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UniProtKB - Q9BYF1 (ACE2_HUMAN)

Entry version 180 (17 Jun 2020)
Sequence version 2 (02 Aug 2005)
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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
(Microbial infection) Acts as a receptor for human coronaviruses SARS-CoV and SARS-CoV-2, as well as human coronavirus NL63/HCoV-NL63.7 Publications

<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

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2022377 Metabolism of Angiotensinogen to Angiotensins

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

<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.-6 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

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000130234.10

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

<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

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>Mutagenesisi24 – 26QAK → KAE: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication3
Mutagenesisi31K → D: Abolishes interaction with SARS-CoV spike glycoprotein. 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
Mutagenesisi41Y → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi68K → D: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi82 – 84MYP → NFS: Inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication3
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
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
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
Mutagenesisi389P → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
Mutagenesisi393R → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 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
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		DB00691 Moexipril
DB05203 SPP1148

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1614

Polymorphism and mutation 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]
79635 [Q9BYF1-2]

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		1012

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 lung alveolar epithelial cells, 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 (PubMed:10969042, PubMed:10924499, PubMed:15231706, PubMed:12459472, PubMed:15671045).7 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.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000130234 Expressed in jejunal mucosa and 128 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 ITGB1 (PubMed:15276642).

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).

By similarity3 Publications

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

3 Publications

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

3 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%27">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

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		121864, 8 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, 16 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
Show more details

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.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3690 Eukaryota
ENOG410XPJ3 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000158077

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_014364_3_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9BYF1

KEGG Orthology (KO)

More...KOi		K09708

Identification of Orthologs from Complete Genome Data

More...OMAi		RWWEMKR

Database of Orthologous Groups

More...OrthoDBi		422699at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9BYF1

TreeFam database of animal gene trees

More...TreeFami		TF312861

Family and domain databases

Conserved Domains Database

More...CDDi		cd06461 M2_ACE, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR031588 Collectrin_dom
IPR001548 Peptidase_M2

The PANTHER Classification System

More...PANTHERi		PTHR10514 PTHR10514, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF16959 Collectrin, 1 hit
PF01401 Peptidase_M2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00791 PEPDIPTASEA

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q9BYF1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSSSSWLLLS LVAVTAAQST IEEQAKTFLD KFNHEAEDLF YQSSLASWNY 
        60         70         80         90        100
NTNITEENVQ NMNNAGDKWS AFLKEQSTLA QMYPLQEIQN LTVKLQLQAL 
       110        120        130        140        150
QQNGSSVLSE DKSKRLNTIL NTMSTIYSTG KVCNPDNPQE CLLLEPGLNE 
       160        170        180        190        200
IMANSLDYNE RLWAWESWRS EVGKQLRPLY EEYVVLKNEM ARANHYEDYG 
       210        220        230        240        250
DYWRGDYEVN GVDGYDYSRG QLIEDVEHTF EEIKPLYEHL HAYVRAKLMN 
       260        270        280        290        300
AYPSYISPIG CLPAHLLGDM WGRFWTNLYS LTVPFGQKPN IDVTDAMVDQ 
       310        320        330        340        350
AWDAQRIFKE AEKFFVSVGL PNMTQGFWEN SMLTDPGNVQ KAVCHPTAWD 
       360        370        380        390        400
LGKGDFRILM CTKVTMDDFL TAHHEMGHIQ YDMAYAAQPF LLRNGANEGF 
       410        420        430        440        450
HEAVGEIMSL SAATPKHLKS IGLLSPDFQE DNETEINFLL KQALTIVGTL 
       460        470        480        490        500
PFTYMLEKWR WMVFKGEIPK DQWMKKWWEM KREIVGVVEP VPHDETYCDP 
       510        520        530        540        550
ASLFHVSNDY SFIRYYTRTL YQFQFQEALC QAAKHEGPLH KCDISNSTEA 
       560        570        580        590        600
GQKLFNMLRL GKSEPWTLAL ENVVGAKNMN VRPLLNYFEP LFTWLKDQNK 
       610        620        630        640        650
NSFVGWSTDW SPYADQSIKV RISLKSALGD KAYEWNDNEM YLFRSSVAYA 
       660        670        680        690        700
MRQYFLKVKN QMILFGEEDV RVANLKPRIS FNFFVTAPKN VSDIIPRTEV 
       710        720        730        740        750
EKAIRMSRSR INDAFRLNDN SLEFLGIQPT LGPPNQPPVS IWLIVFGVVM 
       760        770        780        790        800
GVIVVGIVIL IFTGIRDRKK KNKARSGENP YASIDISKGE NNPGFQNTDD 

