HUMAN:ACE

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 AK301988 EU332840 AB208971 AC113554
CCDS	CCDS11637.1 CCDS45755.1 CCDS54155.1
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 4APH 4APJ 4BXK 4BZR 4BZS 4C2N 4C2O 4C2P 4C2Q 4C2R 4CA5 4CA6
PDBsum	1O86 1O8A 1UZE 1UZF 2C6F 2C6N 2IUL 2IUX 2OC2 2XY9 2XYD 2YDM 3BKK 3BKL 3L3N 3NXQ 4APH 4APJ 4BXK 4BZR 4BZS 4C2N 4C2O 4C2P 4C2Q 4C2R 4CA5 4CA6
ProteinModelPortal	P12821
SMR	P12821
BioGrid	108004
MINT	MINT-127316
STRING	9606.ENSP00000290866
BindingDB	P12821
ChEMBL	CHEMBL1808
DrugBank	DB00542 DB00616 DB01197 DB01340 DB00584 DB00492 DB00722 DB00691 DB00790 DB00881 DB00178 DB01180 DB01348 DB00519
GuidetoPHARMACOLOGY	1613
MEROPS	M02.001
PhosphoSite	P12821
DMDM	113045
MaxQB	P12821
PaxDb	P12821
PeptideAtlas	P12821
PRIDE	P12821
Ensembl	ENST00000290863 ENST00000290866 ENST00000413513
GeneID	1636
KEGG	hsa:1636
UCSC	uc002jau.2 uc002jav.2
CTD	1636
GeneCards	GC17P061554
HGNC	HGNC:2707
HPA	CAB002426 CAB002921 HPA029298
MIM	106180 267430 601367 612624 614519
neXtProt	NX_P12821
Orphanet	97369
PharmGKB	PA139
eggNOG	NOG71044
GeneTree	ENSGT00520000055576
HOGENOM	HOG000292210
HOVERGEN	HBG000264
InParanoid	P12821
KO	K01283
OrthoDB	EOG76HQ13
PhylomeDB	P12821
TreeFam	TF312861
BioCyc	MetaCyc:HS08412-MONOMER
BRENDA	3.4.15.1
Reactome	REACT_147707
SABIO-RK	P12821
SignaLink	P12821
EvolutionaryTrace	P12821
GeneWiki	Angiotensin-converting_enzyme
GenomeRNAi	1636
NextBio	6722
PMAP-CutDB	P12821
PRO	PR:P12821
Proteomes	UP000005640
Bgee	P12821
CleanEx	HS_ACE
ExpressionAtlas	P12821
Genevestigator	P12821
GO	GO:0005768 GO:0009897 GO:0005576 GO:0005615 GO:0070062 GO:0016021 GO:0005886 GO:0003779 GO:0031711 GO:0004180 GO:0031404 GO:0008144 GO:0004175 GO:0008237 GO:0008241 GO:0008270 GO:0002005 GO:0002003 GO:0050482 GO:0001974 GO:0044267 GO:0060218 GO:0042447 GO:0001822 GO:0032943 GO:0043171 GO:0008217 GO:0002019 GO:0014910 GO:0003081 GO:0019229 GO:0042312
InterPro	IPR001548
PANTHER	PTHR10514
Pfam	PF01401
PRINTS	PR00791
PROSITE	PS00142

