HUMAN:ACE

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Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	ACE (synonyms: DCP, DCP1)
Protein Name(s)	Angiotensin-converting enzyme ACE Dipeptidyl carboxypeptidase I Kininase II Angiotensin-converting enzyme, soluble form
External Links
UniProt	P12821
EMBL	J04144 M26657 X16295 AF118569 AY436326 EU332840 AB208971
IPI	IPI00028147 IPI00437751 IPI00877100
PIR	A31759 PW0053 S05238
RefSeq	NP_000780.1 NP_001171528.1 NP_690043.1
UniGene	Hs.298469
PDB	1O86 1O8A 1UZE 1UZF 2C6F 2C6N 2IUL 2IUX 2OC2 2XY9 2XYD 2YDM 3BKK 3BKL 3L3N 3NXQ
PDBsum	1O86 1O8A 1UZE 1UZF 2C6F 2C6N 2IUL 2IUX 2OC2 2XY9 2XYD 2YDM 3BKK 3BKL 3L3N 3NXQ
ProteinModelPortal	P12821
SMR	P12821
STRING	P12821
MEROPS	M02.001
PhosphoSite	P12821
DMDM	113045
PeptideAtlas	P12821
PRIDE	P12821
Ensembl	ENST00000290866
GeneID	1636
KEGG	hsa:1636
UCSC	uc002jau.1
CTD	1636
GeneCards	GC17P061554
H-InvDB	HIX0027185
HGNC	HGNC:2707
HPA	CAB002426 CAB002921 HPA029298
MIM	106180 267430 601367 612624
neXtProt	NX_P12821
Orphanet	97369
eggNOG	prNOG16721
HOGENOM	HBG356536
HOVERGEN	HBG000264
InParanoid	P12821
OMA	EFWDKSM
OrthoDB	EOG495ZQZ
PhylomeDB	P12821
BioCyc	MetaCyc:HS08412-MONOMER
BRENDA	3.4.15.1
DrugBank	DB00542 DB01197 DB01089 DB00584 DB00492 DB00722 DB00691 DB00790 DB00881 DB00178 DB01180 DB01348 DB00519
NextBio	6722
PMAP-CutDB	P12821
ArrayExpress	P12821
Bgee	P12821
CleanEx	HS_ACE
Genevestigator	P12821
GermOnline	ENSG00000159640
GO	GO:0005768 GO:0009897 GO:0005615 GO:0016021 GO:0005624 GO:0005886 GO:0003779 GO:0031711 GO:0004180 GO:0031404 GO:0008144 GO:0008237 GO:0008241 GO:0008270 GO:0002005 GO:0050482 GO:0001974 GO:0060218 GO:0042447 GO:0001822 GO:0032943 GO:0043171 GO:0006508 GO:0002019 GO:0014910 GO:0019229 GO:0042312
InterPro	IPR001548
KO	K01283
PANTHER	PTHR10514
Pfam	PF01401
PRINTS	PR00791
PROSITE	PS00142

