Search Results

Overview

Uniprot ID	Q9BTE7
Protein Name	DCN1-like protein 5
Gene Name	DCUN1D5
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
23	VAEDGGLKKCKISSY
24	AEDGGLKKCKISSYC
26	DGGLKKCKISSYCRS
8	MPVKKKRKSPGVAAA

Function

Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes which is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs) (PubMed:19617556, PubMed:23201271, PubMed:26906416). May play a role in DNA damage response and may participate in cell proliferation and anchorage-independent cell growth (PubMed:23098533, PubMed:24192928)

Protein Sequence

10 MPVKKKRKSP 20 GVAAAVAEDG 30 GLKKCKISSY 40 CRSQPPARLI 50 SGEEHFSSKK 60 CLAWFYEYAG 70 PDEVVGPEGM 80 EKFCEDIGVE 90 PENIIMLVLA 100 WKLEAESMGF 110 FTKEEWLKGM 120 TSLQCDCTEK 130 LQNKFDFLRS 140 QLNDISSFKN 150 IYRYAFDFAR 160 DKDQRSLDID 170 TAKSMLALLL 180 GRTWPLFSVF 190 YQYLEQSKYR 200 VMNKDQWYNV 210 LEFSRTVHAD 220 LSNYDEDGAW 230 PVLLDEFVEW QKVRQTS

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0005819	spindle
Cellular Component	GO:0000151	ubiquitin ligase complex
Molecular Function	GO:0097602	cullin family protein binding
Molecular Function	GO:0031624	ubiquitin conjugating enzyme binding
Molecular Function	GO:0032182	ubiquitin-like protein binding
Biological Process	GO:0006974	DNA damage response
Biological Process	GO:2000436	positive regulation of protein neddylation
Biological Process	GO:0045116	protein neddylation
Biological Process	GO:0001558	regulation of cell growth
Biological Process	GO:2000434	regulation of protein neddylation

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] 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] 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.

[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.