Search Results

Overview

Uniprot IDQ99829
Protein NameCopine-1
Gene NameCPNE1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
256 QQKKKSYKNSGTIRV

Function

Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes (PubMed:14674885). Involved in the TNF receptor signaling pathway in a calcium-dependent manner (PubMed:14674885). Exhibits calcium-dependent phospholipid binding properties (PubMed:19539605, PubMed:9430674). Plays a role in neuronal progenitor cell differentiation; induces neurite outgrowth via a AKT-dependent signaling cascade and calcium-independent manner (PubMed:23263657, PubMed:25450385). May recruit target proteins to the cell membrane in a calcium-dependent manner (PubMed:12522145). May function in membrane trafficking (PubMed:9430674). Involved in TNF-induced NF-kappa-B transcriptional repression by inducing endoprotease processing of the transcription factor NF-kappa-B p65/RELA subunit (PubMed:18212740). Also induces endoprotease processing of NF-kappa-B p50/NFKB1, p52/NFKB2, RELB and REL (PubMed:18212740)

Protein Sequence

10 MAHCVTLVQL 20 SISCDHLIDK 30 DIGSKSDPLC 40 VLLQDVGGGS 50 WAELGRTERV 60 RNCSSPEFSK 70 TLQLEYRFET 80 VQKLRFGIYD 90 IDNKTPELRD 100 DDFLGGAECS 110 LGQIVSSQVL 120 TLPLMLKPGK 130 PAGRGTITVS 140 AQELKDNRVV 150 TMEVEARNLD 160 KKDFLGKSDP 170 FLEFFRQGDG 180 KWHLVYRSEV 190 IKNNLNPTWK 200 RFSVPVQHFC 210 GGNPSTPIQV 220 QCSDYDSDGS 230 HDLIGTFHTS 240 LAQLQAVPAE 250 FECIHPEKQQ 260 KKKSYKNSGT 270 IRVKICRVET 280 EYSFLDYVMG 290 GCQINFTVGV 300 DFTGSNGDPS 310 SPDSLHYLSP 320 TGVNEYLMAL 330 WSVGSVVQDY 340 DSDKLFPAFG 350 FGAQVPPDWQ 360 VSHEFALNFN 370 PSNPYCAGIQ 380 GIVDAYRQAL 390 PQVRLYGPTN 400 FAPIINHVAR 410 FAAQAAHQGT 420 ASQYFMLLLL 430 TDGAVTDVEA 440 TREAVVRASN 450 LPMSVIIVGV 460 GGADFEAMEQ 470 LDADGGPLHT 480 RSGQAAARDI 490 VQFVPYRRFQ 500 NAPREALAQT 510 VLAEVPTQLV 520 SYFRAQGWAP 530 LKPLPPSAKD PAQAPQA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0035577 azurophil granule membrane
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0016020 membrane
Cellular Component GO:0031965 nuclear membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0005509 calcium ion binding
Molecular Function GO:0005544 calcium-dependent phospholipid binding
Molecular Function GO:0004175 endopeptidase activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0051059 NF-kappaB binding
Molecular Function GO:0001786 phosphatidylserine binding
Molecular Function GO:0043495 protein-membrane adaptor activity
Biological Process GO:0071277 cellular response to calcium ion
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0046474 glycerophospholipid biosynthetic process
Biological Process GO:0006629 lipid metabolic process
Biological Process GO:0043392 negative regulation of DNA binding
Biological Process GO:0010629 negative regulation of gene expression
Biological Process GO:1901223 negative regulation of non-canonical NF-kappaB signal transduction
Biological Process GO:1990138 neuron projection extension
Biological Process GO:0045666 positive regulation of neuron differentiation
Biological Process GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
Biological Process GO:1903265 positive regulation of tumor necrosis factor-mediated signaling pathway
Biological Process GO:0006508 proteolysis
Biological Process GO:0043122 regulation of canonical NF-kappaB signal transduction
Biological Process GO:0016192 vesicle-mediated transport

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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[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] 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.