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    CANX calnexin [ Homo sapiens ]

    Gene ID: 821, updated on 19-May-2012
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    Summary

    Official Symbol
    CANXprovided by HGNC
    Official Full Name
    calnexinprovided by HGNC
    Primary source
    HGNC:1473
    See related
    Ensembl:ENSG00000127022; HPRD:00252; MIM:114217; Vega:OTTHUMG00000130910
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Homo sapiens
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
    Also known as
    CNX; P90; IP90; FLJ26570
    Summary
    This gene encodes a member of the calnexin family of molecular chaperones. The encoded protein is a calcium-binding, endoplasmic reticulum (ER)-associated protein that interacts transiently with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. It may also play a central role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Alternatively spliced transcript variants encoding the same protein have been described. [provided by RefSeq, Jul 2008]
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    Genomic context

    Location :
    5q35
    Sequence :
    Chromosome: 5; NC_000005.9 (179125930..179158642)
    See CANX in Epigenomics, MapViewer

    Chromosome 5 - NC_000005.9Genomic Context describing neighboring genes Neighboring gene chibby homolog 3 (Drosophila) Neighboring gene high mobility group box 3 pseudogene 22 Neighboring gene uncharacterized LOC100652779 Neighboring gene mastermind-like 1 (Drosophila) Neighboring gene leukotriene C4 synthase

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    Genomic regions, transcripts, and products

    Go to nucleotideGraphics FASTA GenBank

    Go to reference sequence details
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    Bibliography

    Related articles in PubMed

    1. Pathomechanistic characterization of two exonic L1CAM variants located in trans in an obligate carrier of X-linked hydrocephalus. Marx M, et al. Neurogenetics, 2012 Feb. PMID 22222883.
    2. Systematic and quantitative assessment of the ubiquitin-modified proteome. Kim W, et al. Mol Cell, 2011 Oct 21. PMID 21906983.
    3. A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Wagner SA, et al. Mol Cell Proteomics, 2011 Oct. PMID 21890473.
    4. Comparative proteomic analysis identifies a role for SUMO in protein quality control. Tatham MH, et al. Sci Signal, 2011 Jun 21. PMID 21693764.
    5. Association of defective HLA-I expression with antigen processing machinery and their association with clinicopathological characteristics in Kazak patients with esophageal cancer. Ayshamgul H, et al. Chin Med J (Engl), 2011 Feb. PMID 21362330.

    See all (123) citations in PubMed

    GeneRIFs: Gene References Into Functions What's a GeneRIF?

    1. HLA-I, TAP1, CNX, LMP7, Erp57, Tapasin and ERAP1 were down-regulated in 68%, 44%, 48%, 40%, 52%, 32% and 20% of esophageal squamous cell carcinoma lesions then, respectively.
      Title: Association of defective HLA-I expression with antigen processing machinery and their association with clinicopathological characteristics in Kazak patients with esophageal cancer.
    2. Nixin/ZNRF4 to be central for the regulation of calnexin turnover.
      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.
    3. Results reveal the P-domain functions as a unique protein-protein interaction domain and implicate a peptidyl prolyl isomerase as a new element in the calnexin cycle.
      Title: Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain.
    4. calnexin could bind PrP both in vitro and in vivo; calnexin prevents caspase-3-mediated cytotoxicity induced by PrP
      Title: Calnexin inhibits thermal aggregation and neurotoxicity of prion protein.
    5. Transmembrane segments prevent surface expression of sodium channel Nav1.8 and promote calnexin-dependent channel degradation
      Title: Transmembrane segments prevent surface expression of sodium channel Nav1.8 and promote calnexin-dependent channel degradation.
    6. human delta opioid receptor (hdeltaOR) exists in a ternary complex with SERCA2b and the ER molecular chaperone calnexin
      Title: Human delta opioid receptor biogenesis is regulated via interactions with SERCA2b and calnexin.
    7. Env interacts with intracellular CNX and extracellular PDI via discrete, largely nonoverlapping, regions.
      Title: Mapping of domains on HIV envelope protein mediating association with calnexin and protein-disulfide isomerase.
    8. Results show that the phosphorylation of calnexin is linked to the efficiency of secretion of the cargo glycoprotein, in this case, alpha1-antitrypsin.
      Title: Calnexin phosphorylation attenuates the release of partially misfolded alpha1-antitrypsin to the secretory pathway.
    9. Data show that demonstrate that Cnx preferentially associates with misfolded mutant opsins associated with retinitis pigmentosa.
      Title: Calnexin improves the folding efficiency of mutant rhodopsin in the presence of pharmacological chaperone 11-cis-retinal.
    10. Data show that The cell surface expression levels of (ICAM)-2 and -3 on the apoptotic cells were markedly lower, while those of calnexin, calreticulin, and (LAMP)-1 and -2 were significantly higher compared to non-apoptotic cells.
      Title: Altered expression of glycoproteins on the cell surface of Jurkat cells during etoposide-induced apoptosis: shedding and intracellular translocation of glycoproteins.
    Submit: New GeneRIF Correction See all (34)
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    Phenotypes