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:1902033	regulation of hematopoietic stem cell proliferation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09470	P		Seeded From UniProt	complete
involved_in	GO:0071838	cell proliferation in bone marrow	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09470	P		Seeded From UniProt	complete
involved_in	GO:1902033	regulation of hematopoietic stem cell proliferation	PMID:7876104^[1]	ECO:0000305	curator inference used in manual assertion	GO:0008241	P		Seeded From UniProt	complete
enables	GO:0008241	peptidyl-dipeptidase activity	PMID:7876104^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P62328:PRO_0000034295)	Seeded From UniProt	complete
involved_in	GO:0043171	peptide catabolic process	PMID:15283675^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000170	positive regulation of peptidyl-cysteine S-nitrosylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09470	P		Seeded From UniProt	complete
involved_in	GO:1903597	negative regulation of gap junction assembly	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09470	P		Seeded From UniProt	complete
involved_in	GO:1900086	positive regulation of peptidyl-tyrosine autophosphorylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09470	P		Seeded From UniProt	complete
involved_in	GO:0061098	positive regulation of protein tyrosine kinase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09470	P		Seeded From UniProt	complete
involved_in	GO:0060047	heart contraction	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09470	P		Seeded From UniProt	complete
involved_in	GO:0007283	spermatogenesis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09470	P		Seeded From UniProt	complete
involved_in	GO:0002446	neutrophil mediated immunity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09470	P		Seeded From UniProt	complete
involved_in	GO:0050435	amyloid-beta metabolic process	PMID:19773553^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008241	peptidyl-dipeptidase activity	PMID:19773553^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P05067:PRO_0000000092) has_output:(UniProtKB:P05067:PRO_0000000093)	Seeded From UniProt	complete
involved_in	GO:0050435	amyloid-beta metabolic process	PMID:18495113^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004175	endopeptidase activity	PMID:18495113^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P05067)	Seeded From UniProt	complete
involved_in	GO:0003081	regulation of systemic arterial blood pressure by renin-angiotensin	PMID:174834^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(GO:0009651)	Seeded From UniProt	complete
enables	GO:0008238	exopeptidase activity	PMID:2983326^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P20366)	Seeded From UniProt	complete
enables	GO:0008240	tripeptidyl-peptidase activity	PMID:2983326^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P01148)	Seeded From UniProt	complete
enables	GO:0008241	peptidyl-dipeptidase activity	PMID:6208535^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P30990)\|has_direct_input:(UniProtKB:P20366:PRO_0000033530)	Seeded From UniProt	complete
involved_in	GO:0060177	regulation of angiotensin metabolic process	PMID:1851160^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008241	peptidyl-dipeptidase activity	PMID:1851160^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	has_input:(CHEBI:2718) has_output:(CHEBI:48432)	Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:11076943^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008241	peptidyl-dipeptidase activity	PMID:15283675^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P01019:PRO_0000032457)\|has_direct_input:(UniProtKB:P01019:PRO_0000420659)\|has_direct_input:(UniProtKB:P01019:PRO_0000420660)	Seeded From UniProt	complete
enables	GO:0008241	peptidyl-dipeptidase activity	PMID:7683654^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P01042)	Seeded From UniProt	complete
enables	GO:0031434	mitogen-activated protein kinase kinase binding	PMID:14615289^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O14733	F		Seeded From UniProt	complete
enables	GO:0051019	mitogen-activated protein kinase binding	PMID:14615289^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P45983	F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[12]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:21082674^[13]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[14]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:15326289^[15]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:16502470^[16]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001914)	Seeded From UniProt	complete
involved_in	GO:0060218	hematopoietic stem cell differentiation	PMID:7876104^[1]	ECO:0000305	curator inference used in manual assertion	GO:0042447	P		Seeded From UniProt	complete
