Details for: ACE

Gene ID: 1636

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: ACE

Ensembl ID: ENSG00000159640

Description: angiotensin I converting enzyme

Cell Significance Landscape

Associated with

Significant Cells

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

  • colonocyte CL1000347
    CSI 7.92
    rCSI 11.35%
    PRS 98.88
  • enterocyte CL0000584
    CSI 7.51
    rCSI 12.1%
    PRS 98.14
  • pulmonary capillary endothelial cell CL4028001
    CSI 7.26
    rCSI 13.85%
    PRS 99.68
  • blood vessel endothelial cell CL0000071
    CSI 6.68
    rCSI 13.85%
    PRS 98.89
  • intestine goblet cell CL0019031
    CSI 6.5
    rCSI 5.77%
    PRS 98.71
  • pulmonary artery endothelial cell CL1001568
    CSI 6.3
    rCSI 8.57%
    PRS 99.62
  • goblet cell CL0000160
    CSI 5.77
    rCSI 5.45%
    PRS 98.86
  • GABAergic neuron CL0000617
    CSI 5.4
    rCSI 18.08%
    PRS 94.63
  • lung macrophage CL1001603
    CSI 5.33
    rCSI 11.91%
    PRS 99.78
  • alveolar macrophage CL0000583
    CSI 4.39
    rCSI 7.23%
    PRS 99.24
  • BEST4+ enteroycte CL4030026
    CSI 4.08
    rCSI 5.07%
    PRS 98.77
  • lung endothelial cell CL1001567
    CSI 3.73
    rCSI 8.7%
    PRS 99.67
  • elicited macrophage CL0000861
    CSI 3.41
    rCSI 3.13%
    PRS 99.69
  • alternatively activated macrophage CL0000890
    CSI 2.95
    rCSI 3.71%
    PRS 99.92
  • intestinal epithelial cell CL0002563
    CSI 2.77
    rCSI 2.9%
    PRS 98.66
  • paneth cell of epithelium of small intestine CL1000343
    CSI 2.73
    rCSI 7.65%
    PRS 99.4
  • type EC enteroendocrine cell CL0000577
    CSI 2.24
    rCSI 7.97%
    PRS 98.86
  • type L enteroendocrine cell CL0002279
    CSI 2.17
    rCSI 4.08%
    PRS 98.8
  • dopaminergic neuron CL0000700
    CSI 2.1
    rCSI 11.88%
    PRS 95.95
  • lung microvascular endothelial cell CL2000016
    CSI 1.19
    rCSI 23.01%
    PRS 99.5
  • enterocyte of epithelium of small intestine CL1000334
    CSI 1.04
    rCSI 16.07%
    PRS 99.24
  • direct pathway medium spiny neuron CL4023026
    CSI 0.44
    rCSI 10.63%
    PRS 95.16
  • indirect pathway medium spiny neuron CL4023029
    CSI 0.37
    rCSI 8.88%
    PRS 94.97

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.

