UniProtKB - Q9BYF1 (ACE2_HUMAN)
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>sp|Q9BYF1|ACE2_HUMAN Angiotensin-converting enzyme 2 OS=Homo sapiens OX=9606 GN=ACE2 PE=1 SV=2 MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNYNTNITEENVQ NMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQQNGSSVLSEDKSKRLNTIL NTMSTIYSTGKVCNPDNPQECLLLEPGLNEIMANSLDYNERLWAWESWRSEVGKQLRPLY EEYVVLKNEMARANHYEDYGDYWRGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHL HAYVRAKLMNAYPSYISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQ AWDAQRIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDFRILM CTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKS IGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEKWRWMVFKGEIPKDQWMKKWWEM KREIVGVVEPVPHDETYCDPASLFHVSNDYSFIRYYTRTLYQFQFQEALCQAAKHEGPLH KCDISNSTEAGQKLFNMLRLGKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNK NSFVGWSTDWSPYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKN QMILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRINDAFRLNDN SLEFLGIQPTLGPPNQPPVSIWLIVFGVVMGVIVVGIVILIFTGIRDRKKKNKARSGENP YASIDISKGENNPGFQNTDDVQTSFCommunity curation ()Add a publicationFeedback
Angiotensin-converting enzyme 2
ACE2
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>Select a section on the left to see content.
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.2"A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase."
Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J.
J. Biol. Chem. 275:33238-33243(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY. - Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR. - Ref.18"Increased angiotensin-(1-7)-forming activity in failing human heart ventricles: evidence for upregulation of the angiotensin-converting enzyme Homologue ACE2."
Zisman L.S., Keller R.S., Weaver B., Lin Q., Speth R., Bristow M.R., Canver C.C.
Circulation 108:1707-1712(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION. - Ref.29"Residues affecting the chloride regulation and substrate selectivity of the angiotensin-converting enzymes (ACE and ACE2) identified by site-directed mutagenesis."
Rushworth C.A., Guy J.L., Turner A.J.
FEBS J. 275:6033-6042(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF ARG-169; TRP-271; LYS-481 AND ARG-514. - Ref.30"A protein complex in the brush-border membrane explains a Hartnup disorder allele."
Kowalczuk S., Broeer A., Tietze N., Vanslambrouck J.M., Rasko J.E., Broeer S.
FASEB J. 22:2880-2887(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.32"Tissue-specific amino acid transporter partners ACE2 and collectrin differentially interact with hartnup mutations."
Camargo S.M., Singer D., Makrides V., Huggel K., Pos K.M., Wagner C.A., Kuba K., Danilczyk U., Skovby F., Kleta R., Penninger J.M., Verrey F.
Gastroenterology 136:872-882(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF ARG-273. - Ref.36"Angiotensin-Converting Enzyme 2 Metabolizes and Partially Inactivates Pyr-Apelin-13 and Apelin-17: Physiological Effects in the Cardiovascular System."
Wang W., McKinnie S.M., Farhan M., Paul M., McDonald T., McLean B., Llorens-Cortes C., Hazra S., Murray A.G., Vederas J.C., Oudit G.Y.
Hypertension 68:365-377(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, ACTIVE SITE.
Manual assertion based on experiment ini
- Ref.8"Interferons and viruses induce a novel truncated ACE2 isoform and not the full-length SARS-CoV-2 receptor."
Onabajo O.O., Banday A.R., Stanifer M.L., Yan W., Obajemu A., Santer D.M., Florez-Vargas O., Piontkivska H., Vargas J.M., Ring T.J., Kee C., Doldan P., Tyrrell D.L., Mendoza J.L., Boulant S., Prokunina-Olsson L.
Nat. Genet. 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), INDUCTION BY IFN (ISOFORM 2), ALTERNATIVE SPLICING.
Manual assertion based on experiment ini
- Ref.19"Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus."
Li W., Moore M.J., Vasilieva N., Sui J., Wong S.-K., Berne M.A., Somasundaran M., Sullivan J.L., Luzuriaga K., Greenough T.C., Choe H., Farzan M.
Nature 426:450-454(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.22"Efficient replication of severe acute respiratory syndrome coronavirus in mouse cells is limited by murine angiotensin-converting enzyme 2."
Li W., Greenough T.C., Moore M.J., Vasilieva N., Somasundaran M., Sullivan J.L., Farzan M., Choe H.
J. Virol. 78:11429-11433(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN (MICROBIAL INFECTION). - Ref.25"Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2."
Li W., Zhang C., Sui J., Kuhn J.H., Moore M.J., Luo S., Wong S.-K., Huang I.-C., Xu K., Vasilieva N., Murakami A., He Y., Marasco W.A., Guan Y., Choe H., Farzan M.
EMBO J. 24:1634-1643(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), MUTAGENESIS. - Ref.27"Human coronavirus NL63 employs the severe acute respiratory syndrome coronavirus receptor for cellular entry."
Hofmann H., Pyrc K., van der Hoek L., Geier M., Berkhout B., Poehlmann S.
Proc. Natl. Acad. Sci. U.S.A. 102:7988-7993(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HCOV-NL63 SPIKE GLYCOPROTEIN (MICROBIAL INFECTION). - Ref.35"TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein."
Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O., Poehlmann S.
J. Virol. 88:1293-1307(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE. - Ref.38"SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor."
Hoffmann M., Kleine-Weber H., Schroeder S., Krueger N., Herrler T., Erichsen S., Schiergens T.S., Herrler G., Wu N.H., Nitsche A., Mueller M.A., Drosten C., Poehlmann S.
Cell 181:1-10(2020) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION). - Ref.40"Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein."
Walls A.C., Park Y.J., Tortorici M.A., Wall A., McGuire A.T., Veesler D.
Cell 180:1-12(2020) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL INFECTION). - Ref.46"Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV."
Ou X., Liu Y., Lei X., Li P., Mi D., Ren L., Guo L., Guo R., Chen T., Hu J., Xiang Z., Mu Z., Chen X., Chen J., Hu K., Jin Q., Wang J., Qian Z.
Nat. Commun. 11:1620-1620(2020) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION). - Ref.49"Neuropilin-1 as a new potential SARS-CoV-2 infection mediator implicated in the neurologic features and central nervous system involvement of COVID-19."
Davies J., Randeva H.S., Chatha K., Hall M., Spandidos D.A., Karteris E., Kyrou I.
Mol. Med. Report. 22:4221-4226(2020) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION). - Ref.51"Neuropilin-1 is a host factor for SARS-CoV-2 infection."
Daly J.L., Simonetti B., Klein K., Chen K.E., Williamson M.K., Anton-Plagaro C., Shoemark D.K., Simon-Gracia L., Bauer M., Hollandi R., Greber U.F., Horvath P., Sessions R.B., Helenius A., Hiscox J.A., Teesalu T., Matthews D.A., Davidson A.D. , Collins B.M., Cullen P.J., Yamauchi Y.
Science 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION). - Ref.58"Structural basis of receptor recognition by SARS-CoV-2."
Shang J., Ye G., Shi K., Wan Y., Luo C., Aihara H., Geng Q., Auerbach A., Li F.
Nature 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 19-615 AND IN COMPLEX WITH SARS-COV-2 SPIKE GLYCOPROTEIN, INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), FUNCTION (MICROBIAL INFECTION).
Manual assertion based on experiment ini
- Ref.8"Interferons and viruses induce a novel truncated ACE2 isoform and not the full-length SARS-CoV-2 receptor."
Onabajo O.O., Banday A.R., Stanifer M.L., Yan W., Obajemu A., Santer D.M., Florez-Vargas O., Piontkivska H., Vargas J.M., Ring T.J., Kee C., Doldan P., Tyrrell D.L., Mendoza J.L., Boulant S., Prokunina-Olsson L.
Nat. Genet. 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), INDUCTION BY IFN (ISOFORM 2), ALTERNATIVE SPLICING.
<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
- angiotensin IIEC:3.4.17.23
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<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.18"Increased angiotensin-(1-7)-forming activity in failing human heart ventricles: evidence for upregulation of the angiotensin-converting enzyme Homologue ACE2."
