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Overview

Uniprot IDQ99459
Protein NameCell division cycle 5-like protein
Gene NameCDC5L
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
200 AAGIEIQKKRKRKRG
201 AGIEIQKKRKRKRGV
218 NAEIPFEKKPALGFY
219 AEIPFEKKPALGFYD
271 KQHLKRKKESDLPSA
290 SGVSEFTKKRSKLVL
291 GVSEFTKKRSKLVLP
294 EFTKKRSKLVLPAPQ
447 GRTPLRDKLNINPED
539 KEMKRMHKAVQKDLP
543 RMHKAVQKDLPRPSE
601 PSGNKKGKTVGFGTN
7 *MPRIMIKGGVWRNT

Function

DNA-binding protein involved in cell cycle control. May act as a transcription activator. Plays a role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes (PubMed:11991638, PubMed:20176811, PubMed:28076346, PubMed:28502770, PubMed:29301961, PubMed:29360106, PubMed:29361316, PubMed:30705154, PubMed:30728453). Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR) (PubMed:20176811). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable)

Protein Sequence

10 MPRIMIKGGV 20 WRNTEDEILK 30 AAVMKYGKNQ 40 WSRIASLLHR 50 KSAKQCKARW 60 YEWLDPSIKK 70 TEWSREEEEK 80 LLHLAKLMPT 90 QWRTIAPIIG 100 RTAAQCLEHY 110 EFLLDKAAQR 120 DNEEETTDDP 130 RKLKPGEIDP 140 NPETKPARPD 150 PIDMDEDELE 160 MLSEARARLA 170 NTQGKKAKRK 180 AREKQLEEAR 190 RLAALQKRRE 200 LRAAGIEIQK 210 KRKRKRGVDY 220 NAEIPFEKKP 230 ALGFYDTSEE 240 NYQALDADFR 250 KLRQQDLDGE 260 LRSEKEGRDR 270 KKDKQHLKRK 280 KESDLPSAIL 290 QTSGVSEFTK 300 KRSKLVLPAP 310 QISDAELQEV 320 VKVGQASEIA 330 RQTAEESGIT 340 NSASSTLLSE 350 YNVTNNSVAL 360 RTPRTPASQD 370 RILQEAQNLM 380 ALTNVDTPLK 390 GGLNTPLHES 400 DFSGVTPQRQ 410 VVQTPNTVLS 420 TPFRTPSNGA 430 EGLTPRSGTT 440 PKPVINSTPG 450 RTPLRDKLNI 460 NPEDGMADYS 470 DPSYVKQMER 480 ESREHLRLGL 490 LGLPAPKNDF 500 EIVLPENAEK 510 ELEEREIDDT 520 YIEDAADVDA 530 RKQAIRDAER 540 VKEMKRMHKA 550 VQKDLPRPSE 560 VNETILRPLN 570 VEPPLTDLQK 580 SEELIKKEMI 590 TMLHYDLLHH 600 PYEPSGNKKG 610 KTVGFGTNNS 620 EHITYLEHNP 630 YEKFSKEELK 640 KAQDVLVQEM 650 EVVKQGMSHG 660 ELSSEAYNQV 670 WEECYSQVLY 680 LPGQSRYTRA 690 NLASKKDRIE 700 SLEKRLEINR 710 GHMTTEAKRA 720 AKMEKKMKIL 730 LGGYQSRAMG 740 LMKQLNDLWD 750 QIEQAHLELR 760 TFEELKKHED 770 SAIPRRLECL 780 KEDVQRQQER 790 EKELQHRYAD 800 LLLEKETLKS KF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0071013 catalytic step 2 spliceosome
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0016020 membrane
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0000974 Prp19 complex
Cellular Component GO:0005681 spliceosomal complex
Cellular Component GO:0071007 U2-type catalytic step 2 spliceosome
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0001228 DNA-binding transcription activator activity, RNA polymerase II-specific
Molecular Function GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0000977 RNA polymerase II transcription regulatory region sequence-specific DNA binding
Molecular Function GO:0071987 WD40-repeat domain binding
Biological Process GO:0000077 DNA damage checkpoint signaling
Biological Process GO:0006281 DNA repair
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0006357 regulation of transcription by RNA polymerase II

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] 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.

[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] 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.

[6] 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.