Details for: CP

Gene ID: 1356

Gene Type:  Protein-coding  - A gene that serves as a template for producing a messenger RNA (mRNA) molecule, which is then translated into a functional protein.

Symbol: CP

Ensembl ID: ENSG00000047457

Description: ceruloplasmin

Selected Context(s):  Overall

Cell Significance Landscape

Contexts:

Associated with

Significant Cells

Cell Significance Index (CSI) scores for the chosen context(s)

  • epithelial cell of lower respiratory tract CL0002632
    CSI 35.8
    rCSI 27.76%
    PRS 97.92
  • hepatocyte CL0000182
    CSI 33.45
    rCSI 59.87%
    PRS 95.01
  • Mueller cell CL0000636
    CSI 21.84
    rCSI 49.83%
    PRS 93.18
  • midzonal region hepatocyte CL0019028
    CSI 21.79
    rCSI 51.12%
    PRS 94.11
  • centrilobular region hepatocyte CL0019029
    CSI 18.52
    rCSI 48.31%
    PRS 93.18
  • duct epithelial cell CL0000068
    CSI 16.65
    rCSI 24.37%
    PRS 98.04
  • nasal mucosa goblet cell CL0002480
    CSI 16.26
    rCSI 18.86%
    PRS 95.99
  • club cell CL0000158
    CSI 16.19
    rCSI 23.71%
    PRS 94.76
  • tracheal goblet cell CL1000329
    CSI 16.18
    rCSI 35.32%
    PRS 96.97
  • goblet cell CL0000160
    CSI 15.1
    rCSI 14.27%
    PRS 95.21
  • conjunctival epithelial cell CL1000432
    CSI 14.36
    rCSI 21.93%
    PRS 95.67
  • periportal region hepatocyte CL0019026
    CSI 13.87
    rCSI 53.93%
    PRS 93.64
  • fallopian tube secretory epithelial cell CL4030006
    CSI 13.65
    rCSI 13.14%
    PRS 95.63
  • pancreatic acinar cell CL0002064
    CSI 13.58
    rCSI 18.04%
    PRS 97.44
  • glandular epithelial cell CL0000150
    CSI 13.32
    rCSI 35.08%
    PRS 98.98
  • skin fibroblast CL0002620
    CSI 12.96
    rCSI 11.17%
    PRS 96.65
  • epithelial cell of lung CL0000082
    CSI 11.71
    rCSI 9.71%
    PRS 97.49
  • bronchial goblet cell CL1000312
    CSI 10.87
    rCSI 43.43%
    PRS 97.8
  • mucus secreting cell CL0000319
    CSI 9.99
    rCSI 15.86%
    PRS 98.26
  • lung ciliated cell CL1000271
    CSI 8.47
    rCSI 9.79%
    PRS 93.38
  • multi-ciliated epithelial cell CL0005012
    CSI 8.29
    rCSI 8.27%
    PRS 93.26
  • ciliated cell CL0000064
    CSI 8.15
    rCSI 13.2%
    PRS 92.22
  • melanocyte CL0000148
    CSI 8.1
    rCSI 6%
    PRS 94.72
  • ependymal cell CL0000065
    CSI 7.95
    rCSI 16.14%
    PRS 85.36
  • secretory cell CL0000151
    CSI 7.57
    rCSI 7.9%
    PRS 96.07
  • lung secretory cell CL1000272
    CSI 7.33
    rCSI 18.15%
    PRS 97.55
  • stem cell CL0000034
    CSI 6.47
    rCSI 6.24%
    PRS 95.09
  • respiratory suprabasal cell CL4033048
    CSI 6.38
    rCSI 8.18%
    PRS 97.24
  • acinar cell CL0000622
    CSI 6.29
    rCSI 9.22%
    PRS 98.24
  • respiratory basal cell CL0002633
    CSI 6.06
    rCSI 6.27%
    PRS 97.32
  • choroid plexus epithelial cell CL0000706
    CSI 5.98
    rCSI 9.8%
    PRS 93.17
  • Kupffer cell CL0000091
    CSI 5.88
    rCSI 13.44%
    PRS 97.07
  • microcirculation associated smooth muscle cell CL0008035
    CSI 5.43
    rCSI 15.71%
    PRS 96.21
  • retinal blood vessel endothelial cell CL0002585
    CSI 5.16
    rCSI 8.24%
    PRS 97.59
  • hepatic stellate cell CL0000632
    CSI 4.88
