Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Angiotensin-converting enzyme 2

Gene

ACE2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. May be an important regulator of heart function.4 Publications
(Microbial infection) Acts as a receptor for SARS coronavirus/SARS-CoV and human coronavirus NL63/HCoV-NL63.4 Publications

Catalytic activityi

Angiotensin II + H2O = angiotensin-1-7 + L-phenylalanine.

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Activated by chloride and fluoride, but not bromide. Inhibited by MLN-4760, cFP_Leu, and EDTA, but not by the ACE inhibitors linosipril, captopril and enalaprilat.4 Publications

Kineticsi

  1. KM=6.9 µM for angiotensin I1 Publication
  2. KM=2 µM for angiotensin II1 Publication
  3. KM=6.8 µM for apelin-131 Publication
  4. KM=5.5 µM for dynorphin-131 Publication

    pH dependencei

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei169Chloride1
    Binding sitei273Substrate1
    Binding sitei345Substrate1
    Binding sitei346Substrate; via carbonyl oxygen1
    Binding sitei371Substrate1
    Metal bindingi374Zinc; catalytic1
    Active sitei3751
    Metal bindingi378Zinc; catalytic1
    Metal bindingi402Zinc; catalytic1
    Binding sitei477Chloride1
    Binding sitei481Chloride1
    Active sitei5051
    Binding sitei515Substrate1

    GO - Molecular functioni

    • carboxypeptidase activity Source: UniProtKB
    • endopeptidase activity Source: UniProtKB
    • glycoprotein binding Source: BHF-UCL
    • metallocarboxypeptidase activity Source: Reactome
    • virus receptor activity Source: UniProtKB
    • zinc ion binding Source: BHF-UCL

    GO - Biological processi

    • angiotensin catabolic process in blood Source: BHF-UCL
    • angiotensin maturation Source: Reactome
    • angiotensin-mediated drinking behavior Source: BHF-UCL
    • positive regulation of cardiac muscle contraction Source: Ensembl
    • positive regulation of gap junction assembly Source: BHF-UCL
    • positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
    • receptor biosynthetic process Source: BHF-UCL
    • receptor-mediated virion attachment to host cell Source: BHF-UCL
    • regulation of cardiac conduction Source: BHF-UCL
    • regulation of cell proliferation Source: BHF-UCL
    • regulation of cytokine production Source: BHF-UCL
    • regulation of inflammatory response Source: BHF-UCL
    • regulation of systemic arterial blood pressure by renin-angiotensin Source: BHF-UCL
    • regulation of vasoconstriction Source: BHF-UCL
    • regulation of vasodilation Source: BHF-UCL
    • tryptophan transport Source: Ensembl
    • viral entry into host cell Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Carboxypeptidase, Host cell receptor for virus entry, Hydrolase, Metalloprotease, Protease, Receptor

    Keywords - Biological processi

    Host-virus interaction

    Keywords - Ligandi

    Chloride, Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.4.15.1. 2681.
    3.4.17.23. 2681.
    ReactomeiR-HSA-2022377. Metabolism of Angiotensinogen to Angiotensins.
    SABIO-RKQ9BYF1.

    Protein family/group databases

    MEROPSiM02.006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Angiotensin-converting enzyme 2 (EC:3.4.17.23)
    Alternative name(s):
    ACE-related carboxypeptidase
    Angiotensin-converting enzyme homolog
    Short name:
    ACEH
    Metalloprotease MPROT15
    Cleaved into the following chain:
    Gene namesi
    Name:ACE2
    ORF Names:UNQ868/PRO1885
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome X

    Organism-specific databases

    HGNCiHGNC:13557. ACE2.

    Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini18 – 740ExtracellularSequence analysisAdd BLAST723
    Transmembranei741 – 761HelicalSequence analysisAdd BLAST21
    Topological domaini762 – 805CytoplasmicSequence analysisAdd BLAST44

    GO - Cellular componenti

    • cell surface Source: UniProtKB
    • cytoplasm Source: UniProtKB-SubCell
    • extracellular exosome Source: UniProtKB
    • extracellular region Source: UniProtKB
    • extracellular space Source: BHF-UCL
    • integral component of membrane Source: UniProtKB-KW
    • membrane raft Source: BHF-UCL
    • plasma membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi24 – 26QAK → KAE: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication3
    Mutagenesisi31K → D: Abolishes interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi37E → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi38D → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi41Y → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi68K → D: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi82 – 84MYP → NFS: Inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication3
    Mutagenesisi110E → P: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi135 – 136PD → SM: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication2
    Mutagenesisi160E → R: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi192R → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi219R → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi239H → Q: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi309K → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi312E → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi324T → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi338 – 340NVQ → DDR: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication3
    Mutagenesisi350D → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi353K → H, A or D: Abolishes interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi355D → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi357R → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi359L → K or A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi383M → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi389P → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi393R → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi425 – 427SPD → PSN: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication3
    Mutagenesisi465 – 467KGE → QDK: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication3
    Mutagenesisi559R → S: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication1
    Mutagenesisi603F → T: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication1

    Organism-specific databases

    DisGeNETi59272.
    OpenTargetsiENSG00000130234.
    PharmGKBiPA425.

    Chemistry databases

    ChEMBLiCHEMBL3736.
    DrugBankiDB00722. Lisinopril.
    DB00691. Moexipril.
    GuidetoPHARMACOLOGYi1614.

    Polymorphism and mutation databases

    BioMutaiACE2.
    DMDMi71658783.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 17Sequence analysisAdd BLAST17
    ChainiPRO_000002857018 – 805Angiotensin-converting enzyme 2Add BLAST788
    ChainiPRO_000029226818 – 708Processed angiotensin-converting enzyme 2Add BLAST691

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi53N-linked (GlcNAc...)1 Publication1
    Glycosylationi90N-linked (GlcNAc...)2 Publications1
    Glycosylationi103N-linked (GlcNAc...)1 Publication1
    Disulfide bondi133 ↔ 1411 Publication
    Glycosylationi322N-linked (GlcNAc...)1 Publication1
    Disulfide bondi344 ↔ 3611 Publication
    Glycosylationi432N-linked (GlcNAc...)1 Publication1
    Disulfide bondi530 ↔ 5421 Publication
    Glycosylationi546N-linked (GlcNAc...)2 Publications1
    Glycosylationi690N-linked (GlcNAc...)Sequence analysis1

    Post-translational modificationi

    N-glycosylation on Asn-90 may limit SARS infectivity.5 Publications
    Proteolytic cleavage by ADAM17 generates a secreted form. Also cleaved by serine proteases: TMPRSS2, TMPRSS11D and HPN/TMPRSS1.4 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    EPDiQ9BYF1.
    PaxDbiQ9BYF1.
    PeptideAtlasiQ9BYF1.
    PRIDEiQ9BYF1.

    PTM databases

    iPTMnetiQ9BYF1.
    PhosphoSitePlusiQ9BYF1.

    Miscellaneous databases

    PMAP-CutDBQ9BYF1.

    Expressioni

    Tissue specificityi

    Expressed in endothelial cells from small and large arteries, and in arterial smooth muscle cells. Expressed in lung alveolar epithelial cells, enterocytes of the small intestine, Leydig cells and Sertoli cells (at protein level). Expressed in heart, kidney, testis, and gastrointestinal system.6 Publications

    Inductioni

    Up-regulated in failing heart.2 Publications

    Gene expression databases

    BgeeiENSG00000130234.
    CleanExiHS_ACE2.
    GenevisibleiQ9BYF1. HS.

    Organism-specific databases

    HPAiCAB026174.
    HPA000288.

    Interactioni

    Subunit structurei

    Interacts with ITGB1. Interacts with the catalytically active form of TMPRSS2.3 Publications
    (Microbial infection) Interacts with SARS coronavirus/SARS-CoV and human coronavirus NL63/HCoV-NL63 spike glycoprotein (PubMed:14647384, PubMed:15452268, PubMed:15791205, PubMed:15897467).4 Publications

    Protein-protein interaction databases

    BioGridi121864. 6 interactors.
    DIPiDIP-44689N.
    IntActiQ9BYF1. 1 interactor.
    MINTiMINT-4538816.
    STRINGi9606.ENSP00000252519.

