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P12821

- ACE_HUMAN

UniProt

P12821 - ACE_HUMAN

Protein

Angiotensin-converting enzyme

Gene

ACE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 188 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    Functioni

    Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety.

    Catalytic activityi

    Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.

    Cofactori

    Binds 2 zinc ions per subunit. Isoform Testis-specific only binds 1 zinc ion per subunit.
    Binds 3 chloride ions per subunit.

    Enzyme regulationi

    Strongly activated by chloride. Specifically inhibited by lisinopril, captopril and enalaprilat.

    Kineticsi

    1. KM=2.51 mM for Hip-His-Leu2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei231 – 2311Chloride 1
    Metal bindingi390 – 3901Zinc 1; catalytic1 Publication
    Active sitei391 – 39111
    Metal bindingi394 – 3941Zinc 1; catalytic1 Publication
    Metal bindingi418 – 4181Zinc 1; catalytic1 Publication
    Binding sitei529 – 5291Chloride 1
    Binding sitei791 – 7911Chloride 2
    Binding sitei829 – 8291Chloride 3
    Metal bindingi988 – 9881Zinc 2; catalytic1 Publication
    Active sitei989 – 98912
    Metal bindingi992 – 9921Zinc 2; catalytic1 Publication
    Metal bindingi1016 – 10161Zinc 2; catalytic1 Publication
    Binding sitei1090 – 10901Chloride 2
    Binding sitei1094 – 10941Chloride 2
    Binding sitei1127 – 11271Chloride 3
    Sitei1225 – 12251Not glycosylated

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. bradykinin receptor binding Source: BHF-UCL
    3. carboxypeptidase activity Source: UniProtKB-KW
    4. chloride ion binding Source: BHF-UCL
    5. drug binding Source: BHF-UCL
    6. endopeptidase activity Source: UniProtKB
    7. metallopeptidase activity Source: UniProtKB
    8. peptidyl-dipeptidase activity Source: UniProtKB
    9. protein binding Source: UniProtKB
    10. zinc ion binding Source: BHF-UCL

    GO - Biological processi

    1. angiotensin catabolic process in blood Source: UniProtKB
    2. angiotensin maturation Source: Reactome
    3. arachidonic acid secretion Source: BHF-UCL
    4. blood vessel remodeling Source: BHF-UCL
    5. cellular protein metabolic process Source: Reactome
    6. hematopoietic stem cell differentiation Source: BHF-UCL
    7. hormone catabolic process Source: BHF-UCL
    8. kidney development Source: BHF-UCL
    9. mononuclear cell proliferation Source: BHF-UCL
    10. peptide catabolic process Source: BHF-UCL
    11. regulation of blood pressure Source: BHF-UCL
    12. regulation of renal output by angiotensin Source: BHF-UCL
    13. regulation of smooth muscle cell migration Source: BHF-UCL
    14. regulation of systemic arterial blood pressure by renin-angiotensin Source: UniProtKB
    15. regulation of vasoconstriction Source: UniProtKB
    16. regulation of vasodilation Source: BHF-UCL

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08412-MONOMER.
    BRENDAi3.4.15.1. 2681.
    ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.
    SABIO-RKP12821.
    SignaLinkiP12821.

    Protein family/group databases

    MEROPSiM02.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Angiotensin-converting enzyme (EC:3.2.1.-, EC:3.4.15.1)
    Short name:
    ACE
    Alternative name(s):
    Dipeptidyl carboxypeptidase I
    Kininase II
    CD_antigen: CD143
    Cleaved into the following chain:
    Gene namesi
    Name:ACE
    Synonyms:DCP, DCP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:2707. ACE.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Cytoplasm By similarity
    Note: Detected in both cell membrane and cytoplasm in neurons.By similarity

    GO - Cellular componenti

    1. endosome Source: BHF-UCL
    2. external side of plasma membrane Source: BHF-UCL
    3. extracellular region Source: Reactome
    4. extracellular space Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProtKB
    6. integral component of membrane Source: UniProtKB-KW
    7. plasma membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Renal tubular dysgenesis (RTD) [MIM:267430]: Autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Microvascular complications of diabetes 3 (MVCD3) [MIM:612624]: Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Intracerebral hemorrhage (ICH) [MIM:614519]: A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1299 – 12991S → A: Abolishes phosphorylation and decreases membrane retention. 1 Publication

