CANX | ENSG00000127022 | NCBI 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 contact site
(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)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 678.6772
Cell Significance Index: -105.5700
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 409.3937
Cell Significance Index: -103.8400
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 328.0271
Cell Significance Index: -135.1300
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 266.5833
Cell Significance Index: -125.8600
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 255.3555
Cell Significance Index: -103.7400
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 229.3028
Cell Significance Index: -117.9500
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 187.8030
Cell Significance Index: -126.0200
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 109.4221
Cell Significance Index: -104.4700
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 92.7324
Cell Significance Index: -114.3400
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 42.7906
Cell Significance Index: -114.6300
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 29.7031
Cell Significance Index: -117.2100
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 25.3593
Cell Significance Index: -77.8900
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 16.3393
Cell Significance Index: -35.7600
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 4.4037
Cell Significance Index: 205.3200
Cell Name: peg cell (CL4033014)
Fold Change: 3.8319
Cell Significance Index: 88.5300
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 3.2903
Cell Significance Index: 171.3900
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 2.9982
Cell Significance Index: 411.7400
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 2.5260
Cell Significance Index: 410.8400
Cell Name: cell in vitro (CL0001034)
Fold Change: 2.4981
Cell Significance Index: 1364.2700
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 2.3639
Cell Significance Index: 63.1200
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 2.3050
Cell Significance Index: 250.7100
Cell Name: neoplastic cell (CL0001063)
Fold Change: 2.0858
Cell Significance Index: 413.9300
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 2.0826
Cell Significance Index: 375.4300
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 1.9224
Cell Significance Index: 52.3300
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 1.8836
Cell Significance Index: 1700.7100
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 1.7691
Cell Significance Index: 217.5300
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 1.6126
Cell Significance Index: 275.3600
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 1.5812
Cell Significance Index: 74.3200
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 1.4108
Cell Significance Index: 283.0100
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 1.3761
Cell Significance Index: 493.5700
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 1.3599
Cell Significance Index: 39.1800
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 1.0975
Cell Significance Index: 485.2400
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 1.0388
Cell Significance Index: 54.5400
Cell Name: odontoblast (CL0000060)
Fold Change: 1.0135
Cell Significance Index: 129.9200
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 0.8716
Cell Significance Index: 61.6400
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.8165
Cell Significance Index: 37.0100
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.7952
Cell Significance Index: 550.0100
Cell Name: lactocyte (CL0002325)
Fold Change: 0.7896
Cell Significance Index: 102.0100
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 0.7689
Cell Significance Index: 57.3100
Cell Name: early pro-B cell (CL0002046)
Fold Change: 0.6068
Cell Significance Index: 39.1500
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 0.5040
Cell Significance Index: 34.8600
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 0.3736
Cell Significance Index: 20.9700
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 0.3205
Cell Significance Index: 16.6500
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.3076
Cell Significance Index: 36.2700
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.2733
Cell Significance Index: 27.0400
Cell Name: granulosa cell (CL0000501)
Fold Change: 0.2681
Cell Significance Index: 7.0500
Cell Name: endothelial cell of venule (CL1000414)
Fold Change: 0.2645
Cell Significance Index: 3.0100
Cell Name: periportal region hepatocyte (CL0019026)
Fold Change: 0.2585
Cell Significance Index: 3.8200
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.2403
Cell Significance Index: 45.7300
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 0.1786
Cell Significance Index: 5.1200
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.1708
Cell Significance Index: 6.0000
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: 0.1665
Cell Significance Index: 122.0900
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: 0.1108
Cell Significance Index: 83.8300
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: 0.1085
Cell Significance Index: 3.7700
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.0636
Cell Significance Index: 119.7600
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 0.0000
Cell Significance Index: 0.0000
Cell Name: anterior lens cell (CL0002223)
Fold Change: -0.0241
Cell Significance Index: -44.5200
Cell Name: lens epithelial cell (CL0002224)
Fold Change: -0.0269
Cell Significance Index: -41.3600
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0483
Cell Significance Index: -35.7700
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0511
Cell Significance Index: -5.2200
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.0518
Cell Significance Index: -70.4000
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0632
Cell Significance Index: -39.4500
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.0875
Cell Significance Index: -55.5400
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: -0.1166
Cell Significance Index: -3.4300
