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UniProtKB - Q9BYF1 (ACE2_HUMAN)

Entry version 184 (10 Feb 2021)
Sequence version 2 (02 Aug 2005)
Previous versions | rss
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Protein

Angiotensin-converting enzyme 2

Gene

ACE2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Essential counter-regulatory carboxypeptidase of the renin-angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis (PubMed:27217402). Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II (PubMed:10969042, PubMed:10924499, PubMed:11815627, PubMed:19021774, PubMed:14504186). Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin (PubMed:10969042, PubMed:11815627). Also cleaves other biological peptides, such as apelins (apelin-13, [Pyr1]apelin-13, apelin-17, apelin-36), casomorphins (beta-casomorphin-7, neocasomorphin) and dynorphin A with high efficiency (PubMed:11815627, PubMed:27217402, PubMed:28293165). In addition, ACE2 C-terminus is homologous to collectrin and is responsible for the trafficking of the neutral amino acid transporter SL6A19 to the plasma membrane of gut epithelial cells via direct interaction, regulating its expression on the cell surface and its catalytic activity (PubMed:18424768, PubMed:19185582).8 Publications
Non-functional as a carboxypeptidase.1 Publication
(Microbial infection) Acts as a receptor for human coronaviruses SARS-CoV and SARS-CoV-2, as well as human coronavirus NL63/HCoV-NL63.11 Publications
(Microbial infection) Non-functional as a receptor for human coronavirus SARS-CoV-2.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Regulated by chloride and fluoride, but not bromide (PubMed:11815627). Chloride increases angiotensin I and decreases angiotensin II cleavage (PubMed:19021774). Inhibited by MLN-4760, cFP_Leu, and EDTA (PubMed:15231706, PubMed:10924499), but not by the ACE inhibitors lisinopril, captopril and enalaprilat (PubMed:10969042, PubMed:10924499). Highly potent and selective in vitro ACE2 inhibitors were identified (PubMed:12358520).6 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 0.034 sec(-1) with angiotensin I as substrate. kcat is 3.5 sec(-1) with angiotensin II as substrate. kcat is 13 sec(-1) with apelin-13 as substrate. kcat is 62 sec(-1) with [des-Arg9]-bradykinin as substrate. kcat is 26 sec(-1) with Lys-[des-Arg9]-bradykinin as substrate. kcat is 6.8 sec(-1) with beta-casomorphin as substrate. kcat is 16 sec(-1) with dynorphin A-(1-13) as substrate. kcat is 57 sec(-1) with neurotensin-1-8 as substrate (PubMed:11815627). kcat is 19.1 sec(-1) with [Pyr1]apelin-13 as substrate. kcat is 7.7 sec(-1) with apelin-17 as substrate (PubMed:27217402).2 Publications
  1. KM=6.9 µM for angiotensin I1 Publication
  2. KM=2.0 µM for angiotensin II1 Publication
  3. KM=6.8 µM for apelin-131 Publication
  4. KM=290 µM for [des-Arg9]-bradykinin1 Publication
  5. KM=130 µM for Lys-[des-Arg9]-bradykinin1 Publication
  6. KM=31 µM for beta-casomorphin1 Publication
  7. KM=5.5 µM for dynorphin A-(1-13)1 Publication
  8. KM=300 µM for neurotensin-1-81 Publication
  9. KM=58.6 µM for angiotensin II1 Publication
  10. KM=12 µM for [Pyr1]apelin-131 Publication
  11. KM=19 µM for apelin-171 Publication
  1. Vmax=28.7 nmol/min/mg enzyme with angiotensin II as substrate1 Publication

pH dependencei

Optimum pH is 6.5 in the presence of 1 M NaCl. Active from pH 6 to 9.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei169Chloride1 Publication1 Publication1
Binding sitei273Substrate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi374Zinc; catalytic1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei375Proton acceptor2 Publications1
Metal bindingi378Zinc; catalytic1 Publication1
Metal bindingi402Zinc; catalytic1 Publication1
Binding sitei477Chloride1 Publication1 Publication1
Binding sitei481Chloride1 Publication1 Publication1
Active sitei505Proton donor1 Publication1
Binding sitei515Substrate1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionCarboxypeptidase, Host cell receptor for virus entry, Hydrolase, Metalloprotease, Protease, Receptor
Biological processHost-virus interaction
LigandChloride, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.15.1, 2681
3.4.17.23, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q9BYF1

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2022377, Metabolism of Angiotensinogen to Angiotensins
R-HSA-9678110, Attachment and Entry
R-HSA-9679191, Potential therapeutics for SARS
R-HSA-9694614, Attachment and Entry