    rCSI 18.29%
    PRS 94.92
  • ciliated columnar cell of tracheobronchial tree CL0002145
    CSI 4.79
    rCSI 10.92%
    PRS 91.73
  • keratocyte CL0002363
    CSI 4.74
    rCSI 11.39%
    PRS 96.86
  • ciliated epithelial cell CL0000067
    CSI 4.7
    rCSI 4.14%
    PRS 91.46
  • respiratory goblet cell CL0002370
    CSI 4.56
    rCSI 49.62%
    PRS 97.74
  • erythroblast CL0000765
    CSI 4.56
    rCSI 12.1%
    PRS 96.19
  • ionocyte CL0005006
    CSI 4.55
    rCSI 4.88%
    PRS 97.03
  • myoepithelial cell CL0000185
    CSI 4.48
    rCSI 11.33%
    PRS 97.69
  • cerebral cortex endothelial cell CL1001602
    CSI 4.39
    rCSI 7.59%
    PRS 94.15
  • chondrocyte CL0000138
    CSI 4.27
    rCSI 6.79%
    PRS 94.15
  • pulmonary ionocyte CL0017000
    CSI 4.14
    rCSI 5.04%
    PRS 97.71
  • squamous epithelial cell CL0000076
    CSI 3.81
    rCSI 9.04%
    PRS 93.17
  • serous secreting cell CL0000313
    CSI 3.79
    rCSI 19.14%
    PRS 97.46
  • brush cell of tracheobronchial tree CL0002075
    CSI 3.63
    rCSI 10.79%
    PRS 98.61
  • mesenchymal stem cell of adipose tissue CL0002570
    CSI 3.57
    rCSI 19.93%
    PRS 97.5
  • luminal epithelial cell of mammary gland CL0002326
    CSI 3.49
    rCSI 6.34%
    PRS 98.19
  • endocardial cell CL0002350
    CSI 3.43
    rCSI 16.44%
    PRS 94.67
  • intrahepatic cholangiocyte CL0002538
    CSI 3.25
    rCSI 7.8%
    PRS 96.04
  • stromal cell CL0000499
    CSI 3.14
    rCSI 8.83%
    PRS 94.93
  • tracheobronchial serous cell CL0019001
    CSI 3.06
    rCSI 13.22%
    PRS 97.33
  • tracheobronchial goblet cell CL0019003
    CSI 3.01
    rCSI 48.37%
    PRS 96.92
  • fibroblast of lung CL0002553
    CSI 2.94
    rCSI 2.74%
    PRS 97.67
  • glial cell CL0000125
    CSI 2.69
    rCSI 10.23%
    PRS 92.76
  • retinal pigment epithelial cell CL0002586
    CSI 2.67
    rCSI 5.3%
    PRS 94.46
  • vascular leptomeningeal cell CL4023051
    CSI 2.66
    rCSI 4.66%
    PRS 94.84
  • endothelial cell of pericentral hepatic sinusoid CL0019022
    CSI 2.65
    rCSI 8.17%
    PRS 96.86
  • smooth muscle cell CL0000192
    CSI 2.57
    rCSI 6.13%
    PRS 93.78
  • deuterosomal cell CL4033044
    CSI 2.22
    rCSI 7.5%
    PRS 92.25
  • macroglial cell CL0000126
    CSI 2.14
    rCSI 5.49%
    PRS 93.96
  • cholangiocyte CL1000488
    CSI 1.87
    rCSI 11.22%
    PRS 94.84
  • pancreatic ductal cell CL0002079
    CSI 1.48
    rCSI 2.88%
    PRS 96.72
  • endothelial cell of uterus CL0009095
    CSI 1.46
    rCSI 10.71%
    PRS 98.65
  • basal cell of epithelium of trachea CL1000348
    CSI 1.25
    rCSI 8.82%
    PRS 96.54
  • airway submucosal gland duct basal cell CL4033024
    CSI 1.23
    rCSI 7.85%
    PRS 97.3
  • lung goblet cell CL1000143
    CSI 1.09
    rCSI 12.21%
    PRS 97.5
  • stratified epithelial cell CL0000079
    CSI 1.08
    rCSI 6.64%
    PRS 96.93
  • pancreatic PP cell CL0002275
    CSI 1.02
    rCSI 4.04%
    PRS 96.78
  • luminal cell of prostate epithelium CL0002340
    CSI 0.77
    rCSI 4.17%
    PRS 97.89
  • exhausted T cell CL0011025
    CSI 0.56
    rCSI 9.51%
    PRS 97.16
  • blood vessel smooth muscle cell CL0019018
    CSI 0.4
    rCSI 3.28%
    PRS 96.04