VQTSF
Length:805
Mass (Da):92,463
Last modified:August 2, 2005 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8EE6EB0A931550E8
GO
Isoform 2 (identifier: Q9BYF1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     555-555: F → L
     556-805: Missing.

Show »
Length:555
Mass (Da):63,912
Checksum:i3A3842AB792E2DBC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti18Q → H in CAB53682 (PubMed:17974005).Curated1
Sequence conflicti508N → D in AAQ89076 (PubMed:12975309).Curated1
Sequence conflicti631K → R in BAB40370 (Ref. 5) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02308226K → R1 PublicationCorresponds to variant dbSNP:rs4646116Ensembl.1
Natural variantiVAR_023083638N → S1 PublicationCorresponds to variant dbSNP:rs183135788Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_014901555F → L in isoform 2. 1 Publication1
Alternative sequenceiVSP_014902556 – 805Missing in isoform 2. 1 PublicationAdd BLAST250

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF291820 mRNA Translation: AAF99721.1
AF241254 mRNA Translation: AAF78220.1
AY623811 mRNA Translation: AAT45083.1
AB193259 mRNA Translation: BAD99266.1
AB193260 mRNA Translation: BAD99267.1
AB046569 mRNA Translation: BAB40370.1
E39033 mRNA No translation available.
GQ262784 mRNA Translation: ACT66268.1
AY358714 mRNA Translation: AAQ89076.1
AY217547 Genomic DNA Translation: AAO25651.1
CH471074 Genomic DNA Translation: EAW98892.1
BC039902 mRNA Translation: AAH39902.1
BC048094 mRNA Translation: AAH48094.2
AL110224 mRNA Translation: CAB53682.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS14169.1 [Q9BYF1-1]

Protein sequence database of the Protein Information Resource

More...PIRi		T14762

NCBI Reference Sequences

More...RefSeqi		NP_068576.1, NM_021804.2 [Q9BYF1-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000252519; ENSP00000252519; ENSG00000130234 [Q9BYF1-1]
ENST00000427411; ENSP00000389326; ENSG00000130234 [Q9BYF1-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		59272

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:59272

UCSC genome browser

More...UCSCi		uc004cxa.2 human [Q9BYF1-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

SeattleSNPs
Protein Spotlight

A way in - Issue 223 of March 2020

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF291820 mRNA Translation: AAF99721.1
AF241254 mRNA Translation: AAF78220.1
AY623811 mRNA Translation: AAT45083.1
AB193259 mRNA Translation: BAD99266.1
AB193260 mRNA Translation: BAD99267.1
AB046569 mRNA Translation: BAB40370.1
E39033 mRNA No translation available.
GQ262784 mRNA Translation: ACT66268.1
AY358714 mRNA Translation: AAQ89076.1
AY217547 Genomic DNA Translation: AAO25651.1
CH471074 Genomic DNA Translation: EAW98892.1
BC039902 mRNA Translation: AAH39902.1
BC048094 mRNA Translation: AAH48094.2
AL110224 mRNA Translation: CAB53682.1
CCDSiCCDS14169.1 [Q9BYF1-1]
PIRiT14762
RefSeqiNP_068576.1, NM_021804.2 [Q9BYF1-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R42X-ray2.20A1-615[»]
1R4LX-ray3.00A1-615[»]
1XJPmodel-B19-615[»]
2AJFX-ray2.90A/B19-615[»]
3D0GX-ray2.80A/B56-615[»]
3D0HX-ray3.10A/B56-615[»]
3D0IX-ray2.90A/B56-615[»]
3KBHX-ray3.31A/B/C/D19-615[»]
3SCIX-ray2.90A/B19-615[»]
3SCJX-ray3.00A/B19-615[»]
3SCKX-ray3.00A/B83-615[»]
3SCLX-ray3.00A/B83-615[»]
6ACGelectron microscopy5.40D19-615[»]
6ACJelectron microscopy4.20D19-615[»]
6ACKelectron microscopy4.50D19-615[»]
6CS2electron microscopy4.40D19-615[»]
6M0JX-ray2.45A19-615[»]
6M17electron microscopy2.90B/D18-805[»]
6M18electron microscopy2.90B/D18-805[»]
6M1Delectron microscopy4.50B/D18-805[»]
6VW1X-ray2.68A/B19-615[»]
SMRiQ9BYF1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi121864, 8 interactors
ComplexPortaliCPX-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
DIPiDIP-44689N
IntActiQ9BYF1, 16 interactors
MINTiQ9BYF1
STRINGi9606.ENSP00000389326

