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Overview

Uniprot IDP35637
Protein NameRNA-binding protein FUS
Gene NameFUS
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
264 SDRGGFNKFGGPRDQ
312 FKQIGIIKTNKKTGQ
316 GIIKTNKKTGQPMIN
334 DRETGKLKGEATVSF
365 EFSGNPIKVSFATRR
510 RGGFGPGKMDSRGEH

Function

DNA/RNA-binding protein that plays a role in various cellular processes such as transcription regulation, RNA splicing, RNA transport, DNA repair and damage response (PubMed:27731383). Binds to ssRNA containing the consensus sequence 5'-AGGUAA-3' (PubMed:21256132). Binds to nascent pre-mRNAs and acts as a molecular mediator between RNA polymerase II and U1 small nuclear ribonucleoprotein thereby coupling transcription and splicing (PubMed:26124092). Also binds its own pre-mRNA and autoregulates its expression; this autoregulation mechanism is mediated by non-sense-mediated decay (PubMed:24204307). Plays a role in DNA repair mechanisms by promoting D-loop formation and homologous recombination during DNA double-strand break repair (PubMed:10567410). In neuronal cells, plays crucial roles in dendritic spine formation and stability, RNA transport, mRNA stability and synaptic homeostasis (By similarity)

Protein Sequence

10 MASNDYTQQA 20 TQSYGAYPTQ 30 PGQGYSQQSS 40 QPYGQQSYSG 50 YSQSTDTSGY 60 GQSSYSSYGQ 70 SQNTGYGTQS 80 TPQGYGSTGG 90 YGSSQSSQSS 100 YGQQSSYPGY 110 GQQPAPSSTS 120 GSYGSSSQSS 130 SYGQPQSGSY 140 SQQPSYGGQQ 150 QSYGQQQSYN 160 PPQGYGQQNQ 170 YNSSSGGGGG 180 GGGGGNYGQD 190 QSSMSSGGGS 200 GGGYGNQDQS 210 GGGGSGGYGQ 220 QDRGGRGRGG 230 SGGGGGGGGG 240 GYNRSSGGYE 250 PRGRGGGRGG 260 RGGMGGSDRG 270 GFNKFGGPRD 280 QGSRHDSEQD 290 NSDNNTIFVQ 300 GLGENVTIES 310 VADYFKQIGI 320 IKTNKKTGQP 330 MINLYTDRET 340 GKLKGEATVS 350 FDDPPSAKAA 360 IDWFDGKEFS 370 GNPIKVSFAT 380 RRADFNRGGG 390 NGRGGRGRGG 400 PMGRGGYGGG 410 GSGGGGRGGF 420 PSGGGGGGGQ 430 QRAGDWKCPN 440 PTCENMNFSW 450 RNECNQCKAP 460 KPDGPGGGPG 470 GSHMGGNYGD 480 DRRGGRGGYD 490 RGGYRGRGGD 500 RGGFRGGRGG 510 GDRGGFGPGK 520 MDSRGEHRQD RRERPY

Gene Ontology

Classification GO ID Description
Molecular Function GO:0008270 zinc ion binding
Cellular Component GO:0098982 GABA-ergic synapse
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0099524 postsynaptic cytosol
Cellular Component GO:0099523 presynaptic cytosol
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0140693 molecular condensate scaffold activity
Molecular Function GO:0003730 mRNA 3'-UTR binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003713 transcription coactivator activity
Molecular Function GO:0003712 transcription coregulator activity
Biological Process GO:1990000 amyloid fibril formation
Biological Process GO:0140694 membraneless organelle assembly
Biological Process GO:0048255 mRNA stabilization
Biological Process GO:1905168 positive regulation of double-strand break repair via homologous recombination
Biological Process GO:0051260 protein homooligomerization
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:0043484 regulation of RNA splicing
Biological Process GO:0006357 regulation of transcription by RNA polymerase II
Biological Process GO:0008380 RNA splicing

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] 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.

[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.