Search Results

Overview

Uniprot IDQ9H3P2
Protein NameNegative elongation factor A
Gene NameNELFA
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
190 TETAQQLKRSAGVPF
215 MDTTTPLKGIPKQAP
276 REAKRRRKTLDAEVV
371 PTLPAQFKQRAPMYN
429 PAQQQPKKNLSLTRE

Function

Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex

Protein Sequence

10 MASMRESDTG 20 LWLHNKLGAT 30 DELWAPPSIA 40 SLLTAAVIDN 50 IRLCFHGLSS 60 AVKLKLLLGT 70 LHLPRRTVDE 80 MKGALMEIIQ 90 LASLDSDPWV 100 LMVADILKSF 110 PDTGSLNLEL 120 EEQNPNVQDI 130 LGELREKVGE 140 CEASAMLPLE 150 CQYLNKNALT 160 TLAGPLTPPV 170 KHFQLKRKPK 180 SATLRAELLQ 190 KSTETAQQLK 200 RSAGVPFHAK 210 GRGLLRKMDT 220 TTPLKGIPKQ 230 APFRSPTAPS 240 VFSPTGNRTP 250 IPPSRTLLRK 260 ERGVKLLDIS 270 ELDMVGAGRE 280 AKRRRKTLDA 290 EVVEKPAKEE 300 TVVENATPDY 310 AAGLVSTQKL 320 GSLNNEPALP 330 STSYLPSTPS 340 VVPASSYIPS 350 SETPPAPSSR 360 EASRPPEEPS 370 APSPTLPAQF 380 KQRAPMYNSG 390 LSPATPTPAA 400 PTSPLTPTTP 410 PAVAPTTQTP 420 PVAMVAPQTQ 430 APAQQQPKKN 440 LSLTREQMFA 450 AQEMFKTANK 460 VTRPEKALIL 470 GFMAGSRENP 480 CQEQGDVIQI 490 KLSEHTEDLP 500 KADGQGSTTM 510 LVDTVFEMNY 520 ATGQWTRFKK YKPMTNVS

Gene Ontology

Classification GO ID Description
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:0060090 molecular adaptor activity
Biological Process GO:0034244 negative regulation of transcription elongation by RNA polymerase II
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] 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.