Search Results

Overview

Uniprot IDQ92541
Protein NameRNA polymerase-associated protein RTF1 homolog
Gene NameRTF1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
251 EEEQEKKKLTQIQES
265 SQVTSHNKERRSKRD
278 RDEKLDKKSQAMEEL
302 RTAELLAKKQPLKTS
303 TAELLAKKQPLKTSE
504 KEKERFRKAPPNYAM
520 KTQLLKEKAMAEDLG
555 ALDRQRTKNISAISY
685 KALAITSKAPPAKDG
690 TSKAPPAKDGAPRRS
705 LNLEDYKKRRGLI**

Function

Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Binds single-stranded DNA. Required for maximal induction of heat-shock genes. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of a SET1 complex (By similarity)

Protein Sequence

10 MRGRLCVGRA 20 AAAAAAVAVP 30 LAGGQEGSPG 40 GGRRGSRGTT 50 MVKKRKGRVV 60 IDSDTEDSGS 70 DENLDQELLS 80 LAKRKRSDSE 90 EKEPPVSQPA 100 ASSDSETSDS 110 DDEWTFGSNK 120 NKKKGKARKI 130 EKKGTMKKQA 140 NKTASSGSSD 150 KDSSAESSAP 160 EEGEVSDSDS 170 NSSSSSSDSD 180 SSSEDEEFHD 190 GYGEDLMGDE 200 EDRARLEQMT 210 EKEREQELFN 220 RIEKREVLKR 230 RFEIKKKLKT 240 AKKKEKKEKK 250 KKQEEEQEKK 260 KLTQIQESQV 270 TSHNKERRSK 280 RDEKLDKKSQ 290 AMEELKAERE 300 KRKNRTAELL 310 AKKQPLKTSE 320 VYSDDEEEEE 330 DDKSSEKSDR 340 SSRTSSSDEE 350 EEKEEIPPKS 360 QPVSLPEELN 370 RVRLSRHKLE 380 RWCHMPFFAK 390 TVTGCFVRIG 400 IGNHNSKPVY 410 RVAEITGVVE 420 TAKVYQLGGT 430 RTNKGLQLRH 440 GNDQRVFRLE 450 FVSNQEFTES 460 EFMKWKEAMF 470 SAGMQLPTLD 480 EINKKELSIK 490 EALNYKFNDQ 500 DIEEIVKEKE 510 RFRKAPPNYA 520 MKKTQLLKEK 530 AMAEDLGDQD 540 KAKQIQDQLN 550 ELEERAEALD 560 RQRTKNISAI 570 SYINQRNREW 580 NIVESEKALV 590 AESHNMKNQQ 600 MDPFTRRQCK 610 PTIVSNSRDP 620 AVQAAILAQL 630 NAKYGSGVLP 640 DAPKEMSKGQ 650 GKDKDLNSKS 660 ASDLSEDLFK 670 VHDFDVKIDL 680 QVPSSESKAL 690 AITSKAPPAK 700 DGAPRRSLNL 710 EDYKKRRGLI

Gene Ontology

Classification GO ID Description
Molecular Function GO:0003723 RNA binding
Cellular Component GO:0016593 Cdc73/Paf1 complex
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003697 single-stranded DNA binding
Biological Process GO:0006325 chromatin organization
Biological Process GO:0001711 endodermal cell fate commitment
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0019827 stem cell population maintenance
Biological Process GO:0006368 transcription elongation by RNA polymerase II
Biological Process GO:0016055 Wnt signaling pathway

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] 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.

[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] 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.

[8] 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.