    Review eQTL and phenotype association data in this region using PheGenI

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    HIV-1 protein interactions

    Protein Gene Interaction Pubs
    Envelope surface glycoprotein gp120 env The signal-sequence-retained form of HIV-1 gp120 is associated with calnexin in the endoplasmic reticulum (ER), while the signal-sequence-cleaved form is disassociated from calnexin and undergoes folding to associate with the CD4 cellular receptor PubMed
    Envelope surface glycoprotein gp160, precursor env The molecular chaperone calnexin binds to newly synthesized HIV-1 gp160; nonglycosylated gp160 is not associated with calnexin, suggesting a requirement for N-linked oligosaccharides on the newly synthesized protein for binding to occur PubMed

    Go to the HIV-1, Human Protein Interaction Database

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    Interactions

    Products Interactant Other Gene Complex Source Pubs Description
    NP_001737.1 NP_000483.2 CFTR    BIND  PubMed CFTR interacts with CANX. 
    NP_001737.1 NP_000483.2 CFTR    BIND  PubMed CFTR interacts with CANX. This interaction was modeled on a demonstrated interaction between human CFTR and hamster CANX. 
    NP_001737.1 NP_056922.1 F    BIND  PubMed The measles virus protein F interacts with the human host chaperone protein calnexin. 
    NP_001737.1 NP_005304.3 PDIA3    BIND  PubMed ERp57 interacts with CNX. This interaction was modeled on a demonstrated interaction between dog CNX and ERp57 from an unspecified source. 
    NP_001737.1 NP_000360.1 TSHR    BIND  PubMed Thyroid-Stimulating Hormone Receptor interacts with the molecular chaperone calnexin. This interaction was modeled on a demonstrated interaction between human TSHR and dog calnexin. 
    NP_001737.1 AAL29687.1     BIND  PubMed The measles virus haemagglutinin interacts with the human host chaperone protein calnexin. 
    P27824 Q92887 ABCC2    HPRD  PubMed  
    P27824 P04114 APOB    HPRD  PubMed  
    P27824 P51572 BCAP31    HPRD  PubMed  
    P27824 P15813 CD1D    HPRD  PubMed  
    P27824 P04234 CD3D    HPRD  PubMed  
    P27824 P27701 CD82    HPRD  PubMed  
    P27824 P13569 CFTR    HPRD  PubMed  
    P27824 Q14213 EBI3    HPRD  PubMed  
    P27824 Q92611 EDEM1    HPRD  PubMed  
    P27824 P00451 F8    HPRD  PubMed  
    P27824 O95990 FAM107A    HPRD  PubMed  
    P27824 P23945 FSHR    HPRD  PubMed  
    P27824 P42261 GRIA1    HPRD  PubMed  
    P27824 Q05586 GRIN1    HPRD  PubMed  
    P27824 P01891 HLA-A    HPRD  PubMed  
    P27824 P46098 HTR3A    HPRD  PubMed  
    P27824 P15260 IFNGR1    HPRD  PubMed  
    P27824 P23229 ITGA6    HPRD  PubMed  
    P27824 P05556 ITGB1    HPRD  PubMed  
    P27824 P09848 LCT    HPRD  PubMed  
    P27824 P22888 LHCGR    HPRD  PubMed  
    P27824 P08519 LPA    HPRD  PubMed  
    P27824 Q07954 LRP1    HPRD  PubMed  
    P27824 Q14703 MBTPS1    HPRD  PubMed  
    P27824 P48039 MTNR1A    HPRD  PubMed  
    P27824 P49286 MTNR1B    HPRD  PubMed  
    P27824 Q92597 NDRG1    HPRD  PubMed  
    P27824 P30101 PDIA3    HPRD  PubMed  