Zisman L.S., Keller R.S., Weaver B., Lin Q., Speth R., Bristow M.R., Canver C.C.
Circulation 108:1707-1712(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION.
Manual assertion based on experiment ini
- Ref.2"A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase."
Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J.
J. Biol. Chem. 275:33238-33243(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY. - Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR. - Ref.29"Residues affecting the chloride regulation and substrate selectivity of the angiotensin-converting enzymes (ACE and ACE2) identified by site-directed mutagenesis."
Rushworth C.A., Guy J.L., Turner A.J.
FEBS J. 275:6033-6042(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF ARG-169; TRP-271; LYS-481 AND ARG-514.
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Manual assertion inferred by curator fromi
- Ref.18"Increased angiotensin-(1-7)-forming activity in failing human heart ventricles: evidence for upregulation of the angiotensin-converting enzyme Homologue ACE2."
Zisman L.S., Keller R.S., Weaver B., Lin Q., Speth R., Bristow M.R., Canver C.C.
Circulation 108:1707-1712(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION.
Manual assertion based on experiment ini
- Ref.2"A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase."
Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J.
J. Biol. Chem. 275:33238-33243(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY. - Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR. - Ref.29"Residues affecting the chloride regulation and substrate selectivity of the angiotensin-converting enzymes (ACE and ACE2) identified by site-directed mutagenesis."
Rushworth C.A., Guy J.L., Turner A.J.
FEBS J. 275:6033-6042(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF ARG-169; TRP-271; LYS-481 AND ARG-514.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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Manual assertion based on experiment ini
- Ref.18"Increased angiotensin-(1-7)-forming activity in failing human heart ventricles: evidence for upregulation of the angiotensin-converting enzyme Homologue ACE2."
Zisman L.S., Keller R.S., Weaver B., Lin Q., Speth R., Bristow M.R., Canver C.C.
Circulation 108:1707-1712(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION.
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angiotensin II- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=angiotensin-(1-7)- Search proteins in UniProtKB for this molecule.
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+L-phenylalanine- Search proteins in UniProtKB for this molecule.
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- angiotensin I
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Manual assertion based on experiment ini
- Ref.1"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.2"A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase."
Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J.
J. Biol. Chem. 275:33238-33243(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY. - Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR. - Ref.29"Residues affecting the chloride regulation and substrate selectivity of the angiotensin-converting enzymes (ACE and ACE2) identified by site-directed mutagenesis."
Rushworth C.A., Guy J.L., Turner A.J.
FEBS J. 275:6033-6042(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF ARG-169; TRP-271; LYS-481 AND ARG-514.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.1"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.2"A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase."
Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J.
J. Biol. Chem. 275:33238-33243(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY. - Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR. - Ref.29"Residues affecting the chloride regulation and substrate selectivity of the angiotensin-converting enzymes (ACE and ACE2) identified by site-directed mutagenesis."
Rushworth C.A., Guy J.L., Turner A.J.
FEBS J. 275:6033-6042(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF ARG-169; TRP-271; LYS-481 AND ARG-514.
Source: Rhea- Search for this reaction in UniProtKB.
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angiotensin I- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=angiotensin-(1-9)- Search proteins in UniProtKB for this molecule.
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+L-leucine- Search proteins in UniProtKB for this molecule.
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- [des-Arg9]-bradykinin
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- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.1"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.1"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
[des-Arg9]-bradykinin- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=[des-Phe8, des-Arg9]-bradykinin- Search proteins in UniProtKB for this molecule.
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+L-phenylalanine- Search proteins in UniProtKB for this molecule.
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- H2O
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.1"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.1"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
H2O- Search proteins in UniProtKB for this molecule.
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+neurotensin- Search proteins in UniProtKB for this molecule.
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=L-leucine- Search proteins in UniProtKB for this molecule.
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+neurotensin-(1-12)- Search proteins in UniProtKB for this molecule.
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- H2O
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
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- Search proteins in UniProtKB for this molecule.
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Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
H2O- Search proteins in UniProtKB for this molecule.
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+neurotensin-(1-8)- Search proteins in UniProtKB for this molecule.
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=L-arginine- Search proteins in UniProtKB for this molecule.
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+neurotensin-(1-7)- Search proteins in UniProtKB for this molecule.
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- H2O
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
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- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.1"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.1"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
Source: Rhea- Search for this reaction in UniProtKB.
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H2O- Search proteins in UniProtKB for this molecule.
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+kinetensin- Search proteins in UniProtKB for this molecule.
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=kinetensin-(1-8)- Search proteins in UniProtKB for this molecule.
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+L-leucine- Search proteins in UniProtKB for this molecule.
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- dynorphin A-(1-13)
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
Source: Rhea- Search for this reaction in UniProtKB.
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dynorphin A-(1-13)- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=dynorphin A-(1-12)- Search proteins in UniProtKB for this molecule.
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+L-lysine- Search proteins in UniProtKB for this molecule.
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- apelin-13
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
Source: Rhea- Search for this reaction in UniProtKB.
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apelin-13- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=apelin-12- Search proteins in UniProtKB for this molecule.
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+L-phenylalanine- Search proteins in UniProtKB for this molecule.
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- [Pyr1]apelin-13
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.36"Angiotensin-Converting Enzyme 2 Metabolizes and Partially Inactivates Pyr-Apelin-13 and Apelin-17: Physiological Effects in the Cardiovascular System."
Wang W., McKinnie S.M., Farhan M., Paul M., McDonald T., McLean B., Llorens-Cortes C., Hazra S., Murray A.G., Vederas J.C., Oudit G.Y.
Hypertension 68:365-377(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, ACTIVE SITE. - Ref.37"[Pyr1]Apelin-13(1-12) Is a Biologically Active ACE2 Metabolite of the Endogenous Cardiovascular Peptide [Pyr1]Apelin-13."
Yang P., Kuc R.E., Brame A.L., Dyson A., Singer M., Glen R.C., Cheriyan J., Wilkinson I.B., Davenport A.P., Maguire J.J.
Front. Neurosci. 11:92-92(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion based on experiment ini
- Ref.36"Angiotensin-Converting Enzyme 2 Metabolizes and Partially Inactivates Pyr-Apelin-13 and Apelin-17: Physiological Effects in the Cardiovascular System."
Wang W., McKinnie S.M., Farhan M., Paul M., McDonald T., McLean B., Llorens-Cortes C., Hazra S., Murray A.G., Vederas J.C., Oudit G.Y.
Hypertension 68:365-377(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, ACTIVE SITE.
Source: Rhea- Search for this reaction in UniProtKB.
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[Pyr1]apelin-13- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=[Pyr1]apelin-12- Search proteins in UniProtKB for this molecule.
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+L-phenylalanine- Search proteins in UniProtKB for this molecule.
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- apelin-17
- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.36"Angiotensin-Converting Enzyme 2 Metabolizes and Partially Inactivates Pyr-Apelin-13 and Apelin-17: Physiological Effects in the Cardiovascular System."
Wang W., McKinnie S.M., Farhan M., Paul M., McDonald T., McLean B., Llorens-Cortes C., Hazra S., Murray A.G., Vederas J.C., Oudit G.Y.
Hypertension 68:365-377(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, ACTIVE SITE.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion based on experiment ini
- Ref.36"Angiotensin-Converting Enzyme 2 Metabolizes and Partially Inactivates Pyr-Apelin-13 and Apelin-17: Physiological Effects in the Cardiovascular System."
Wang W., McKinnie S.M., Farhan M., Paul M., McDonald T., McLean B., Llorens-Cortes C., Hazra S., Murray A.G., Vederas J.C., Oudit G.Y.
Hypertension 68:365-377(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, ACTIVE SITE.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
apelin-17- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=apelin-16- Search proteins in UniProtKB for this molecule.
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+L-phenylalanine- Search proteins in UniProtKB for this molecule.
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- β-casomorphin-7
- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
β-casomorphin-7- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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=β-casomorphin-6- Search proteins in UniProtKB for this molecule.
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+L-isoleucine- Search proteins in UniProtKB for this molecule.
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- H2O
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
H2O- Search proteins in UniProtKB for this molecule.