    Organism-specific databases

    MIMi106180. gene+phenotype.
    267430. phenotype.
    601367. phenotype.
    612624. phenotype.
    614519. phenotype.
    Orphaneti97369. Renal tubular dysgenesis of genetic origin.
    PharmGKBiPA139.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 29291 PublicationAdd
    BLAST
    Chaini30 – 13061277Angiotensin-converting enzymePRO_0000028530Add
    BLAST
    Chaini30 – 12321203Angiotensin-converting enzyme, soluble formPRO_0000028531Add
    BLAST
    Propeptidei1233 – 130674Removed in soluble formPRO_0000028532Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)1 Publication
    Glycosylationi54 – 541N-linked (GlcNAc...)2 Publications
    Glycosylationi74 – 741N-linked (GlcNAc...)1 Publication
    Glycosylationi111 – 1111N-linked (GlcNAc...)2 Publications
    Glycosylationi146 – 1461N-linked (GlcNAc...)2 Publications
    Disulfide bondi157 ↔ 1651 Publication
    Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi318 – 3181N-linked (GlcNAc...)1 Publication
    Glycosylationi445 – 4451N-linked (GlcNAc...)1 Publication
    Glycosylationi509 – 5091N-linked (GlcNAc...)3 Publications
    Glycosylationi677 – 6771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi695 – 6951N-linked (GlcNAc...) (complex)2 Publications
    Glycosylationi714 – 7141N-linked (GlcNAc...) (complex)3 Publications
    Disulfide bondi757 ↔ 7631 Publication
    Glycosylationi760 – 7601N-linked (GlcNAc...); partial1 Publication
    Glycosylationi942 – 9421N-linked (GlcNAc...); partial1 Publication
    Disulfide bondi957 ↔ 9751 Publication
    Disulfide bondi1143 ↔ 11551 Publication
    Glycosylationi1191 – 11911N-linked (GlcNAc...); partial1 Publication
    Modified residuei1299 – 12991Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by CK2 on Ser-1299; which allows membrane retention.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP12821.
    PaxDbiP12821.
    PeptideAtlasiP12821.
    PRIDEiP12821.

    PTM databases

    PhosphoSiteiP12821.

    Miscellaneous databases

    PMAP-CutDBP12821.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed, with highest levels in lung, kidney, heart, gastrointestinal system and prostate. Isoform Testis-specific is expressed in spermatocytes and adult testis.4 Publications

    Inductioni

    Up-regulated in failing heart.2 Publications

    Gene expression databases

    ArrayExpressiP12821.
    BgeeiP12821.
    CleanExiHS_ACE.
    GenevestigatoriP12821.

    Organism-specific databases

    HPAiCAB002426.
    CAB002921.
    HPA029298.

    Interactioni

    Protein-protein interaction databases

    BioGridi108004. 7 interactions.
    MINTiMINT-127316.
    STRINGi9606.ENSP00000290866.

    Structurei

    Secondary structure

    1
    1306
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi32 – 343
    Helixi43 – 7230
    Helixi77 – 10529
    Turni106 – 1083
    Helixi109 – 1113
    Helixi115 – 12410
    Helixi128 – 1314
    Helixi134 – 15320
    Beta strandi155 – 1573
    Beta strandi159 – 1613
    Beta strandi165 – 1673
    Turni168 – 1703
    Helixi171 – 1788
    Helixi182 – 21736
    Helixi223 – 2297
    Helixi236 – 26631
    Turni268 – 2703
    Beta strandi281 – 2844
    Helixi291 – 2933
    Helixi294 – 2974
    Helixi309 – 3157
    Helixi319 – 33214
    Helixi340 – 3456
    Beta strandi352 – 3543
    Beta strandi362 – 3654
    Beta strandi367 – 3704
    Beta strandi372 – 3754
    Helixi382 – 40120
    Helixi406 – 4083
    Helixi414 – 42815
    Helixi431 – 4366
    Helixi447 – 46115
    Helixi464 – 47916
    Helixi485 – 4873
    Helixi488 – 50013
    Helixi514 – 5174
    Turni519 – 5246
    Helixi528 – 54720
    Helixi554 – 5563
    Helixi563 – 57513
    Helixi581 – 5899
    Helixi597 – 61620
    Turni634 – 6374
    Helixi646 – 67530
    Helixi680 – 70425
    Helixi709 – 7113
    Helixi715 – 72410
    Helixi728 – 7314
    Helixi734 – 75320
    Beta strandi755 – 7573
    Beta strandi759 – 7613
    Beta strandi763 – 7653
    Turni766 – 7683
    Helixi769 – 7768
    Helixi780 – 79314
    Helixi795 – 7995
    Helixi802 – 81514
    Helixi821 – 8277
    Helixi834 – 84411
    Helixi846 – 86419
    Helixi866 – 8683
    Beta strandi879 – 8824
    Helixi889 – 8913
    Helixi892 – 8954
    Helixi906 – 9127
    Helixi917 – 93014
    Helixi938 – 9436
    Beta strandi945 – 9473
    Beta strandi950 – 9523
    Beta strandi960 – 9634
    Beta strandi965 – 9684
    Beta strandi970 – 9734
    Helixi980 – 99819
    Turni999 – 10013
    Helixi1004 – 10063
    Helixi1012 – 102615
    Helixi1029 – 10346
    Helixi1045 – 107733
    Turni1083 – 10853
    Helixi1086 – 109813
    Helixi1112 – 11154
    Turni1117 – 11226
    Helixi1126 – 114520
    Helixi1152 – 11543
    Helixi1161 – 117111
    Turni1172 – 11754
    Helixi1179 – 11879
    Beta strandi1188 – 11914
    Helixi1195 – 121521