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.1429
Cell Significance Index: -80.6000
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.1441
Cell Significance Index: -65.4200
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: -0.1753
Cell Significance Index: -4.9000
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -0.2066
Cell Significance Index: -10.4400
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.2203
Cell Significance Index: -46.4000
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.2818
Cell Significance Index: -81.0900
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.3633
Cell Significance Index: -6.0800
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.4076
Cell Significance Index: -46.5300
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: -0.4864
Cell Significance Index: -37.3300
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.4894
Cell Significance Index: -56.0700
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.5759
Cell Significance Index: -83.7100
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -0.6371
Cell Significance Index: -17.0700
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.7027
Cell Significance Index: -81.9000
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -0.7084
Cell Significance Index: -4.2800
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.7156
Cell Significance Index: -22.9200
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: -0.9130
Cell Significance Index: -19.7800
Cell Name: neuron associated cell (CL0000095)
Fold Change: -0.9140
Cell Significance Index: -37.4500
Cell Name: retinal rod cell (CL0000604)
Fold Change: -0.9530
Cell Significance Index: -11.3600
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.9694
Cell Significance Index: -61.1000
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: -1.0427
Cell Significance Index: -21.8300
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -1.0507
Cell Significance Index: -109.4000
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: -1.1006
Cell Significance Index: -10.1400
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -1.2160
Cell Significance Index: -96.3100
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -1.2302
Cell Significance Index: -26.2000
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -1.4732
Cell Significance Index: -20.1000
Cell Name: pro-T cell (CL0000827)
Fold Change: -1.5873
Cell Significance Index: -40.5500
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -1.6382
Cell Significance Index: -72.4600
Cell Name: preadipocyte (CL0002334)
Fold Change: -1.6421
Cell Significance Index: -32.0500
Cell Name: gut absorptive cell (CL0000677)
Fold Change: -1.6995
Cell Significance Index: -102.0300
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -1.7524
Cell Significance Index: -107.4400
Cell Name: kidney cell (CL1000497)
Fold Change: -1.8154
Cell Significance Index: -14.5000
Cell Name: seromucus secreting cell (CL0000159)
Fold Change: -1.8223
Cell Significance Index: -38.0100
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: -1.9238
Cell Significance Index: -48.0900
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -2.0184
Cell Significance Index: -76.4300
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -2.0836
Cell Significance Index: -61.3700
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -2.1342
Cell Significance Index: -54.8600

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics:** Calnexin is a transmembrane protein that is primarily expressed in the ER, where it is involved in the folding and assembly of proteins. It has a unique structure, consisting of a luminal domain and a cytoplasmic domain, which allows it to interact with other ER proteins and chaperones. Calnexin is also a calcium-binding protein, which is essential for its function in the ER quality control compartment. **Pathways and Functions:** Calnexin is involved in several key pathways, including: 1. **Adaptive Immune System:** Calnexin plays a crucial role in the presentation of antigens to the immune system through the assembly and loading of class I MHC molecules onto antigen-presenting cells. 2. **Antigen Presentation:** Calnexin is involved in the processing and presentation of antigens to CD8+ T cells, which is essential for the activation of the adaptive immune response. 3. **Endoplasmic Reticulum Quality Control:** Calnexin is a key component of the ER quality control compartment, where it helps to identify and remove misfolded proteins. 4. **Protein Folding:** Calnexin assists in the folding of proteins, particularly those that are destined for the cell surface or the ER lumen. 5. **Viral Infection:** Calnexin is involved in the processing and presentation of viral antigens to the immune system, which is essential for the control of viral infections. **Clinical Significance:** Calnexin has been implicated in various diseases, including: 1. **Immunodeficiency Disorders:** Mutations in the CANX gene have been associated with immunodeficiency disorders, such as severe combined immunodeficiency (SCID). 2. **Autoimmune Diseases:** Calnexin has been implicated in the pathogenesis of autoimmune diseases, such as rheumatoid arthritis and lupus. 3. **Cancer:** Calnexin has been shown to be overexpressed in certain types of cancer, including breast and lung cancer. 4. **Infectious Diseases:** Calnexin has been implicated in the pathogenesis of viral infections, such as HIV and influenza. In conclusion, calnexin is a multifunctional protein that plays a crucial role in the endoplasmic reticulum quality control compartment and the presentation of antigens to the immune system. Its dysregulation has been implicated in various diseases, highlighting the importance of calnexin in maintaining immune homeostasis and preventing disease. Further research is needed to fully understand the mechanisms by which calnexin regulates immune function and to develop therapeutic strategies to target calnexin in disease prevention and treatment.

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. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. 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