involved_in	GO:0050482	arachidonic acid secretion	PMID:17077303^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043171	peptide catabolic process	PMID:4322742^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042447	hormone catabolic process	PMID:7876104^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042447	hormone catabolic process	PMID:11303049^[19]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09470	P		Seeded From UniProt	complete
involved_in	GO:0097746	regulation of blood vessel diameter	PMID:4322742^[18]	ECO:0000305	curator inference used in manual assertion	GO:0043171	P		Seeded From UniProt	complete
involved_in	GO:0032943	mononuclear cell proliferation	PMID:7876104^[1]	ECO:0000305	curator inference used in manual assertion	GO:0042447	P		Seeded From UniProt	complete
enables	GO:0031711	bradykinin receptor binding	PMID:17077303^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P30411	F		Seeded From UniProt	complete
enables	GO:0031404	chloride ion binding	PMID:12540854^[20]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0014910	regulation of smooth muscle cell migration	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P47820	P		Seeded From UniProt	complete
part_of	GO:0009897	external side of plasma membrane	PMID:9449382^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:12540854^[20]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0008217	regulation of blood pressure	PMID:11303049^[19]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09470	P		Seeded From UniProt	complete
involved_in	GO:0008217	regulation of blood pressure	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P47820	P		Seeded From UniProt	complete
enables	GO:0008144	drug binding	PMID:1320019^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:17077303^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005768	endosome	PMID:17077303^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:4322742^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:1668266^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002019	regulation of renal output by angiotensin	PMID:1668266^[23]	ECO:0000305	curator inference used in manual assertion	GO:0008241	P		Seeded From UniProt	complete
involved_in	GO:0001974	blood vessel remodeling	PMID:1668266^[23]	ECO:0000305	curator inference used in manual assertion	GO:0008241	P		Seeded From UniProt	complete
involved_in	GO:0001822	kidney development	PMID:16116425^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019229	regulation of vasoconstriction	PMID:1668266^[23]	ECO:0000305	curator inference used in manual assertion	GO:0008237	P		Seeded From UniProt	complete
enables	GO:0008241	peptidyl-dipeptidase activity	PMID:2849100^[25]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008241	peptidyl-dipeptidase activity	PMID:17077303^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008241	peptidyl-dipeptidase activity	PMID:1668266^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008241	peptidyl-dipeptidase activity	PMID:1320019^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008241	peptidyl-dipeptidase activity	PMID:11303049^[19]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09470	F		Seeded From UniProt	complete
enables	GO:0008237	metallopeptidase activity	PMID:17077303^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008237	metallopeptidase activity	PMID:2849100^[25]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008237	metallopeptidase activity	PMID:1320019^[22]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008237	metallopeptidase activity	PMID:1668266^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008237	metallopeptidase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P09470	F		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:15283675^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004175	endopeptidase activity	PMID:15283675^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P01019)	Seeded From UniProt	complete
involved_in	GO:0003081	regulation of systemic arterial blood pressure by renin-angiotensin	PMID:1668266^[23]	ECO:0000305	curator inference used in manual assertion	GO:0008237	P		Seeded From UniProt	complete
involved_in	GO:0002003	angiotensin maturation	PMID:1668266^[23]	ECO:0000305	curator inference used in manual assertion	GO:0008237	P		Seeded From UniProt	complete
involved_in	GO:0003081	regulation of systemic arterial blood pressure by renin-angiotensin	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000053931 UniProtKB:P12821	P		Seeded From UniProt	complete
involved_in	GO:0045777	positive regulation of blood pressure	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000053931 RGD:2493	P		Seeded From UniProt	complete
enables	GO:0008241	peptidyl-dipeptidase activity	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0012037 FB:FBgn0016122 MGI:MGI:87874 PANTHER:PTN000053976 RGD:2493 UniProtKB:P12821	F		Seeded From UniProt	complete
enables	GO:0008239	dipeptidyl-peptidase activity	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000053976 UniProtKB:F1NYM0 UniProtKB:Q10751	F		Seeded From UniProt	complete
enables	GO:0008238	exopeptidase activity	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001630211 UniProtKB:P12821	F		Seeded From UniProt	complete
