Search Results

Overview

Uniprot IDQ96AE4
Protein NameFar upstream element-binding protein 1
Gene NameFUBP1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
161 PESVQSAKRLLDQIV
170 LLDQIVEKGRPAPGF
203 KAGLVIGKGGETIKQ
243 RITGDPYKVQQAKEM
394 KTGLIIGKGGETIKS
44 RARQIAAKIGGDAGT
592 AWEEYYKKMGQAVPA
64 DYGYGGQKRPLEDGD

Function

Regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. May act both as activator and repressor of transcription

Protein Sequence

10 MADYSTVPPP 20 SSGSAGGGGG 30 GGGGGGVNDA 40 FKDALQRARQ 50 IAAKIGGDAG 60 TSLNSNDYGY 70 GGQKRPLEDG 80 DQPDAKKVAP 90 QNDSFGTQLP 100 PMHQQQSRSV 110 MTEEYKVPDG 120 MVGFIIGRGG 130 EQISRIQQES 140 GCKIQIAPDS 150 GGLPERSCML 160 TGTPESVQSA 170 KRLLDQIVEK 180 GRPAPGFHHG 190 DGPGNAVQEI 200 MIPASKAGLV 210 IGKGGETIKQ 220 LQERAGVKMV 230 MIQDGPQNTG 240 ADKPLRITGD 250 PYKVQQAKEM 260 VLELIRDQGG 270 FREVRNEYGS 280 RIGGNEGIDV 290 PIPRFAVGIV 300 IGRNGEMIKK 310 IQNDAGVRIQ 320 FKPDDGTTPE 330 RIAQITGPPD 340 RCQHAAEIIT 350 DLLRSVQAGN 360 PGGPGPGGRG 370 RGRGQGNWNM 380 GPPGGLQEFN 390 FIVPTGKTGL 400 IIGKGGETIK 410 SISQQSGARI 420 ELQRNPPPNA 430 DPNMKLFTIR 440 GTPQQIDYAR 450 QLIEEKIGGP 460 VNPLGPPVPH 470 GPHGVPGPHG 480 PPGPPGPGTP 490 MGPYNPAPYN 500 PGPPGPAPHG 510 PPAPYAPQGW 520 GNAYPHWQQQ 530 APPDPAKAGT 540 DPNSAAWAAY 550 YAHYYQQQAQ 560 PPPAAPAGAP 570 TTTQTNGQGD 580 QQNPAPAGQV 590 DYTKAWEEYY 600 KKMGQAVPAP 610 TGAPPGGQPD 620 YSAAWAEYYR 630 QQAAYYAQTS 640 PQGMPQHPPA PQGQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003730 mRNA 3'-UTR binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003697 single-stranded DNA binding
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0010628 positive regulation of gene expression
Biological Process GO:0006357 regulation of transcription by RNA polymerase II

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] 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.

[4] 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.

[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.