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+neocasomorphin- Search proteins in UniProtKB for this molecule.
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=L-isoleucine- Search proteins in UniProtKB for this molecule.
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+neocasomorphin-(1-5)- Search proteins in UniProtKB for this molecule.
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<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:- Zn2+
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
- chloride
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
<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
Manual assertion based on experiment ini
- Ref.1"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.2"A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase."
Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J.
J. Biol. Chem. 275:33238-33243(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY. - Ref.3"The novel angiotensin-converting enzyme (ACE) homolog, ACE2, is selectively expressed by adult Leydig cells of the testis."
Douglas G.C., O'Bryan M.K., Hedger M.P., Lee D.K.L., Yarski M.A., Smith A.I., Lew R.A.
Endocrinology 145:4703-4711(2004) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.16"Substrate-based design of the first class of angiotensin-converting enzyme-related carboxypeptidase (ACE2) inhibitors."
Dales N.A., Gould A.E., Brown J.A., Calderwood E.F., Guan B., Minor C.A., Gavin J.M., Hales P., Kaushik V.K., Stewart M., Tummino P.J., Vickers C.S., Ocain T.D., Patane M.A.
J. Am. Chem. Soc. 124:11852-11853(2002) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION. - Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR. - Ref.29"Residues affecting the chloride regulation and substrate selectivity of the angiotensin-converting enzymes (ACE and ACE2) identified by site-directed mutagenesis."
Rushworth C.A., Guy J.L., Turner A.J.
FEBS J. 275:6033-6042(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF ARG-169; TRP-271; LYS-481 AND ARG-514.
<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
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR. - Ref.36"Angiotensin-Converting Enzyme 2 Metabolizes and Partially Inactivates Pyr-Apelin-13 and Apelin-17: Physiological Effects in the Cardiovascular System."
Wang W., McKinnie S.M., Farhan M., Paul M., McDonald T., McLean B., Llorens-Cortes C., Hazra S., Murray A.G., Vederas J.C., Oudit G.Y.
Hypertension 68:365-377(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, ACTIVE SITE.
- KM=6.9 µM for angiotensin I1 Publication
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
- KM=2.0 µM for angiotensin II1 Publication
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
- KM=6.8 µM for apelin-131 Publication
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
- KM=290 µM for [des-Arg9]-bradykinin1 Publication
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
- KM=130 µM for Lys-[des-Arg9]-bradykinin1 Publication
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
- KM=31 µM for beta-casomorphin1 Publication
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
- KM=5.5 µM for dynorphin A-(1-13)1 Publication
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
- KM=300 µM for neurotensin-1-81 Publication
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
- KM=58.6 µM for angiotensin II1 Publication
Manual assertion based on experiment ini
- Ref.29"Residues affecting the chloride regulation and substrate selectivity of the angiotensin-converting enzymes (ACE and ACE2) identified by site-directed mutagenesis."
Rushworth C.A., Guy J.L., Turner A.J.
FEBS J. 275:6033-6042(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF ARG-169; TRP-271; LYS-481 AND ARG-514.
- KM=12 µM for [Pyr1]apelin-131 Publication
Manual assertion based on experiment ini
- Ref.36"Angiotensin-Converting Enzyme 2 Metabolizes and Partially Inactivates Pyr-Apelin-13 and Apelin-17: Physiological Effects in the Cardiovascular System."
Wang W., McKinnie S.M., Farhan M., Paul M., McDonald T., McLean B., Llorens-Cortes C., Hazra S., Murray A.G., Vederas J.C., Oudit G.Y.
Hypertension 68:365-377(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, ACTIVE SITE.
- KM=19 µM for apelin-171 Publication
Manual assertion based on experiment ini
- Ref.36"Angiotensin-Converting Enzyme 2 Metabolizes and Partially Inactivates Pyr-Apelin-13 and Apelin-17: Physiological Effects in the Cardiovascular System."
Wang W., McKinnie S.M., Farhan M., Paul M., McDonald T., McLean B., Llorens-Cortes C., Hazra S., Murray A.G., Vederas J.C., Oudit G.Y.
Hypertension 68:365-377(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, ACTIVE SITE.
- Vmax=28.7 nmol/min/mg enzyme with angiotensin II as substrate1 Publication
Manual assertion based on experiment ini
- Ref.29"Residues affecting the chloride regulation and substrate selectivity of the angiotensin-converting enzymes (ACE and ACE2) identified by site-directed mutagenesis."
Rushworth C.A., Guy J.L., Turner A.J.
FEBS J. 275:6033-6042(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF ARG-169; TRP-271; LYS-481 AND ARG-514.
pH dependencei
Manual assertion based on experiment ini
- Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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 sitei | 169 | Chloride1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| 1 | |
Binding sitei | 273 | Substrate1 Publication Manual assertion inferred by curator fromi
| 1 | |
<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 bindingi | 374 | Zinc; catalytic1 Publication Manual assertion based on experiment ini
| 1 | |
<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 sitei | 375 | Proton acceptor2 Publications Manual assertion inferred by curator fromi
| 1 | |
Metal bindingi | 378 | Zinc; catalytic1 Publication Manual assertion based on experiment ini
| 1 | |
Metal bindingi | 402 | Zinc; catalytic1 Publication Manual assertion based on experiment ini
| 1 | |
Binding sitei | 477 | Chloride1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| 1 | |
Binding sitei | 481 | Chloride1 Publication Manual assertion inferred by curator fromi
Manual assertion based on experiment ini
| 1 | |
Active sitei | 505 | Proton donor1 Publication Manual assertion inferred by curator fromi
| 1 | |
Binding sitei | 515 | Substrate1 Publication Manual assertion inferred by curator fromi
| 1 |
<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
- carboxypeptidase activity Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.1"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
- endopeptidase activity Source: UniProtKBInferred from direct assayi
- "Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism."
Rice G.I., Thomas D.A., Grant P.J., Turner A.J., Hooper N.M.
Biochem. J. 383:45-51(2004) [PubMed] [Europe PMC] [Abstract]
- metallocarboxypeptidase activity Source: ReactomeInferred from experimenti
- Ref.2"A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase."
Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J.
J. Biol. Chem. 275:33238-33243(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY. - Ref.1"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.17"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, COFACTOR.
- metallopeptidase activity Source: UniProtKBInferred from direct assayi
- Ref.2"A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase."
Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J.
J. Biol. Chem. 275:33238-33243(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
- peptidyl-dipeptidase activity Source: UniProtKBInferred from direct assayi
- Ref.2"A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase."
Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J.
J. Biol. Chem. 275:33238-33243(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
- virus receptor activity Source: FlyBaseInferred from direct assayi
- "LSECtin interacts with filovirus glycoproteins and the spike protein of SARS coronavirus."
Gramberg T., Hofmann H., Moeller P., Lalor P.F., Marzi A., Geier M., Krumbiegel M., Winkler T., Kirchhoff F., Adams D.H., Becker S., Muench J., Poehlmann S.
Virology 340:224-236(2005) [PubMed] [Europe PMC] [Abstract]
- zinc ion binding Source: BHF-UCL
<p>Traceable Author Statement</p>
<p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p>
Traceable author statementi
- Ref.2"A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase."
Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J.
J. Biol. Chem. 275:33238-33243(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
GO - Biological processi
- angiotensin maturation Source: Reactome
- angiotensin-mediated drinking behavior Source: BHF-UCL
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- "Angiotensin-converting enzyme 2 overexpression in the subfornical organ prevents the angiotensin II-mediated pressor and drinking responses and is associated with angiotensin II type 1 receptor downregulation."
Feng Y., Yue X., Xia H., Bindom S.M., Hickman P.J., Filipeanu C.M., Wu G., Lazartigues E.
Circ Res 102:729-736(2008) [PubMed] [Europe PMC] [Abstract]
- negative regulation of signaling receptor activity Source: ARUK-UCLInferred from mutant phenotypei
- "Angiotensin-converting enzyme 2 overexpression in the subfornical organ prevents the angiotensin II-mediated pressor and drinking responses and is associated with angiotensin II type 1 receptor downregulation."
Feng Y., Yue X., Xia H., Bindom S.M., Hickman P.J., Filipeanu C.M., Wu G., Lazartigues E.