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.

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 cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

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 cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Network Configuration

Explore relationships of the current gene. Select an Interaction Source: 'ONTOLOGY' for shared pathways (GO/Reactome) or 'STRING' for protein-protein interactions. Further refine by selecting context genes and comparing Cell Significance Index (CSI) scores between baseline and target cell types and their specific contexts.

Comma-separated if multiple.
Comma-separated if multiple.
Legend:
  • Query Gene
  • Node Color (Target Cell CSI, relative to current network):
    • Very High
    • High
    • Medium
    • Low
    • Very Low
    • CSI N/A
  • Node Size: Proportional to Target Cell CSI magnitude
  • STRING PPI Edge
  • Shared Pathway Edge (ONTOLOGY)

Loading network (please wait)...

Other Information

This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.

## Summary [CP](/details-gene/1356), or ceruloplasmin, is a protein-coding gene located on chromosome 3 that encodes the enzyme ceruloplasmin, a major copper-carrying protein in the blood. Functionally, it is a multicopper ferroxidase that plays a central role in iron and copper metabolism by converting toxic ferrous iron (Fe2+) to its non-toxic ferric form (Fe3+). **Overall**, expression data indicates that [CP](/details-gene/1356) is most significantly expressed in secretory and metabolic tissues, with particularly high significance in [epithelial cells of the lower respiratory tract](/details-cell/CL0002632) and [hepatocytes](/details-cell/CL0000182). Mutations in this gene are associated with the autosomal recessive disorder aceruloplasminemia ([117700](https://omim.org/entry/117700)), characterized by iron accumulation in various tissues. ## Cellular Roles and Expression Landscape The expression profile of [CP](/details-gene/1356) highlights its essential function in tissues responsible for metabolism, secretion, and barrier defense. The highest significance is observed in [hepatocytes](/details-cell/CL0000182) (CSI: 33.45), the primary site of ceruloplasmin synthesis for systemic circulation, with strong expression noted across all liver zones, including [midzonal](/details-cell/CL0019028), [centrilobular](/details-cell/CL0019029), and [periportal](/details-cell/CL0019026) regions. This underscores its foundational role in systemic iron homeostasis. Interestingly, the top-ranked cell type is the [epithelial cell of the lower respiratory tract](/details-cell/CL0002632) (CSI: 35.80), suggesting a critical local function in the lungs. This is further supported by high significance in other secretory epithelial cells, such as [nasal mucosa goblet cells](/details-cell/CL0002480), [club cells](/details-cell/CL0000158), and [pancreatic acinar cells](/details-cell/CL0002064). This pattern suggests that in addition to its systemic role as a plasma protein, locally produced ceruloplasmin may be crucial for managing iron and providing antioxidant protection at mucosal surfaces and in exocrine glands. ## Pathways and Molecular Function The functions of [CP](/details-gene/1356) are tightly linked to metal ion handling and redox chemistry. Its primary molecular function is [ferroxidase activity](/details-go/GO:0004322), which is essential for the biological process of [iron ion transport](/details-go/GO:0006826). By oxidizing ferrous iron, it facilitates iron's binding to transferrin for safe transport in the circulation, a key step in the [Iron uptake and transport](/details-pathway/R-HSA-917937) pathway. This activity is critical for maintaining [intracellular iron ion homeostasis](/details-go/GO:0006879). Beyond its role in iron metabolism, [CP](/details-gene/1356) is a key player in [copper ion binding](/details-go/GO:0005507) and homeostasis. The gene product is also implicated in antioxidant defense through [cellular oxidant detoxification](/details-go/GO:0098869) and has demonstrated [glutathione peroxidase activity](/details-go/GO:0004602), which may be particularly relevant in its high-expression sites like the lung ([Link](https://doi.org/10.1016/s0014-5793(99)01142-4)). Its