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0001666	response to hypoxia	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	P	Seeded From UniProt
	GO:0001822	kidney development	PMID:16116425^[1]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0001974	blood vessel remodeling	PMID:1668266^[2]	IC: Inferred by Curator	GO:0008241	P	Seeded From UniProt
	GO:0002005	angiotensin catabolic process in blood	PMID:1668266^[2]	IC: Inferred by Curator	GO:0008237	P	Seeded From UniProt
	GO:0002019	regulation of renal output by angiotensin	PMID:1668266^[2]	IC: Inferred by Curator	GO:0008241	P	Seeded From UniProt
	GO:0002446	neutrophil mediated immunity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000001963	P	Seeded From UniProt
	GO:0003081	regulation of systemic arterial blood pressure by renin-angiotensin	PMID:1668266^[2]	IC: Inferred by Curator	GO:0008237	P	Seeded From UniProt
	GO:0003779	actin binding	PMID:16186248^[3]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0004175	endopeptidase activity	PMID:15283675^[4]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0004180	carboxypeptidase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0121	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16186248^[3]	IPI: Inferred from Physical Interaction	UniProtKB:P35579	F	Seeded From UniProt
	GO:0005576	extracellular region	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0964	C	Seeded From UniProt
	GO:0005576	extracellular region	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0243	C	Seeded From UniProt
	GO:0005615	extracellular space	PMID:15283675^[4]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005615	extracellular space	PMID:1668266^[2]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005615	extracellular space	PMID:4322742^[5]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005624	membrane fraction	PMID:1668266^[2]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005624	membrane fraction	PMID:2849100^[6]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005768	endosome	PMID:17077303^[7]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005886	plasma membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-1003	C	Seeded From UniProt
	GO:0005886	plasma membrane	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	C	Seeded From UniProt
	GO:0005886	plasma membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0039	C	Seeded From UniProt
	GO:0005886	plasma membrane	PMID:16186248^[3]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005886	plasma membrane	PMID:17077303^[7]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0006508	proteolysis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001548	P	Seeded From UniProt
	GO:0006508	proteolysis	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0645	P	Seeded From UniProt
	GO:0006508	proteolysis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	P	Seeded From UniProt
	GO:0006518	peptide metabolic process	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	P	Seeded From UniProt
	GO:0008144	drug binding	PMID:1320019^[8]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0008217	regulation of blood pressure	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000001963	P	Seeded From UniProt
	GO:0008217	regulation of blood pressure	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	P	Seeded From UniProt
	GO:0008217	regulation of blood pressure	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P47820	P	Seeded From UniProt
	GO:0008217	regulation of blood pressure	PMID:11303049^[9]	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P09470	P	Seeded From UniProt
	GO:0008233	peptidase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0645	F	Seeded From UniProt
	GO:0008237	metallopeptidase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001548	F	Seeded From UniProt
	GO:0008237	metallopeptidase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0482	F	Seeded From UniProt
	GO:0008237	metallopeptidase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000001963	F	Seeded From UniProt
	GO:0008237	metallopeptidase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	F	Seeded From UniProt
	GO:0008237	metallopeptidase activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P09470	F	Seeded From UniProt
	GO:0008237	metallopeptidase activity	PMID:1320019^[8]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0008237	metallopeptidase activity	PMID:1668266^[2]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0008237	metallopeptidase activity	PMID:17077303^[7]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0008237	metallopeptidase activity	PMID:2849100^[6]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0008241	peptidyl-dipeptidase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001548	F	Seeded From UniProt
	GO:0008241	peptidyl-dipeptidase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000001963	F	Seeded From UniProt
	GO:0008241	peptidyl-dipeptidase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	F	Seeded From UniProt
	GO:0008241	peptidyl-dipeptidase activity	PMID:11303049^[9]	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P09470	F	Seeded From UniProt
	GO:0008241	peptidyl-dipeptidase activity	PMID:1320019^[8]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0008241	peptidyl-dipeptidase activity	PMID:1668266^[2]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0008241	peptidyl-dipeptidase activity	PMID:17077303^[7]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0008241	peptidyl-dipeptidase activity	PMID:2849100^[6]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0008270	zinc ion binding	PMID:12540854^[10]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0009897	external side of plasma membrane	PMID:9449382^[11]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0014910	regulation of smooth muscle cell migration	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	P	Seeded From UniProt
	GO:0014910	regulation of smooth muscle cell migration	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P47820	P	Seeded From UniProt
	GO:0016020	membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001548	C	Seeded From UniProt
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C	Seeded From UniProt
	GO:0016021	integral to membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0812	C	Seeded From UniProt
	GO:0016787	hydrolase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0378	F	Seeded From UniProt
	GO:0019229	regulation of vasoconstriction	PMID:1668266^[2]	IC: Inferred by Curator	GO:0008237	P	Seeded From UniProt
	GO:0019233	sensory perception of pain	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	P	Seeded From UniProt
	GO:0031404	chloride ion binding	PMID:12540854^[10]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0031667	response to nutrient levels	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	P	Seeded From UniProt
	GO:0031711	bradykinin receptor binding	PMID:17077303^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P30411	F	Seeded From UniProt
	GO:0032496	response to lipopolysaccharide	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	P	Seeded From UniProt
	GO:0032943	mononuclear cell proliferation	PMID:7876104^[12]	IC: Inferred by Curator	GO:0042447	P	Seeded From UniProt
	GO:0042277	peptide binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	F	Seeded From UniProt
	GO:0042310	vasoconstriction	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	P	Seeded From UniProt
	GO:0042312	regulation of vasodilation	PMID:4322742^[5]	IC: Inferred by Curator	GO:0043171	P	Seeded From UniProt
	GO:0042447	hormone catabolic process	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000001963	P	Seeded From UniProt
	GO:0042447	hormone catabolic process	PMID:11303049^[9]	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P09470	P	Seeded From UniProt
	GO:0042447	hormone catabolic process	PMID:7876104^[12]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0042755	eating behavior	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	P	Seeded From UniProt
	GO:0043065	positive regulation of apoptotic process	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	P	Seeded From UniProt
	GO:0043171	peptide catabolic process	PMID:4322742^[5]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0046872	metal ion binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0479	F	Seeded From UniProt
	GO:0050482	arachidonic acid secretion	PMID:17077303^[7]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0050729	positive regulation of inflammatory response	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	P	Seeded From UniProt
	GO:0050769	positive regulation of neurogenesis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000010627	P	Seeded From UniProt
	GO:0060047	heart contraction	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000001963	P	Seeded From UniProt
	GO:0060218	hemopoietic stem cell differentiation	PMID:7876104^[12]	IC: Inferred by Curator	GO:0042447	P	Seeded From UniProt
	GO:0007519	skeletal muscle tissue development	PMID:21956137^[13]	IGI: Inferred from Genetic Interaction	UniProtKB:Q08043	P	The ACE I and ACTN3 X alleles determine speed and power for Lithuanian athletes. Table 3 shows that Lithuanian athletes who are carriers of the ACE I/I and I/D as well as ACTN3 X/X and R/X genotypes have the potential to achieve better results in power-requiring sports	complete
	GO:0007519	skeletal muscle tissue development	PMID:21956137^[13]	IMP: Inferred from Mutant Phenotype		P	Table 2 shows male and female athletes with the ACE I/I genotype had higher handgrip strength and STEMP compared with male and female athletes having the ACE D/D genotype.	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ Gribouval O et al. (2005) Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis. Nat Genet 37: 964-8 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 ^2.7 ^2.8 Ehlers MR et al. (1991) Purification and characterization of recombinant human testis angiotensin-converting enzyme expressed in Chinese hamster ovary cells. Protein Expr Purif 2: 1-9 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Kohlstedt K et al. (2006) Signaling via the angiotensin-converting enzyme results in the phosphorylation of the nonmuscle myosin heavy chain IIA. Mol Pharmacol 69: 19-26 PubMed GONUTS page
↑ ^4.0 ^4.1 Rice GI et al. (2004) Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism. Biochem J 383: 45-51 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Yang HY et al. (1970) A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin. Biochim Biophys Acta 214: 374-6 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Soubrier F et al. (1988) Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. Proc Natl Acad Sci U S A 85: 9386-90 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 Chen Z et al. (2006) Human ACE and bradykinin B2 receptors form a complex at the plasma membrane. FASEB J 20: 2261-70 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Wei L et al. (1992) The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors. J Biol Chem 267: 13398-405 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Junot C et al. (2001) RXP 407, a selective inhibitor of the N-domain of angiotensin I-converting enzyme, blocks in vivo the degradation of hemoregulatory peptide acetyl-Ser-Asp-Lys-Pro with no effect on angiotensin I hydrolysis. J Pharmacol Exp Ther 297: 606-11 PubMed GONUTS page
↑ ^10.0 ^10.1 Natesh R et al. (2003) Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature 421: 551-4 PubMed GONUTS page
↑ Barnes K et al. (1998) Endothelin-converting enzyme: ultrastructural localization and its recycling from the cell surface. Hypertension 31: 3-9 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Rousseau A et al. (1995) The hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme. J Biol Chem 270: 3656-61 PubMed GONUTS page
↑ ^13.0 ^13.1 Ginevičienė V et al. (2011) Genetic variation of the human ACE and ACTN3 genes and their association with functional muscle properties in Lithuanian elite athletes. Medicina (Kaunas) 47: 284-90 PubMed GONUTS page