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q9BYF1

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q9BYF1

Protein family/group databases

MEROPS protease database

More...MEROPSi		M02.006

Transport Classification Database

More...TCDBi		2.A.22.6.3, the neurotransmitter:sodium symporter (nss) family
8.A.139.1.1, the angiotensin-onverting enzyme 2 (ace2) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Angiotensin-converting enzyme 2 (EC:3.4.17.233 Publications)
Alternative name(s):
Angiotensin-converting enzyme homolog1 Publication
Short name:
ACEH1 Publication
Angiotensin-converting enzyme-related carboxypeptidase1 Publication (EC:3.4.17.-7 Publications)
Short name:
ACE-related carboxypeptidase
Metalloprotease MPROT151 Publication
Cleaved into the following chain:
Processed angiotensin-converting enzyme 21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ACE2Imported
ORF Names:UNQ868/PRO1885
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:13557, ACE2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		300335, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9BYF1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000130234.10

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini18 – 740ExtracellularSequence analysisAdd BLAST723
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei741 – 761HelicalSequence analysisAdd BLAST21
Topological domaini762 – 805CytoplasmicSequence analysisAdd BLAST44

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

An engeneered stable, dimeric and secreted receptor with combined mutations that increase the affinity for human coronavirus SARS-CoV-2 spike protein shows potent SARS-CoV and SARS-CoV-2 neutralization in vitro.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi19S → P: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi24 – 26QAK → KAE: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication3
Mutagenesisi24Q → T: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi25A → V: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi27T → Y: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. In sACE2.v2.2; increases interaction with RBD domain of SARS-CoV-2 spike protein; when associated with Y-330 and L-386. 1 Publication1
Mutagenesisi29L → F: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi31K → D: Abolishes interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi31K → Y: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi33N → D: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi34H → A: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi37E → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi38D → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi39L → R: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi40F → D: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi41Y → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi41Y → R: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi42Q → L: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi68K → D: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi69W → V: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi72F → Y: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi75E → K: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi76Q → T: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi79L → T: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi82 – 84MYP → NFS: Inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication3
Mutagenesisi89Q → P: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi90N → Q: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi91L → P: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi92T → Q: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi110E → P: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi135 – 136PD → SM: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication2
Mutagenesisi160E → R: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi169R → Q: About 95% loss of angiotensin I cleavage. 1 Publication1
Mutagenesisi192R → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi219R → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi239H → Q: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi271W → Q: About 95% loss of angiotensin I cleavage. 1 Publication1
Mutagenesisi273R → Q: Complete loss of enzyme activity. Does not affect amino acid transport activity of SLC6A19. 2 Publications1
Mutagenesisi309K → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi312E → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi324T → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi324T → P: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi325Q → P: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi330N → Y: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. In sACE2.v2.2; increases interaction with RBD domain of SARS-CoV-2 spike protein; when associated with Y-27 and L-386. 1 Publication1
Mutagenesisi338 – 340NVQ → DDR: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication3
Mutagenesisi345H → A: Complete loss of enzyme activity. 1 Publication1
Mutagenesisi350D → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi351L → F: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi353K → H, A or D: Abolishes interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi355D → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi357R → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi359L → K or A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi383M → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi386A → L: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. In sACE2.v2.2; increases interaction with RBD domain of SARS-CoV-2 spike protein; when associated with Y-27 and Y-330. 1 Publication1
Mutagenesisi389P → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi389P → D: Increases very slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi393R → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi393R → K: Increases very slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi425 – 427SPD → PSN: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication3
Mutagenesisi465 – 467KGE → QDK: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication3
Mutagenesisi481K → Q: About 80% loss of angiotensin I cleavage. 1 Publication1
Mutagenesisi505H → A: Complete loss of enzyme activity. 1 Publication1
Mutagenesisi514R → Q: About 50% loss of angiotensin I cleavage but two-fold greater activity with angiotensin II. 1 Publication1
Mutagenesisi518R → G: Increases very slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication1
Mutagenesisi559R → S: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi603F → T: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		59272

Open Targets

More...OpenTargetsi		ENSG00000130234

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA425

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9BYF1, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3736

Drug and drug target database

More...DrugBanki		DB00608, Chloroquine
DB01611, Hydroxychloroquine
DB15643, N-(2-Aminoethyl)-1-aziridineethanamine
DB05203, SPP1148

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1614

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ACE2

Domain mapping of disease mutations (DMDM)

More...DMDMi		71658783

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 17Sequence analysisAdd BLAST17
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002857018 – 805Angiotensin-converting enzyme 2Add BLAST788
ChainiPRO_000029226818 – 708Processed angiotensin-converting enzyme 2Add BLAST691

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi53N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi90N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi103N-linked (GlcNAc...) asparagine1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi133 ↔ 1411 Publication
Glycosylationi322N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi344 ↔ 3611 Publication
Glycosylationi432N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi530 ↔ 5421 Publication
Glycosylationi546N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi690N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylation on Asn-90 may limit SARS infectivity.5 Publications
Proteolytic cleavage by ADAM17 generates a secreted form (PubMed:15983030). Also cleaved by serine proteases: TMPRSS2, TMPRSS11D and HPN/TMPRSS1.5 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9BYF1