localization to the [extracellular space](/details-go/GO:0005615) and presence in [blood microparticles](/details-go/GO:0072562) are consistent with its role as a secreted plasma protein. Clinically, the significance of [CP](/details-gene/1356) is underscored by its involvement in the Reactome pathway [Defective cp causes aceruloplasminemia](/details-pathway/R-HSA-5619060), a disorder of iron metabolism. ## Research Directions The expression profile and known functions of [CP](/details-gene/1356) suggest several avenues for future investigation, particularly concerning its tissue-specific roles beyond systemic iron transport. **Testable Hypotheses:** 1. Given its exceptionally high significance in [epithelial cells of the lower respiratory tract](/details-cell/CL0002632) and its known antioxidant properties, local [CP](/details-gene/1356) expression may be a primary defense mechanism against oxidative damage from inhaled pollutants and pathogens, with its ferroxidase activity preventing iron-driven Fenton reactions. 2. The consistent high expression in diverse secretory cells ([goblet cells](/details-cell/CL0000160), [pancreatic acinar cells](/details-cell/CL0002064), [fallopian tube secretory epithelial cells](/details-cell/CL4030006)) suggests that ceruloplasmin secretion into luminal fluids is a conserved mechanism to regulate local iron availability, potentially influencing mucus properties or exerting antimicrobial effects by sequestering essential microbial nutrients. **Proposed Experiment:** To test the first hypothesis regarding the protective role of [CP](/details-gene/1356) in the lung, a lung-specific conditional knockout mouse model (e.g., using a Cre-Lox system with a lung epithelial-specific promoter like SPC-Cre) could be generated. These knockout mice and wild-type controls would be exposed to an oxidative challenge, such as hyperoxia, ozone, or cigarette smoke. The resulting lung injury could be assessed via bronchoalveolar lavage fluid (BALF) cell counts, histological analysis for inflammation and edema, and biochemical assays for lipid peroxidation and protein oxidation. Additionally, iron deposition in lung tissue could be quantified using Perl's Prussian blue staining to directly link the loss of local ferroxidase activity to pathological iron accumulation and subsequent oxidative stress. **Therapeutic Potential:** [CP](/details-gene/1356) is not a conventional therapeutic target for inhibition, as its loss of function leads to severe disease (aceruloplasminemia). Instead, therapeutic strategies would focus on **restoration or replacement**. For patients with aceruloplasminemia, enzyme replacement therapy using purified or recombinant human ceruloplasmin is a logical approach to restore systemic ferroxidase activity and mitigate tissue iron overload. Because ceruloplasmin is a secreted, circulating protein, systemic administration is a feasible delivery strategy. Furthermore, enhancing its local expression or activity in the lung could be explored as a protective strategy against chronic inflammatory lung diseases characterized by high oxidative stress, such as COPD, although this would require advanced gene or protein delivery technologies.

Genular Protein ID: 1840105270

Symbol: CERU_HUMAN

Name: Ferroxidase ceruloplasmin

UniProtKB Accession Codes:

P00450 Q14063 Q2PP18 Q9UKS4

Database IDs:

AGR 1 AlphaFoldDB 1 Antibodypedia 1 BRENDA 1 Bgee 1 BioCyc 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 1 CDD 6 CORUM 1 CPTAC 4 CTD 1 CarbonylDB 1 ChEBI 65 ChiTaRS 1 DMDM 1 DNASU 1 DisGeNET 1 DrugBank 16 EC 4 EMBL 11 Ensembl 1 EvolutionaryTrace 1 ExpressionAtlas 1 GO 17 Gene3D 1 GeneCards 1 GeneReviews 1 GeneTree 1 GeneWiki 1 GenomeRNAi 1 GlyConnect 1 GlyCosmos 1 GlyGen 1 HGNC 1 HPA 1 InParanoid 1 IntAct 1 InterPro 8 KEGG 1 MANE-Select 1 MIM 3 MINT 1 MalaCards 1 MassIVE 1 NCBI Taxonomy 1 OpenTargets 1 Orphanet 1 OrthoDB 1 PANTHER 2 PCDDB 1 PDB 4 PDBsum 4 PIR 1 PRIDE 1 PRO 1 PROSITE 2 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 3 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 1 Pumba 1 RNAct 1 Reactome 6 RefSeq 1 Rhea 10 SABIO-RK 1 SASBDB 1 SIGNOR 1 SMR 1 STRING 1 SUPFAM 1 SignaLink 1 SwissPalm 1 TCDB 1 TreeFam 1 UCSC 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 2873574