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1O86X-ray2.00A642-1230[»]
    1O8AX-ray2.00A642-1230[»]
    1UZEX-ray1.82A642-1230[»]
    1UZFX-ray2.00A642-1230[»]
    2C6FX-ray3.01A/B30-641[»]
    2C6NX-ray3.00A/B30-641[»]
    2IULX-ray2.01A642-1232[»]
    2IUXX-ray2.80A642-1232[»]
    2OC2X-ray2.25A642-1232[»]
    2XY9X-ray1.97A645-1228[»]
    2XYDX-ray2.15A/B30-639[»]
    2YDMX-ray2.44A642-1230[»]
    3BKKX-ray2.17A642-1232[»]
    3BKLX-ray2.18A642-1232[»]
    3L3NX-ray2.30A642-1232[»]
    3NXQX-ray1.99A/B30-658[»]
    4APHX-ray1.99A642-1230[»]
    4APJX-ray2.60A642-1230[»]
    4BXKX-ray2.20A/B30-657[»]
    4BZRX-ray1.84A642-1230[»]
    4BZSX-ray2.10A/B30-657[»]
    4C2NX-ray2.59A642-1230[»]
    4C2OX-ray1.80A642-1230[»]
    4C2PX-ray1.99A642-1230[»]
    4C2QX-ray2.40A642-1230[»]
    4C2RX-ray2.30A642-1230[»]
    4CA5X-ray1.85A642-1230[»]
    4CA6X-ray1.91A/B30-639[»]
    ProteinModelPortaliP12821.
    SMRiP12821. Positions 30-641, 645-1230.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12821.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini30 – 12561227ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1278 – 130629CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1257 – 127721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 630601Peptidase M2 1Add
    BLAST
    Regioni631 – 1232602Peptidase M2 2Add
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M2 family.Curated

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG71044.
    HOGENOMiHOG000292210.
    HOVERGENiHBG000264.
    InParanoidiP12821.
    KOiK01283.
    OMAiMEINESF.
    OrthoDBiEOG76HQ13.
    PhylomeDBiP12821.
    TreeFamiTF312861.

    Family and domain databases

    InterProiIPR001548. Peptidase_M2.
    [Graphical view]
    PANTHERiPTHR10514. PTHR10514. 1 hit.
    PfamiPF01401. Peptidase_M2. 2 hits.
    [Graphical view]
    PRINTSiPR00791. PEPDIPTASEA.
    PROSITEiPS00142. ZINC_PROTEASE. 2 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform Somatic-1 (identifier: P12821-1) [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