Chemistry databases

BindingDBiQ9BYF1
ChEMBLiCHEMBL3736
DrugBankiDB00691 Moexipril
DB05203 SPP1148
GuidetoPHARMACOLOGYi1614

Protein family/group databases

MEROPSiM02.006
TCDBi2.A.22.6.3 the neurotransmitter:sodium symporter (nss) family

PTM databases

GlyConnecti1012
iPTMnetiQ9BYF1
PhosphoSitePlusiQ9BYF1

Polymorphism and mutation databases

BioMutaiACE2
DMDMi71658783

Proteomic databases

jPOSTiQ9BYF1
MassIVEiQ9BYF1
PaxDbiQ9BYF1
PeptideAtlasiQ9BYF1
PRIDEiQ9BYF1
ProteomicsDBi79634 [Q9BYF1-1]
79635 [Q9BYF1-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		344 903 antibodies

Genome annotation databases

EnsembliENST00000252519; ENSP00000252519; ENSG00000130234 [Q9BYF1-1]
ENST00000427411; ENSP00000389326; ENSG00000130234 [Q9BYF1-1]
GeneIDi59272
KEGGihsa:59272
UCSCiuc004cxa.2 human [Q9BYF1-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		59272
DisGeNETi59272
EuPathDBiHostDB:ENSG00000130234.10

GeneCards: human genes, protein and diseases

More...GeneCardsi		ACE2
HGNCiHGNC:13557 ACE2
HPAiENSG00000130234 Tissue enriched (intestine)
MIMi300335 gene
neXtProtiNX_Q9BYF1
OpenTargetsiENSG00000130234
PharmGKBiPA425

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3690 Eukaryota
ENOG410XPJ3 LUCA
GeneTreeiENSGT00940000158077
HOGENOMiCLU_014364_3_0_1
InParanoidiQ9BYF1
KOiK09708
OMAiRWWEMKR
OrthoDBi422699at2759
PhylomeDBiQ9BYF1
TreeFamiTF312861

Enzyme and pathway databases

BRENDAi3.4.15.1 2681
3.4.17.23 2681
ReactomeiR-HSA-2022377 Metabolism of Angiotensinogen to Angiotensins
SABIO-RKiQ9BYF1
SIGNORiQ9BYF1

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		59272 1 hit in 413 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		ACE2 human
EvolutionaryTraceiQ9BYF1

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Angiotensin-converting_enzyme_2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		59272
PharosiQ9BYF1 Tchem

Protein Ontology

More...PROi		PR:Q9BYF1
RNActiQ9BYF1 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000130234 Expressed in jejunal mucosa and 128 other tissues
GenevisibleiQ9BYF1 HS

Family and domain databases

CDDicd06461 M2_ACE, 1 hit
InterProiView protein in InterPro
IPR031588 Collectrin_dom
IPR001548 Peptidase_M2
PANTHERiPTHR10514 PTHR10514, 1 hit
PfamiView protein in Pfam
PF16959 Collectrin, 1 hit
PF01401 Peptidase_M2, 1 hit
PRINTSiPR00791 PEPDIPTASEA
PROSITEiView protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiACE2_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9BYF1
Secondary accession number(s): C7ECU1
, Q6UWP0, Q86WT0, Q9NRA7, Q9UFZ6
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 2, 2005
Last sequence update: August 2, 2005
Last modified: June 17, 2020
This is version 180 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  8. Peptidase families
    Classification of peptidase families and list of entries
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