Circ Res 102:729-736(2008) [PubMed] [Europe PMC] [Abstract]
- positive regulation of amino acid transport Source: UniProtKBInferred from mutant phenotypei
- Ref.32"Tissue-specific amino acid transporter partners ACE2 and collectrin differentially interact with hartnup mutations."
Camargo S.M., Singer D., Makrides V., Huggel K., Pos K.M., Wagner C.A., Kuba K., Danilczyk U., Skovby F., Kleta R., Penninger J.M., Verrey F.
Gastroenterology 136:872-882(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF ARG-273.
- positive regulation of cardiac muscle contraction Source: Ensembl
- positive regulation of gap junction assembly Source: BHF-UCLInferred from mutant phenotypei
- "Heart block, ventricular tachycardia, and sudden death in ACE2 transgenic mice with downregulated connexins."
Donoghue M., Wakimoto H., Maguire C.T., Acton S., Hales P., Stagliano N., Fairchild-Huntress V., Xu J., Lorenz J.N., Kadambi V., Berul C.I., Breitbart R.E.
J. Mol. Cell. Cardiol. 35:1043-1053(2003) [PubMed] [Europe PMC] [Abstract]
- positive regulation of L-proline import across plasma membrane Source: ARUK-UCL
<p>Inferred from Genetic Interaction</p>
<p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p>
Inferred from genetic interactioni
- "Human intestine luminal ACE2 and amino acid transporter expression increased by ACE-inhibitors."
Vuille-dit-Bille R.N., Camargo S.M., Emmenegger L., Sasse T., Kummer E., Jando J., Hamie Q.M., Meier C.F., Hunziker S., Forras-Kaufmann Z., Kuyumcu S., Fox M., Schwizer W., Fried M., Lindenmeyer M., Gotze O., Verrey F.
Amino Acids 47:693-705(2015) [PubMed] [Europe PMC] [Abstract]
- positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
<p>Inferred by Curator</p>
<p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence<br />is available.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ic">GO evidence code guide</a></p>
Inferred by curatori
- "Cloning and characterization of a secreted form of angiotensin-converting enzyme 2."
Huentelman M.J., Zubcevic J., Katovich M.J., Raizada M.K.
Regul Pept 122:61-67(2004) [PubMed] [Europe PMC] [Abstract]
- receptor-mediated virion attachment to host cell Source: UniProtKBInferred from direct assayi
- Ref.46"Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV."
Ou X., Liu Y., Lei X., Li P., Mi D., Ren L., Guo L., Guo R., Chen T., Hu J., Xiang Z., Mu Z., Chen X., Chen J., Hu K., Jin Q., Wang J., Qian Z.
Nat. Commun. 11:1620-1620(2020) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION).
- regulation of blood vessel diameter Source: BHF-UCLInferred by curatori
- "Cloning and characterization of a secreted form of angiotensin-converting enzyme 2."
Huentelman M.J., Zubcevic J., Katovich M.J., Raizada M.K.
Regul Pept 122:61-67(2004) [PubMed] [Europe PMC] [Abstract]
- regulation of cardiac conduction Source: BHF-UCLInferred from mutant phenotypei
- "Heart block, ventricular tachycardia, and sudden death in ACE2 transgenic mice with downregulated connexins."
Donoghue M., Wakimoto H., Maguire C.T., Acton S., Hales P., Stagliano N., Fairchild-Huntress V., Xu J., Lorenz J.N., Kadambi V., Berul C.I., Breitbart R.E.
J. Mol. Cell. Cardiol. 35:1043-1053(2003) [PubMed] [Europe PMC] [Abstract]
- regulation of cell population proliferation Source: BHF-UCLTraceable author statementi
- "ACE2: a new target for cardiovascular disease therapeutics."
Raizada M.K., Ferreira A.J.
J Cardiovasc Pharmacol 50:112-119(2007) [PubMed] [Europe PMC] [Abstract]
- regulation of cytokine production Source: BHF-UCLInferred by curatori
- "Cloning and characterization of a secreted form of angiotensin-converting enzyme 2."
Huentelman M.J., Zubcevic J., Katovich M.J., Raizada M.K.
Regul Pept 122:61-67(2004) [PubMed] [Europe PMC] [Abstract]
- regulation of inflammatory response Source: BHF-UCLInferred by curatori
- "Cloning and characterization of a secreted form of angiotensin-converting enzyme 2."
Huentelman M.J., Zubcevic J., Katovich M.J., Raizada M.K.
Regul Pept 122:61-67(2004) [PubMed] [Europe PMC] [Abstract]
- regulation of systemic arterial blood pressure by renin-angiotensin Source: BHF-UCLInferred from mutant phenotypei
- "Angiotensin-converting enzyme 2 overexpression in the subfornical organ prevents the angiotensin II-mediated pressor and drinking responses and is associated with angiotensin II type 1 receptor downregulation."
Feng Y., Yue X., Xia H., Bindom S.M., Hickman P.J., Filipeanu C.M., Wu G., Lazartigues E.
Circ Res 102:729-736(2008) [PubMed] [Europe PMC] [Abstract]
- regulation of transmembrane transporter activity Source: ARUK-UCLInferred from genetic interactioni
- "Human intestine luminal ACE2 and amino acid transporter expression increased by ACE-inhibitors."
Vuille-dit-Bille R.N., Camargo S.M., Emmenegger L., Sasse T., Kummer E., Jando J., Hamie Q.M., Meier C.F., Hunziker S., Forras-Kaufmann Z., Kuyumcu S., Fox M., Schwizer W., Fried M., Lindenmeyer M., Gotze O., Verrey F.
Amino Acids 47:693-705(2015) [PubMed] [Europe PMC] [Abstract]
- regulation of vasoconstriction Source: BHF-UCLInferred by curatori
- "Cloning and characterization of a secreted form of angiotensin-converting enzyme 2."
Huentelman M.J., Zubcevic J., Katovich M.J., Raizada M.K.
Regul Pept 122:61-67(2004) [PubMed] [Europe PMC] [Abstract]
- tryptophan transport Source: Ensembl
- viral entry into host cell Source: UniProtKBInferred from direct assayi
- Ref.46"Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV."
Ou X., Liu Y., Lei X., Li P., Mi D., Ren L., Guo L., Guo R., Chen T., Hu J., Xiang Z., Mu Z., Chen X., Chen J., Hu K., Jin Q., Wang J., Qian Z.
Nat. Commun. 11:1620-1620(2020) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION).
<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 function | Carboxypeptidase, Host cell receptor for virus entry, Hydrolase, Metalloprotease, Protease, Receptor |
Biological process | Host-virus interaction |
Ligand | Chloride, 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:3.4.17.23
Manual assertion based on experiment ini
Alternative name(s): Angiotensin-converting enzyme homolog1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Short name: ACEH1 Publication Manual assertion based on opinion ini
Angiotensin-converting enzyme-related carboxypeptidase1 Publication Manual assertion based on opinion ini
Manual assertion based on experiment ini
Short name: ACE-related carboxypeptidase Metalloprotease MPROT151 Publication Manual assertion based on opinion ini
Cleaved into the following chain: Processed angiotensin-converting enzyme 21 Publication Manual assertion based on opinion ini
|
<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 <p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi 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>Organismi | Homo 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 identifieri | 9606 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 |
|
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
- Secreted 1 Publication
Manual assertion based on experiment ini
- Ref.26"Tumor necrosis factor-alpha convertase (ADAM17) mediates regulated ectodomain shedding of the severe-acute respiratory syndrome-coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 (ACE2)."
Lambert D.W., Yarski M., Warner F.J., Thornhill P., Parkin E.T., Smith A.I., Hooper N.M., Turner A.J.
J. Biol. Chem. 280:30113-30119(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION.
- Secreted 1 Publication
Plasma membrane
- Cell membrane 1 Publication
Manual assertion based on experiment ini
- Ref.30"A protein complex in the brush-border membrane explains a Hartnup disorder allele."
Kowalczuk S., Broeer A., Tietze N., Vanslambrouck J.M., Rasko J.E., Broeer S.