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9BYF1

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q9BYF1

PeptideAtlas

More...PeptideAtlasi		Q9BYF1

PRoteomics IDEntifications database

More...PRIDEi		Q9BYF1

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		79634 [Q9BYF1-1]

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		1012, 4 N-Linked glycans (3 sites)
2841, 103 N-Linked glycans (7 sites), 3 O-Linked glycans (3 sites)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q9BYF1, 7 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9BYF1

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q9BYF1

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in endothelial cells from small and large arteries, and in arterial smooth muscle cells (at protein level) (PubMed:15141377). Expressed in enterocytes of the small intestine, Leydig cells and Sertoli cells (at protein level) (PubMed:15141377). Expressed in the renal proximal tubule and the small intestine (at protein level) (PubMed:18424768). Expressed in heart, kidney, testis, and gastrointestinal system (at protein level) (PubMed:10969042, PubMed:10924499, PubMed:15231706, PubMed:12459472, PubMed:15671045, PubMed:32715618, PubMed:32170560). In lung, expressed at low levels in some alveolar type 2 cells, the expression seems to be individual-specific (at protein level) (PubMed:32425701, PubMed:15141377, PubMed:32715618, PubMed:32170560). Coexpressed with TMPRSS2 within some lung alveolar type 2 cells, ileal absorptive enterocytes, intestinal epithelial cells, cornea, gallbladder and nasal goblet secretory cells (PubMed:32413319, PubMed:32327758, PubMed:32358202). Coexpressed with TMPRSS4 within mature enterocytes (PubMed:32404436).14 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated in failing heart (PubMed:14504186, PubMed:15151696, PubMed:15671045). Expression is induced by IFNA and IFNG (PubMed:32413319, PubMed:32425701). Exposure to cigarette smoke increases expression in lungs (PubMed:32425701).5 Publications
Not induced by interferons such as IFNA, IFNB and IFNG.1 Publication
Expression is induced by interferons such as IFNA, IFNB and IFNG. It seems that isoform 2 is an interferon-stimulated gene (ISG) but not isoform 1.1 Publication
(Microbial infection) In airway epithelial cells, expression is increased upon influenza A virus infection (PubMed:32413319).1 Publication
(Microbial infection) In airway epithelial cells, expression is induced by viruses such rhinoviruses and influenza virus.1 Publication
(Microbial infection) Induced by human coronavirus SARS-CoV-2.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000130234, Expressed in jejunal mucosa and 142 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9BYF1, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000130234, Tissue enriched (intestine)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:32132184).

Interacts with the catalytically active form of TMPRSS2 (PubMed:21068237).

Interacts with SLC6A19; this interaction is essential for expression and function of SLC6A19 in intestine (By similarity).

Interacts with ITGA5:ITGB1 (PubMed:15276642, PubMed:33102950).

By similarity4 Publications

(Microbial infection) Interacts with SARS coronavirus/SARS-CoV spike protein.

4 Publications

(Microbial infection) Interacts with SARS coronavirus-2/SARS-CoV-2 spike protein.

6 Publications

(Microbial infection) Interacts with human coronavirus NL63/HCoV-NL63 spike glycoprotein.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		121864, 17 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-5683, SARS-CoV-2 Spike - human ACE2 receptor complex
CPX-5684, SARS-CoV-2 Spike - human ACE2-SLC6A19 complex
CPX-5695, SARS-CoV Spike - human ACE2 receptor complex

Database of interacting proteins

More...DIPi		DIP-44689N

Protein interaction database and analysis system

More...IntActi		Q9BYF1, 23 interactors

Molecular INTeraction database

More...MINTi		Q9BYF1

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000389326

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9BYF1

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9BYF1, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1805
Legend: HelixTurnBeta strandPDB Structure known for this area
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3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q9BYF1

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9BYF1

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni30 – 41Interaction with SARS-CoV spike glycoprotein1 PublicationAdd BLAST12
Regioni82 – 84Interaction with SARS-CoV spike glycoprotein1 Publication3
Regioni345 – 346Substrate binding1 Publication2
Regioni353 – 357Interaction with SARS-CoV spike glycoprotein1 Publication5
Regioni652 – 659Essential for cleavage by ADAM171 Publication8
Regioni697 – 716Essential for cleavage by TMPRSS11D and TMPRSS21 PublicationAdd BLAST20

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The extracellular region of the ACE2 enzyme is composed of two domains. The first is a zinc metallopeptidase domain (residues 19-611). The second domain is located at the C-terminus (residues 612-740) and is 48% identical to human collectrin.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase M2 family.