enables	GO:0008237	metallopeptidase activity	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:87874 PANTHER:PTN000053976 RGD:2493 UniProtKB:P12821	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1917258 MGI:MGI:87874 PANTHER:PTN001630211 RGD:2493 UniProtKB:P12821 UniProtKB:Q9BYF1	C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0012037 FB:FBgn0016122 PANTHER:PTN001630211 RGD:2493 RGD:728890 UniProtKB:F1NYM0 UniProtKB:P12821 UniProtKB:Q9BYF1	C		Seeded From UniProt	complete
involved_in	GO:0003084	positive regulation of systemic arterial blood pressure	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:87874 PANTHER:PTN000053931 RGD:2493	P		Seeded From UniProt	complete
enables	GO:0070573	metallodipeptidase activity	PMID:2846041^[27]	ECO:0000269	experimental evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0070573	metallodipeptidase activity	PMID:20011602^[28]	ECO:0000269	experimental evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0070573	metallodipeptidase activity	PMID:1851160^[8]	ECO:0000269	experimental evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0070573	metallodipeptidase activity	PMID:1848554^[29]	ECO:0000269	experimental evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:2000170	positive regulation of peptidyl-cysteine S-nitrosylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
involved_in	GO:1903597	negative regulation of gap junction assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
involved_in	GO:1902033	regulation of hematopoietic stem cell proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
involved_in	GO:1900086	positive regulation of peptidyl-tyrosine autophosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
involved_in	GO:0071838	cell proliferation in bone marrow	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
involved_in	GO:0061098	positive regulation of protein tyrosine kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
involved_in	GO:0060047	heart contraction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
involved_in	GO:0042447	hormone catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
involved_in	GO:0032092	positive regulation of protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
involved_in	GO:0032091	negative regulation of protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
involved_in	GO:0010629	negative regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
involved_in	GO:0010608	posttranscriptional regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
enables	GO:0008241	peptidyl-dipeptidase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	F		Seeded From UniProt	complete
enables	GO:0008237	metallopeptidase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	F		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	F		Seeded From UniProt	complete
involved_in	GO:0008217	regulation of blood pressure	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
involved_in	GO:0007283	spermatogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	C		Seeded From UniProt	complete
involved_in	GO:0003084	positive regulation of systemic arterial blood pressure	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
involved_in	GO:0002446	neutrophil mediated immunity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
involved_in	GO:0001822	kidney development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P09470 ensembl:ENSMUSP00000001963	P		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001548	P		Seeded From UniProt	complete
enables	GO:0008237	metallopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001548	F		Seeded From UniProt	complete
enables	GO:0008241	peptidyl-dipeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001548	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001548	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:16186248^[30]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003779	actin binding	PMID:16186248^[30]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0002474	antigen processing and presentation of peptide antigen via MHC class I	PMID:23257181^[31]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008241	peptidyl-dipeptidase activity	PMID:2554286^[32]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008237	metallopeptidase activity	PMID:2554286^[32]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	PMID:2554286^[32]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-HSA-2022405 Reactome:R-HSA-2022398	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-9614933 Reactome:R-HSA-2065355	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002003	angiotensin maturation	Reactome:R-HSA-2065355 Reactome:R-HSA-2022405 Reactome:R-HSA-2022398 Reactome:R-HSA-2022377	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008237	metallopeptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0482	F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
enables	GO:0004180	carboxypeptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0121	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
edit table