    P27824 P60201 PLP1    HPRD  PubMed  
    P27824 Q01453 PMP22    HPRD  PubMed  
    P27824 P14314 PRKCSH    HPRD  PubMed  
    P27824 Stress associated endoplasmic reticulum protein 1 SERP1    HPRD  PubMed  
    P27824 P11166 SLC2A1    HPRD  PubMed  
    P27824 P02730 SLC4A1    HPRD  PubMed  
    P27824 Q9HAU4 SMURF2    HPRD  PubMed  
    P27824 P02787 TF    HPRD  PubMed  
    P27824 P01266 TG    HPRD  PubMed  
    P27824 P16473 TSHR    HPRD  PubMed  
    P27824 T cell antigen receptor, alpha     HPRD  PubMed  
    BioGRID:107271 BioGRID:223223 AI837181    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:107271 BioGRID:106764 AMFR    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:107271 BioGRID:106835 APOB    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:107271 BioGRID:117749 BSCL2    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:107271 BioGRID:107262 CALR    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:107271 BioGRID:107350 CD1D    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:107271 BioGRID:107353 CD3D    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:107271 BioGRID:115450 EBI3    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:107271 BioGRID:115047 EDEM1    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:107271 BioGRID:108455 F8    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:107271 BioGRID:115331 HDAC5    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:107271 BioGRID:109894 ITGB1    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:107271 BioGRID:110094 L1CAM    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:107271 BioGRID:110130 LCT    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:107271 BioGRID:110202 LPA    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:107271 BioGRID:110215 LRP1    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:107271 BioGRID:204968 Mapk13    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:107271 BioGRID:115669 NDRG1    BioGRID  PubMed Affinity Capture-MS; Affinity Capture-Western 
    BioGRID:107271 BioGRID:115343 PIGK    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:107271 BioGRID:112404 SLC2A1    BioGRID  PubMed Reconstituted Complex 
    BioGRID:107271 BioGRID:112412 SLC4A1    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:107271 BioGRID:112423 SLC6A4    BioGRID  PubMed Reconstituted Complex 
    BioGRID:107271 BioGRID:112497 SUMO2    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:107271 BioGRID:129222 SVIP    BioGRID  PubMed Co-fractionation 
    BioGRID:107271 BioGRID:112876 TF    BioGRID  PubMed Reconstituted Complex 
    BioGRID:107271 BioGRID:113104 TSHR    BioGRID  PubMed Affinity Capture-Western 
    BioGRID:107271 BioGRID:228970 Tor1aip1    BioGRID  PubMed Affinity Capture-MS 
    BioGRID:107271 BioGRID:113164 UBC    BioGRID  PubMed Affinity Capture-MS; Affinity Capture-Western 
    BioGRID:107271 BioGRID:127116 ZNRF4    BioGRID  PubMed Affinity Capture-Western 
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    General gene information

