Search Results

Overview

Uniprot ID	Q9BT78
Protein Name	COP9 signalosome complex subunit 4
Gene Name	COPS4
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
20	MNSSGSHKDLAGKYR

Function

Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. Also involved in the deneddylation of non-cullin subunits such as STON2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1, IRF8/ICSBP and SNAPIN, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively

Protein Sequence

10 MAAAVRQDLA 20 QLMNSSGSHK 30 DLAGKYRQIL 40 EKAIQLSGAE 50 QLEALKAFVE 60 AMVNENVSLV 70 ISRQLLTDFC 80 THLPNLPDST 90 AKEIYHFTLE 100 KIQPRVISFE 110 EQVASIRQHL 120 ASIYEKEEDW 130 RNAAQVLVGI 140 PLETGQKQYN 150 VDYKLETYLK 160 IARLYLEDDD 170 PVQAEAYINR 180 ASLLQNESTN 190 EQLQIHYKVC 200 YARVLDYRRK 210 FIEAAQRYNE 220 LSYKTIVHES 230 ERLEALKHAL 240 HCTILASAGQ 250 QRSRMLATLF 260 KDERCQQLAA 270 YGILEKMYLD 280 RIIRGNQLQE 290 FAAMLMPHQK 300 ATTADGSSIL 310 DRAVIEHNLL 320 SASKLYNNIT 330 FEELGALLEI 340 PAAKAEKIAS 350 QMITEGRMNG 360 FIDQIDGIVH 370 FETREALPTW 380 DKQIQSLCFQ 390 VNNLLEKISQ 400 TAPEWTAQAM EAQMAQ

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0008180	COP9 signalosome
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0016607	nuclear speck
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0008021	synaptic vesicle
Molecular Function	GO:0019784	deNEDDylase activity
Biological Process	GO:0000338	protein deneddylation
Biological Process	GO:0045116	protein neddylation
Biological Process	GO:2000434	regulation of protein neddylation

Reference

[1] 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.

[2] 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.

[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] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[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.