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  • Node Color (Target Cell CSI, relative to current network):
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    • High
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    • CSI N/A
  • Node Size: Proportional to Target Cell CSI magnitude
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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 [ACE](/details-gene/1636) (angiotensin I converting enzyme) is a protein-coding gene located on chromosome 17q23.3. It encodes a peptidyl-dipeptidase that is a central component of the renin-angiotensin system (RAS), which regulates blood pressure and fluid-electrolyte balance. The enzyme, located on the external side of the plasma membrane, converts angiotensin I to the potent vasoconstrictor angiotensin II and also inactivates the vasodilator bradykinin ([Link](https://pubmed.ncbi.nlm.nih.gov/4322742/)). Reflecting its systemic role, [ACE](/details-gene/1636) shows high significance in vascular endothelial cells, particularly in the lungs, as well as in epithelial cells of the intestine, such as [colonocytes](/details-cell/CL1000347) and [enterocytes](/details-cell/CL0000584). Its function is clinically significant, with variations and activity levels associated with cardiovascular diseases ([106180](https://omim.org/entry/106180)) and renal tubular dysgenesis ([267430](https://omim.org/entry/267430)). ## Cellular Roles and Expression Landscape The expression profile of [ACE](/details-gene/1636) highlights its critical function in tissues forming major physiological barriers and exchange surfaces. **Overall**, the gene exhibits its highest significance in epithelial cells of the gastrointestinal tract, including [colonocyte](/details-cell/CL1000347) (CSI: 7.92) and [enterocyte](/details-cell/CL0000584) (CSI: 7.51), where it is localized to the brush border membrane ([GO:0031526](https://www.ebi.ac.uk/QuickGO/term/GO:0031526)). This suggests a role in local intestinal processes beyond its systemic functions. Concurrently, [ACE](/details-gene/1636) is a defining marker for the vascular endothelium, with particularly high significance in [pulmonary capillary endothelial cell](/details-cell/CL4028001) (CSI: 7.26), [blood vessel endothelial cell](/details-cell/CL0000071) (CSI: 6.68), and [pulmonary artery endothelial cell](/details-cell/CL1001568) (CSI: 6.30). This is consistent with the lung's primary role in converting circulating angiotensin I. The enzyme's presence has been confirmed in purified human lung tissue ([Link](https://pubmed.ncbi.nlm.nih.gov/2558109/)). Beyond these primary sites, [ACE](/details-gene/1636) also shows notable significance in specific immune cell populations, such as [lung macrophage](/details-cell/CL1001603) (CSI: 5.33) and [alveolar macrophage](/details-cell/CL0000583) (CSI: 4.39), suggesting a potential role in modulating local inflammation and immune responses within the lung microenvironment. A more specialized expression is noted in the nervous system within [GABAergic neuron](/details-cell/CL0000617) (CSI: 5.40), hinting at a function in neuropeptide metabolism. ## Pathways and Molecular Function The primary function of [ACE](/details-gene/1636) is its peptidyl-dipeptidase activity ([GO:0008241](https://www.ebi.ac.uk/QuickGO/term/GO:0008241)), which underpins its involvement in the '[Metabolism of angiotensinogen to angiotensins](/details-pathway/R-HSA-2022377)' pathway. This central activity drives critical physiological processes, most notably the '[Regulation of systemic arterial blood pressure by renin-angiotensin](/details-ontology/GO:0003081)' and '[Positive regulation of vasoconstriction](/details-ontology/GO:0045907)'. The enzyme is a metallopeptidase requiring a zinc ion cofactor ([GO:0008270](https://www.ebi.ac.uk/QuickGO/term/GO:0008270)) for its catalytic function. In addition to its canonical substrates, [ACE](/details-gene/1636) is involved in a broader '[Peptide catabolic process](/details-ontology/GO:0043171)', including the breakdown of bradykinin ([GO:0010815](https://www.ebi.ac.uk/QuickGO/term/GO:0010815)), substance P ([GO:0010814](https://www.ebi.ac.uk/QuickGO/term/GO:0010814)) ([Link](https://pubmed.ncbi.nlm.nih.gov/6208535/)), and enkephalins ([Link](https://pubmed.ncbi.nlm.nih.gov/656131/)). This broader substrate specificity connects it to diverse processes such as '[Neutrophil mediated immunity](/details-ontology/GO:0002446)' and the regulation of synaptic plasticity ([GO:0048167](https://www.ebi.ac.uk/QuickGO/term/GO:0048167)). Its localization to the '[External side of plasma membrane](/details-ontology/GO:0009897)' positions it to act on circulating or locally produced peptide hormones and signaling molecules. ## Research Directions While the systemic cardiovascular role of [ACE](/details-gene/1636) is well-characterized, its high expression in non-classical cell types presents new avenues for investigation. ### Proposed Hypotheses: 1. The high significance of [ACE](/details-gene/1636) in [colonocytes](/details-cell/CL1000347) and [enterocytes](/details-cell/CL0000584) suggests it is a key component of a local gut renin-angiotensin system. This local system may be critical for regulating intestinal epithelial barrier function, nutrient transport, and mucosal immune responses, independent of systemic blood pressure control. 2. The notable expression of [ACE](/details-gene/1636) in [lung macrophages](/details-cell/CL1001603) indicates a direct role in modulating innate immune responses in the lung. By degrading pro-inflammatory peptides like bradykinin or generating angiotensin II, [ACE](/details-gene/1636) on macrophages could fine-tune the local inflammatory milieu during infection or injury, potentially influencing macrophage polarization and cytokine release. ### Experimental Approach: To test the hypothesis regarding the role of [ACE](/details-gene/1636) in lung macrophages, one could perform an *in vitro* study using primary human alveolar macrophages or a differentiated macrophage cell line (e.g., THP-1). The experiment would involve treating macrophage cultures with a specific ACE inhibitor (e.g., captopril) versus a vehicle control, followed by stimulation with an inflammatory agent like lipopolysaccharide (a model for bacterial infection, relevant to [GO:0032496](https://www.ebi.ac.uk/QuickGO/term/GO:0032496)). The impact of ACE inhibition on macrophage function could be assessed by measuring the secretion of key inflammatory cytokines (e.g., TNF-α, IL-6, IL-10) using ELISA and by analyzing changes in gene expression related to M1/M2 polarization markers via qPCR or RNA-sequencing. ### Therapeutic Potential: [ACE](/details-gene/1636) is already one of the most successful therapeutic targets in modern medicine. Its role as a cell surface enzyme makes it highly accessible to small molecule drugs. The therapeutic strategy is **inhibition**, with ACE inhibitors being a first-line treatment for hypertension, heart failure, and diabetic nephropathy. The data showing high expression in intestinal and immune cells suggests that ACE inhibition may have unexplored therapeutic benefits or side effects related to gut health and inflammation. Future therapeutic development could focus on tissue-specific ACE inhibitors to isolate the cardiovascular benefits from effects in other organ systems, potentially reducing side effects like the characteristic ACE inhibitor-induced cough, which is thought to be mediated by bradykinin accumulation in the lungs.

