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Overview

Uniprot IDQ14684
Protein NameRibosomal RNA processing protein 1 homolog B
Gene NameRRP1B
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
269 KKKTALGKNHSRKDG
314 LLEMTSRKNTPHFNR
369 KHKKKGNKLLEKTNL
373 KGNKLLEKTNLEKEK
398 DSESSLQKRRRKKKK
406 RRRKKKKKHHLQPEN
522 TGGAQLLKRKRKLGV
574 RRRLQKKKAGPGSLE
589 LCGLPSQKTASLKKR
632 SGTCSSLKKQKLRAE
633 GTCSSLKKQKLRAES
660 PLFFRRAKSSTATHP
676 GPAVQLNKTPSSSKK
683 KTPSSSKKVTFGLNR
701 AEFKKTDKSILVSPT
720 VAFDPEQKPLHGVLK
727 KPLHGVLKTPTSSPA
741 ASSPLVAKKPLTTTP
742 SSPLVAKKPLTTTPR

Function

Positively regulates DNA damage-induced apoptosis by acting as a transcriptional coactivator of proapoptotic target genes of the transcriptional activator E2F1 (PubMed:20040599). Likely to play a role in ribosome biogenesis by targeting serine/threonine protein phosphatase PP1 to the nucleolus (PubMed:20926688). Involved in regulation of mRNA splicing (By similarity). Inhibits SIPA1 GTPase activity (By similarity). Involved in regulating expression of extracellular matrix genes (By similarity). Associates with chromatin and may play a role in modulating chromatin structure (PubMed:19710015)

Protein Sequence

10 MAPAMQPAEI 20 QFAQRLASSE 30 KGIRDRAVKK 40 LRQYISVKTQ 50 RETGGFSQEE 60 LLKIWKGLFY 70 CMWVQDEPLL 80 QEELANTIAQ 90 LVHAVNNSAA 100 QHLFIQTFWQ 110 TMNREWKGID 120 RLRLDKYYML 130 IRLVLRQSFE 140 VLKRNGWEES 150 RIKVFLDVLM 160 KEVLCPESQS 170 PNGVRFHFID 180 IYLDELSKVG 190 GKELLADQNL 200 KFIDPFCKIA 210 AKTKDHTLVQ 220 TIARGVFEAI 230 VDQSPFVPEE 240 TMEEQKTKVG 250 DGDLSAEEIP 260 ENEVSLRRAV 270 SKKKTALGKN 280 HSRKDGLSDE 290 RGRDDCGTFE 300 DTGPLLQFDY 310 KAVADRLLEM 320 TSRKNTPHFN 330 RKRLSKLIKK 340 FQDLSEGSSI 350 SQLSFAEDIS 360 ADEDDQILSQ 370 GKHKKKGNKL 380 LEKTNLEKEK 390 GSRVFCVEEE 400 DSESSLQKRR 410 RKKKKKHHLQ 420 PENPGPGGAA 430 PSLEQNRGRE 440 PEASGLKALK 450 ARVAEPGAEA 460 TSSTGEESGS 470 EHPPAVPMHN 480 KRKRPRKKSP 490 RAHREMLESA 500 VLPPEDMSQS 510 GPSGSHPQGP 520 RGSPTGGAQL 530 LKRKRKLGVV 540 PVNGSGLSTP 550 AWPPLQQEGP 560 PTGPAEGANS 570 HTTLPQRRRL 580 QKKKAGPGSL 590 ELCGLPSQKT 600 ASLKKRKKMR 610 VMSNLVEHNG 620 VLESEAGQPQ 630 ALGSSGTCSS 640 LKKQKLRAES 650 DFVKFDTPFL 660 PKPLFFRRAK 670 SSTATHPPGP 680 AVQLNKTPSS 690 SKKVTFGLNR 700 NMTAEFKKTD 710 KSILVSPTGP 720 SRVAFDPEQK 730 PLHGVLKTPT 740 SSPASSPLVA 750 KKPLTTTPRR RPRAMDFF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005694 chromosome
Cellular Component GO:0005829 cytosol
Cellular Component GO:0000791 euchromatin
Cellular Component GO:0001652 granular component
Cellular Component GO:0000792 heterochromatin
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0030688 preribosome, small subunit precursor
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0003713 transcription coactivator activity
Biological Process GO:0006915 apoptotic process
Biological Process GO:0098586 cellular response to virus
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0043923 host-mediated activation of viral transcription
Biological Process GO:0006397 mRNA processing
Biological Process GO:0034260 negative regulation of GTPase activity
Biological Process GO:0043065 positive regulation of apoptotic process
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0043484 regulation of RNA splicing
Biological Process GO:0006357 regulation of transcription by RNA polymerase II
Biological Process GO:0008380 RNA splicing
Biological Process GO:0006364 rRNA processing

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] 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.

[3] 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.

[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] 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.