    MGAASGRRGP GLLLPLPLLL LLPPQPALAL DPGLQPGNFS ADEAGAQLFA     50
    QSYNSSAEQV LFQSVAASWA HDTNITAENA RRQEEAALLS QEFAEAWGQK 100
    AKELYEPIWQ NFTDPQLRRI IGAVRTLGSA NLPLAKRQQY NALLSNMSRI 150
    YSTAKVCLPN KTATCWSLDP DLTNILASSR SYAMLLFAWE GWHNAAGIPL 200
    KPLYEDFTAL SNEAYKQDGF TDTGAYWRSW YNSPTFEDDL EHLYQQLEPL 250
    YLNLHAFVRR ALHRRYGDRY INLRGPIPAH LLGDMWAQSW ENIYDMVVPF 300
    PDKPNLDVTS TMLQQGWNAT HMFRVAEEFF TSLELSPMPP EFWEGSMLEK 350
    PADGREVVCH ASAWDFYNRK DFRIKQCTRV TMDQLSTVHH EMGHIQYYLQ 400
    YKDLPVSLRR GANPGFHEAI GDVLALSVST PEHLHKIGLL DRVTNDTESD 450
    INYLLKMALE KIAFLPFGYL VDQWRWGVFS GRTPPSRYNF DWWYLRTKYQ 500
    GICPPVTRNE THFDAGAKFH VPNVTPYIRY FVSFVLQFQF HEALCKEAGY 550
    EGPLHQCDIY RSTKAGAKLR KVLQAGSSRP WQEVLKDMVG LDALDAQPLL 600
    KYFQPVTQWL QEQNQQNGEV LGWPEYQWHP PLPDNYPEGI DLVTDEAEAS 650
    KFVEEYDRTS QVVWNEYAEA NWNYNTNITT ETSKILLQKN MQIANHTLKY 700
    GTQARKFDVN QLQNTTIKRI IKKVQDLERA ALPAQELEEY NKILLDMETT 750
    YSVATVCHPN GSCLQLEPDL TNVMATSRKY EDLLWAWEGW RDKAGRAILQ 800
    FYPKYVELIN QAARLNGYVD AGDSWRSMYE TPSLEQDLER LFQELQPLYL 850
    NLHAYVRRAL HRHYGAQHIN LEGPIPAHLL GNMWAQTWSN IYDLVVPFPS 900
    APSMDTTEAM LKQGWTPRRM FKEADDFFTS LGLLPVPPEF WNKSMLEKPT 950
    DGREVVCHAS AWDFYNGKDF RIKQCTTVNL EDLVVAHHEM GHIQYFMQYK 1000
    DLPVALREGA NPGFHEAIGD VLALSVSTPK HLHSLNLLSS EGGSDEHDIN 1050
    FLMKMALDKI AFIPFSYLVD QWRWRVFDGS ITKENYNQEW WSLRLKYQGL 1100
    CPPVPRTQGD FDPGAKFHIP SSVPYIRYFV SFIIQFQFHE ALCQAAGHTG 1150
    PLHKCDIYQS KEAGQRLATA MKLGFSRPWP EAMQLITGQP NMSASAMLSY 1200
    FKPLLDWLRT ENELHGEKLG WPQYNWTPNS ARSEGPLPDS GRVSFLGLDL 1250
    DAQQARVGQW LLLFLGIALL VATLGLSQRL FSIRHRSLHR HSHGPQFGSE 1300
    VELRHS 1306
    Length:1,306
    Mass (Da):149,715
    Last modified:October 1, 1989 - v1
    Checksum:i1B33BCA7301A26AA
    GO
    Isoform Somatic-2 (identifier: P12821-2) [UniParc]FASTAAdd to Basket

    Also known as: Soluble

    The sequence of this isoform differs from the canonical sequence as follows:
         1137-1145: QFHEALCQA → HPFSQHTAA
         1146-1306: Missing.

    Note: Incomplete sequence.

    Show »
    Length:1,145
    Mass (Da):131,659
    Checksum:iB7EED12CAB675583
    GO
    Isoform Testis-specific (identifier: P12821-3) [UniParc] [UniParc]FASTAAdd to Basket

    Also known as: ACE-T

    The sequence of this isoform differs from the canonical sequence as follows:
         1-574: Missing.
         575-641: AGSSRPWQEV...LPDNYPEGID → MGQGWATAGL...AHQTSAQSPN

    Show »
    Length:732
    Mass (Da):83,330
    Checksum:i80E0D19CFA642313
    GO
    Isoform 4 (identifier: P12821-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-641: MGAASGRRGP...LPDNYPEGID → MGQGWATAGL...AHQTSAQSPN
         1128-1168: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:691
    Mass (Da):78,694
    Checksum:iF31FE078F52FF0B2
    GO

