Gene CANX - ENSG00000127022 | NCBI Gene ID: 821

Details for: CANX

Gene ID: 821

Symbol: CANX

Ensembl ID: ENSG00000127022

Description: calnexin

Associated with

Adaptive immune system
(R-HSA-1280218)
Antigen presentation: folding, assembly and peptide loading of class i mhc
(R-HSA-983170)
Asparagine n-linked glycosylation
(R-HSA-446203)
Assembly of viral components at the budding site
(R-HSA-168316)
Calnexin/calreticulin cycle
(R-HSA-901042)
Class i mhc mediated antigen processing & presentation
(R-HSA-983169)
Cytokine signaling in immune system
(R-HSA-1280215)
Disease
(R-HSA-1643685)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Influenza infection
(R-HSA-168255)
Interleukin-12 family signaling
(R-HSA-447115)
Interleukin-27 signaling
(R-HSA-9020956)
Interleukin-35 signalling
(R-HSA-8984722)
Late sars-cov-2 infection events
(R-HSA-9772573)
Maturation of spike protein
(R-HSA-9694548)
Metabolism of proteins
(R-HSA-392499)
Mhc class ii antigen presentation
(R-HSA-2132295)
N-glycan trimming in the er and calnexin/calreticulin cycle
(R-HSA-532668)
Post-translational protein modification
(R-HSA-597592)
Sars-cov-1 infection
(R-HSA-9678108)
Sars-cov-2 infection
(R-HSA-9694516)
Sars-cov infections
(R-HSA-9679506)
Signaling by interleukins
(R-HSA-449147)
Translation of structural proteins
(R-HSA-9694635)
Viral infection pathways
(R-HSA-9824446)
Virus assembly and release
(R-HSA-168268)
Calcium ion binding
(GO:0005509)
Carbohydrate binding
(GO:0030246)
Clathrin-dependent endocytosis
(GO:0072583)
Endoplasmic reticulum
(GO:0005783)
Endoplasmic reticulum lumen
(GO:0005788)
Endoplasmic reticulum membrane
(GO:0005789)
Endoplasmic reticulum quality control compartment
(GO:0044322)
Erad pathway
(GO:0036503)
Extracellular exosome
(GO:0070062)
Lumenal side of endoplasmic reticulum membrane
(GO:0098553)
Melanosome membrane
(GO:0033162)
Membrane
(GO:0016020)
Mitochondria-associated endoplasmic reticulum membrane
(GO:0044233)
Mitochondrial membrane
(GO:0031966)
Nuclear membrane
(GO:0031965)
Presynapse
(GO:0098793)
Protein binding
(GO:0005515)
Protein folding
(GO:0006457)
Protein folding in endoplasmic reticulum
(GO:0034975)
Protein secretion
(GO:0009306)
Rna binding
(GO:0003723)
Synaptic vesicle endocytosis
(GO:0048488)
Unfolded protein binding
(GO:0051082)
Viral protein processing
(GO:0019082)

