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Overview

Uniprot IDP60002
Protein NameTranscription elongation factor 1 homolog
Gene NameELOF1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
15 RKPPPKKKMTGTLET

Function

Factor involved in transcription-coupled nucleotide excision repair (TC-NER), a mechanism that rapidly removes RNA polymerase II-blocking lesions from the transcribed strand of active genes (PubMed:34108662, PubMed:34108663, PubMed:38316879). Acts as a key adapter required to anchor TC-NER factors to RNA polymerase II: stably positions UVSSA and the DCX(ERCC8) complex (also named CSA complex) on arrested RNA polymerase II, leading to neddylation and activation of the DCX(ERCC8) complex and ubiquitination of RNA polymerase II (PubMed:38316879)

Protein Sequence

10 MGRRKSKRKP 20 PPKKKMTGTL 30 ETQFTCPFCN 40 HEKSCDVKMD 50 RARNTGVISC 60 TVCLEEFQTP 70 ITYLSEPVDV 80 YSDWIDACEA ANQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005694 chromosome
Cellular Component GO:0005634 nucleus
Cellular Component GO:0008023 transcription elongation factor complex
Molecular Function GO:0030674 protein-macromolecule adaptor activity
Molecular Function GO:0000993 RNA polymerase II complex binding
Biological Process GO:0006368 transcription elongation by RNA polymerase II
Biological Process GO:0006283 transcription-coupled nucleotide-excision repair

Reference

[1] 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.

[2] 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.