    Sequence cautioni

    The sequence BAD92208.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351Q → E AA sequence (PubMed:2558109)Curated
    Sequence conflicti42 – 421D → R AA sequence (PubMed:2558109)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti154 – 1541A → T.
    Corresponds to variant rs13306087 [ dbSNP | Ensembl ].
    VAR_029139
    Natural varianti183 – 1831A → T.
    Corresponds to variant rs12720754 [ dbSNP | Ensembl ].
    VAR_029140
    Natural varianti244 – 2441Y → C.
    Corresponds to variant rs3730025 [ dbSNP | Ensembl ].
    VAR_023430
    Natural varianti260 – 2601R → C.
    Corresponds to variant rs4302 [ dbSNP | Ensembl ].
    VAR_054000
    Natural varianti260 – 2601R → L.
    Corresponds to variant rs4303 [ dbSNP | Ensembl ].
    VAR_054001
    Natural varianti261 – 2611A → S.1 Publication
    Corresponds to variant rs4303 [ dbSNP | Ensembl ].
    VAR_011707
    Natural varianti351 – 3511P → L.
    Corresponds to variant rs2229839 [ dbSNP | Ensembl ].
    VAR_023431
    Natural varianti354 – 3541G → R.1 Publication
    Corresponds to variant rs56394458 [ dbSNP | Ensembl ].
    VAR_035434
    Natural varianti379 – 3791R → Q.
    Corresponds to variant rs13306085 [ dbSNP | Ensembl ].
    VAR_029141
    Natural varianti524 – 5241V → A.
    Corresponds to variant rs12720746 [ dbSNP | Ensembl ].
    VAR_029142
    Natural varianti561 – 5611R → W.1 Publication
    Corresponds to variant rs4314 [ dbSNP | Ensembl ].
    VAR_011708
    Natural varianti592 – 5921D → G.
    Corresponds to variant rs12709426 [ dbSNP | Ensembl ].
    VAR_020053
    Natural varianti828 – 8281M → T.
    Corresponds to variant rs13306091 [ dbSNP | Ensembl ].
    VAR_034602
    Natural varianti916 – 9161T → M.
    Corresponds to variant rs3730043 [ dbSNP | Ensembl ].
    VAR_023432
    Natural varianti1018 – 10181I → T.1 Publication
    Corresponds to variant rs4976 [ dbSNP | Ensembl ].
    VAR_014189
    Natural varianti1051 – 10511F → V.1 Publication
    Corresponds to variant rs4977 [ dbSNP | Ensembl ].
    VAR_014190
    Natural varianti1187 – 11871T → M.
    Corresponds to variant rs12709442 [ dbSNP | Ensembl ].
    VAR_023433
    Natural varianti1228 – 12281P → L No effect on activity; increases secretion; rate of solubilization is 2.5-fold higher than wild-type. 2 Publications
    VAR_023434
    Natural varianti1279 – 12791R → Q.1 Publication
    Corresponds to variant rs4980 [ dbSNP | Ensembl ].
    VAR_014191
    Natural varianti1286 – 12861R → S.2 Publications
    Corresponds to variant rs4364 [ dbSNP | Ensembl ].
    VAR_011709
    Natural varianti1296 – 12961Q → P.1 Publication
    Corresponds to variant rs4981 [ dbSNP | Ensembl ].
    VAR_014192
    Isoform Testis-specific (identifier: P12821-3)
    Natural varianti32 – 321S → P.
    Corresponds to variant rs4317 [ dbSNP | Ensembl ].
    Natural varianti49 – 491S → G.
    Corresponds to variant rs4318 [ dbSNP | Ensembl ].

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 641641MGAAS…PEGID → MGQGWATAGLPSLLFLLLCY GHPLLVPSQEASQQVTVTHG TSSQATTSSQTTTHQATAHQ TSAQSPN in isoform 4. 1 PublicationVSP_054836Add
    BLAST
    Alternative sequencei1 – 574574Missing in isoform Testis-specific. 2 PublicationsVSP_035120Add
    BLAST
    Alternative sequencei575 – 64167AGSSR…PEGID → MGQGWATAGLPSLLFLLLCY GHPLLVPSQEASQQVTVTHG TSSQATTSSQTTTHQATAHQ TSAQSPN in isoform Testis-specific. 2 PublicationsVSP_035121Add
    BLAST
    Alternative sequencei1128 – 116841Missing in isoform 4. 1 PublicationVSP_054837Add
    BLAST
    Alternative sequencei1137 – 11459QFHEALCQA → HPFSQHTAA in isoform Somatic-2. 1 PublicationVSP_029932
    Alternative sequencei1146 – 1306161Missing in isoform Somatic-2. 1 PublicationVSP_029933Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04144 mRNA. Translation: AAA51684.1.
    M26657 mRNA. Translation: AAA60611.1.
    X16295 mRNA. Translation: CAA34362.1.
    AF118569 Genomic DNA. Translation: AAD28560.1.
    AY436326 Genomic DNA. Translation: AAR03504.1.
    AK301988 mRNA. Translation: BAG63395.1.
    EU332840 Genomic DNA. Translation: ABY87529.1.
    AB208971 mRNA. Translation: BAD92208.1. Different initiation.
    AC113554 Genomic DNA. No translation available.
    CCDSiCCDS11637.1. [P12821-1]
    CCDS45755.1. [P12821-3]
    CCDS54155.1. [P12821-4]
    PIRiA31759.
    PW0053.
    S05238.
    RefSeqiNP_000780.1. NM_000789.3. [P12821-1]
    NP_001171528.1. NM_001178057.1. [P12821-4]
    NP_690043.1. NM_152830.2. [P12821-3]
    UniGeneiHs.298469.

