Search Results

Overview

Uniprot IDQ92945
Protein NameFar upstream element-binding protein 2
Gene NameKHSRP
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
109 DFGFGGQKRQLEDGD
121 DGDQPESKKLASQGD
122 GDQPESKKLASQGDS
169 RGGEQINKIQQDSGC
177 IQQDSGCKVQISPDS
203 GAPESVQKAKMMLDD
205 PESVQKAKMMLDDIV
251 KAGLVIGKGGETIKQ
347 RSGEMIKKIQNDAGV
627 KAWEEYYKKIGQQPQ
628 AWEEYYKKIGQQPQQ
71 GGGPGIRKDAFADAV
87 RARQIAAKIGGDAAT

Function

Binds to the dendritic targeting element and may play a role in mRNA trafficking (By similarity). Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting degradation machinery to ARE-containing mRNAs

Protein Sequence

10 MSDYSTGGPP 20 PGPPPPAGGG 30 GGAGGAGGGP 40 PPGPPGAGDR 50 GGGGPGGGGP 60 GGGSAGGPSQ 70 PPGGGGPGIR 80 KDAFADAVQR 90 ARQIAAKIGG 100 DAATTVNNST 110 PDFGFGGQKR 120 QLEDGDQPES 130 KKLASQGDSI 140 SSQLGPIHPP 150 PRTSMTEEYR 160 VPDGMVGLII 170 GRGGEQINKI 180 QQDSGCKVQI 190 SPDSGGLPER 200 SVSLTGAPES 210 VQKAKMMLDD 220 IVSRGRGGPP 230 GQFHDNANGG 240 QNGTVQEIMI 250 PAGKAGLVIG 260 KGGETIKQLQ 270 ERAGVKMILI 280 QDGSQNTNVD 290 KPLRIIGDPY 300 KVQQACEMVM 310 DILRERDQGG 320 FGDRNEYGSR 330 IGGGIDVPVP 340 RHSVGVVIGR 350 SGEMIKKIQN 360 DAGVRIQFKQ 370 DDGTGPEKIA 380 HIMGPPDRCE 390 HAARIINDLL 400 QSLRSGPPGP 410 PGGPGMPPGG 420 RGRGRGQGNW 430 GPPGGEMTFS 440 IPTHKCGLVI 450 GRGGENVKAI 460 NQQTGAFVEI 470 SRQLPPNGDP 480 NFKLFIIRGS 490 PQQIDHAKQL 500 IEEKIEGPLC 510 PVGPGPGGPG 520 PAGPMGPFNP 530 GPFNQGPPGA 540 PPHAGGPPPH 550 QYPPQGWGNT 560 YPQWQPPAPH 570 DPSKAAAAAA 580 DPNAAWAAYY 590 SHYYQQPPGP 600 VPGPAPAPAA 610 PPAQGEPPQP 620 PPTGQSDYTK 630 AWEEYYKKIG 640 QQPQQPGAPP 650 QQDYTKAWEE 660 YYKKQAQVAT 670 GGGPGAPPGS 680 QPDYSAAWAE 690 YYRQQAAYYG 700 QTPGPGGPQP 710 PPTQQGQQQA Q

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0016020 membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0035925 mRNA 3'-UTR AU-rich region binding
Molecular Function GO:0003730 mRNA 3'-UTR binding
Molecular Function GO:0044183 protein folding chaperone
Molecular Function GO:0003723 RNA binding
Biological Process GO:0061158 3'-UTR-mediated mRNA destabilization
Biological Process GO:0071345 cellular response to cytokine stimulus
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0010586 miRNA metabolic process
Biological Process GO:0006397 mRNA processing
Biological Process GO:0051028 mRNA transport
Biological Process GO:0010989 negative regulation of low-density lipoprotein particle clearance
Biological Process GO:0045019 negative regulation of nitric oxide biosynthetic process
Biological Process GO:0061014 positive regulation of mRNA catabolic process
Biological Process GO:0006355 regulation of DNA-templated transcription
Biological Process GO:0043488 regulation of mRNA stability
Biological Process GO:0008380 RNA splicing
Biological Process GO:0000375 RNA splicing, via transesterification reactions

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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[5] 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.

[6] 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.

[7] 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.

[8] 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.

[9] 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.

[10] 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.

[11] 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.