Skip Header

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

P12821

- ACE_HUMAN

UniProt

P12821 - ACE_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Angiotensin-converting enzyme

Gene

ACE

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

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP12821.
CleanExiHS_ACE.
ExpressionAtlasiP12821. baseline and differential.
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.
GeneTreeiENSGT00520000055576.
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

        10         20         30         40         50
MGAASGRRGP GLLLPLPLLL LLPPQPALAL DPGLQPGNFS ADEAGAQLFA
60 70 80 90 100
QSYNSSAEQV LFQSVAASWA HDTNITAENA RRQEEAALLS QEFAEAWGQK
110 120 130 140 150
AKELYEPIWQ NFTDPQLRRI IGAVRTLGSA NLPLAKRQQY NALLSNMSRI
160 170 180 190 200
YSTAKVCLPN KTATCWSLDP DLTNILASSR SYAMLLFAWE GWHNAAGIPL
210 220 230 240 250
KPLYEDFTAL SNEAYKQDGF TDTGAYWRSW YNSPTFEDDL EHLYQQLEPL
260 270 280 290 300
YLNLHAFVRR ALHRRYGDRY INLRGPIPAH LLGDMWAQSW ENIYDMVVPF
310 320 330 340 350
PDKPNLDVTS TMLQQGWNAT HMFRVAEEFF TSLELSPMPP EFWEGSMLEK
360 370 380 390 400
PADGREVVCH ASAWDFYNRK DFRIKQCTRV TMDQLSTVHH EMGHIQYYLQ
410 420 430 440 450
YKDLPVSLRR GANPGFHEAI GDVLALSVST PEHLHKIGLL DRVTNDTESD
460 470 480 490 500
INYLLKMALE KIAFLPFGYL VDQWRWGVFS GRTPPSRYNF DWWYLRTKYQ
510 520 530 540 550
GICPPVTRNE THFDAGAKFH VPNVTPYIRY FVSFVLQFQF HEALCKEAGY
560 570 580 590 600
EGPLHQCDIY RSTKAGAKLR KVLQAGSSRP WQEVLKDMVG LDALDAQPLL
610 620 630 640 650
KYFQPVTQWL QEQNQQNGEV LGWPEYQWHP PLPDNYPEGI DLVTDEAEAS
660 670 680 690 700
KFVEEYDRTS QVVWNEYAEA NWNYNTNITT ETSKILLQKN MQIANHTLKY
710 720 730 740 750
GTQARKFDVN QLQNTTIKRI IKKVQDLERA ALPAQELEEY NKILLDMETT
760 770 780 790 800
YSVATVCHPN GSCLQLEPDL TNVMATSRKY EDLLWAWEGW RDKAGRAILQ
810 820 830 840 850
FYPKYVELIN QAARLNGYVD AGDSWRSMYE TPSLEQDLER LFQELQPLYL
860 870 880 890 900
NLHAYVRRAL HRHYGAQHIN LEGPIPAHLL GNMWAQTWSN IYDLVVPFPS
910 920 930 940 950
APSMDTTEAM LKQGWTPRRM FKEADDFFTS LGLLPVPPEF WNKSMLEKPT
960 970 980 990 1000
DGREVVCHAS AWDFYNGKDF RIKQCTTVNL EDLVVAHHEM GHIQYFMQYK
1010 1020 1030 1040 1050
DLPVALREGA NPGFHEAIGD VLALSVSTPK HLHSLNLLSS EGGSDEHDIN
1060 1070 1080 1090 1100
FLMKMALDKI AFIPFSYLVD QWRWRVFDGS ITKENYNQEW WSLRLKYQGL
1110 1120 1130 1140 1150
CPPVPRTQGD FDPGAKFHIP SSVPYIRYFV SFIIQFQFHE ALCQAAGHTG
1160 1170 1180 1190 1200
PLHKCDIYQS KEAGQRLATA MKLGFSRPWP EAMQLITGQP NMSASAMLSY
1210 1220 1230 1240 1250
FKPLLDWLRT ENELHGEKLG WPQYNWTPNS ARSEGPLPDS GRVSFLGLDL
1260 1270 1280 1290 1300
DAQQARVGQW LLLFLGIALL VATLGLSQRL FSIRHRSLHR HSHGPQFGSE

VELRHS
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]
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.
DB00616. Candoxatril.
DB01197. Captopril.
DB01340. Cilazapril.
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 ]
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.
GeneTreei ENSGT00520000055576.
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

Bgeei P12821.
CleanExi HS_ACE.
ExpressionAtlasi P12821. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 189 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