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 3.56
Marker Score: 8105
Cell Name: thyroid follicular cell (CL0002258)
Fold Change: 3.49
Marker Score: 2732
Cell Name: kidney loop of Henle thick ascending limb epithelial cell (CL1001106)
Fold Change: 3.34
Marker Score: 8940
Cell Name: IgG plasmablast (CL0000982)
Fold Change: 3.27
Marker Score: 902
Cell Name: acinar cell (CL0000622)
Fold Change: 3.15
Marker Score: 2220
Cell Name: myeloid leukocyte (CL0000766)
Fold Change: 3.13
Marker Score: 3773
Cell Name: kidney collecting duct principal cell (CL1001431)
Fold Change: 3.03
Marker Score: 7631
Cell Name: GABAergic neuron (CL0000617)
Fold Change: 2.93
Marker Score: 12206
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: 2.89
Marker Score: 51346
Cell Name: stromal cell (CL0000499)
Fold Change: 2.87
Marker Score: 3357
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 2.87
Marker Score: 25146
Cell Name: IgA plasmablast (CL0000984)
Fold Change: 2.84
Marker Score: 746
Cell Name: cell in vitro (CL0001034)
Fold Change: 2.8
Marker Score: 96846
Cell Name: luminal cell of prostate epithelium (CL0002340)
Fold Change: 2.68
Marker Score: 1562
Cell Name: epithelial cell of proximal tubule (CL0002306)
Fold Change: 2.61
Marker Score: 9261
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 2.59
Marker Score: 88248
Cell Name: skeletal muscle satellite stem cell (CL0008011)
Fold Change: 2.58
Marker Score: 2757
Cell Name: kidney loop of Henle thin ascending limb epithelial cell (CL1001107)
Fold Change: 2.58
Marker Score: 2616
Cell Name: lung macrophage (CL1001603)
Fold Change: 2.51
Marker Score: 2869
Cell Name: fibroblast of breast (CL4006000)
Fold Change: 2.5
Marker Score: 1424
Cell Name: kidney connecting tubule epithelial cell (CL1000768)
Fold Change: 2.5
Marker Score: 3533
Cell Name: kidney distal convoluted tubule epithelial cell (CL1000849)
Fold Change: 2.49
Marker Score: 2642
Cell Name: nasal mucosa goblet cell (CL0002480)
Fold Change: 2.48
Marker Score: 1655
Cell Name: basal cell of epithelium of trachea (CL1000348)
Fold Change: 2.47
Marker Score: 18408
Cell Name: luminal epithelial cell of mammary gland (CL0002326)
Fold Change: 2.44
Marker Score: 4318
Cell Name: ciliated cell (CL0000064)
Fold Change: 2.43
Marker Score: 8367
Cell Name: type II pneumocyte (CL0002063)
Fold Change: 2.43
Marker Score: 15848
Cell Name: pneumocyte (CL0000322)
Fold Change: 2.43
Marker Score: 3899
Cell Name: epithelial cell of lung (CL0000082)
Fold Change: 2.42
Marker Score: 12708
Cell Name: kidney collecting duct intercalated cell (CL1001432)
Fold Change: 2.41
Marker Score: 3992
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 2.38
Marker Score: 569
Cell Name: neural progenitor cell (CL0011020)
Fold Change: 2.38
Marker Score: 9198
Cell Name: myoepithelial cell of mammary gland (CL0002324)
Fold Change: 2.37
Marker Score: 11659
Cell Name: duct epithelial cell (CL0000068)
Fold Change: 2.35
Marker Score: 1097
Cell Name: blood cell (CL0000081)
Fold Change: 2.34
Marker Score: 27208
Cell Name: hepatoblast (CL0005026)
Fold Change: 2.34
Marker Score: 7656
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 2.34
Marker Score: 26314
Cell Name: serous secreting cell (CL0000313)
Fold Change: 2.32
Marker Score: 927
Cell Name: GABAergic amacrine cell (CL4030027)
Fold Change: 2.32
Marker Score: 4716
Cell Name: alveolar macrophage (CL0000583)
Fold Change: 2.32
Marker Score: 59384
Cell Name: Kupffer cell (CL0000091)
Fold Change: 2.31
Marker Score: 2310
Cell Name: mucous neck cell (CL0000651)
Fold Change: 2.31
Marker Score: 5239
Cell Name: epithelial cell of lower respiratory tract (CL0002632)
Fold Change: 2.3
Marker Score: 9607
Cell Name: endocardial cell (CL0002350)
Fold Change: 2.3
Marker Score: 1299
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 2.29
Marker Score: 128245
Cell Name: ciliated columnar cell of tracheobronchial tree (CL0002145)
Fold Change: 2.26
Marker Score: 19652
Cell Name: ovarian surface epithelial cell (CL2000064)
Fold Change: 2.18
Marker Score: 5930
Cell Name: endocrine cell (CL0000163)
Fold Change: 2.18
Marker Score: 1125.5
Cell Name: mesothelial cell of epicardium (CL0011019)