Genular Protein ID: 1119782848

Symbol: ACE_HUMAN

Name: Angiotensin-converting enzyme, soluble form

UniProtKB Accession Codes:

P12821 B0LPF0 B4DXI3 E7EU16 P22966 Q53YX9 Q59GY8 Q7M4L4

Database IDs:

ABCD 1 AGR 1 AlphaFoldDB 1 Antibodypedia 1 BRENDA 1 Bgee 1 BindingDB 1 BioCyc 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 3 CDD 1 CORUM 1 CPTAC 1 CTD 1 ChEBI 60 ChEMBL 1 ChiTaRS 1 DMDM 1 DNASU 1 DisGeNET 1 DrugBank 21 DrugCentral 1 EC 3 EMBL 9 EMDB 12 Ensembl 3 EvolutionaryTrace 1 ExpressionAtlas 1 GO 83 GeneCards 1 GeneTree 1 GeneWiki 1 GenomeRNAi 1 GlyConnect 1 GlyCosmos 1 GlyGen 1 GuidetoPHARMACOLOGY 1 HGNC 1 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 1 KEGG 1 MANE-Select 1 MEROPS 2 MIM 9 MINT 1 MalaCards 1 MassIVE 1 NCBI Taxonomy 1 OMA 1 OpenTargets 1 Orphanet 1 OrthoDB 1 PANTHER 2 PDB 65 PDBsum 65 PIR 3 PRINTS 1 PRO 1 PROSITE 2 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 1 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 4 RNAct 1 Reactome 1 RefSeq 3 Rhea 20 SABIO-RK 1 SIGNOR 1 SMR 1 STRING 1 SUPFAM 1 SignaLink 1 TreeFam 1 UCSC 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 2849100

Title: Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning.