    Genome annotation databases

    EnsembliENST00000290863; ENSP00000290863; ENSG00000159640. [P12821-3]
    ENST00000290866; ENSP00000290866; ENSG00000159640. [P12821-1]
    ENST00000413513; ENSP00000392247; ENSG00000159640. [P12821-4]
    ENST00000428043; ENSP00000397593; ENSG00000159640. [P12821-2]
    GeneIDi1636.
    KEGGihsa:1636.
    UCSCiuc002jau.2. human. [P12821-1]
    uc002jav.2. human. [P12821-3]

    Polymorphism databases

    DMDMi113045.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04144 mRNA. Translation: AAA51684.1 .
    M26657 mRNA. Translation: AAA60611.1 .
    X16295 mRNA. Translation: CAA34362.1 .
    AF118569 Genomic DNA. Translation: AAD28560.1 .
    AY436326 Genomic DNA. Translation: AAR03504.1 .
    AK301988 mRNA. Translation: BAG63395.1 .
    EU332840 Genomic DNA. Translation: ABY87529.1 .
    AB208971 mRNA. Translation: BAD92208.1 . Different initiation.
    AC113554 Genomic DNA. No translation available.
    CCDSi CCDS11637.1. [P12821-1 ]
    CCDS45755.1. [P12821-3 ]
    CCDS54155.1. [P12821-4 ]
    PIRi A31759.
    PW0053.
    S05238.
    RefSeqi NP_000780.1. NM_000789.3. [P12821-1 ]
    NP_001171528.1. NM_001178057.1. [P12821-4 ]
    NP_690043.1. NM_152830.2. [P12821-3 ]
    UniGenei Hs.298469.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1O86 X-ray 2.00 A 642-1230 [» ]
    1O8A X-ray 2.00 A 642-1230 [» ]
    1UZE X-ray 1.82 A 642-1230 [» ]
    1UZF X-ray 2.00 A 642-1230 [» ]
    2C6F X-ray 3.01 A/B 30-641 [» ]
    2C6N X-ray 3.00 A/B 30-641 [» ]
    2IUL X-ray 2.01 A 642-1232 [» ]
    2IUX X-ray 2.80 A 642-1232 [» ]
    2OC2 X-ray 2.25 A 642-1232 [» ]
    2XY9 X-ray 1.97 A 645-1228 [» ]
    2XYD X-ray 2.15 A/B 30-639 [» ]
    2YDM X-ray 2.44 A 642-1230 [» ]
    3BKK X-ray 2.17 A 642-1232 [» ]
    3BKL X-ray 2.18 A 642-1232 [» ]
    3L3N X-ray 2.30 A 642-1232 [» ]
    3NXQ X-ray 1.99 A/B 30-658 [» ]
    4APH X-ray 1.99 A 642-1230 [» ]
    4APJ X-ray 2.60 A 642-1230 [» ]
    4BXK X-ray 2.20 A/B 30-657 [» ]
    4BZR X-ray 1.84 A 642-1230 [» ]
    4BZS X-ray 2.10 A/B 30-657 [» ]
    4C2N X-ray 2.59 A 642-1230 [» ]
    4C2O X-ray 1.80 A 642-1230 [» ]
    4C2P X-ray 1.99 A 642-1230 [» ]
    4C2Q X-ray 2.40 A 642-1230 [» ]
    4C2R X-ray 2.30 A 642-1230 [» ]
    4CA5 X-ray 1.85 A 642-1230 [» ]
    4CA6 X-ray 1.91 A/B 30-639 [» ]
    ProteinModelPortali P12821.
    SMRi P12821. Positions 30-641, 645-1230.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108004. 7 interactions.
    MINTi MINT-127316.
    STRINGi 9606.ENSP00000290866.

    Chemistry

    BindingDBi P12821.
    ChEMBLi CHEMBL1808.
    DrugBanki DB00542. Benazepril.
    DB01197. Captopril.
    DB01089. Deserpidine.
    DB00584. Enalapril.
    DB00492. Fosinopril.
    DB00722. Lisinopril.
    DB00691. Moexipril.
    DB00790. Perindopril.
    DB00881. Quinapril.
    DB00178. Ramipril.
    DB01180. Rescinnamine.
    DB01348. Spirapril.
    DB00519. Trandolapril.
    GuidetoPHARMACOLOGYi 1613.

    Protein family/group databases

    MEROPSi M02.001.

    PTM databases

    PhosphoSitei P12821.

    Polymorphism databases

    DMDMi 113045.

    Proteomic databases

    MaxQBi P12821.
    PaxDbi P12821.
    PeptideAtlasi P12821.
    PRIDEi P12821.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290863 ; ENSP00000290863 ; ENSG00000159640 . [P12821-3 ]
    ENST00000290866 ; ENSP00000290866 ; ENSG00000159640 . [P12821-1 ]
    ENST00000413513 ; ENSP00000392247 ; ENSG00000159640 . [P12821-4 ]
    ENST00000428043 ; ENSP00000397593 ; ENSG00000159640 . [P12821-2 ]
    GeneIDi 1636.
    KEGGi hsa:1636.
    UCSCi uc002jau.2. human. [P12821-1 ]
    uc002jav.2. human. [P12821-3 ]