Title: Complete cDNA sequence of human preceruloplasmin.

PubMed ID: 2873574

DOI: 10.1073/pnas.83.14.5086

PubMed ID: 7702601

Title: Fine structure of the human ceruloplasmin gene.

PubMed ID: 7702601

DOI: 10.1006/bbrc.1995.1437

PubMed ID: 3755405

Title: Isolation of a human ceruloplasmin cDNA clone that includes the N-terminal leader sequence.

PubMed ID: 3755405

DOI: 10.1016/0014-5793(86)80739-6

PubMed ID: 3486416

Title: Characterization, mapping, and expression of the human ceruloplasmin gene.

PubMed ID: 3486416

DOI: 10.1073/pnas.83.10.3257

PubMed ID: 6582496

Title: Single-chain structure of human ceruloplasmin: the complete amino acid sequence of the whole molecule.

PubMed ID: 6582496

DOI: 10.1073/pnas.81.2.390

PubMed ID: 6571985

Title: Internal triplication in the structure of human ceruloplasmin.

PubMed ID: 6571985

DOI: 10.1073/pnas.80.1.115

PubMed ID: 6940148

Title: Complete amino acid sequence of a 50,000-dalton fragment of human ceruloplasmin.

PubMed ID: 6940148

DOI: 10.1073/pnas.78.2.790

PubMed ID: 6987229

Title: Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. I. Amino acid sequence of the cyanogen bromide peptides.

PubMed ID: 6987229

DOI: 10.1016/s0021-9258(19)85822-2

PubMed ID: 6987230

Title: Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. II. Amino acid sequence of the tryptic peptides.

PubMed ID: 6987230

DOI: 10.1016/s0021-9258(19)85823-4

PubMed ID: 2355023

Title: Human ceruloplasmin. Tissue-specific expression of transcripts produced by alternative splicing.

PubMed ID: 2355023

DOI: 10.1016/s0021-9258(18)87015-6

PubMed ID: 5912351

Title: The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum.

PubMed ID: 5912351

DOI: 10.1016/s0021-9258(18)96527-0

PubMed ID: 4643313

Title: A method for obtaining linear reciprocal plots with caeruloplasmin and its application in a study of the kinetic parameters of caeruloplasmin substrates.

PubMed ID: 4643313

DOI: 10.1042/bj1290273

PubMed ID: 10508415

Title: Ceruloplasmin has a distinct active site for the catalyzing glutathione-dependent reduction of alkyl hydroperoxide.

PubMed ID: 10508415

DOI: 10.1021/bi990444b

PubMed ID: 10481051

Title: Glutathione peroxidase-like activity of caeruloplasmin as an important lung antioxidant.

PubMed ID: 10481051

DOI: 10.1016/s0014-5793(99)01142-4

PubMed ID: 12055353

Title: Ceruloplasmin metabolism and function.

PubMed ID: 12055353

DOI: 10.1146/annurev.nutr.22.012502.114457

PubMed ID: 14623105

Title: Cuprous oxidase activity of yeast Fet3p and human ceruloplasmin: implication for function.

PubMed ID: 14623105

DOI: 10.1016/s0014-5793(03)01218-3

PubMed ID: 15084671

Title: A proteomic analysis of human bile.

PubMed ID: 15084671

DOI: 10.1074/mcp.m400015-mcp200

PubMed ID: 14760718

Title: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.

PubMed ID: 14760718

DOI: 10.1002/pmic.200300556

PubMed ID: 16335952

Title: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.

PubMed ID: 16335952

DOI: 10.1021/pr0502065

PubMed ID: 16906150

Title: Ceruloplasmin is a NO oxidase and nitrite synthase that determines endocrine NO homeostasis.

