Search Results

Overview

Uniprot IDP27824
Protein NameCalnexin
Gene NameCANX
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
103 EIAKYDGKWEVEEMK
113 VEEMKESKLPGDKGL
118 ESKLPGDKGLVLMSR
127 LVLMSRAKHHAISAK
134 KHHAISAKLNKPFLF
137 AISAKLNKPFLFDTK
170 AYVKLLSKTPELNLD
210 IFRHKNPKTGIYEEK
217 KTGIYEEKHAKRPDA
227 KRPDADLKTYFTDKK
233 LKTYFTDKKTHLYTL
234 KTYFTDKKTHLYTLI
380 VIDNPNYKGKWKPPM
458 ANDGWGLKKAADGAA
515 QTSGMEYKKTDAPQP
516 TSGMEYKKTDAPQPD
87 LSGWILSKAKKDDTD
90 WILSKAKKDDTDDEI
99 DTDDEIAKYDGKWEV

Function

Calcium-binding protein that interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse

Protein Sequence

10 MEGKWLLCML 20 LVLGTAIVEA 30 HDGHDDDVID 40 IEDDLDDVIE 50 EVEDSKPDTT 60 APPSSPKVTY 70 KAPVPTGEVY 80 FADSFDRGTL 90 SGWILSKAKK 100 DDTDDEIAKY 110 DGKWEVEEMK 120 ESKLPGDKGL 130 VLMSRAKHHA 140 ISAKLNKPFL 150 FDTKPLIVQY 160 EVNFQNGIEC 170 GGAYVKLLSK 180 TPELNLDQFH 190 DKTPYTIMFG 200 PDKCGEDYKL 210 HFIFRHKNPK 220 TGIYEEKHAK 230 RPDADLKTYF 240 TDKKTHLYTL 250 ILNPDNSFEI 260 LVDQSVVNSG 270 NLLNDMTPPV 280 NPSREIEDPE 290 DRKPEDWDER 300 PKIPDPEAVK 310 PDDWDEDAPA 320 KIPDEEATKP 330 EGWLDDEPEY 340 VPDPDAEKPE 350 DWDEDMDGEW 360 EAPQIANPRC 370 ESAPGCGVWQ 380 RPVIDNPNYK 390 GKWKPPMIDN 400 PSYQGIWKPR 410 KIPNPDFFED 420 LEPFRMTPFS 430 AIGLELWSMT 440 SDIFFDNFII 450 CADRRIVDDW 460 ANDGWGLKKA 470 ADGAAEPGVV 480 GQMIEAAEER 490 PWLWVVYILT 500 VALPVFLVIL 510 FCCSGKKQTS 520 GMEYKKTDAP 530 QPDVKEEEEE 540 KEEEKDKGDE 550 EEEGEEKLEE 560 KQKSDAEEDG 570 GTVSQEEEDR 580 KPKAEEDEIL 590 NRSPRNRKPR RE

Gene Ontology

Classification GO ID Description
Biological Process GO:0048488 synaptic vesicle endocytosis
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0005788 endoplasmic reticulum lumen
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0044322 endoplasmic reticulum quality control compartment
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0098553 lumenal side of endoplasmic reticulum membrane
Cellular Component GO:0033162 melanosome membrane
Cellular Component GO:0016020 membrane
Cellular Component GO:0044233 mitochondria-associated endoplasmic reticulum membrane contact site
Cellular Component GO:0031966 mitochondrial membrane
Cellular Component GO:0031965 nuclear membrane
Cellular Component GO:0098793 presynapse
Molecular Function GO:0005509 calcium ion binding
Molecular Function GO:0030246 carbohydrate binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0051082 unfolded protein binding
Biological Process GO:0072583 clathrin-dependent endocytosis
Biological Process GO:0036503 ERAD pathway
Biological Process GO:0006457 protein folding
Biological Process GO:0034975 protein folding in endoplasmic reticulum
Biological Process GO:0009306 protein secretion
Biological Process GO:0019082 viral protein processing

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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[5] 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.

[6] 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.

[7] 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.

[8] 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.

[9] 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.