    Chemistry databases

    BindingDBiQ9BYF1.

    Structurei

    Secondary structure

    1805
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi23 – 52Combined sources30
    Helixi56 – 77Combined sources22
    Turni78 – 82Combined sources5
    Helixi85 – 87Combined sources3
    Helixi91 – 100Combined sources10
    Helixi104 – 107Combined sources4
    Helixi110 – 129Combined sources20
    Beta strandi131 – 134Combined sources4
    Beta strandi137 – 143Combined sources7
    Turni144 – 146Combined sources3
    Helixi148 – 154Combined sources7
    Helixi158 – 171Combined sources14
    Helixi173 – 193Combined sources21
    Beta strandi196 – 198Combined sources3
    Helixi199 – 204Combined sources6
    Turni205 – 207Combined sources3
    Turni213 – 215Combined sources3
    Helixi220 – 251Combined sources32
    Turni253 – 255Combined sources3
    Beta strandi258 – 260Combined sources3
    Helixi264 – 266Combined sources3
    Beta strandi267 – 271Combined sources5
    Helixi276 – 278Combined sources3
    Helixi279 – 282Combined sources4
    Turni284 – 287Combined sources4
    Turni294 – 297Combined sources4
    Helixi298 – 300Combined sources3
    Helixi304 – 316Combined sources13
    Turni317 – 319Combined sources3
    Helixi327 – 330Combined sources4
    Beta strandi338 – 340Combined sources3
    Beta strandi347 – 352Combined sources6
    Beta strandi355 – 359Combined sources5
    Helixi366 – 384Combined sources19
    Turni385 – 387Combined sources3
    Helixi390 – 392Combined sources3
    Helixi400 – 413Combined sources14
    Helixi415 – 420Combined sources6
    Turni422 – 426Combined sources5
    Helixi432 – 446Combined sources15
    Helixi449 – 465Combined sources17
    Beta strandi466 – 468Combined sources3
    Helixi470 – 472Combined sources3
    Helixi473 – 483Combined sources11
    Beta strandi486 – 488Combined sources3
    Helixi499 – 502Combined sources4
    Helixi504 – 507Combined sources4
    Helixi514 – 531Combined sources18
    Turni532 – 534Combined sources3
    Helixi539 – 541Combined sources3
    Helixi548 – 558Combined sources11
    Turni559 – 562Combined sources4
    Helixi566 – 574Combined sources9
    Beta strandi575 – 578Combined sources4
    Helixi582 – 598Combined sources17
    Beta strandi600 – 602Combined sources3
    Beta strandi607 – 609Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1R42X-ray2.20A1-615[»]
    1R4LX-ray3.00A1-615[»]
    1XJPmodel-B19-615[»]
    2AJFX-ray2.90A/B19-615[»]
    3D0GX-ray2.80A/B56-615[»]
    3D0HX-ray3.10A/B56-615[»]
    3D0IX-ray2.90A/B56-615[»]
    3KBHX-ray3.31A/B/C/D19-615[»]
    3SCIX-ray2.90A/B19-615[»]
    3SCJX-ray3.00A/B19-615[»]
    3SCKX-ray3.00A/B83-615[»]
    3SCLX-ray3.00A/B83-615[»]
    ProteinModelPortaliQ9BYF1.
    SMRiQ9BYF1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BYF1.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni30 – 41Interaction with SARS-CoV spike glycoproteinAdd BLAST12
    Regioni82 – 84Interaction with SARS-CoV spike glycoprotein3
    Regioni353 – 357Interaction with SARS-CoV spike glycoprotein5
    Regioni652 – 659Essential for cleavage by ADAM178
    Regioni697 – 716Essential for cleavage by TMPRSS11D and TMPRSS2Add BLAST20

    Sequence similaritiesi

    Belongs to the peptidase M2 family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG3690. Eukaryota.
    ENOG410XPJ3. LUCA.
    GeneTreeiENSGT00520000055576.
    HOGENOMiHOG000292210.
    HOVERGENiHBG000265.
    InParanoidiQ9BYF1.
    KOiK09708.
    OMAiCNPNNPQ.
    OrthoDBiEOG091G033S.
    PhylomeDBiQ9BYF1.
    TreeFamiTF312861.

