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    CP ceruloplasmin [ Homo sapiens (human) ]

    Gene ID: 1356, updated on 27-Nov-2024

    Summary

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    Official Symbol
    CPprovided by HGNC
    Official Full Name
    ceruloplasminprovided by HGNC
    Primary source
    HGNC:HGNC:2295
    See related
    Ensembl:ENSG00000047457 MIM:117700; AllianceGenome:HGNC:2295
    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
    CP-2; AB073614
    Summary
    The protein encoded by this gene is a metalloprotein that binds most of the copper in plasma and is involved in the peroxidation of Fe(II)transferrin to Fe(III) transferrin. Mutations in this gene cause aceruloplasminemia, which results in iron accumulation and tissue damage, and is associated with diabetes and neurologic abnormalities. Two transcript variants, one protein-coding and the other not protein-coding, have been found for this gene. [provided by RefSeq, Feb 2012]
    Expression
    Biased expression in liver (RPKM 413.3) and urinary bladder (RPKM 15.0) See more
    Orthologs
    mouse all
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    Genomic context

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    Location:
    3q24-q25.1
    Exon count:
    21
    Annotation release Status Assembly Chr Location
    RS_2024_08 current GRCh38.p14 (GCF_000001405.40) 3 NC_000003.12 (149162414..149221829, complement)
    RS_2024_08 current T2T-CHM13v2.0 (GCF_009914755.1) 3 NC_060927.1 (151913150..151972585, complement)
    RS_2024_09 previous assembly GRCh37.p13 (GCF_000001405.25) 3 NC_000003.11 (148880201..148939616, complement)

    Chromosome 3 - NC_000003.12Genomic Context describing neighboring genes Neighboring gene glycogenin 1 Neighboring gene helicase like transcription factor Neighboring gene OCT4-NANOG-H3K27ac hESC enhancers GRCh37_chr3:148803647-148804164 and GRCh37_chr3:148804165-148804682 Neighboring gene HLTF antisense RNA 1 Neighboring gene mediator complex subunit 28 pseudogene 2 Neighboring gene H3K27ac hESC enhancer GRCh37_chr3:148847467-148847966 Neighboring gene HPS3 biogenesis of lysosomal organelles complex 2 subunit 1 Neighboring gene OCT4-NANOG-H3K27ac hESC enhancer GRCh37_chr3:148914047-148914842 Neighboring gene OCT4-NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr3:148914843-148915640 Neighboring gene OCT4-NANOG-H3K27ac-H3K4me1 hESC enhancer GRCh37_chr3:148915641-148916436 Neighboring gene OCT4-NANOG-H3K27ac hESC enhancer GRCh37_chr3:148916437-148917233 Neighboring gene uncharacterized LOC101927942 Neighboring gene ATAC-STARR-seq lymphoblastoid active region 20680 Neighboring gene ceruloplasmin and hephaestin like 1, pseudogene Neighboring gene MED14-independent group 3 enhancer GRCh37_chr3:148987331-148988530

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: HPA RNA-seq normal tissues
    • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
    • BioProject: PRJEB4337
    • Publication: PMID 24309898
    • Analysis date: Wed Apr 4 07:08:55 2018

    Bibliography

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    Related articles in PubMed

    1. Increased oxidized low density lipoprotein associated with high ceruloplasmin activity in patients with active acromegaly. Boero L, et al. Clin Endocrinol (Oxf), 2010 May. PMID 19681912
    2. Plasma ceruloplasmin ferroxidase activity correlates with the nigral sonographic area in Parkinson's disease patients: a pilot study. Martínez-Hernández R, et al. Neurochem Res, 2011 Nov. PMID 21706376
    3. Label-free quantitative proteomics reveals differentially regulated proteins influencing urolithiasis. Wright CA, et al. Mol Cell Proteomics, 2011 Aug. PMID 21474797, Free PMC Article
    4. Decreased serum ceruloplasmin levels characteristically aggravate nigral iron deposition in Parkinson's disease. Jin L, et al. Brain, 2011 Jan. PMID 21109502
    5. Hepatic but not brain iron is rapidly chelated by deferasirox in aceruloplasminemia due to a novel gene mutation. Finkenstedt A, et al. J Hepatol, 2010 Dec. PMID 20801540, Free PMC Article