    Markers

    Genotypes

    Homology

    Pathways from BioSystems

    • Adaptive Immune System, organism-specific biosystem (from REACTOME)
      Adaptive Immune System, organism-specific biosystemAdaptive immunity refers to antigen-specific immune response efficiently involved in clearing the pathogens. The adaptive immune system is comprised of B and T lymphocytes that express receptors with...
    • Antigen Presentation: Folding, assembly and peptide loading of class I MHC, organism-specific biosystem (from REACTOME)
      Antigen Presentation: Folding, assembly and peptide loading of class I MHC, organism-specific biosystemUnlike other glycoproteins, correct folding of MHC class I molecules is not sufficient to trigger their exit from the ER, they exit only after peptide loading. Described here is the process of antige...
    • Antigen processing and presentation, organism-specific biosystem (from KEGG)
      Antigen processing and presentation, organism-specific biosystem
      Antigen processing and presentation
    • Antigen processing and presentation, conserved biosystem (from KEGG)
      Antigen processing and presentation, conserved biosystem
      Antigen processing and presentation
    • Asparagine N-linked glycosylation, organism-specific biosystem (from REACTOME)
      Asparagine N-linked glycosylation, organism-specific biosystemN-linked glycosylation is the most important form of post-translational modification for proteins synthesized and folded in the Endoplasmic Reticulum (Stanley P et al, 2009). An early study in 1999 r...
    • Assembly of Viral Components at the Budding Site, organism-specific biosystem (from REACTOME)
      Assembly of Viral Components at the Budding Site, organism-specific biosystemFollowing synthesis on membrane-bound ribosomes, the three viral integral membrane proteins, HA (hemagglutinin), NA (neuraminidase) and M2 (ion channel) enter the host endoplasmic reticulum (ER) wher...
    • Calnexin/calreticulin cycle, organism-specific biosystem (from REACTOME)
      Calnexin/calreticulin cycle, organism-specific biosystemThe unfolded protein is recognized by a chaperon protein (calnexin or calreticulin) and the folding process starts. The binding of these protein requires a mono-glucosylated glycan (Caramelo JJ and P...
    • Class I MHC mediated antigen processing & presentation, organism-specific biosystem (from REACTOME)
      Class I MHC mediated antigen processing & presentation, organism-specific biosystemMajor histocompatibility complex (MHC) class I molecules play an important role in cell mediated immunity by reporting on intracellular events such as viral infection, the presence of intracellular b...
    • Disease, organism-specific biosystem (from REACTOME)
      Disease, organism-specific biosystemBiological processes are captured in Reactome by identifying the molecules (DNA, RNA, protein, small molecules) involved in them and describing the details of their interactions. From this molecular ...
    • HTLV-I infection, organism-specific biosystem (from KEGG)
      HTLV-I infection, organism-specific biosystemHuman T-lymphotropic virus type 1 (HTLV-1) is a pathogenic retrovirus that is associated with adult T-cell leukemia/lymphoma (ATL). It is also strongly implicated in non-neoplastic chronic inflammato...
    • HTLV-I infection, conserved biosystem (from KEGG)
      HTLV-I infection, conserved biosystemHuman T-lymphotropic virus type 1 (HTLV-1) is a pathogenic retrovirus that is associated with adult T-cell leukemia/lymphoma (ATL). It is also strongly implicated in non-neoplastic chronic inflammato...
    • Immune System, organism-specific biosystem (from REACTOME)
      Immune System, organism-specific biosystemHumans are exposed to millions of potential pathogens daily, through contact, ingestion, and inhalation. Our ability to avoid infection depends on the adaptive immune system and during the first crit...
    • Influenza Infection, organism-specific biosystem (from REACTOME)
      Influenza Infection, organism-specific biosystemFor centuries influenza epidemics have plagued man, and influenza was probably the disease described by Hippocrates in 412 BC. Today it remains a major cause of morbidity and mortality worldwide with...
    • Influenza Life Cycle, organism-specific biosystem (from REACTOME)
      Influenza Life Cycle, organism-specific biosystemThe virus particle initially associates with a human host cell by binding to sialic acid-containing receptors on the host cell surface. The bound virus is endocytosed by one of four distinct mechanis...
    • Metabolism of proteins, organism-specific biosystem (from REACTOME)
      Metabolism of proteins, organism-specific biosystemProtein metabolism comprises the pathways of translation, post-translational modification and protein folding.
    • N-glycan trimming in the ER and Calnexin/Calreticulin cycle, organism-specific biosystem (from REACTOME)
      N-glycan trimming in the ER and Calnexin/Calreticulin cycle, organism-specific biosystemAfter being synthesized in the ER membrane the 14-sugars lipid-linked oligosaccharide is co-translationally transferred to an unfolded protein, as described in the previous steps. After this point th...
    • Phagosome, organism-specific biosystem (from KEGG)
      Phagosome, organism-specific biosystemPhagocytosis is the process of taking in relatively large particles by a cell, and is a central mechanism in the tissue remodeling, inflammation, and defense against infectious agents. A phagosome is...
    • Phagosome, conserved biosystem (from KEGG)
      Phagosome, conserved biosystemPhagocytosis is the process of taking in relatively large particles by a cell, and is a central mechanism in the tissue remodeling, inflammation, and defense against infectious agents. A phagosome is...
    • Post-translational protein modification, organism-specific biosystem (from REACTOME)
      Post-translational protein modification, organism-specific biosystemAfter translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the...
    • Protein processing in endoplasmic reticulum, organism-specific biosystem (from KEGG)
      Protein processing in endoplasmic reticulum, organism-specific biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
    • Protein processing in endoplasmic reticulum, conserved biosystem (from KEGG)
      Protein processing in endoplasmic reticulum, conserved biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
    • Virus Assembly and Release, organism-specific biosystem (from REACTOME)
      Virus Assembly and Release, organism-specific biosystemInfluenza viruses assemble and bud from the apical plasma membrane of polarized cells e.g. lung epithelial cells of the infected host. This asymmetrical process (i.e. apical [Influenza virus] or baso...