PubMed ID: 2849100

DOI: 10.1073/pnas.85.24.9386

PubMed ID: 2547653

Title: The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, non-duplicated form of the enzyme.

PubMed ID: 2547653

DOI: 10.1016/0014-5793(89)80897-x

PubMed ID: 2554286

Title: Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme.

PubMed ID: 2554286

DOI: 10.1073/pnas.86.20.7741

PubMed ID: 10319862

Title: Sequence variation in the human angiotensin converting enzyme.

PubMed ID: 10319862

DOI: 10.1038/8760

PubMed ID: 14702039

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

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16625196

Title: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.

PubMed ID: 16625196

DOI: 10.1038/nature04689

PubMed ID: 2558109

Title: Purification of human lung angiotensin-converting enzyme by high-performance liquid chromatography: properties and N-terminal amino acid sequence.

PubMed ID: 2558109

DOI: 10.1093/oxfordjournals.jbchem.a122871

PubMed ID: 9642152

Title: Alternative splicing of the mRNA coding for the human endothelial angiotensin-converting enzyme: a new mechanism for solubilization.

PubMed ID: 9642152

DOI: 10.1006/bbrc.1998.8813

PubMed ID: 6055465

Title: Second kininase in human blood plasma.

PubMed ID: 6055465

DOI: 10.1038/2151402a0

PubMed ID: 4322742

Title: A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin.

PubMed ID: 4322742

DOI: 10.1016/0005-2795(70)90017-6

PubMed ID: 656131

Title: Hydrolysis of enkephalin by cultured human endothelial cells and by purified peptidyl dipeptidase.

PubMed ID: 656131

DOI: 10.1016/0006-2952(78)90542-7

PubMed ID: 6270633

Title: Purification and characterization of human converting enzyme (kininase II).

PubMed ID: 6270633

DOI: 10.1016/s0196-9781(81)80027-7

PubMed ID: 6208535

Title: Hydrolysis of substance p and neurotensin by converting enzyme and neutral endopeptidase.

PubMed ID: 6208535

DOI: 10.1016/0196-9781(84)90020-2

PubMed ID: 2982830

Title: Proteolytic conversion of [Met]enkephalin-Arg6-Gly7-Leu8 by brain synaptic membranes. Characterization of formed peptides and mechanism of proteolysis.

PubMed ID: 2982830

DOI: 10.1016/s0021-9258(18)89410-8

PubMed ID: 2983326

Title: Novel activity of human angiotensin I converting enzyme: release of the NH2- and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone.

PubMed ID: 2983326

DOI: 10.1073/pnas.82.4.1025

PubMed ID: 1649623

Title: Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes.

PubMed ID: 1649623

DOI: 10.1021/bi00243a012

PubMed ID: 1651327

Title: Structure of the angiotensin I-converting enzyme gene. Two alternate promoters correspond to evolutionary steps of a duplicated gene.

PubMed ID: 1651327

DOI: 10.1016/s0021-9258(18)98626-6

PubMed ID: 1668266

Title: Purification and characterization of recombinant human testis angiotensin-converting enzyme expressed in Chinese hamster ovary cells.

PubMed ID: 1668266

DOI: 10.1016/1046-5928(91)90001-y

PubMed ID: 1851160

Title: The two homologous domains of human angiotensin I-converting enzyme are both catalytically active.

PubMed ID: 1851160

DOI: 10.1016/s0021-9258(18)31543-6

PubMed ID: 1320019

Title: The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors.

PubMed ID: 1320019

DOI: 10.1016/s0021-9258(18)42224-7

PubMed ID: 8257427

Title: Involvement of human plasma angiotensin I-converting enzyme in the degradation of the haemoregulatory peptide N-acetyl-seryl-aspartyl-lysyl-proline.