FASEB J. 22:2880-2887(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- Cell membrane 1 Publication
Other locations
- Cytoplasm By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
Note: Detected in both cell membrane and cytoplasm in neurons.By similarity- Cytoplasm By similarity
Manual assertion inferred from sequence similarity toi
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- "Large-scale proteomics and phosphoproteomics of urinary exosomes."
Gonzales P.A., Pisitkun T., Hoffert J.D., Tchapyjnikov D., Star R.A., Kleta R., Wang N.S., Knepper M.A.
J Am Soc Nephrol 20:363-379(2009) [PubMed] [Europe PMC] [Abstract] - "In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine."
Principe S., Jones E.E., Kim Y., Sinha A., Nyalwidhe J.O., Brooks J., Semmes O.J., Troyer D.A., Lance R.S., Kislinger T., Drake R.R.
Proteomics 13:1667-1671(2013) [PubMed] [Europe PMC] [Abstract]
- extracellular region Source: UniProtKBInferred from direct assayi
- Ref.1"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
- extracellular space Source: BHF-UCLInferred from direct assayi
- "Angiotensin-converting enzyme 2 overexpression in the subfornical organ prevents the angiotensin II-mediated pressor and drinking responses and is associated with angiotensin II type 1 receptor downregulation."
Feng Y., Yue X., Xia H., Bindom S.M., Hickman P.J., Filipeanu C.M., Wu G., Lazartigues E.
Circ Res 102:729-736(2008) [PubMed] [Europe PMC] [Abstract]
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Plasma Membrane
- apical plasma membrane Source: ARUK-UCLInferred from direct assayi
- "Human intestine luminal ACE2 and amino acid transporter expression increased by ACE-inhibitors."
Vuille-dit-Bille R.N., Camargo S.M., Emmenegger L., Sasse T., Kummer E., Jando J., Hamie Q.M., Meier C.F., Hunziker S., Forras-Kaufmann Z., Kuyumcu S., Fox M., Schwizer W., Fried M., Lindenmeyer M., Gotze O., Verrey F.
Amino Acids 47:693-705(2015) [PubMed] [Europe PMC] [Abstract]
- brush border membrane Source: ARUK-UCLInferred from direct assayi
- "Human intestine luminal ACE2 and amino acid transporter expression increased by ACE-inhibitors."
Vuille-dit-Bille R.N., Camargo S.M., Emmenegger L., Sasse T., Kummer E., Jando J., Hamie Q.M., Meier C.F., Hunziker S., Forras-Kaufmann Z., Kuyumcu S., Fox M., Schwizer W., Fried M., Lindenmeyer M., Gotze O., Verrey F.
Amino Acids 47:693-705(2015) [PubMed] [Europe PMC] [Abstract]
- plasma membrane Source: UniProtKBInferred from direct assayi
- Ref.34"A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry."
Shulla A., Heald-Sargent T., Subramanya G., Zhao J., Perlman S., Gallagher T.
J. Virol. 85:873-882(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, INTERACTION WITH TMPRSS2.
- apical plasma membrane Source: ARUK-UCLInferred from direct assayi
Other locations
- cell surface Source: UniProtKBInferred from direct assayi
- Ref.35"TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein."
Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O., Poehlmann S.
J. Virol. 88:1293-1307(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
- cytoplasm Source: UniProtKB-SubCell
- integral component of membrane Source: UniProtKB-KW
- membrane raft Source: BHF-UCLTraceable author statementi
- "Lipid rafts are involved in SARS-CoV entry into Vero E6 cells."
Lu Y., Liu D.X., Tam J.P.
Biochem Biophys Res Commun 369:344-349(2008) [PubMed] [Europe PMC] [Abstract]
- cell surface Source: UniProtKBInferred from direct assayi
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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 domaini | 18 – 740 | ExtracellularSequence analysisAdd BLAST | 723 | |
<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>Transmembranei | 741 – 761 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 762 – 805 | CytoplasmicSequence analysisAdd BLAST | 44 |
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
Manual assertion based on experiment ini
- Ref.50"Engineering human ACE2 to optimize binding to the spike protein of SARS coronavirus 2."
Chan K.K., Dorosky D., Sharma P., Abbasi S.A., Dye J.M., Kranz D.M., Herbert A.S., Procko E.
Science 369:1261-1265(2020) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), MUTAGENESIS OF SER-19; GLN-24; ALA-25; THR-27; LEU-29; LYS-31; ASN-33; HIS-34; LEU-39; PHE-40; TYR-41; GLN-42; TRP-69; PHE-72; GLU-75; GLN-76; LEU-79; GLN-89; ASN-90; LEU-91; THR-92; THR-324; GLN-325; ASN-330; LEU-351; ALA-386; PRO-389; ARG-393 AND ARG-518, BIOTECHNOLOGY.
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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>Mutagenesisi | 19 | S → P: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 24 – 26 | QAK → KAE: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 3 | |
Mutagenesisi | 24 | Q → T: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 25 | A → V: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 27 | T → 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 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 29 | L → F: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 31 | K → D: Abolishes interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 31 | K → Y: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 33 | N → D: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 34 | H → A: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 37 | E → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 38 | D → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 39 | L → R: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 40 | F → D: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 41 | Y → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 41 | Y → R: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 42 | Q → L: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 68 | K → D: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 69 | W → V: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 72 | F → Y: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 75 | E → K: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 76 | Q → T: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 79 | L → T: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 82 – 84 | MYP → NFS: Inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 3 | |
Mutagenesisi | 89 | Q → P: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 90 | N → Q: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 91 | L → P: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 92 | T → Q: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 110 | E → P: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 135 – 136 | PD → SM: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 2 | |
Mutagenesisi | 160 | E → R: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 169 | R → Q: About 95% loss of angiotensin I cleavage. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 192 | R → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 219 | R → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 239 | H → Q: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 271 | W → Q: About 95% loss of angiotensin I cleavage. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 273 | R → Q: Complete loss of enzyme activity. Does not affect amino acid transport activity of SLC6A19. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 309 | K → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 312 | E → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 324 | T → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 324 | T → P: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 325 | Q → P: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 330 | N → 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 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 338 – 340 | NVQ → DDR: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 3 | |
Mutagenesisi | 345 | H → A: Complete loss of enzyme activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 350 | D → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 351 | L → F: Increases slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 353 | K → H, A or D: Abolishes interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 355 | D → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 357 | R → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 359 | L → K or A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 383 | M → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 386 | A → 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 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 389 | P → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 389 | P → D: Increases very slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 393 | R → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 393 | R → K: Increases very slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 425 – 427 | SPD → PSN: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 3 | |
Mutagenesisi | 465 – 467 | KGE → QDK: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 3 | |
Mutagenesisi | 481 | K → Q: About 80% loss of angiotensin I cleavage. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 505 | H → A: Complete loss of enzyme activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 514 | R → Q: About 50% loss of angiotensin I cleavage but two-fold greater activity with angiotensin II. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 518 | R → G: Increases very slightly the interaction with RBD domain of SARS-CoV-2 spike protein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 559 | R → S: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 603 | F → T: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication Manual assertion based on experiment ini
| 1 |
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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 peptidei | 1 – 17 | Sequence analysisAdd BLAST | 17 | |
<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_0000028570 | 18 – 805 | Angiotensin-converting enzyme 2Add BLAST | 788 | |
ChainiPRO_0000292268 | 18 – 708 | Processed angiotensin-converting enzyme 2Add BLAST | 691 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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>Glycosylationi | 53 | N-linked (GlcNAc...) asparagine1 Publication Manual assertion inferred by curator fromi
| 1 | |
Glycosylationi | 90 | N-linked (GlcNAc...) asparagine2 Publications Manual assertion based on experiment ini
| 1 | |
Glycosylationi | 103 | N-linked (GlcNAc...) asparagine1 Publication Manual assertion based on experiment ini
| 1 | |
<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 bondi | 133 ↔ 141 | 1 Publication Manual assertion based on experiment ini
| ||
Glycosylationi | 322 | N-linked (GlcNAc...) asparagine1 Publication Manual assertion inferred by curator fromi
| 1 | |
Disulfide bondi | 344 ↔ 361 | 1 Publication Manual assertion based on experiment ini
| ||
Glycosylationi | 432 | N-linked (GlcNAc...) asparagine1 Publication Manual assertion based on experiment ini
| 1 | |
Disulfide bondi | 530 ↔ 542 | 1 Publication Manual assertion based on experiment ini
| ||
Glycosylationi | 546 | N-linked (GlcNAc...) asparagine2 Publications Manual assertion based on experiment ini
| 1 | |
Glycosylationi | 690 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
<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
Manual assertion based on experiment ini
- Ref.2"A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase."
Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J.
J. Biol. Chem. 275:33238-33243(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY. - Ref.19"Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus."
Li W., Moore M.J., Vasilieva N., Sui J., Wong S.-K., Berne M.A., Somasundaran M., Sullivan J.L., Luzuriaga K., Greenough T.C., Choe H., Farzan M.
Nature 426:450-454(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.23"A proteomic analysis of human bile."
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.
Mol. Cell. Proteomics 3:715-728(2004) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-90. - Ref.31"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-546. - Ref.53"ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis."
Towler P., Staker B., Prasad S.G., Menon S., Tang J., Parsons T., Ryan D., Fisher M., Williams D., Dales N.A., Patane M.A., Pantoliano M.W.
J. Biol. Chem. 279:17996-18007(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-615 IN COMPLEXES WITH ZINC; CHLORIDE AND MLN-4760 INHIBITOR, DOMAIN, REACTION MECHANISM, ACTIVE SITE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-53; ASN-90; ASN-103; ASN-322; ASN-432 AND ASN-546.
Manual assertion based on experiment ini
- Ref.26"Tumor necrosis factor-alpha convertase (ADAM17) mediates regulated ectodomain shedding of the severe-acute respiratory syndrome-coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 (ACE2)."
Lambert D.W., Yarski M., Warner F.J., Thornhill P., Parkin E.T., Smith A.I., Hooper N.M., Turner A.J.
J. Biol. Chem. 280:30113-30119(2005) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION. - Ref.33"Angiotensin-converting enzyme 2 ectodomain shedding cleavage-site identification: determinants and constraints."
Lai Z.W., Hanchapola I., Steer D.L., Smith A.I.
Biochemistry 50:5182-5194(2011) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEOLYTIC CLEAVAGE. - Ref.34"A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry."
Shulla A., Heald-Sargent T., Subramanya G., Zhao J., Perlman S., Gallagher T.
J. Virol. 85:873-882(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, INTERACTION WITH TMPRSS2. - Ref.35"TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein."
Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O., Poehlmann S.
J. Virol. 88:1293-1307(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE. - Ref.59"Structural basis for the recognition of the SARS-CoV-2 by full-length human ACE2."
Yan R., Zhang Y., Li Y., Xia L., Guo Y., Zhou Q.
Science 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 18-805, INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), INTERACTION WITH SLC6A19, SUBUNIT, PROTEOLYTIC CLEAVAGE.
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic 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
Manual assertion based on experiment ini
- Ref.1"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY. - Ref.2"A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase."
Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J.
J. Biol. Chem. 275:33238-33243(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GLYCOSYLATION, FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY. - Ref.3"The novel angiotensin-converting enzyme (ACE) homolog, ACE2, is selectively expressed by adult Leydig cells of the testis."
Douglas G.C., O'Bryan M.K., Hedger M.P., Lee D.K.L., Yarski M.A., Smith A.I., Lew R.A.
Endocrinology 145:4703-4711(2004) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.15"Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme."
Harmer D., Gilbert M., Borman R., Clark K.L.
FEBS Lett. 532:107-110(2002) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY. - Ref.21"Tissue distribution of ACE2 protein, the functional receptor for SARS coronavirus. A first step in understanding SARS pathogenesis."
Hamming I., Timens W., Bulthuis M.L.C., Lely A.T., Navis G.J., van Goor H.
J. Pathol. 203:631-637(2004) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY. - Ref.24"Myocardial infarction increases ACE2 expression in rat and humans."
Burrell L.M., Risvanis J., Kubota E., Dean R.G., MacDonald P.S., Lu S., Tikellis C., Grant S.L., Lew R.A., Smith A.I., Cooper M.E., Johnston C.I.
Eur. Heart J. 26:369-375(2005) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, INDUCTION. - Ref.30"A protein complex in the brush-border membrane explains a Hartnup disorder allele."
Kowalczuk S., Broeer A., Tietze N., Vanslambrouck J.M., Rasko J.E., Broeer S.
FASEB J. 22:2880-2887(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. - Ref.41"SARS-CoV-2 Receptor ACE2 Is an Interferon-Stimulated Gene in Human Airway Epithelial Cells and Is Detected in Specific Cell Subsets across Tissues."
HCA Lung Biological Network. Electronic address: lung-network@humancellatlas.org, HCA Lung Biological Network
Ziegler C.G.K., Allon S.J., Nyquist S.K., Mbano I.M., Miao V.N., Tzouanas C.N., Cao Y., Yousif A.S., Bals J., Hauser B.M., Feldman J., Muus C., Wadsworth M.H. II, Kazer S.W., Hughes T.K., Doran B., Gatter G.J., Vukovic M. , Taliaferro F., Mead B.E., Guo Z., Wang J.P., Gras D., Plaisant M., Ansari M., Angelidis I., Adler H., Sucre J.M.S., Taylor C.J., Lin B., Waghray A., Mitsialis V., Dwyer D.F., Buchheit K.M., Boyce J.A., Barrett N.A., Laidlaw T.M., Carroll S.L., Colonna L., Tkachev V., Peterson C.W., Yu A., Zheng H.B., Gideon H.P., Winchell C.G., Lin P.L., Bingle C.D., Snapper S.B., Kropski J.A., Theis F.J., Schiller H.B., Zaragosi L.E., Barbry P., Leslie A., Kiem H.P., Flynn J.L., Fortune S.M., Berger B., Finberg R.W., Kean L.S., Garber M., Schmidt A.G., Lingwood D., Shalek A.K., Ordovas-Montanes J.
Cell 181:1016-1035.e19(2020) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, INDUCTION BY ISR. - Ref.42"Cigarette smoke exposure and inflammatory signaling increase the expression of the SARS-CoV-2 receptor ACE2 in the respiratory tract."
Smith J.C., Sausville E.L., Girish V., Yuan M.L., Vasudevan A., John K.M., Sheltzer J.M.
Dev. Cell 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, INDUCTION BY CIGARETTE SMOKE. - Ref.43"Single-cell RNA-seq data analysis on the receptor ACE2 expression reveals the potential risk of different human organs vulnerable to 2019-nCoV infection."
Zou X., Chen K., Zou J., Han P., Hao J., Han Z.
Front. Med. 14:185-192(2020) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY. - Ref.45"The protein expression profile of ACE2 in human tissues."
Hikmet F., Mear L., Edvinsson A., Micke P., Uhlen M., Lindskog C.
Mol. Syst. Biol. 16:e9610-e9610(2020) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY. - Ref.47"SARS-CoV-2 entry factors are highly expressed in nasal epithelial cells together with innate immune genes."
HCA Lung Biological Network
Sungnak W., Huang N., Becavin C., Berg M., Queen R., Litvinukova M., Talavera-Lopez C., Maatz H., Reichart D., Sampaziotis F., Worlock K.B., Yoshida M., Barnes J.L.
Nat. Med. 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY. - Ref.48"SARS-CoV-2 productively infects human gut enterocytes."
Lamers M.M., Beumer J., van der Vaart J., Knoops K., Puschhof J., Breugem T.I., Ravelli R.B.G., Paul van Schayck J., Mykytyn A.Z., Duimel H.Q., van Donselaar E., Riesebosch S., Kuijpers H.J.H., Schippers D., van de Wetering W.J., de Graaf M., Koopmans M., Cuppen E. , Peters P.J., Haagmans B.L., Clevers H.
Science 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY. - Ref.52"TMPRSS2 and TMPRSS4 promote SARS-CoV-2 infection of human small intestinal enterocytes."