    Family and domain databases

    CDDicd06461. M2_ACE. 1 hit.
    InterProiIPR033591. ACE2.
    IPR031588. Collectrin_dom.
    IPR001548. Peptidase_M2.
    [Graphical view]
    PANTHERiPTHR10514. PTHR10514. 2 hits.
    PTHR10514:SF24. PTHR10514:SF24. 2 hits.
    PfamiPF16959. Collectrin. 1 hit.
    PF01401. Peptidase_M2. 1 hit.
    [Graphical view]
    PRINTSiPR00791. PEPDIPTASEA.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9BYF1-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

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

    VQTSF
    Length:805
    Mass (Da):92,463
    Last modified:August 2, 2005 - v2
    Checksum:i8EE6EB0A931550E8
    GO
    Isoform 2 (identifier: Q9BYF1-2) [UniParc]FASTAAdd to basket

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

    Note: No experimental confirmation available.
    Show »
    Length:555
    Mass (Da):63,912
    Checksum:i3A3842AB792E2DBC
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti18Q → H in CAB53682 (PubMed:17974005).Curated1
    Sequence conflicti508N → D in AAQ89076 (PubMed:12975309).Curated1
    Sequence conflicti631K → R in BAB40370 (Ref. 5) Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_02308226K → R.1 PublicationCorresponds to variant rs4646116dbSNPEnsembl.1
    Natural variantiVAR_023083638N → S.1 PublicationCorresponds to variant rs183135788dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_014901555F → L in isoform 2. 1 Publication1
    Alternative sequenceiVSP_014902556 – 805Missing in isoform 2. 1 PublicationAdd BLAST250

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF291820 mRNA. Translation: AAF99721.1.
    AF241254 mRNA. Translation: AAF78220.1.
    AY623811 mRNA. Translation: AAT45083.1.
    AB193259 mRNA. Translation: BAD99266.1.
    AB193260 mRNA. Translation: BAD99267.1.
    AB046569 mRNA. Translation: BAB40370.1.
    E39033 mRNA. No translation available.
    GQ262784 mRNA. Translation: ACT66268.1.
    AY358714 mRNA. Translation: AAQ89076.1.
    AY217547 Genomic DNA. Translation: AAO25651.1.
    CH471074 Genomic DNA. Translation: EAW98892.1.
    BC039902 mRNA. Translation: AAH39902.1.
    BC048094 mRNA. Translation: AAH48094.2.
    AL110224 mRNA. Translation: CAB53682.1.
    CCDSiCCDS14169.1. [Q9BYF1-1]
    PIRiT14762.
    RefSeqiNP_068576.1. NM_021804.2. [Q9BYF1-1]
    UniGeneiHs.178098.