    Organism-specific databases

    CTDi 1636.
    GeneCardsi GC17P061554.
    HGNCi HGNC:2707. ACE.
    HPAi CAB002426.
    CAB002921.
    HPA029298.
    MIMi 106180. gene+phenotype.
    267430. phenotype.
    601367. phenotype.
    612624. phenotype.
    614519. phenotype.
    neXtProti NX_P12821.
    Orphaneti 97369. Renal tubular dysgenesis of genetic origin.
    PharmGKBi PA139.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG71044.
    HOGENOMi HOG000292210.
    HOVERGENi HBG000264.
    InParanoidi P12821.
    KOi K01283.
    OMAi MEINESF.
    OrthoDBi EOG76HQ13.
    PhylomeDBi P12821.
    TreeFami TF312861.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS08412-MONOMER.
    BRENDAi 3.4.15.1. 2681.
    Reactomei REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
    SABIO-RK P12821.
    SignaLinki P12821.

    Miscellaneous databases

    EvolutionaryTracei P12821.
    GeneWikii Angiotensin-converting_enzyme.
    GenomeRNAii 1636.
    NextBioi 6722.
    PMAP-CutDB P12821.
    PROi P12821.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P12821.
    Bgeei P12821.
    CleanExi HS_ACE.
    Genevestigatori P12821.