    See all (228) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Ceruloplasmin expression in renal cell carcinoma correlates with higher-grade and shortened survival.
      Title: Ceruloplasmin expression in renal cell carcinoma correlates with higher-grade and shortened survival.
    2. Tumor associated macrophages transfer ceruloplasmin mRNA to fibrosarcoma cells and protect them from ferroptosis.
      Title: Tumor associated macrophages transfer ceruloplasmin mRNA to fibrosarcoma cells and protect them from ferroptosis.
    3. Ceruloplasmin Reduces the Lactoferrin/Oleic Acid Antitumor Complex-Mediated Release of Heme-Containing Proteins from Blood Cells.
      Title: Ceruloplasmin Reduces the Lactoferrin/Oleic Acid Antitumor Complex-Mediated Release of Heme-Containing Proteins from Blood Cells.
    4. Wilson's disease: overview.
      Title: Wilson's disease: overview.
    5. Ceruloplasmin gene variants are associated with hyperferritinemia and increased liver iron in patients with NAFLD.
      Title: Ceruloplasmin gene variants are associated with hyperferritinemia and increased liver iron in patients with NAFLD.
    6. Ceruloplasmin overexpression is associated with oncogenic pathways and poorer survival rates in clear-cell renal cell carcinoma.
      Title: Ceruloplasmin overexpression is associated with oncogenic pathways and poorer survival rates in clear-cell renal cell carcinoma.
    7. Iron Deficiency in Inflammatory Bowel Disease Is Associated With Low Levels of Vitamin D Modulating Serum Hepcidin and Intestinal Ceruloplasmin Expression.
      Title: Iron Deficiency in Inflammatory Bowel Disease Is Associated With Low Levels of Vitamin D Modulating Serum Hepcidin and Intestinal Ceruloplasmin Expression.
    8. Ceruloplasmin as Redox Marker Related to Heart Failure Severity.
      Title: Ceruloplasmin as Redox Marker Related to Heart Failure Severity.
    9. Genetic Variability in the Iron Homeostasis Pathway and Patient Outcomes After Aneurysmal Subarachnoid Hemorrhage.
      Title: Genetic Variability in the Iron Homeostasis Pathway and Patient Outcomes After Aneurysmal Subarachnoid Hemorrhage.
    10. Urinary levels of ceruloplasmin and monocyte chemoattractant protein-1 correlate with extra-capillary proliferation and chronic damage in patients with lupus nephritis.
      Title: Urinary levels of ceruloplasmin and monocyte chemoattractant protein-1 correlate with extra-capillary proliferation and chronic damage in patients with lupus nephritis.
    Submit: New GeneRIF Correction See all GeneRIFs (141)

    Phenotypes

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    Find tests for this gene in the NIH Genetic Testing Registry (GTR)

    Review eQTL and phenotype association data in this region using PheGenI

    EBI GWAS Catalog

    Description
    Clinical and genetic association of serum ceruloplasmin with cardiovascular risk.
    EBI GWAS Catalog
    Genome-wide association for abdominal subcutaneous and visceral adipose reveals a novel locus for visceral fat in women.
    EBI GWAS Catalog

    Variation

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    See variants in ClinVar

    See studies and variants in dbVar

    See Variation Viewer (GRCh37.p13)

    See Variation Viewer (GRCh38)

    HIV-1 interactions

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    Protein interactions

    Protein Gene Interaction Pubs
    Tat tat Microarray analysis indicates HIV-1 Tat-induced upregulation of ceruloplasmin (CP; ferroxidase) in primary human brain microvascular endothelial cells PubMed

    Go to the HIV-1, Human Interaction Database

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Markers

    Homology

    Gene Ontology Provided by GOA

    Function Evidence Code Pubs
    enables copper ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ferroxidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ferroxidase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables ferroxidase activity TAS
    Traceable Author Statement
    more info
    		  
    enables glutathione peroxidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables oxidoreductase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables oxidoreductase activity, acting on metal ions, oxygen as acceptor IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables phospholipid-hydroperoxide glutathione peroxidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein-folding chaperone binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in cellular oxidant detoxification IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in intracellular copper ion homeostasis IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in intracellular iron ion homeostasis IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in intracellular iron ion homeostasis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in intracellular iron ion homeostasis TAS
    Traceable Author Statement
    more info
    		  