    Genome annotation databases

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

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF291820 mRNA. Translation: AAF99721.1.
    AF241254 mRNA. Translation: AAF78220.1.
    AY623811 mRNA. Translation: AAT45083.1.
    AB193259 mRNA. Translation: BAD99266.1.
    AB193260 mRNA. Translation: BAD99267.1.
    AB046569 mRNA. Translation: BAB40370.1.
    E39033 mRNA. No translation available.
    GQ262784 mRNA. Translation: ACT66268.1.
    AY358714 mRNA. Translation: AAQ89076.1.
    AY217547 Genomic DNA. Translation: AAO25651.1.
    CH471074 Genomic DNA. Translation: EAW98892.1.
    BC039902 mRNA. Translation: AAH39902.1.
    BC048094 mRNA. Translation: AAH48094.2.
    AL110224 mRNA. Translation: CAB53682.1.
    CCDSiCCDS14169.1. [Q9BYF1-1]
    PIRiT14762.
    RefSeqiNP_068576.1. NM_021804.2. [Q9BYF1-1]
    UniGeneiHs.178098.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1R42X-ray2.20A1-615[»]
    1R4LX-ray3.00A1-615[»]
    1XJPmodel-B19-615[»]
    2AJFX-ray2.90A/B19-615[»]
    3D0GX-ray2.80A/B56-615[»]
    3D0HX-ray3.10A/B56-615[»]
    3D0IX-ray2.90A/B56-615[»]
    3KBHX-ray3.31A/B/C/D19-615[»]
    3SCIX-ray2.90A/B19-615[»]
    3SCJX-ray3.00A/B19-615[»]
    3SCKX-ray3.00A/B83-615[»]
    3SCLX-ray3.00A/B83-615[»]
    ProteinModelPortaliQ9BYF1.
    SMRiQ9BYF1.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi121864. 6 interactors.
    DIPiDIP-44689N.
    IntActiQ9BYF1. 1 interactor.
    MINTiMINT-4538816.
    STRINGi9606.ENSP00000252519.

    Chemistry databases

    BindingDBiQ9BYF1.
    ChEMBLiCHEMBL3736.
    DrugBankiDB00722. Lisinopril.
    DB00691. Moexipril.
    GuidetoPHARMACOLOGYi1614.

    Protein family/group databases

    MEROPSiM02.006.

    PTM databases

    iPTMnetiQ9BYF1.
    PhosphoSitePlusiQ9BYF1.

    Polymorphism and mutation databases

    BioMutaiACE2.
    DMDMi71658783.

    Proteomic databases

    EPDiQ9BYF1.
    PaxDbiQ9BYF1.
    PeptideAtlasiQ9BYF1.
    PRIDEiQ9BYF1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi59272.
    DisGeNETi59272.
    GeneCardsiACE2.
    HGNCiHGNC:13557. ACE2.
    HPAiCAB026174.
    HPA000288.
    MIMi300335. gene.
    neXtProtiNX_Q9BYF1.
    OpenTargetsiENSG00000130234.
    PharmGKBiPA425.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3690. Eukaryota.
    ENOG410XPJ3. LUCA.
    GeneTreeiENSGT00520000055576.
    HOGENOMiHOG000292210.
    HOVERGENiHBG000265.
    InParanoidiQ9BYF1.
    KOiK09708.
    OMAiCNPNNPQ.
    OrthoDBiEOG091G033S.
    PhylomeDBiQ9BYF1.
    TreeFamiTF312861.

    Enzyme and pathway databases

    BRENDAi3.4.15.1. 2681.
    3.4.17.23. 2681.
    ReactomeiR-HSA-2022377. Metabolism of Angiotensinogen to Angiotensins.
    SABIO-RKQ9BYF1.

    Miscellaneous databases

    ChiTaRSiACE2. human.
    EvolutionaryTraceiQ9BYF1.
    GeneWikiiAngiotensin-converting_enzyme_2.
    GenomeRNAii59272.
    PMAP-CutDBQ9BYF1.
    PROiQ9BYF1.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000130234.
    CleanExiHS_ACE2.
    GenevisibleiQ9BYF1. HS.

    Family and domain databases

    CDDicd06461. M2_ACE. 1 hit.
    InterProiIPR033591. ACE2.
    IPR031588. Collectrin_dom.
    IPR001548. Peptidase_M2.
    [Graphical view]
    PANTHERiPTHR10514. PTHR10514. 2 hits.
    PTHR10514:SF24. PTHR10514:SF24. 2 hits.
    PfamiPF16959. Collectrin. 1 hit.
    PF01401. Peptidase_M2. 1 hit.
    [Graphical view]
    PRINTSiPR00791. PEPDIPTASEA.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiACE2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BYF1
    Secondary accession number(s): C7ECU1
    , Q6UWP0, Q86WT0, Q9NRA7, Q9UFZ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 2, 2005
    Last sequence update: August 2, 2005
    Last modified: November 30, 2016
    This is version 153 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.