PEPEPDTEPD 50 STAAVPSQPA 60 PSAATTTTTA 70 VTAAAASDDS 80 PSEDEQEAVQ 90 EVPRVVQNPP 100 KPVMTTRPTA 110 VKATGGLCLL 120 GAYADSDDDD 130 NDVSEKLAQS 140 KETNGNQSTD 150 IDSTLANFLA 160 EIDAITAPQP 170 AAPVGASAPP 180 PTPPRPEPKE 190 AATSTLSSST 200 SNGTDSTQTS 210 GWQYDTQCSL 220 AGVGIEMGDW 230 QEVWDENTGC 240 YYYWNTQTNE 250 VTWELPQYLA 260 TQVQGLQHYQ 270 PSSVPGAETS 280 FVVNTDIYSK 290 EKTISVSSSK 300 SGPVIAKREV 310 KKEVNEGIQA 320 LSNSEEEKKG 330 VAASLLAPLL 340 PEGIKEEEER 350 WRRKVICKEE 360 PVSEVKETST 370 TVEEATTIVK 380 PQEIMLDNIE 390 DPSQEDLCSV 400 VQSGESEEEE 410 EQDTLELELV 420 LERKKAELRA 430 LEEGDGSVSG 440 SSPRSDISQP 450 ASQDGMRRLM 460 SKRGKWKMFV 470 RATSPESTSR 480 SSSKTGRDTP 490 ENGETAIGAE 500 NSEKIDENSD 510 KEMEVEESPE 520 KIKVQTTPKV 530 EEEQDLKFQI 540 GELANTLTSK 550 FEFLGINRQS 560 ISNFHVLLLQ 570 TETRIADWRE 580 GALNGNYLKR 590 KLQDAAEQLK 600 QYEINATPKG 610 WSCHWDRDHR 620 RYFYVNEQSG 630 ESQWEFPDGE 640 EEEEESQAQE 650 NRDETLAKQT 660 LKDKTGTDSN 670 STESSETSTG 680 SLCKESFSGQ 690 VSSSSLMPLT 700 PFWTLLQSNV 710 PVLQPPLPLE 720 MPPPPPPPPE 730 SPPPPPPPPP 740 PAEDGEIQEV 750 EMEDEGSEEP 760 PAPGTEEDTP 770 LKPSAQTTVV 780 TSQSSVDSTI 790 SSSSSTKGIK 800 RKATEISTAV 810 VQRSATIGSS 820 PVLYSQSAIA 830 TGHQAAGIGN 840 QATGIGHQTI 850 PVSLPAAGMG 860 HQARGMSLQS 870 NYLGLAAAPA 880 IMSYAECSVP 890 IGVTAPSLQP 900 VQARGAVPTA 910 TIIEPPPPPP 920 PPPPPPPPAP 930 KMPPPEKTKK 940 GRKDKAKKSK 950 TKMPSLVKKW 960 QSIQRELDEE 970 DNSSSSEEDR 980 ESTAQKRIEE 990 WKQQQLVSGM 1000 AERNANFEAL 1010 PEDWRARLKR RKMAPNT

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005654 nucleoplasm

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] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[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.