PubMed ID: 8257427

DOI: 10.1042/bj2960373

PubMed ID: 7683654

Title: Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other natural peptides.

PubMed ID: 7683654

DOI: 10.1016/s0021-9258(18)98378-x

PubMed ID: 8253769

Title: Proteolytic release of human angiotensin-converting enzyme. Localization of the cleavage site.

PubMed ID: 8253769

DOI: 10.1016/s0021-9258(19)74332-4

PubMed ID: 7523412

Title: Structure-function analysis of angiotensin I-converting enzyme using monoclonal antibodies. Selective inhibition of the amino-terminal active site.

PubMed ID: 7523412

DOI: 10.1016/s0021-9258(18)47091-3

PubMed ID: 7961923

Title: Identification of two active site residues in human angiotensin I-converting enzyme.

PubMed ID: 7961923

DOI: 10.1016/s0021-9258(18)43897-5

PubMed ID: 7876104

Title: The hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme.

PubMed ID: 7876104

DOI: 10.1074/jbc.270.8.3656

PubMed ID: 7499427

Title: Cell surface localization of proteolysis of human endothelial angiotensin I-converting enzyme. Effect of the amino-terminal domain in the solubilization process.

PubMed ID: 7499427

DOI: 10.1074/jbc.270.48.28962

PubMed ID: 8755737

Title: Assignment of free and disulfide-bonded cysteine residues in testis angiotensin-converting enzyme: functional implications.

PubMed ID: 8755737

DOI: 10.1021/bi960243x

PubMed ID: 8626443

Title: Different glycosylation requirements for the synthesis of enzymatically active angiotensin-converting enzyme in mammalian cells and yeast.

PubMed ID: 8626443

DOI: 10.1074/jbc.271.11.6429

PubMed ID: 8609242

Title: Acute angiotensin-converting enzyme inhibition increases the plasma level of the natural stem cell regulator N-acetyl-seryl-aspartyl-lysyl-proline.

PubMed ID: 8609242

DOI: 10.1172/jci118484

PubMed ID: 9371719

Title: Cleavage of arginyl-arginine and lysyl-arginine from the C-terminus of pro-hormone peptides by human germinal angiotensin I-converting enzyme (ACE) and the C-domain of human somatic ACE.

PubMed ID: 9371719

DOI: 10.1042/bj3280587

PubMed ID: 9013598

Title: Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.

PubMed ID: 9013598

DOI: 10.1074/jbc.272.6.3511

PubMed ID: 10336644

Title: Hydrolysis by somatic angiotensin-I converting enzyme of basic dipeptides from a cholecystokinin/gastrin and a LH-RH peptide extended at the C-terminus with gly-Arg/Lys-arg, but not from diarginyl insulin.

PubMed ID: 10336644

DOI: 10.1046/j.1432-1327.1999.00419.x

PubMed ID: 10913258

Title: Peptidase specificity characterization of C- and N-terminal catalytic sites of angiotensin I-converting enzyme.

PubMed ID: 10913258

DOI: 10.1021/bi9928905

PubMed ID: 10769174

Title: Shedding of somatic angiotensin-converting enzyme (ACE) is inefficient compared with testis ACE despite cleavage at identical stalk sites.

PubMed ID: 10769174

DOI: 10.1042/bj3470711

PubMed ID: 10969042

Title: A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9.

PubMed ID: 10969042

DOI: 10.1161/01.res.87.5.e1

PubMed ID: 10924499

Title: A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase.

PubMed ID: 10924499

DOI: 10.1074/jbc.m002615200

PubMed ID: 11076943

Title: Increased shedding of angiotensin-converting enzyme by a mutation identified in the stalk region.

PubMed ID: 11076943

DOI: 10.1074/jbc.m007706200

PubMed ID: 11432860

Title: Arg(1098) is critical for the chloride dependence of human angiotensin I-converting enzyme C-domain catalytic activity.