[PMID:16116425-0] Gribouval O et al. (2005) Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis. Nat Genet 37: 964-8 PubMed GONUTS page

[PMID:1668266-1] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 ^2.7 ^2.8 Ehlers MR et al. (1991) Purification and characterization of recombinant human testis angiotensin-converting enzyme expressed in Chinese hamster ovary cells. Protein Expr Purif 2: 1-9 PubMed GONUTS page

[PMID:16186248-2] 3.0 ^3.1 ^3.2 Kohlstedt K et al. (2006) Signaling via the angiotensin-converting enzyme results in the phosphorylation of the nonmuscle myosin heavy chain IIA. Mol Pharmacol 69: 19-26 PubMed GONUTS page

[PMID:15283675-3] 4.0 ^4.1 Rice GI et al. (2004) Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism. Biochem J 383: 45-51 PubMed GONUTS page

[PMID:4322742-4] 5.0 ^5.1 ^5.2 Yang HY et al. (1970) A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin. Biochim Biophys Acta 214: 374-6 PubMed GONUTS page

[PMID:2849100-5] 6.0 ^6.1 ^6.2 Soubrier F et al. (1988) Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning. Proc Natl Acad Sci U S A 85: 9386-90 PubMed GONUTS page

[PMID:17077303-6] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 Chen Z et al. (2006) Human ACE and bradykinin B2 receptors form a complex at the plasma membrane. FASEB J 20: 2261-70 PubMed GONUTS page

[PMID:1320019-7] 8.0 ^8.1 ^8.2 Wei L et al. (1992) The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors. J Biol Chem 267: 13398-405 PubMed GONUTS page

[PMID:11303049-8] 9.0 ^9.1 ^9.2 Junot C et al. (2001) RXP 407, a selective inhibitor of the N-domain of angiotensin I-converting enzyme, blocks in vivo the degradation of hemoregulatory peptide acetyl-Ser-Asp-Lys-Pro with no effect on angiotensin I hydrolysis. J Pharmacol Exp Ther 297: 606-11 PubMed GONUTS page

[PMID:12540854-9] 10.0 ^10.1 Natesh R et al. (2003) Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature 421: 551-4 PubMed GONUTS page

[PMID:9449382-10] Barnes K et al. (1998) Endothelin-converting enzyme: ultrastructural localization and its recycling from the cell surface. Hypertension 31: 3-9 PubMed GONUTS page

[PMID:7876104-11] 12.0 ^12.1 ^12.2 Rousseau A et al. (1995) The hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme. J Biol Chem 270: 3656-61 PubMed GONUTS page

[PMID:21956137-12] 13.0 ^13.1 Ginevičienė V et al. (2011) Genetic variation of the human ACE and ACTN3 genes and their association with functional muscle properties in Lithuanian elite athletes. Medicina (Kaunas) 47: 284-90 PubMed GONUTS page

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HUMAN:ACE

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