Fold Change: 2.17
Marker Score: 698
Cell Name: lung ciliated cell (CL1000271)
Fold Change: 2.17
Marker Score: 1029
Cell Name: peptic cell (CL0000155)
Fold Change: 2.16
Marker Score: 906
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 2.16
Marker Score: 4549
Cell Name: ependymal cell (CL0000065)
Fold Change: 2.15
Marker Score: 749
Cell Name: lung secretory cell (CL1000272)
Fold Change: 2.15
Marker Score: 1913.5
Cell Name: glandular cell of esophagus (CL0002657)
Fold Change: 2.13
Marker Score: 676
Cell Name: myofibroblast cell (CL0000186)
Fold Change: 2.13
Marker Score: 2632
Cell Name: paneth cell (CL0000510)
Fold Change: 2.13
Marker Score: 1479
Cell Name: decidual cell (CL2000002)
Fold Change: 2.12
Marker Score: 9130
Cell Name: endothelial cell (CL0000115)
Fold Change: 2.11
Marker Score: 1895
Cell Name: kidney cell (CL1000497)
Fold Change: 2.11
Marker Score: 1406
Cell Name: hematopoietic cell (CL0000988)
Fold Change: 2.11
Marker Score: 1400
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: 2.1
Marker Score: 13685
Cell Name: type I NK T cell (CL0000921)
Fold Change: 2.1
Marker Score: 1650.5
Cell Name: podocyte (CL0000653)
Fold Change: 2.1
Marker Score: 776
Cell Name: colon epithelial cell (CL0011108)
Fold Change: 2.1
Marker Score: 6582
Cell Name: inhibitory interneuron (CL0000498)
Fold Change: 2.09
Marker Score: 9688
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: 2.09
Marker Score: 2202
Cell Name: endothelial cell of uterus (CL0009095)
Fold Change: 2.09
Marker Score: 4176
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 2.09
Marker Score: 3071
Cell Name: secretory cell (CL0000151)
Fold Change: 2.07
Marker Score: 3783
Cell Name: erythroblast (CL0000765)
Fold Change: 2.07
Marker Score: 1292
Cell Name: plasmablast (CL0000980)
Fold Change: 2.07
Marker Score: 2749
Cell Name: CD34-positive, CD38-negative hematopoietic stem cell (CL0001024)
Fold Change: 2.05
Marker Score: 1483
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: 2.04
Marker Score: 2157
Cell Name: CD14-positive monocyte (CL0001054)
Fold Change: 2.04
Marker Score: 5079
Cell Name: bronchus fibroblast of lung (CL2000093)
Fold Change: 2.03
Marker Score: 2797
Cell Name: intestinal crypt stem cell (CL0002250)
Fold Change: 2.03
Marker Score: 764
Cell Name: respiratory goblet cell (CL0002370)
Fold Change: 2.03
Marker Score: 586
Cell Name: CD14-positive, CD16-positive monocyte (CL0002397)
Fold Change: 2.02
Marker Score: 3943
Cell Name: epithelial cell of nephron (CL1000449)
Fold Change: 2.02
Marker Score: 4216
Cell Name: Unknown (CL0000548)
Fold Change: 2.01
Marker Score: 1466
Cell Name: oligodendrocyte (CL0000128)
Fold Change: 2
Marker Score: 4798
Cell Name: primitive red blood cell (CL0002355)
Fold Change: 2
Marker Score: 1502
Cell Name: stem cell (CL0000034)
Fold Change: 2
Marker Score: 4754
Cell Name: capillary endothelial cell (CL0002144)
Fold Change: 2
Marker Score: 2151
Cell Name: P/D1 enteroendocrine cell (CL0002268)
Fold Change: 2
Marker Score: 745
Cell Name: hepatocyte (CL0000182)
Fold Change: 2
Marker Score: 1363
Cell Name: granulosa cell (CL0000501)
Fold Change: 1.99
Marker Score: 20019
Cell Name: foveolar cell of stomach (CL0002179)
Fold Change: 1.99
Marker Score: 12680
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 1.99
Marker Score: 7662
Cell Name: fibroblast of lung (CL0002553)
Fold Change: 1.99
Marker Score: 5198
Cell Name: epithelial cell (CL0000066)
Fold Change: 1.98
Marker Score: 3148
Cell Name: promonocyte (CL0000559)
Fold Change: 1.98
Marker Score: 1275
Cell Name: starburst amacrine cell (CL0004232)
Fold Change: 1.98
Marker Score: 561
Cell Name: choroid plexus epithelial cell (CL0000706)
Fold Change: 1.97
Marker Score: 1807.5
Cell Name: epithelial cell of esophagus (CL0002252)
Fold Change: 1.97
Marker Score: 16948
Cell Name: enterocyte (CL0000584)
Fold Change: 1.97
Marker Score: 9432
Cell Name: tracheobronchial serous cell (CL0019001)
Fold Change: 1.97
Marker Score: 718
Cell Name: CD4-positive helper T cell (CL0000492)
Fold Change: 1.96
Marker Score: 2129
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 1.96
Marker Score: 558