PubMed ID: 16906150

DOI: 10.1038/nchembio813

PubMed ID: 19159218

Title: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.

PubMed ID: 19159218

DOI: 10.1021/pr8008012

PubMed ID: 19139490

Title: A strategy for precise and large scale identification of core fucosylated glycoproteins.

PubMed ID: 19139490

DOI: 10.1074/mcp.m800504-mcp200

PubMed ID: 19838169

Title: Enrichment of glycopeptides for glycan structure and attachment site identification.

PubMed ID: 19838169

DOI: 10.1038/nmeth.1392

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: 26091039

Title: A single kinase generates the majority of the secreted phosphoproteome.

PubMed ID: 26091039

DOI: 10.1016/j.cell.2015.05.028

PubMed ID: 29183916

Title: Ceruloplasmin replacement therapy ameliorates neurological symptoms in a preclinical model of aceruloplasminemia.

PubMed ID: 29183916

DOI: 10.15252/emmm.201708361

PubMed ID: 17242517

Title: Ceruloplasmin revisited: structural and functional roles of various metal cation-binding sites.

PubMed ID: 17242517

DOI: 10.1107/s090744490604947x

PubMed ID: 23843990

Title: Ceruloplasmin: macromolecular assemblies with iron-containing acute phase proteins.

PubMed ID: 23843990

DOI: 10.1371/journal.pone.0067145

PubMed ID: 7708681

Title: Aceruloplasminemia: molecular characterization of this disorder of iron metabolism.

PubMed ID: 7708681

DOI: 10.1073/pnas.92.7.2539

PubMed ID: 15557511

Title: Ceruloplasmin gene variations and substantia nigra hyperechogenicity in Parkinson disease.

PubMed ID: 15557511

DOI: 10.1212/01.wnl.0000144276.29988.c3

PubMed ID: 16150804

Title: Functional relevance of ceruloplasmin mutations in Parkinson's disease.

PubMed ID: 16150804

DOI: 10.1096/fj.04-3486fje

Sequence Information:

  • Length: 1065
  • Mass: 122219
  • Checksum: 2F2F76BB47D30F58
  • Sequence:
    • MKILILGIFL FLCSTPAWAK EKHYYIGIIE TTWDYASDHG EKKLISVDTE HSNIYLQNGP 
DRIGRLYKKA LYLQYTDETF RTTIEKPVWL GFLGPIIKAE TGDKVYVHLK NLASRPYTFH 
SHGITYYKEH EGAIYPDNTT DFQRADDKVY PGEQYTYMLL ATEEQSPGEG DGNCVTRIYH 
SHIDAPKDIA SGLIGPLIIC KKDSLDKEKE KHIDREFVVM FSVVDENFSW YLEDNIKTYC 
SEPEKVDKDN EDFQESNRMY SVNGYTFGSL PGLSMCAEDR VKWYLFGMGN EVDVHAAFFH 
GQALTNKNYR IDTINLFPAT LFDAYMVAQN PGEWMLSCQN LNHLKAGLQA FFQVQECNKS 
SSKDNIRGKH VRHYYIAAEE IIWNYAPSGI DIFTKENLTA PGSDSAVFFE QGTTRIGGSY 
KKLVYREYTD ASFTNRKERG PEEEHLGILG PVIWAEVGDT IRVTFHNKGA YPLSIEPIGV 
RFNKNNEGTY YSPNYNPQSR SVPPSASHVA PTETFTYEWT VPKEVGPTNA DPVCLAKMYY 
SAVEPTKDIF TGLIGPMKIC KKGSLHANGR QKDVDKEFYL FPTVFDENES LLLEDNIRMF 
TTAPDQVDKE DEDFQESNKM HSMNGFMYGN QPGLTMCKGD SVVWYLFSAG NEADVHGIYF 
SGNTYLWRGE RRDTANLFPQ TSLTLHMWPD TEGTFNVECL TTDHYTGGMK QKYTVNQCRR 
QSEDSTFYLG ERTYYIAAVE VEWDYSPQRE WEKELHHLQE QNVSNAFLDK GEFYIGSKYK 
KVVYRQYTDS TFRVPVERKA EEEHLGILGP QLHADVGDKV KIIFKNMATR PYSIHAHGVQ 
TESSTVTPTL PGETLTYVWK IPERSGAGTE DSACIPWAYY STVDQVKDLY SGLIGPLIVC 
RRPYLKVFNP RRKLEFALLF LVFDENESWY LDDNIKTYSD HPEKVNKDDE EFIESNKMHA 
INGRMFGNLQ GLTMHVGDEV NWYLMGMGNE IDLHTVHFHG HSFQYKHRGV YSSDVFDIFP 
GTYQTLEMFP RTPGIWLLHC HVTDHIHAGM ETTYTVLQNE DTKSG