Notes

References

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

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 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
↑ ^2.0 ^2.1 ^2.2 ^2.3 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
↑ ^3.0 ^3.1 Zou, K et al. (2009) Abeta42-to-Abeta40- and angiotensin-converting activities in different domains of angiotensin-converting enzyme. J. Biol. Chem. 284 31914-20 PubMed GONUTS page
↑ ^4.0 ^4.1 Sun, X et al. (2008) Catabolic attacks of membrane-bound angiotensin-converting enzyme on the N-terminal part of species-specific amyloid-beta peptides. Eur. J. Pharmacol. 588 18-25 PubMed GONUTS page
↑ Sancho, J et al. (1976) The role of the renin-angiotensin-aldosterone system in cardiovascular homeostasis in normal human subjects. Circulation 53 400-5 PubMed GONUTS page
↑ ^6.0 ^6.1 Skidgel, RA & Erdös, EG (1985) Novel activity of human angiotensin I converting enzyme: release of the NH2- and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone. Proc. Natl. Acad. Sci. U.S.A. 82 1025-9 PubMed GONUTS page
↑ Skidgel, RA et al. () Hydrolysis of substance p and neurotensin by converting enzyme and neutral endopeptidase. Peptides 5 769-76 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Wei, L et al. (1991) The two homologous domains of human angiotensin I-converting enzyme are both catalytically active. J. Biol. Chem. 266 9002-8 PubMed GONUTS page
↑ Eyries, M et al. (2001) Increased shedding of angiotensin-converting enzyme by a mutation identified in the stalk region. J. Biol. Chem. 276 5525-32 PubMed GONUTS page
↑ Jaspard, E et al. (1993) Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other natural peptides. J. Biol. Chem. 268 9496-503 PubMed GONUTS page
↑ ^11.0 ^11.1 Kohlstedt, K et al. (2004) Angiotensin-converting enzyme is involved in outside-in signaling in endothelial cells. Circ. Res. 94 60-7 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Zhang, Y et al. (2010) Comprehensive analysis of low-abundance proteins in human urinary exosomes using peptide ligand library technology, peptide OFFGEL fractionation and nanoHPLC-chip-MS/MS. Electrophoresis 31 3797-807 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ Pisitkun, T et al. (2004) Identification and proteomic profiling of exosomes in human urine. Proc. Natl. Acad. Sci. U.S.A. 101 13368-73 PubMed GONUTS page
↑ Palmer, DJ et al. (2006) Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 6 2208-16 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 ^17.4 ^17.5 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
↑ ^18.0 ^18.1 ^18.2 Yang, HY et al. (1970) A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin. Biochim. Biophys. Acta 214 374-6 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 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
↑ ^20.0 ^20.1 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
↑ ^22.0 ^22.1 ^22.2 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
↑ ^23.0 ^23.1 ^23.2 ^23.3 ^23.4 ^23.5 ^23.6 ^23.7 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
↑ 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
↑ ^25.0 ^25.1 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
↑ ^26.0 ^26.1 ^26.2 ^26.3 ^26.4 ^26.5 ^26.6 ^26.7 ^26.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Ehlers, MR & Kirsch, RE (1988) Catalysis of angiotensin I hydrolysis by human angiotensin-converting enzyme: effect of chloride and pH. Biochemistry 27 5538-44 PubMed GONUTS page
↑ Nesterovitch, AB et al. (2009) Angiotensin I-converting enzyme mutation (Trp1197Stop) causes a dramatic increase in blood ACE. PLoS ONE 4 e8282 PubMed GONUTS page
↑ Wei, L et al. (1991) Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes. J. Biol. Chem. 266 5540-6 PubMed GONUTS page
↑ ^30.0 ^30.1 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
↑ Bernstein, KE et al. (2013) A modern understanding of the traditional and nontraditional biological functions of angiotensin-converting enzyme. Pharmacol. Rev. 65 1-46 PubMed GONUTS page
↑ ^32.0 ^32.1 ^32.2 Ehlers, MR et al. (1989) Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc. Natl. Acad. Sci. U.S.A. 86 7741-5 PubMed GONUTS page

[PMID:7876104-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 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:15283675-2] 2.0 ^2.1 ^2.2 ^2.3 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:19773553-3] 3.0 ^3.1 Zou, K et al. (2009) Abeta42-to-Abeta40- and angiotensin-converting activities in different domains of angiotensin-converting enzyme. J. Biol. Chem. 284 31914-20 PubMed GONUTS page

[PMID:18495113-4] 4.0 ^4.1 Sun, X et al. (2008) Catabolic attacks of membrane-bound angiotensin-converting enzyme on the N-terminal part of species-specific amyloid-beta peptides. Eur. J. Pharmacol. 588 18-25 PubMed GONUTS page

[PMID:174834-5] Sancho, J et al. (1976) The role of the renin-angiotensin-aldosterone system in cardiovascular homeostasis in normal human subjects. Circulation 53 400-5 PubMed GONUTS page