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    calcium ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    sugar binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    unfolded protein binding NAS
    Non-traceable Author Statement
    more info
    		  
    Process Evidence Code Pubs
    antigen processing and presentation of peptide antigen via MHC class I TAS
    Traceable Author Statement
    more info
    		  
    cellular protein metabolic process TAS
    Traceable Author Statement
    more info
    		  
    post-translational protein modification TAS
    Traceable Author Statement
    more info
    		  
    protein N-linked glycosylation via asparagine TAS
    Traceable Author Statement
    more info
    		  
    protein folding TAS
    Traceable Author Statement
    more info
    		  
    protein secretion TAS
    Traceable Author Statement
    more info
    		 PubMed 
    Component Evidence Code Pubs
    endoplasmic reticulum IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    endoplasmic reticulum lumen TAS
    Traceable Author Statement
    more info
    		  
    endoplasmic reticulum membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    integral to lumenal side of endoplasmic reticulum membrane TAS
    Traceable Author Statement
    more info
    		  
    integral to membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    melanosome IEA
    Inferred from Electronic Annotation
    more info
    		  
    membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
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    General protein information

    Preferred Names
    calnexin
    Names
    calnexin
    major histocompatibility complex class I antigen-binding protein p88
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    NCBI Reference Sequences (RefSeq)

    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001024649.1 → NP_001019820.1  calnexin precursor

      Status: REVIEWED

      Description
      Transcript Variant: This variant (2) differs in the 5' UTR compared to variant 1. Variants 1 and 2 encode the same protein.
      Source sequence(s)
      AC113426, BC042843
      Consensus CDS
      CCDS4447.1
      UniProtKB/Swiss-Prot
      P27824
      Related
      ENSP00000391646, OTTHUMP00000223187, ENST00000452673, OTTHUMT00000371747
      Conserved Domains (1) summary
      pfam00262
      Location:69 – 440
      Blast Score: 1358
      Calreticulin; Calreticulin family

    2. NM_001746.3 → NP_001737.1  calnexin precursor

      Status: REVIEWED

      Description
      Transcript Variant: This variant (1) represents the longer transcript. Variants 1 and 2 encode the same protein.
      Source sequence(s)
      AC113426, BC003552
      Consensus CDS
      CCDS4447.1
      UniProtKB/Swiss-Prot
      P27824
      Related
      ENSP00000247461, OTTHUMP00000161516, ENST00000247461, OTTHUMT00000253500
      Conserved Domains (1) summary
      pfam00262
      Location:69 – 440
      Blast Score: 1358
      Calreticulin; Calreticulin family

    RefSeqs of Annotated Genomes: Build 37.3

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCh37.p5 Primary Assembly

    Genomic

    1. NC_000005.9 Reference GRCh37.p5 Primary Assembly

      Range
      179125930..179158642
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Alternate HuRef

    Genomic

    1. AC_000137.1 Alternate HuRef

      Range
      173852686..173884832
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)
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    Related Sequences

    Nucleotide Protein
    Heading Accession and Version
    genomic AC113426.2 (88286..120999) None
    genomic CH471165.2 EAW53802.1
      EAW53803.1
      EAW53804.1
      EAW53805.1
    genomic JA462402.1 CCD35249.1
    mRNA AF070646.1 None
    mRNA AJ271880.1 CAB72137.1
    mRNA AK129990.1 BAC85269.1
    mRNA AK130080.1 None
    mRNA AK294702.1 BAG57859.1
    mRNA AK304420.1 BAG65250.1
    mRNA AK312334.1 BAG35255.1
    mRNA BC003552.1 AAH03552.1
    mRNA BC042843.1 AAH42843.1
    mRNA BC050534.1 None
    mRNA L10284.1 AAA36125.1
    mRNA L18887.1 AAA21013.1
    mRNA M94859.1 AAA21749.1
    mRNA M98452.1 AAA35696.1
    other-genetic DQ890627.2 ABM92244.1
    other-genetic DQ893794.2 ABM84720.1
    Protein Accession Links
    GenPept Link UniProtKB Link
    P27824.2 GenPept UniProtKB/Swiss-Prot:P27824
    Q6ZP56 GenPept UniProtKB/TrEMBL:Q6ZP56
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    Additional Links

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Chemical Information
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