PubMed ID: 11432860

DOI: 10.1074/jbc.m101495200

PubMed ID: 11274151

Title: A point mutation in the juxtamembrane stalk of human angiotensin I-converting enzyme invokes the action of a distinct secretase.

PubMed ID: 11274151

DOI: 10.1074/jbc.m100339200

PubMed ID: 11604391

Title: Angiotensin-converting enzyme degrades Alzheimer amyloid beta-peptide (A beta); retards A beta aggregation, deposition, fibril formation; and inhibits cytotoxicity.

PubMed ID: 11604391

DOI: 10.1074/jbc.m104068200

PubMed ID: 12386153

Title: CK2 phosphorylates the angiotensin-converting enzyme and regulates its retention in the endothelial cell plasma membrane.

PubMed ID: 12386153

DOI: 10.1161/01.res.0000038114.17939.c8

PubMed ID: 12459472

Title: Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme.

PubMed ID: 12459472

DOI: 10.1016/s0014-5793(02)03640-2

PubMed ID: 12542396

Title: Deglycosylation, processing and crystallization of human testis angiotensin-converting enzyme.

PubMed ID: 12542396

DOI: 10.1042/bj20021842

PubMed ID: 15151696

Title: ACE2 gene expression is up-regulated in the human failing heart.

PubMed ID: 15151696

DOI: 10.1186/1741-7015-2-19

PubMed ID: 15671045

Title: Myocardial infarction increases ACE2 expression in rat and humans.

PubMed ID: 15671045

DOI: 10.1093/eurheartj/ehi114

PubMed ID: 15615692

Title: Molecular basis of exopeptidase activity in the C-terminal domain of human angiotensin I-converting enzyme: insights into the origins of its exopeptidase activity.

PubMed ID: 15615692

DOI: 10.1074/jbc.m412638200

PubMed ID: 16154999

Title: Amyloid beta-protein is degraded by cellular angiotensin-converting enzyme (ACE) and elevated by an ACE inhibitor.

PubMed ID: 16154999

DOI: 10.1074/jbc.m508460200

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: 16476786

Title: Angiotensin-converting enzyme (ACE) dimerization is the initial step in the ACE inhibitor-induced ACE signaling cascade in endothelial cells.

PubMed ID: 16476786

DOI: 10.1124/mol.105.020636

PubMed ID: 18077343

Title: Hemopressin is an inverse agonist of CB1 cannabinoid receptors.

PubMed ID: 18077343

DOI: 10.1073/pnas.0706980105

PubMed ID: 19773553

Title: Abeta42-to-Abeta40- and angiotensin-converting activities in different domains of angiotensin-converting enzyme.

PubMed ID: 19773553

DOI: 10.1074/jbc.m109.011437

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: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21901117

Title: ACE as a mechanosensor to shear stress influences the control of its own regulation via phosphorylation of cytoplasmic Ser(1270).

PubMed ID: 21901117

DOI: 10.1371/journal.pone.0022803

PubMed ID: 12540854

Title: Crystal structure of the human angiotensin-converting enzyme-lisinopril complex.

PubMed ID: 12540854

DOI: 10.1038/nature01370

PubMed ID: 15236580

Title: Structural details on the binding of antihypertensive drugs captopril and enalaprilat to human testicular angiotensin I-converting enzyme.

PubMed ID: 15236580

DOI: 10.1021/bi049480n

PubMed ID: 16476442

Title: Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design.

PubMed ID: 16476442

DOI: 10.1016/j.jmb.2006.01.048

PubMed ID: 20826823

Title: The N domain of human angiotensin-I-converting enzyme: the role of N-glycosylation and the crystal structure in complex with an N domain-specific phosphinic inhibitor, RXP407.