    involved_in iron ion transport IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Component Evidence Code Pubs
    located_in blood microparticle HDA PubMed 
    located_in endoplasmic reticulum lumen TAS
    Traceable Author Statement
    more info
    		  
    located_in extracellular exosome HDA PubMed 
    located_in extracellular region NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    located_in extracellular region TAS
    Traceable Author Statement
    more info
    		  
    located_in extracellular space HDA PubMed 
    located_in extracellular space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in lysosomal membrane HDA PubMed 
    is_active_in plasma membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    ceruloplasmin
    Names
    ceruloplasmin (ferroxidase)
    cuproxidase ceruloplasmin
    ferroxidase ceruloplasmin
    glutathione peroxidase ceruloplasmin
    glutathione-dependent peroxiredoxin ceruloplasmin
    NP_000087.2
    XP_006713562.1
    XP_006713563.1
    XP_006713564.1
    XP_011510737.1
    XP_016861223.1
    XP_016861224.1
    XP_054201271.1
    XP_054201272.1
    XP_054201273.1
    XP_054201274.1
    XP_054201275.1
    XP_054201276.1

    NCBI Reference Sequences (RefSeq)

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    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.

    Genomic

    1. NG_011800.3 RefSeqGene

      Range
      5217..54549
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_000096.4 → NP_000087.2  ceruloplasmin precursor

      Status: REVIEWED

      Description
      Transcript Variant: This variant (1) represents the longer, protein-coding transcript.
      Source sequence(s)
      AC093001, AC131209
      Consensus CDS
      CCDS3141.1
      UniProtKB/Swiss-Prot
      P00450, Q14063, Q2PP18, Q9UKS4
      UniProtKB/TrEMBL
      A5PL27
      Related
      ENSP00000264613.6, ENST00000264613.11
      Conserved Domains (6) summary
      cd04222
      Location:22 → 202
      CuRO_1_ceruloplasmin; The first cupredoxin domain of Ceruloplasmin
      cd04224
      Location:369 → 572
      CuRO_3_ceruloplasmin; The third cupredoxin domain of Ceruloplasmin
      cd04225
      Location:732 → 902
      CuRO_5_ceruloplasmin; The fifth cupredoxin domain of Ceruloplasmin
      cd11012
      Location:913 → 1057
      CuRO_6_ceruloplasmin; The sixth cupredoxin domain of Ceruloplasmin
      cd11021
      Location:214 → 354
      CuRO_2_ceruloplasmin; The second cupredoxin domain of Ceruloplasmin
      cd11022
      Location:575 → 718
      CuRO_4_ceruloplasmin; The fourth cupredoxin domain of Ceruloplasmin

    RNA

    1. NR_046371.2 RNA Sequence

      Status: REVIEWED

      Description
      Transcript Variant: This variant (2) lacks an alternate internal exons and has a different 3' end structure compared to variant 1. This variant is represented as non-coding because the use of the 5'-most supported translational start codon, as used in variant 1, renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).
      Source sequence(s)
      AC093001, AC131209
      Related
      ENST00000481169.5

    RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

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

    Reference GRCh38.p14 Primary Assembly

    Genomic

    1. NC_000003.12 Reference GRCh38.p14 Primary Assembly

      Range
      149162414..149221829 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_006713499.4 → XP_006713562.1  ceruloplasmin isoform X2

      UniProtKB/TrEMBL
      A5PL27
      Conserved Domains (6) summary
      cd04222
      Location:22 → 202
      CuRO_1_ceruloplasmin; The first cupredoxin domain of Ceruloplasmin
      cd04224
      Location:369 → 572
      CuRO_3_ceruloplasmin; The third cupredoxin domain of Ceruloplasmin
      cd04225
      Location:732 → 902
      CuRO_5_ceruloplasmin; The fifth cupredoxin domain of Ceruloplasmin
      cd11012
      Location:913 → 1057
      CuRO_6_ceruloplasmin; The sixth cupredoxin domain of Ceruloplasmin
      cd11021
      Location:214 → 354
      CuRO_2_ceruloplasmin; The second cupredoxin domain of Ceruloplasmin
      cd11022
      Location:575 → 718
      CuRO_4_ceruloplasmin; The fourth cupredoxin domain of Ceruloplasmin