Zang R., Gomez Castro M.F., McCune B.T., Zeng Q., Rothlauf P.W., Sonnek N.M., Liu Z., Brulois K.F., Wang X., Greenberg H.B., Diamond M.S., Ciorba M.A., Whelan S.P.J., Ding S.
Sci. Immunol. 5:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY.
<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
Manual assertion based on experiment ini
- Ref.18"Increased angiotensin-(1-7)-forming activity in failing human heart ventricles: evidence for upregulation of the angiotensin-converting enzyme Homologue ACE2."
Zisman L.S., Keller R.S., Weaver B., Lin Q., Speth R., Bristow M.R., Canver C.C.
Circulation 108:1707-1712(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION. - Ref.20"ACE2 gene expression is up-regulated in the human failing heart."
Goulter A.B., Goddard M.J., Allen J.C., Clark K.L.
BMC Med. 2:19-19(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION. - Ref.24"Myocardial infarction increases ACE2 expression in rat and humans."
Burrell L.M., Risvanis J., Kubota E., Dean R.G., MacDonald P.S., Lu S., Tikellis C., Grant S.L., Lew R.A., Smith A.I., Cooper M.E., Johnston C.I.
Eur. Heart J. 26:369-375(2005) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, INDUCTION. - Ref.41"SARS-CoV-2 Receptor ACE2 Is an Interferon-Stimulated Gene in Human Airway Epithelial Cells and Is Detected in Specific Cell Subsets across Tissues."
HCA Lung Biological Network. Electronic address: lung-network@humancellatlas.org, HCA Lung Biological Network
Ziegler C.G.K., Allon S.J., Nyquist S.K., Mbano I.M., Miao V.N., Tzouanas C.N., Cao Y., Yousif A.S., Bals J., Hauser B.M., Feldman J., Muus C., Wadsworth M.H. II, Kazer S.W., Hughes T.K., Doran B., Gatter G.J., Vukovic M. , Taliaferro F., Mead B.E., Guo Z., Wang J.P., Gras D., Plaisant M., Ansari M., Angelidis I., Adler H., Sucre J.M.S., Taylor C.J., Lin B., Waghray A., Mitsialis V., Dwyer D.F., Buchheit K.M., Boyce J.A., Barrett N.A., Laidlaw T.M., Carroll S.L., Colonna L., Tkachev V., Peterson C.W., Yu A., Zheng H.B., Gideon H.P., Winchell C.G., Lin P.L., Bingle C.D., Snapper S.B., Kropski J.A., Theis F.J., Schiller H.B., Zaragosi L.E., Barbry P., Leslie A., Kiem H.P., Flynn J.L., Fortune S.M., Berger B., Finberg R.W., Kean L.S., Garber M., Schmidt A.G., Lingwood D., Shalek A.K., Ordovas-Montanes J.
Cell 181:1016-1035.e19(2020) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, INDUCTION BY ISR. - Ref.42"Cigarette smoke exposure and inflammatory signaling increase the expression of the SARS-CoV-2 receptor ACE2 in the respiratory tract."
Smith J.C., Sausville E.L., Girish V., Yuan M.L., Vasudevan A., John K.M., Sheltzer J.M.
Dev. Cell 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, INDUCTION BY CIGARETTE SMOKE.
Manual assertion based on experiment ini
- Ref.8"Interferons and viruses induce a novel truncated ACE2 isoform and not the full-length SARS-CoV-2 receptor."
Onabajo O.O., Banday A.R., Stanifer M.L., Yan W., Obajemu A., Santer D.M., Florez-Vargas O., Piontkivska H., Vargas J.M., Ring T.J., Kee C., Doldan P., Tyrrell D.L., Mendoza J.L., Boulant S., Prokunina-Olsson L.
Nat. Genet. 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), INDUCTION BY IFN (ISOFORM 2), ALTERNATIVE SPLICING.
Manual assertion based on experiment ini
- Ref.8"Interferons and viruses induce a novel truncated ACE2 isoform and not the full-length SARS-CoV-2 receptor."
Onabajo O.O., Banday A.R., Stanifer M.L., Yan W., Obajemu A., Santer D.M., Florez-Vargas O., Piontkivska H., Vargas J.M., Ring T.J., Kee C., Doldan P., Tyrrell D.L., Mendoza J.L., Boulant S., Prokunina-Olsson L.
Nat. Genet. 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), INDUCTION BY IFN (ISOFORM 2), ALTERNATIVE SPLICING.
Manual assertion based on experiment ini
- Ref.41"SARS-CoV-2 Receptor ACE2 Is an Interferon-Stimulated Gene in Human Airway Epithelial Cells and Is Detected in Specific Cell Subsets across Tissues."
HCA Lung Biological Network. Electronic address: lung-network@humancellatlas.org, HCA Lung Biological Network
Ziegler C.G.K., Allon S.J., Nyquist S.K., Mbano I.M., Miao V.N., Tzouanas C.N., Cao Y., Yousif A.S., Bals J., Hauser B.M., Feldman J., Muus C., Wadsworth M.H. II, Kazer S.W., Hughes T.K., Doran B., Gatter G.J., Vukovic M. , Taliaferro F., Mead B.E., Guo Z., Wang J.P., Gras D., Plaisant M., Ansari M., Angelidis I., Adler H., Sucre J.M.S., Taylor C.J., Lin B., Waghray A., Mitsialis V., Dwyer D.F., Buchheit K.M., Boyce J.A., Barrett N.A., Laidlaw T.M., Carroll S.L., Colonna L., Tkachev V., Peterson C.W., Yu A., Zheng H.B., Gideon H.P., Winchell C.G., Lin P.L., Bingle C.D., Snapper S.B., Kropski J.A., Theis F.J., Schiller H.B., Zaragosi L.E., Barbry P., Leslie A., Kiem H.P., Flynn J.L., Fortune S.M., Berger B., Finberg R.W., Kean L.S., Garber M., Schmidt A.G., Lingwood D., Shalek A.K., Ordovas-Montanes J.
Cell 181:1016-1035.e19(2020) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY, INDUCTION BY ISR.
Manual assertion based on experiment ini
- Ref.8"Interferons and viruses induce a novel truncated ACE2 isoform and not the full-length SARS-CoV-2 receptor."
Onabajo O.O., Banday A.R., Stanifer M.L., Yan W., Obajemu A., Santer D.M., Florez-Vargas O., Piontkivska H., Vargas J.M., Ring T.J., Kee C., Doldan P., Tyrrell D.L., Mendoza J.L., Boulant S., Prokunina-Olsson L.
Nat. Genet. 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), INDUCTION BY IFN (ISOFORM 2), ALTERNATIVE SPLICING.
Manual assertion based on experiment ini
- Ref.8"Interferons and viruses induce a novel truncated ACE2 isoform and not the full-length SARS-CoV-2 receptor."
Onabajo O.O., Banday A.R., Stanifer M.L., Yan W., Obajemu A., Santer D.M., Florez-Vargas O., Piontkivska H., Vargas J.M., Ring T.J., Kee C., Doldan P., Tyrrell D.L., Mendoza J.L., Boulant S., Prokunina-Olsson L.
Nat. Genet. 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), INDUCTION BY IFN (ISOFORM 2), ALTERNATIVE SPLICING.
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 similarityManual assertion inferred from sequence similarity toi
4 PublicationsManual assertion based on experiment ini
- Ref.14"Interaction of ACE2 and integrin beta1 in failing human heart."
Lin Q., Keller R.S., Weaver B., Zisman L.S.
Biochim. Biophys. Acta 1689:175-178(2004) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 679-689, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ITGB1. - Ref.34"A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry."
Shulla A., Heald-Sargent T., Subramanya G., Zhao J., Perlman S., Gallagher T.
J. Virol. 85:873-882(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, INTERACTION WITH TMPRSS2. - Ref.44"The Integrin Binding Peptide, ATN-161, as a Novel Therapy for SARS-CoV-2 Infection."
Beddingfield B.J., Iwanaga N., Chapagain P.P., Zheng W., Roy C.J., Hu T.Y., Kolls J.K., Bix G.J.