PubMed ID: 20826823

DOI: 10.1074/jbc.m110.167866

PubMed ID: 21810173

Title: Structural characterization of angiotensin I-converting enzyme in complex with a selenium analogue of captopril.

PubMed ID: 21810173

DOI: 10.1111/j.1742-4658.2011.08276.x

PubMed ID: 23056909

Title: Molecular recognition and regulation of human angiotensin-I converting enzyme (ACE) activity by natural inhibitory peptides.

PubMed ID: 23056909

DOI: 10.1038/srep00717

PubMed ID: 24297181

Title: Molecular and thermodynamic mechanisms of the chloride-dependent human angiotensin-I-converting enzyme (ACE).

PubMed ID: 24297181

DOI: 10.1074/jbc.m113.512335

PubMed ID: 26403559

Title: Structural basis of Ac-SDKP hydrolysis by Angiotensin-I converting enzyme.

PubMed ID: 26403559

DOI: 10.1038/srep13742

PubMed ID: 10099885

Title: The DD genotype of the ACE gene polymorphism is associated with progression of diabetic nephropathy to end stage renal failure in IDDM.

PubMed ID: 10099885

PubMed ID: 10391210

Title: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis.

PubMed ID: 10391210

DOI: 10.1038/10297

PubMed ID: 11551873

Title: Point mutation in the stalk of angiotensin-converting enzyme causes a dramatic increase in serum angiotensin-converting enzyme but no cardiovascular disease.

PubMed ID: 11551873

DOI: 10.1161/hc3601.095932

PubMed ID: 14694062

Title: Hereditary elevation of angiotensin converting enzyme suggesting neurosarcoidosis.

PubMed ID: 14694062

DOI: 10.1212/01.wnl.0000098990.12845.da

PubMed ID: 15534175

Title: Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls.

PubMed ID: 15534175

DOI: 10.1001/archneur.61.11.1652

PubMed ID: 15277638

Title: DD genotype of ACE gene is a risk factor for intracerebral hemorrhage.

PubMed ID: 15277638

DOI: 10.1212/01.wnl.0000130200.12993.0c

PubMed ID: 16116425

Title: Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis.

PubMed ID: 16116425

DOI: 10.1038/ng1623

PubMed ID: 25787250

Title: Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in insulin-producing adenomas.

PubMed ID: 25787250

DOI: 10.1073/pnas.1503696112

Sequence Information:

  • Length: 1306
  • Mass: 149715
  • Checksum: 1B33BCA7301A26AA
  • Sequence:
    • MGAASGRRGP GLLLPLPLLL LLPPQPALAL DPGLQPGNFS ADEAGAQLFA QSYNSSAEQV 
LFQSVAASWA HDTNITAENA RRQEEAALLS QEFAEAWGQK AKELYEPIWQ NFTDPQLRRI 
IGAVRTLGSA NLPLAKRQQY NALLSNMSRI YSTAKVCLPN KTATCWSLDP DLTNILASSR 
SYAMLLFAWE GWHNAAGIPL KPLYEDFTAL SNEAYKQDGF TDTGAYWRSW YNSPTFEDDL 
EHLYQQLEPL YLNLHAFVRR ALHRRYGDRY INLRGPIPAH LLGDMWAQSW ENIYDMVVPF 
PDKPNLDVTS TMLQQGWNAT HMFRVAEEFF TSLELSPMPP EFWEGSMLEK PADGREVVCH 
ASAWDFYNRK DFRIKQCTRV TMDQLSTVHH EMGHIQYYLQ YKDLPVSLRR GANPGFHEAI 
GDVLALSVST PEHLHKIGLL DRVTNDTESD INYLLKMALE KIAFLPFGYL VDQWRWGVFS 
GRTPPSRYNF DWWYLRTKYQ GICPPVTRNE THFDAGAKFH VPNVTPYIRY FVSFVLQFQF 
HEALCKEAGY EGPLHQCDIY RSTKAGAKLR KVLQAGSSRP WQEVLKDMVG LDALDAQPLL 
KYFQPVTQWL QEQNQQNGEV LGWPEYQWHP PLPDNYPEGI DLVTDEAEAS KFVEEYDRTS 
QVVWNEYAEA NWNYNTNITT ETSKILLQKN MQIANHTLKY GTQARKFDVN QLQNTTIKRI 
IKKVQDLERA ALPAQELEEY NKILLDMETT YSVATVCHPN GSCLQLEPDL TNVMATSRKY 
EDLLWAWEGW RDKAGRAILQ FYPKYVELIN QAARLNGYVD AGDSWRSMYE TPSLEQDLER 
LFQELQPLYL NLHAYVRRAL HRHYGAQHIN LEGPIPAHLL GNMWAQTWSN IYDLVVPFPS 
APSMDTTEAM LKQGWTPRRM FKEADDFFTS LGLLPVPPEF WNKSMLEKPT DGREVVCHAS 
AWDFYNGKDF RIKQCTTVNL EDLVVAHHEM GHIQYFMQYK DLPVALREGA NPGFHEAIGD 
VLALSVSTPK HLHSLNLLSS EGGSDEHDIN FLMKMALDKI AFIPFSYLVD QWRWRVFDGS 
ITKENYNQEW WSLRLKYQGL CPPVPRTQGD FDPGAKFHIP SSVPYIRYFV SFIIQFQFHE 
ALCQAAGHTG PLHKCDIYQS KEAGQRLATA MKLGFSRPWP EAMQLITGQP NMSASAMLSY 
FKPLLDWLRT ENELHGEKLG WPQYNWTPNS ARSEGPLPDS GRVSFLGLDL DAQQARVGQW 
LLLFLGIALL VATLGLSQRL FSIRHRSLHR HSHGPQFGSE VELRHS

Genular Protein ID: 1766050588

Symbol: B4DKH4_HUMAN

Name: N/A

UniProtKB Accession Codes:

B4DKH4

Database IDs:

ARBA 22 AlphaFoldDB 1 BioGRID-ORCS 1 CDD 1 CTD 1 ChEBI 42 DNASU 1 DisGeNET 1 EC 2 EMBL 2 GO 8 InterPro 1 KEGG 1 MEROPS 2 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PIRSR 3 PRINTS 1 PROSITE 1 PROSITE-ProRule 1 PeptideAtlas 1 Pfam 1 RefSeq 1 Rhea 20 RuleBase 1 SAM 1 SMR 1 SUPFAM 1

Sequence Information:

  • Length: 475
  • Mass: 53750
  • Checksum: 0474ADD420A70C7F
  • Sequence:
    • MGAASGRRGP GLLLPLPLLL LLPPQPALAL DPGLQPGNFS ADEAGAQLFA QSYNSSAEQV 
LFQSVAASWA HDTNITAENA RRQEEAALLS QEFAEAWGQK AKELYEPIWQ NFTDPQLRRI 
IGAVRTLGSA NLPLAKRQQY NALLSNMSRI YSTAKVCLPN KTATCWSLDP DLTNILASSR 
SYAMLLFAWE GWHNAAGIPL KPLYEDFTAL SNEAYKQDGF TDTGAYWRSW YNSPTFEDDL 
EHLYQQLEPL YLNLHAFVRR ALHRRYGDRY INLRGPIPAH LLGDMWAQSW ENIYDMVVPF 
PDKPNLDVTS TMLQQGWNAT HMFRVAEEFF TSLELSPMPP GFWEGSMLEK PADGREVVCH 
ASAWDFYNRK DFRIKQCTRV TMDQLSTVHH EMGHIQYYLQ YKDLPVSLRR GANPGFHEAI 
GDVLALSVST PEHLHKIGLL DRVTNDTEPS IRGSVLLLPE TKPTLMLELS FMFQM