Hover over a box to see details here...

**Key characteristics:** * It is a type I transmembrane protein with three extracellular domains: N-terminal domain, cytoplasmic domain, and C-terminal domain. * It is expressed in various cell types, including acinar cells of the salivary gland, thyroid follicular cells, kidney loop cells, and myeloid cells. * It is a major protein of the endoplasmic reticulum (ER) and is involved in the folding and assembly of MHC molecules. * It is a regulator of the immune response and plays a role in regulating the activation of CD8+ T cells. **Pathways and functions:** * **Adaptive immune system:** CANX is a key protein in the adaptive immune system and plays a crucial role in the recognition and presentation of antigens to CD8+ T cells. * **Antigen presentation:** It is involved in the folding, assembly, and peptide loading of class I MHC molecules. * **Cytokine signaling in immune system:** It is involved in the regulation of cytokine signaling pathways, which are essential for the immune response. * **Disease:** CANX is also involved in the pathogenesis of several diseases, including SARS-CoV infections, viral infections, and autoimmune diseases. **Clinical significance:** * Dysfunction of CANX has been linked to several diseases, including autoimmune diseases, viral infections, and cancer. * Targeting CANX has been investigated as a potential therapeutic strategy for these diseases. * Studies have shown that blocking CANX can inhibit the immune response and reduce the severity of viral infections.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Calnexin

Genular Protein ID: 4218414032

Symbol: CALX_HUMAN

Name: Calnexin

UniProtKB Accession Codes:

P27824 B2R5V8 B4DGP8 B4E2T8 D3DWQ3 D6R9K3

Database IDs:

Citations:

PubMed ID: 8486646

Title: Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin).

PubMed ID: 8486646

DOI: 10.1016/s0021-9258(18)98391-2

PubMed ID: 8136357

Title: Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5.

PubMed ID: 8136357

DOI: 10.1021/bi00177a013

PubMed ID: 8055875

Title: The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin exhibit strikingly different levels in quiescent keratinocytes as compared to their proliferating normal and transformed counterparts: cDNA cloning and expression of calnexin.

PubMed ID: 8055875

DOI: 10.1002/elps.1150150166

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15372022

Title: The DNA sequence and comparative analysis of human chromosome 5.

PubMed ID: 15372022

DOI: 10.1038/nature02919

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 1326756

Title: The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene.

PubMed ID: 1326756

DOI: 10.1073/pnas.89.18.8452

PubMed ID: 1286667

Title: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.

PubMed ID: 1286667

DOI: 10.1002/elps.11501301199

PubMed ID: 9188622

Title: Formation of intracellular particles by hepatitis B virus large surface protein.

PubMed ID: 9188622

DOI: 10.1128/jvi.71.7.5487-5494.1997

PubMed ID: 9420286

Title: Role for calnexin and N-linked glycosylation in the assembly and secretion of hepatitis B virus middle envelope protein particles.

PubMed ID: 9420286

DOI: 10.1128/jvi.72.1.778-782.1998

PubMed ID: 12643545

Title: Proteomic analysis of early melanosomes: identification of novel melanosomal proteins.

PubMed ID: 12643545

DOI: 10.1021/pr025562r

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16361248

Title: Mechanisms of pharmacological rescue of trafficking-defective hERG mutant channels in human long QT syndrome.

PubMed ID: 16361248

DOI: 10.1074/jbc.m511765200

PubMed ID: 17081065

Title: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.

PubMed ID: 17081065

DOI: 10.1021/pr060363j

PubMed ID: 18088087

Title: Phosphoproteome of resting human platelets.

PubMed ID: 18088087

DOI: 10.1021/pr0704130

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18318008

Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.

PubMed ID: 18318008

DOI: 10.1002/pmic.200700884

PubMed ID: 19369195

Title: Large-scale proteomics analysis of the human kinome.

PubMed ID: 19369195

DOI: 10.1074/mcp.m800588-mcp200

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20801878

Title: Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain.

PubMed ID: 20801878

DOI: 10.1074/jbc.m110.160101

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21205830

Title: A systematic search for endoplasmic reticulum (ER) membrane-associated RING finger proteins identifies Nixin/ZNRF4 as a regulator of calnexin stability and ER homeostasis.

PubMed ID: 21205830

DOI: 10.1074/jbc.m110.197459

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22314232

Title: Palmitoylated calnexin is a key component of the ribosome-translocon complex.

PubMed ID: 22314232

DOI: 10.1038/emboj.2012.15

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23826168

Title: SERPINA2 is a novel gene with a divergent function from SERPINA1.

PubMed ID: 23826168

DOI: 10.1371/journal.pone.0066889

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24196833

Title: Mutations in Fis1 disrupt orderly disposal of defective mitochondria.

PubMed ID: 24196833

DOI: 10.1091/mbc.e13-09-0525

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 29765154

Title: The cancer-associated microprotein CASIMO1 controls cell proliferation and interacts with squalene epoxidase modulating lipid droplet formation.

PubMed ID: 29765154

DOI: 10.1038/s41388-018-0281-5

PubMed ID: 31735293

Title: TMX2 is a crucial regulator of cellular redox state, and its dysfunction causes severe brain developmental abnormalities.

