Search Results

Overview

Uniprot IDQ8N7H5
Protein NameRNA polymerase II-associated factor 1 homolog
Gene NamePAF1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
119 IQAPTSSKRSQQHAK
126 KRSQQHAKVVPWMRK
133 KVVPWMRKTEYISTE
302 YNWNVKNKASKGYEE
338 RLSKRRAKAGVQSGT
62 QNRFVQYKATSLEKQ

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. Connects PAF1C with the RNF20/40 E3 ubiquitin-protein ligase complex. Involved in polyadenylation of mRNA precursors. Has oncogenic activity in vivo and in vitro

Protein Sequence

10 MAPTIQTQAQ 20 REDGHRPNSH 30 RTLPERSGVV 40 CRVKYCNSLP 50 DIPFDPKFIT 60 YPFDQNRFVQ 70 YKATSLEKQH 80 KHDLLTEPDL 90 GVTIDLINPD 100 TYRIDPNVLL 110 DPADEKLLEE 120 EIQAPTSSKR 130 SQQHAKVVPW 140 MRKTEYISTE 150 FNRYGISNEK 160 PEVKIGVSVK 170 QQFTEEEIYK 180 DRDSQITAIE 190 KTFEDAQKSI 200 SQHYSKPRVT 210 PVEVMPVFPD 220 FKMWINPCAQ 230 VIFDSDPAPK 240 DTSGAAALEM 250 MSQAMIRGMM 260 DEEGNQFVAY 270 FLPVEETLKK 280 RKRDQEEEMD 290 YAPDDVYDYK 300 IAREYNWNVK 310 NKASKGYEEN 320 YFFIFREGDG 330 VYYNELETRV 340 RLSKRRAKAG 350 VQSGTNALLV 360 VKHRDMNEKE 370 LEAQEARKAQ 380 LENHEPEEEE 390 EEEMETEEKE 400 AGGSDEEQEK 410 GSSSEKEGSE 420 DEHSGSESER 430 EEGDRDEASD 440 KSGSGEDESS 450 EDEARAARDK 460 EEIFGSDADS 470 EDDADSDDED 480 RGQAQGGSDN 490 DSDSGSNGGG 500 QRSRSHSRSA 510 SPFPSGSEHS 520 AQEDGSEAAA 530 SDSSEADSDS D

Gene Ontology

Classification GO ID Description
Cellular Component GO:0016593 Cdc73/Paf1 complex
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0001650 fibrillar center
Cellular Component GO:0016020 membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0000993 RNA polymerase II complex binding
Biological Process GO:0071222 cellular response to lipopolysaccharide
Biological Process GO:0001711 endodermal cell fate commitment
Biological Process GO:0031124 mRNA 3'-end processing
Biological Process GO:0045638 negative regulation of myeloid cell differentiation
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:1902808 positive regulation of cell cycle G1/S phase transition
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0034504 protein localization to nucleus
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] 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] 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.

[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] 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.