Search Results

Overview

Uniprot IDQ9UHX1
Protein NamePoly(U)-binding-splicing factor PUF60
Gene NamePUF60
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
168 SWDSVTMKHKGFAFV
253 FEAFGKIKSCTLARD
454 ARHMVMQKLLRKQES
458 VMQKLLRKQESTVMV
541 GRWFAGRKVVAEVYD
72 EALQKAKKYAMEQSI
80 YAMEQSIKSVLVKQT

Function

DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation. In association with FUBP1 regulates MYC transcription at the P2 promoter through the core-TFIIH basal transcription factor. Acts as a transcriptional repressor through the core-TFIIH basal transcription factor. Represses FUBP1-induced transcriptional activation but not basal transcription. Decreases ERCC3 helicase activity. Does not repress TFIIH-mediated transcription in xeroderma pigmentosum complementation group B (XPB) cells. Is also involved in pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice site and pyrimidine tract in a cooperative manner with U2AF2. Involved in apoptosis induction when overexpressed in HeLa cells. Isoform 6 failed to repress MYC transcription and inhibited FIR-induced apoptosis in colorectal cancer. Isoform 6 may contribute to tumor progression by enabling increased MYC expression and greater resistance to apoptosis in tumors than in normal cells. Modulates alternative splicing of several mRNAs. Binds to relaxed DNA of active promoter regions. Binds to the pyrimidine tract and 3'-splice site regions of pre-mRNA; binding is enhanced in presence of U2AF2. Binds to Y5 RNA in association with RO60. Binds to poly(U) RNA

Protein Sequence

10 MATATIALQV 20 NGQQGGGSEP 30 AAAAAVVAAG 40 DKWKPPQGTD 50 SIKMENGQST 60 AAKLGLPPLT 70 PEQQEALQKA 80 KKYAMEQSIK 90 SVLVKQTIAH 100 QQQQLTNLQM 110 AAVTMGFGDP 120 LSPLQSMAAQ 130 RQRALAIMCR 140 VYVGSIYYEL 150 GEDTIRQAFA 160 PFGPIKSIDM 170 SWDSVTMKHK 180 GFAFVEYEVP 190 EAAQLALEQM 200 NSVMLGGRNI 210 KVGRPSNIGQ 220 AQPIIDQLAE 230 EARAFNRIYV 240 ASVHQDLSDD 250 DIKSVFEAFG 260 KIKSCTLARD 270 PTTGKHKGYG 280 FIEYEKAQSS 290 QDAVSSMNLF 300 DLGGQYLRVG 310 KAVTPPMPLL 320 TPATPGGLPP 330 AAAVAAAAAT 340 AKITAQEAVA 350 GAAVLGTLGT 360 PGLVSPALTL 370 AQPLGTLPQA 380 VMAAQAPGVI 390 TGVTPARPPI 400 PVTIPSVGVV 410 NPILASPPTL 420 GLLEPKKEKE 430 EEELFPESER 440 PEMLSEQEHM 450 SISGSSARHM 460 VMQKLLRKQE 470 STVMVLRNMV 480 DPKDIDDDLE 490 GEVTEECGKF 500 GAVNRVIIYQ 510 EKQGEEEDAE 520 IIVKIFVEFS 530 IASETHKAIQ 540 ALNGRWFAGR 550 KVVAEVYDQE RFDNSDLSA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:1990904 ribonucleoprotein complex
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0000380 alternative mRNA splicing, via spliceosome
Biological Process GO:0006915 apoptotic process
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006376 mRNA splice site recognition
Biological Process GO:0000381 regulation of alternative mRNA splicing, via spliceosome

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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[5] 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.

[6] 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.

[7] 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.

[8] 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.

[9] 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.