PubMed ID: 31735293

DOI: 10.1016/j.ajhg.2019.10.009

PubMed ID: 32783947

Title: NACHO Engages N-Glycosylation ER Chaperone Pathways for alpha7 Nicotinic Receptor Assembly.

PubMed ID: 32783947

DOI: 10.1016/j.celrep.2020.108025

PubMed ID: 34338405

Title: Role of FAM134 paralogues in endoplasmic reticulum remodeling, ER-phagy, and Collagen quality control.

PubMed ID: 34338405

DOI: 10.15252/embr.202052289

Sequence Information:

Length: 592
Mass: 67568
Checksum: EDE094D9B82261EE
Sequence:

MEGKWLLCML LVLGTAIVEA HDGHDDDVID IEDDLDDVIE EVEDSKPDTT APPSSPKVTY 
KAPVPTGEVY FADSFDRGTL SGWILSKAKK DDTDDEIAKY DGKWEVEEMK ESKLPGDKGL 
VLMSRAKHHA ISAKLNKPFL FDTKPLIVQY EVNFQNGIEC GGAYVKLLSK TPELNLDQFH 
DKTPYTIMFG PDKCGEDYKL HFIFRHKNPK TGIYEEKHAK RPDADLKTYF TDKKTHLYTL 
ILNPDNSFEI LVDQSVVNSG NLLNDMTPPV NPSREIEDPE DRKPEDWDER PKIPDPEAVK 
PDDWDEDAPA KIPDEEATKP EGWLDDEPEY VPDPDAEKPE DWDEDMDGEW EAPQIANPRC 
ESAPGCGVWQ RPVIDNPNYK GKWKPPMIDN PSYQGIWKPR KIPNPDFFED LEPFRMTPFS 
AIGLELWSMT SDIFFDNFII CADRRIVDDW ANDGWGLKKA ADGAAEPGVV GQMIEAAEER 
PWLWVVYILT VALPVFLVIL FCCSGKKQTS GMEYKKTDAP QPDVKEEEEE KEEEKDKGDE 
EEEGEEKLEE KQKSDAEEDG GTVSQEEEDR KPKAEEDEIL NRSPRNRKPR RE

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. For the full schema, download it here.

Details for: CANX

Associated with

Cells (max top 100)

Other Information

Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin). PubMed ID: 8486646

Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5. PubMed ID: 8136357

The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin exhibit strikingly different levels in quiescent keratinocytes as compared to their proliferating normal and transformed counterparts: cDNA cloning and expression of calnexin. PubMed ID: 8055875

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The DNA sequence and comparative analysis of human chromosome 5. PubMed ID: 15372022

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene. PubMed ID: 1326756

Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. PubMed ID: 1286667

Formation of intracellular particles by hepatitis B virus large surface protein. PubMed ID: 9188622

Role for calnexin and N-linked glycosylation in the assembly and secretion of hepatitis B virus middle envelope protein particles. PubMed ID: 9420286

Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. PubMed ID: 12643545

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

Mechanisms of pharmacological rescue of trafficking-defective hERG mutant channels in human long QT syndrome. PubMed ID: 16361248

Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. PubMed ID: 17081065

Phosphoproteome of resting human platelets. PubMed ID: 18088087

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PubMed ID: 18691976

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. PubMed ID: 18318008

Large-scale proteomics analysis of the human kinome. PubMed ID: 19369195

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain. PubMed ID: 20801878

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

A systematic search for endoplasmic reticulum (ER) membrane-associated RING finger proteins identifies Nixin/ZNRF4 as a regulator of calnexin stability and ER homeostasis. PubMed ID: 21205830

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

Palmitoylated calnexin is a key component of the ribosome-translocon complex. PubMed ID: 22314232

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

SERPINA2 is a novel gene with a divergent function from SERPINA1. PubMed ID: 23826168

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Mutations in Fis1 disrupt orderly disposal of defective mitochondria. PubMed ID: 24196833

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

The cancer-associated microprotein CASIMO1 controls cell proliferation and interacts with squalene epoxidase modulating lipid droplet formation. PubMed ID: 29765154

TMX2 is a crucial regulator of cellular redox state, and its dysfunction causes severe brain developmental abnormalities. PubMed ID: 31735293

NACHO Engages N-Glycosylation ER Chaperone Pathways for alpha7 Nicotinic Receptor Assembly. PubMed ID: 32783947

Role of FAM134 paralogues in endoplasmic reticulum remodeling, ER-phagy, and Collagen quality control. PubMed ID: 34338405