JACC Basic Transl. Sci. 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ITGA5:ITGB1, INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL INFECTION). - Ref.59"Structural basis for the recognition of the SARS-CoV-2 by full-length human ACE2."
Yan R., Zhang Y., Li Y., Xia L., Guo Y., Zhou Q.
Science 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 18-805, INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), INTERACTION WITH SLC6A19, SUBUNIT, PROTEOLYTIC CLEAVAGE.
(Microbial infection) Interacts with SARS coronavirus/SARS-CoV spike protein.
4 PublicationsManual assertion based on experiment ini
- Ref.19"Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus."
Li W., Moore M.J., Vasilieva N., Sui J., Wong S.-K., Berne M.A., Somasundaran M., Sullivan J.L., Luzuriaga K., Greenough T.C., Choe H., Farzan M.
Nature 426:450-454(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.22"Efficient replication of severe acute respiratory syndrome coronavirus in mouse cells is limited by murine angiotensin-converting enzyme 2."
Li W., Greenough T.C., Moore M.J., Vasilieva N., Somasundaran M., Sullivan J.L., Farzan M., Choe H.
J. Virol. 78:11429-11433(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN (MICROBIAL INFECTION). - Ref.25"Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2."
Li W., Zhang C., Sui J., Kuhn J.H., Moore M.J., Luo S., Wong S.-K., Huang I.-C., Xu K., Vasilieva N., Murakami A., He Y., Marasco W.A., Guan Y., Choe H., Farzan M.
EMBO J. 24:1634-1643(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), MUTAGENESIS. - Ref.58"Structural basis of receptor recognition by SARS-CoV-2."
Shang J., Ye G., Shi K., Wan Y., Luo C., Aihara H., Geng Q., Auerbach A., Li F.
Nature 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 19-615 AND IN COMPLEX WITH SARS-COV-2 SPIKE GLYCOPROTEIN, INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), FUNCTION (MICROBIAL INFECTION).
(Microbial infection) Interacts with SARS coronavirus-2/SARS-CoV-2 spike protein.
6 PublicationsManual assertion based on experiment ini
- Ref.39"Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation."
Wrapp D., Wang N., Corbett K.S., Goldsmith J.A., Hsieh C.L., Abiona O., Graham B.S., McLellan J.S.
Science 367:1260-1263(2020) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL INFECTION). - Ref.40"Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein."
Walls A.C., Park Y.J., Tortorici M.A., Wall A., McGuire A.T., Veesler D.
Cell 180:1-12(2020) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL INFECTION). - Ref.44"The Integrin Binding Peptide, ATN-161, as a Novel Therapy for SARS-CoV-2 Infection."
Beddingfield B.J., Iwanaga N., Chapagain P.P., Zheng W., Roy C.J., Hu T.Y., Kolls J.K., Bix G.J.
JACC Basic Transl. Sci. 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ITGA5:ITGB1, INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL INFECTION). - Ref.50"Engineering human ACE2 to optimize binding to the spike protein of SARS coronavirus 2."
Chan K.K., Dorosky D., Sharma P., Abbasi S.A., Dye J.M., Kranz D.M., Herbert A.S., Procko E.
Science 369:1261-1265(2020) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), MUTAGENESIS OF SER-19; GLN-24; ALA-25; THR-27; LEU-29; LYS-31; ASN-33; HIS-34; LEU-39; PHE-40; TYR-41; GLN-42; TRP-69; PHE-72; GLU-75; GLN-76; LEU-79; GLN-89; ASN-90; LEU-91; THR-92; THR-324; GLN-325; ASN-330; LEU-351; ALA-386; PRO-389; ARG-393 AND ARG-518, BIOTECHNOLOGY. - Ref.58"Structural basis of receptor recognition by SARS-CoV-2."
Shang J., Ye G., Shi K., Wan Y., Luo C., Aihara H., Geng Q., Auerbach A., Li F.
Nature 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 19-615 AND IN COMPLEX WITH SARS-COV-2 SPIKE GLYCOPROTEIN, INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), FUNCTION (MICROBIAL INFECTION). - Ref.59"Structural basis for the recognition of the SARS-CoV-2 by full-length human ACE2."
Yan R., Zhang Y., Li Y., Xia L., Guo Y., Zhou Q.
Science 0:0-0(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 18-805, INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL INFECTION), INTERACTION WITH SLC6A19, SUBUNIT, PROTEOLYTIC CLEAVAGE.
(Microbial infection) Interacts with human coronavirus NL63/HCoV-NL63 spike glycoprotein.
1 PublicationManual assertion based on experiment ini
- Ref.27"Human coronavirus NL63 employs the severe acute respiratory syndrome coronavirus receptor for cellular entry."
Hofmann H., Pyrc K., van der Hoek L., Geier M., Berkhout B., Poehlmann S.
Proc. Natl. Acad. Sci. U.S.A. 102:7988-7993(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HCOV-NL63 SPIKE GLYCOPROTEIN (MICROBIAL INFECTION).
<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
Show more detailsHide detailsQ9BYF1
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
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 23 – 52 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 30 | |
Helixi | 56 – 77 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 22 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 78 – 82 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 85 – 87 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 91 – 100 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
Helixi | 104 – 107 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 110 – 129 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 131 – 134 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 137 – 143 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Turni | 144 – 146 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 148 – 154 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 158 – 171 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
Helixi | 173 – 193 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 21 | |
Beta strandi | 196 – 198 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 199 – 204 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Turni | 205 – 207 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 213 – 215 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 220 – 251 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 32 | |
Turni | 253 – 255 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 258 – 260 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 264 – 266 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 267 – 271 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 276 – 278 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 279 – 282 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 284 – 287 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 294 – 297 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 298 – 300 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 304 – 316 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
Turni | 317 – 319 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 327 – 330 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 337 – 339 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 347 – 352 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 355 – 359 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 366 – 384 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
Turni | 385 – 387 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 390 – 392 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 396 – 399 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 400 – 413 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
Helixi | 415 – 420 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Turni | 422 – 426 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 432 – 446 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
Helixi | 449 – 465 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
Beta strandi | 466 – 468 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 470 – 472 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 473 – 483 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Beta strandi | 486 – 488 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 499 – 502 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 504 – 507 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 514 – 531 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
Turni | 532 – 534 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 539 – 541 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 548 – 558 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Turni | 559 – 562 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 566 – 574 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Beta strandi | 575 – 578 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 582 – 598 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
Beta strandi | 600 – 602 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 607 – 609 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 612 – 615 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 618 – 622 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 624 – 627 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 629 – 631 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 637 – 657 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 21 | |
Helixi | 667 – 669 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 670 – 673 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 677 – 686 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
Beta strandi | 690 – 694 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 697 – 706 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
Helixi | 708 – 715 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 719 – 724 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 741 – 766 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 26 |
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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>Regioni | 30 – 41 | Interaction with SARS-CoV spike glycoprotein1 Publication Manual assertion based on experiment ini
| 12 | |
Regioni | 82 – 84 | Interaction with SARS-CoV spike glycoprotein1 Publication Manual assertion based on experiment ini
| 3 | |
Regioni | 345 – 346 | Substrate binding1 Publication Manual assertion inferred by curator fromi
| 2 | |
Regioni | 353 – 357 | Interaction with SARS-CoV spike glycoprotein1 Publication Manual assertion based on experiment ini
| 5 | |
Regioni | 652 – 659 | Essential for cleavage by ADAM171 Publication Manual assertion based on experiment ini
| 8 | |
Regioni | 697 – 716 | Essential for cleavage by TMPRSS11D and TMPRSS21 Publication Manual assertion based on experiment ini
| 20 |
<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
Manual assertion based on experiment ini
- Ref.53"ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis."
Towler P., Staker B., Prasad S.G., Menon S., Tang J., Parsons T., Ryan D., Fisher M., Williams D., Dales N.A., Patane M.A., Pantoliano M.W.
J. Biol. Chem. 279:17996-18007(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-615 IN COMPLEXES WITH ZINC; CHLORIDE AND MLN-4760 INHIBITOR, DOMAIN, REACTION MECHANISM, ACTIVE SITE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-53; ASN-90; ASN-103; ASN-322; ASN-432 AND ASN-546.