[PMID:2983326-6] 6.0 ^6.1 Skidgel, RA & Erdös, EG (1985) Novel activity of human angiotensin I converting enzyme: release of the NH2- and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone. Proc. Natl. Acad. Sci. U.S.A. 82 1025-9 PubMed GONUTS page

[PMID:6208535-7] Skidgel, RA et al. () Hydrolysis of substance p and neurotensin by converting enzyme and neutral endopeptidase. Peptides 5 769-76 PubMed GONUTS page

[PMID:1851160-8] 8.0 ^8.1 ^8.2 Wei, L et al. (1991) The two homologous domains of human angiotensin I-converting enzyme are both catalytically active. J. Biol. Chem. 266 9002-8 PubMed GONUTS page

[PMID:11076943-9] Eyries, M et al. (2001) Increased shedding of angiotensin-converting enzyme by a mutation identified in the stalk region. J. Biol. Chem. 276 5525-32 PubMed GONUTS page

[PMID:7683654-10] Jaspard, E et al. (1993) Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other natural peptides. J. Biol. Chem. 268 9496-503 PubMed GONUTS page

[PMID:14615289-11] 11.0 ^11.1 Kohlstedt, K et al. (2004) Angiotensin-converting enzyme is involved in outside-in signaling in endothelial cells. Circ. Res. 94 60-7 PubMed GONUTS page

[PMID:23533145-12] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:21082674-13] Zhang, Y et al. (2010) Comprehensive analysis of low-abundance proteins in human urinary exosomes using peptide ligand library technology, peptide OFFGEL fractionation and nanoHPLC-chip-MS/MS. Electrophoresis 31 3797-807 PubMed GONUTS page

[PMID:19056867-14] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:15326289-15] Pisitkun, T et al. (2004) Identification and proteomic profiling of exosomes in human urine. Proc. Natl. Acad. Sci. U.S.A. 101 13368-73 PubMed GONUTS page

[PMID:16502470-16] Palmer, DJ et al. (2006) Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 6 2208-16 PubMed GONUTS page

[PMID:17077303-17] 17.0 ^17.1 ^17.2 ^17.3 ^17.4 ^17.5 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:4322742-18] 18.0 ^18.1 ^18.2 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:11303049-19] 19.0 ^19.1 ^19.2 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:12540854-20] 20.0 ^20.1 Natesh, R et al. (2003) Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature 421 551-4 PubMed GONUTS page

[PMID:9449382-21] 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:1320019-22] 22.0 ^22.1 ^22.2 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:1668266-23] 23.0 ^23.1 ^23.2 ^23.3 ^23.4 ^23.5 ^23.6 ^23.7 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:16116425-24] 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:2849100-25] 25.0 ^25.1 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:21873635-26] 26.0 ^26.1 ^26.2 ^26.3 ^26.4 ^26.5 ^26.6 ^26.7 ^26.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:2846041-27] Ehlers, MR & Kirsch, RE (1988) Catalysis of angiotensin I hydrolysis by human angiotensin-converting enzyme: effect of chloride and pH. Biochemistry 27 5538-44 PubMed GONUTS page

[PMID:20011602-28] Nesterovitch, AB et al. (2009) Angiotensin I-converting enzyme mutation (Trp1197Stop) causes a dramatic increase in blood ACE. PLoS ONE 4 e8282 PubMed GONUTS page

[PMID:1848554-29] Wei, L et al. (1991) Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes. J. Biol. Chem. 266 5540-6 PubMed GONUTS page

[PMID:16186248-30] 30.0 ^30.1 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:23257181-31] Bernstein, KE et al. (2013) A modern understanding of the traditional and nontraditional biological functions of angiotensin-converting enzyme. Pharmacol. Rev. 65 1-46 PubMed GONUTS page

[PMID:2554286-32] 32.0 ^32.1 ^32.2 Ehlers, MR et al. (1989) Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc. Natl. Acad. Sci. U.S.A. 86 7741-5 PubMed GONUTS page

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