Genular Protein ID: 786062727

Symbol: A5PL27_HUMAN

Name: N/A

UniProtKB Accession Codes:

A5PL27

Database IDs:

ARBA 4 AlphaFoldDB 1 BioGRID-ORCS 1 CDD 6 CTD 1 ChiTaRS 1 DNASU 1 DisGeNET 1 EMBL 7 GO 5 Gene3D 1 InterPro 8 KEGG 1 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PROSITE 2 Pfam 6 PharmGKB 1 RefSeq 1 SAM 1 SMR 1 SUPFAM 1

Citations:

PubMed ID: 11181995

Title: The sequence of the human genome.

PubMed ID: 11181995

DOI: 10.1126/science.1058040

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

Sequence Information:

  • Length: 1065
  • Mass: 122205
  • Checksum: 2F2F1294E2D30F58
  • Sequence:
    • MKILILGIFL FLCSTPAWAK EKHYYIGIIE TTWDYASDHG EKKLISVDTE HSNIYLQNGP 
DRIGRLYKKA LYLQYTDETF RTTIEKPVWL GFLGPIIKAE TGDKVYVHLK NLASRPYTFH 
SHGITYYKEH EGAIYPDNTT DFQRADDKVY PGEQYTYMLL ATEEQSPGEG DGNCVTRIYH 
SHIDAPKDIA SGLIGPLIIC KKDSLDKEKE KHIDREFVVM FSVVDENFSW YLEDNIKTYC 
SEPEKVDKDN EDFQESNRMY SVNGYTFGSL PGLSMCAEDR VKWYLFGMGN EVDVHAAFFH 
GQALTNKNYR IDTINLFPAT LFDAYMVAQN PGEWMLSCQN LNHLKAGLQA FFQVQECNKS 
SSKDNIRGKH VRHYYIAAEE IIWNYAPSGI DIFTKENLTA PGSDSAVFFE QGTTRIGGSY 
KKLVYREYTD ASFTNRKERG PEEEHLGILG PVIWAEVGDT IRVTFHNKGA YPLSIEPIGV 
RFNKNNEGTY YSPNYNPQSR SVPPSASHVA PTETFTYEWT VPKEVGPTNA DPVCLAKMYY 
SAVDPTKDIF TGLIGPMKIC KKGSLHANGR QKDVDKEFYL FPTVFDENES LLLEDNIRMF 
TTAPDQVDKE DEDFQESNKM HSMNGFMYGN QPGLTMCKGD SVVWYLFSAG NEADVHGIYF 
SGNTYLWRGE RRDTANLFPQ TSLTLHMWPD TEGTFNVECL TTDHYTGGMK QKYTVNQCRR 
QSEDSTFYLG ERTYYIAAVE VEWDYSPQRE WEKELHHLQE QNVSNAFLDK GEFYIGSKYK 
KVVYRQYTDS TFRVPVERKA EEEHLGILGP QLHADVGDKV KIIFKNMATR PYSIHAHGVQ 
TESSTVTPTL PGETLTYVWK IPERSGAGTE DSACIPWAYY STVDQVKDLY SGLIGPLIVC 
RRPYLKVFNP RRKLEFALLF LVFDENESWY LDDNIKTYSD HPEKVNKDDE EFIESNKMHA 
INGRMFGNLQ GLTMHVGDEV NWYLMGMGNE IDLHTVHFHG HSFQYKHRGV YSSDVFDIFP 
GTYQTLEMFP RTPGIWLLHC HVTDHIHAGM ETTYTVLQNE DTKSG