Search Results

Overview

Uniprot IDP18615
Protein NameNegative elongation factor E
Gene NameNELFE
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
130 SSRRPQRKSLYESFV
260 PERRAPRKGNTLYVY
27 NKLKKKKKALLALKK
33 KKALLALKKQSSSST
34 KALLALKKQSSSSTT
355 LAVQNSPKGCHRDKR
70 EQAKQLVKSGAISAI
78 SGAISAIKAETKNSG
82 SAIKAETKNSGFKRS
95 RSRTLEGKLKDPEKG
97 RTLEGKLKDPEKGPV

Function

Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II (PubMed:10199401, PubMed:27256882). The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex (PubMed:11940650, PubMed:12612062, PubMed:27256882). Provides the strongest RNA binding activity of the NELF complex and may initially recruit the NELF complex to RNA (PubMed:18303858, PubMed:27256882, PubMed:27282391)

Protein Sequence

10 MLVIPPGLSE 20 EEEALQKKFN 30 KLKKKKKALL 40 ALKKQSSSST 50 TSQGGVKRSL 60 SEQPVMDTAT 70 ATEQAKQLVK 80 SGAISAIKAE 90 TKNSGFKRSR 100 TLEGKLKDPE 110 KGPVPTFQPF 120 QRSISADDDL 130 QESSRRPQRK 140 SLYESFVSSS 150 DRLRELGPDG 160 EEAEGPGAGD 170 GPPRSFDWGY 180 EERSGAHSSA 190 SPPRSRSRDR 200 SHERNRDRDR 210 DRERDRDRDR 220 DRDRERDRDR 230 DRDRDRDRER 240 DRDRERDRDR 250 DREGPFRRSD 260 SFPERRAPRK 270 GNTLYVYGED 280 MTPTLLRGAF 290 SPFGNIIDLS 300 MDPPRNCAFV 310 TYEKMESADQ 320 AVAELNGTQV 330 ESVQLKVNIA 340 RKQPMLDAAT 350 GKSVWGSLAV 360 QNSPKGCHRD 370 KRTQIVYSDD 380 VYKENLVDGF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0032021 NELF complex
Cellular Component GO:0016604 nuclear body
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0034244 negative regulation of transcription elongation by RNA polymerase II
Biological Process GO:0070374 positive regulation of ERK1 and ERK2 cascade
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0160239 transcription pausing 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] 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] 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] 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.

[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.