    2. XM_011512435.3 → XP_011510737.1  ceruloplasmin isoform X1

      UniProtKB/TrEMBL
      A5PL27
      Conserved Domains (6) summary
      cd04222
      Location:22 → 202
      CuRO_1_ceruloplasmin; The first cupredoxin domain of Ceruloplasmin
      cd04224
      Location:369 → 572
      CuRO_3_ceruloplasmin; The third cupredoxin domain of Ceruloplasmin
      cd04225
      Location:732 → 902
      CuRO_5_ceruloplasmin; The fifth cupredoxin domain of Ceruloplasmin
      cd11012
      Location:913 → 1057
      CuRO_6_ceruloplasmin; The sixth cupredoxin domain of Ceruloplasmin
      cd11021
      Location:214 → 354
      CuRO_2_ceruloplasmin; The second cupredoxin domain of Ceruloplasmin
      cd11022
      Location:575 → 718
      CuRO_4_ceruloplasmin; The fourth cupredoxin domain of Ceruloplasmin

    3. XM_017005735.3 → XP_016861224.1  ceruloplasmin isoform X6

      UniProtKB/TrEMBL
      Q1L857

    4. XM_006713500.5 → XP_006713563.1  ceruloplasmin isoform X3

      UniProtKB/TrEMBL
      A5PL27
      Conserved Domains (6) summary
      cd04222
      Location:22 → 202
      CuRO_1_ceruloplasmin; The first cupredoxin domain of Ceruloplasmin
      cd04224
      Location:369 → 572
      CuRO_3_ceruloplasmin; The third cupredoxin domain of Ceruloplasmin
      cd04225
      Location:732 → 902
      CuRO_5_ceruloplasmin; The fifth cupredoxin domain of Ceruloplasmin
      cd11012
      Location:913 → 1057
      CuRO_6_ceruloplasmin; The sixth cupredoxin domain of Ceruloplasmin
      cd11021
      Location:214 → 354
      CuRO_2_ceruloplasmin; The second cupredoxin domain of Ceruloplasmin
      cd11022
      Location:575 → 718
      CuRO_4_ceruloplasmin; The fourth cupredoxin domain of Ceruloplasmin

    5. XM_006713501.4 → XP_006713564.1  ceruloplasmin isoform X5

      UniProtKB/TrEMBL
      A5PL27
      Conserved Domains (6) summary
      cd04222
      Location:22 → 202
      CuRO_1_ceruloplasmin; The first cupredoxin domain of Ceruloplasmin
      cd04224
      Location:369 → 572
      CuRO_3_ceruloplasmin; The third cupredoxin domain of Ceruloplasmin
      cd04225
      Location:732 → 902
      CuRO_5_ceruloplasmin; The fifth cupredoxin domain of Ceruloplasmin
      cd11012
      Location:913 → 1057
      CuRO_6_ceruloplasmin; The sixth cupredoxin domain of Ceruloplasmin
      cd11021
      Location:214 → 354
      CuRO_2_ceruloplasmin; The second cupredoxin domain of Ceruloplasmin
      cd11022
      Location:575 → 718
      CuRO_4_ceruloplasmin; The fourth cupredoxin domain of Ceruloplasmin

    6. XM_017005734.3 → XP_016861223.1  ceruloplasmin isoform X4

      UniProtKB/TrEMBL
      A5PL27

    RNA

    1. XR_427361.4 RNA Sequence

      Related
      ENST00000490639.5

    Alternate T2T-CHM13v2.0

    Genomic

    1. NC_060927.1 Alternate T2T-CHM13v2.0

      Range
      151913150..151972585 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_054345297.1 → XP_054201272.1  ceruloplasmin isoform X2

    2. XM_054345296.1 → XP_054201271.1  ceruloplasmin isoform X1

    3. XM_054345301.1 → XP_054201276.1  ceruloplasmin isoform X6

    4. XM_054345298.1 → XP_054201273.1  ceruloplasmin isoform X3

    5. XM_054345300.1 → XP_054201275.1  ceruloplasmin isoform X5

    6. XM_054345299.1 → XP_054201274.1  ceruloplasmin isoform X4

    RNA

    1. XR_008486661.1 RNA Sequence

    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P00450.2 GenPept UniProtKB/Swiss-Prot:P00450

    Gene LinkOut

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