Search Results

Overview

Uniprot ID	Q13523
Protein Name	Serine/threonine-protein kinase PRP4 homolog
Gene Name	PRP4K
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
168	STRSSSTKGKLELVD
170	RSSSTKGKLELVDNK
177	KLELVDNKITTKKRS
202	RSDKKKSKGGIEIVK
209	KGGIEIVKEKTTRSK
505	KVKEDKFKGSLSEGM
551	QRQAIVQKYKYLAED
553	QAIVQKYKYLAEDSN
608	DTFEASVKAKHNLMT
656	LRAAGIGKDFKENPN
99	MSPAKRTKLDDLALL

Function

Serine/threonine kinase involved in spliceosomal assembly as well as mitosis and signaling regulation (PubMed:10799319, PubMed:12077342, PubMed:17513757, PubMed:17998396). Connects chromatin mediated regulation of transcription and pre-mRNA splicing (PubMed:12077342). During spliceosomal assembly, interacts with and phosphorylates PRPF6 and PRPF31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), to facilitate the formation of the spliceosome B complex. Plays a role in regulating transcription and the spindle assembly checkpoint (SAC) (PubMed:20118938). Associates with U5 snRNP and NCOR1 deacetylase complexes which may allow a coordination of pre-mRNA splicing with chromatin remodeling events involved in transcriptional regulation (PubMed:12077342). Associates and probably phosphorylates SMARCA4 and NCOR1 (PubMed:12077342). Phosphorylates SRSF1 (PubMed:11418604). Associates with kinetochores during mitosis and is necessary for recruitment and maintenance of the checkpoint proteins such as MAD1L1 and MAD12L1 at the kinetochores (PubMed:17998396). Phosphorylates and regulates the activity of the transcription factors such as ELK1 and KLF13 (PubMed:10799319, PubMed:17513757). Phosphorylates nuclear YAP1 and WWTR1/TAZ which induces nuclear exclusion and regulates Hippo signaling pathway, involved in tissue growth control (PubMed:29695716)

Protein Sequence

10 MAAAETQSLR 20 EQPEMEDANS 30 EKSINEENGE 40 VSEDQSQNKH 50 SRHKKKKHKH 60 RSKHKKHKHS 70 SEEDKDKKHK 80 HKHKHKKHKR 90 KEIIDASDKE 100 GMSPAKRTKL 110 DDLALLEDLE 120 KQRALIKAEL 130 DNELMEGKVQ 140 SGMGLILQGY 150 ESGSEEEGEI 160 HEKARNGNRS 170 STRSSSTKGK 180 LELVDNKITT 190 KKRSKSRSKE 200 RTRHRSDKKK 210 SKGGIEIVKE 220 KTTRSKSKER 230 KKSKSPSKRS 240 KSQDQARKSK 250 SPTLRRRSQE 260 KIGKARSPTD 270 DKVKIEDKSK 280 SKDRKKSPII 290 NESRSRDRGK 300 KSRSPVDLRG 310 KSKDRRSRSK 320 ERKSKRSETD 330 KEKKPIKSPS 340 KDASSGKENR 350 SPSRRPGRSP 360 KRRSLSPKPR 370 DKSRRSRSPL 380 LNDRRSKQSK 390 SPSRTLSPGR 400 RAKSRSLERK 410 RREPERRRLS 420 SPRTRPRDDI 430 LSRRERSKDA 440 SPINRWSPTR 450 RRSRSPIRRR 460 SRSPLRRSRS 470 PRRRSRSPRR 480 RDRGRRSRSR 490 LRRRSRSRGG 500 RRRRSRSKVK 510 EDKFKGSLSE 520 GMKVEQESSS 530 DDNLEDFDVE 540 EEDEEALIEQ 550 RRIQRQAIVQ 560 KYKYLAEDSN 570 MSVPSEPSSP 580 QSSTRTRSPS 590 PDDILERVAA 600 DVKEYERENV 610 DTFEASVKAK 620 HNLMTVEQNN 630 GSSQKKLLAP 640 DMFTESDDMF 650 AAYFDSARLR 660 AAGIGKDFKE 670 NPNLRDNWTD 680 AEGYYRVNIG 690 EVLDKRYNVY 700 GYTGQGVFSN 710 VVRARDNARA 720 NQEVAVKIIR 730 NNELMQKTGL 740 KELEFLKKLN 750 DADPDDKFHC 760 LRLFRHFYHK 770 QHLCLVFEPL 780 SMNLREVLKK 790 YGKDVGLHIK 800 AVRSYSQQLF 810 LALKLLKRCN 820 ILHADIKPDN 830 ILVNESKTIL 840 KLCDFGSASH 850 VADNDITPYL 860 VSRFYRAPEI 870 IIGKSYDYGI 880 DMWSVGCTLY 890 ELYTGKILFP 900 GKTNNHMLKL 910 AMDLKGKMPN 920 KMIRKGVFKD 930 QHFDQNLNFM 940 YIEVDKVTER 950 EKVTVMSTIN 960 PTKDLLADLI 970 GCQRLPEDQR 980 KKVHQLKDLL 990 DQILMLDPAK 1000 RISINQALQH AFIQEKI

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0071013	catalytic step 2 spliceosome
Cellular Component	GO:0000776	kinetochore
Cellular Component	GO:0016607	nuclear speck
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Molecular Function	GO:0005524	ATP binding
Molecular Function	GO:0106310	protein serine kinase activity
Molecular Function	GO:0004674	protein serine/threonine kinase activity
Molecular Function	GO:0003723	RNA binding
Biological Process	GO:0045292	mRNA cis splicing, via spliceosome
Biological Process	GO:0000398	mRNA splicing, via spliceosome
Biological Process	GO:0035332	positive regulation of hippo signaling
Biological Process	GO:0046827	positive regulation of protein export from nucleus
Biological Process	GO:0090266	regulation of mitotic cell cycle spindle assembly checkpoint
Biological Process	GO:0000387	spliceosomal snRNP assembly
Biological Process	GO:0000244	spliceosomal tri-snRNP complex assembly
Biological Process	GO:0000388	spliceosome conformational change to release U4 (or U4atac) and U1 (or U11)

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.