    Family and domain databases

    InterProi IPR001548. Peptidase_M2.
    [Graphical view ]
    PANTHERi PTHR10514. PTHR10514. 1 hit.
    Pfami PF01401. Peptidase_M2. 2 hits.
    [Graphical view ]
    PRINTSi PR00791. PEPDIPTASEA.
    PROSITEi PS00142. ZINC_PROTEASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning."
      Soubrier F., Alhenc-Gelas F., Hubert C., Allegrini J., John M., Tregear G., Corbol P.
      Proc. Natl. Acad. Sci. U.S.A. 85:9386-9390(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC-1).
    2. "The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, non-duplicated form of the enzyme."
      Lattion A.L., Soubrier F., Allegrini J., Hubert C., Corvol P., Alhenc-Gelas F.
      FEBS Lett. 252:99-104(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC).
    3. "Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme."
      Ehlers M.R.W., Fox E.A., Strydom D.J., Riordan J.F.
      Proc. Natl. Acad. Sci. U.S.A. 86:7741-7745(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC).
    4. "Sequence variation in the human angiotensin converting enzyme."
      Rieder M.J., Taylor S.L., Clark A.G., Nickerson D.A.
      Nat. Genet. 22:59-62(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-261; TRP-561 AND SER-1286.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Testis.
    6. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1239 (ISOFORM SOMATIC-1).
      Tissue: Brain.
    8. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "Purification of human lung angiotensin-converting enzyme by high-performance liquid chromatography: properties and N-terminal amino acid sequence."
      Takeuchi K., Shimizu T., Ohishi N., Seyama Y., Takaku F., Yotsumoto H.
      J. Biochem. 106:442-445(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 30-46.
      Tissue: Lung.
    10. "Alternative splicing of the mRNA coding for the human endothelial angiotensin-converting enzyme: a new mechanism for solubilization."
      Sugimura K., Tian X.-L., Hoffmann S., Ganten D., Bader M.
      Biochem. Biophys. Res. Commun. 247:466-472(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1114-1306 (ISOFORM SOMATIC-2), ALTERNATIVE SPLICING.
      Tissue: Umbilical vein endothelial cell.
    11. "Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes."
      Ehlers M.R.W., Riordan J.F.
      Biochemistry 30:7118-7126(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: ZINC-BINDING.
    12. "Assignment of free and disulfide-bonded cysteine residues in testis angiotensin-converting enzyme: functional implications."
      Sturrock E.D., Yu X.C., Wu Z., Biemann K., Riordan J.F.
      Biochemistry 35:9560-9566(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    13. "Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form."
      Yu X.C., Sturrock E.D., Wu Z., Biemann K., Ehlers M.R.W., Riordan J.F.
      J. Biol. Chem. 272:3511-3519(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-38; ASN-54; ASN-111; ASN-146; ASN-509; ASN-695; ASN-714; ASN-760; ASN-942 AND ASN-1191, IDENTIFICATION BY MASS SPECTROMETRY.
    14. "Shedding of somatic angiotensin-converting enzyme (ACE) is inefficient compared with testis ACE despite cleavage at identical stalk sites."
      Woodman Z.L., Oppong S.Y., Cook S., Hooper N.M., Schwager S.L.U., Brandt W.F., Ehlers M.R.W., Sturrock E.D.
      Biochem. J. 347:711-718(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE SITE, IDENTIFICATION BY MASS SPECTROMETRY.
    15. "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: TISSUE SPECIFICITY.
    16. "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: TISSUE SPECIFICITY.
    17. "Increased shedding of angiotensin-converting enzyme by a mutation identified in the stalk region."
      Eyries M., Michaud A., Deinum J., Agrapart M., Chomilier J., Kramers C., Soubrier F.
      J. Biol. Chem. 276:5525-5532(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANT LEU-1228.
    18. "CK2 phosphorylates the angiotensin-converting enzyme and regulates its retention in the endothelial cell plasma membrane."
      Kohlstedt K., Shoghi F., Mueller-Esterl W., Busse R., Fleming I.
      Circ. Res. 91:749-756(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-1299, MUTAGENESIS OF SER-1299.
    19. "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.
    20. "Deglycosylation, processing and crystallization of human testis angiotensin-converting enzyme."
      Gordon K., Redelinghuys P., Schwager S.L.U., Ehlers M.R.W., Papageorgiou A.C., Natesh R., Acharya K.R., Sturrock E.D.
      Biochem. J. 371:437-442(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CLEAVAGE SITE.
    21. "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.
    22. Cited for: TISSUE SPECIFICITY, INDUCTION.
    23. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-509; ASN-695 AND ASN-714.
      Tissue: Plasma.
    24. "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-111; ASN-445 AND ASN-714.
      Tissue: Liver.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "Crystal structure of the human angiotensin-converting enzyme-lisinopril complex."
      Natesh R., Schwager S.L.U., Sturrock E.D., Acharya K.R.
      Nature 421:551-554(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 642-1230, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 642-1230 IN COMPLEX WITH LISINOPRIL.
    27. "Structural details on the binding of antihypertensive drugs captopril and enalaprilat to human testicular angiotensin I-converting enzyme."
      Natesh R., Schwager S.L.U., Evans H.R., Sturrock E.D., Acharya K.R.
      Biochemistry 43:8718-8724(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 642-1230 IN COMPLEX WITH ENALAPRILAT, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 642-1230 IN COMPLEX WITH CAPTOPRIL.
    28. "Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design."
      Corradi H.R., Schwager S.L.U., Nchinda A.T., Sturrock E.D., Acharya K.R.
      J. Mol. Biol. 357:964-974(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 30-641 IN COMPLEX WITH LISINOPRIL; ZINC AND CHLORIDE IONS, GLYCOSYLATION AT ASN-54; ASN-74; ASN-146; ASN-318 AND ASN-509.
    29. "The DD genotype of the ACE gene polymorphism is associated with progression of diabetic nephropathy to end stage renal failure in IDDM."
      Vleming L.J., van der Pijl J.W., Lemkes H.H.P.J., Westendorp R.G.J., Maassen J.A., Daha M.R., van Es L.A., van Kooten C.
      Clin. Nephrol. 51:133-140(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN DIABETIC NEPHROPATHY SUSCEPTIBILITY.
    30. "Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis."
      Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A.
      Nat. Genet. 22:239-247(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS THR-1018; VAL-1051; GLN-1279; SER-1286 AND PRO-1296.
    31. "Point mutation in the stalk of angiotensin-converting enzyme causes a dramatic increase in serum angiotensin-converting enzyme but no cardiovascular disease."
      Kramers C., Danilov S.M., Deinum J., Balyasnikova I.V., Scharenborg N., Looman M., Boomsma F., de Keijzer M.H., van Duijn C., Martin S., Soubrier F., Adema G.J.
      Circulation 104:1236-1240(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LEU-1228, ASSOCIATION WITH BENIGN SERUM INCREASE OF ANGIOTENSIN-CONVERTING ENZYME.
    32. "Hereditary elevation of angiotensin converting enzyme suggesting neurosarcoidosis."
      Linnebank M., Kesper K., Jeub M., Urbach H., Wuellner U., Klockgether T., Schmidt S.
      Neurology 61:1819-1820(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LEU-1228, ASSOCIATION WITH BENIGN SERUM INCREASE OF ANGIOTENSIN-CONVERTING ENZYME.
    33. "Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls."
      Casas J.P., Hingorani A.D., Bautista L.E., Sharma P.
      Arch. Neurol. 61:1652-1661(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ISCHSTR.
    34. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ICH.
    35. Cited for: INVOLVEMENT IN RTD, VARIANT ARG-354.

    Entry informationi

    Entry nameiACE_HUMAN
    AccessioniPrimary (citable) accession number: P12821
    Secondary accession number(s): B0LPF0
    , B4DXI3, E7EU16, P22966, Q53YX9, Q59GY8, Q7M4L4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 188 of the entry and version 1 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

    Miscellaneous

    Inhibitors of ACE are commonly used to treat hypertension and some types of renal and cardiac dysfunction.
    The glycosidase activity probably uses different active site residues than the metalloprotease activity.

    Keywords - Technical termi

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

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    7. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    8. Peptidase families
      Classification of peptidase families and list of entries
    9. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3