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P42892

- ECE1_HUMAN

UniProt

P42892 - ECE1_HUMAN

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Protein

Endothelin-converting enzyme 1

Gene
ECE1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Converts big endothelin-1 to endothelin-1.1 Publication

Catalytic activityi

Hydrolysis of the 21-Trp-|-Val-22 bond in big endothelin to form endothelin 1.

Cofactori

Binds 1 zinc ion per subunit.1 Publication

Enzyme regulationi

Inhibited by phosphoramidon.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi607 – 6071Zinc; catalytic
Active sitei608 – 6081
Metal bindingi611 – 6111Zinc; catalytic
Metal bindingi667 – 6671Zinc; catalytic
Active sitei671 – 6711Proton donor By similarity

GO - Molecular functioni

  1. endopeptidase activity Source: BHF-UCL
  2. metal ion binding Source: UniProtKB-KW
  3. metalloendopeptidase activity Source: BHF-UCL
  4. peptide hormone binding Source: BHF-UCL
  5. protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  1. bradykinin catabolic process Source: BHF-UCL
  2. calcitonin catabolic process Source: BHF-UCL
  3. ear development Source: BHF-UCL
  4. embryonic digit morphogenesis Source: BHF-UCL
  5. endothelin maturation Source: BHF-UCL
  6. heart development Source: BHF-UCL
  7. hormone catabolic process Source: BHF-UCL
  8. peptide hormone processing Source: BHF-UCL
  9. pharyngeal system development Source: Ensembl
  10. positive regulation of receptor recycling Source: BHF-UCL
  11. protein processing Source: BHF-UCL
  12. regulation of systemic arterial blood pressure by endothelin Source: BHF-UCL
  13. regulation of vasoconstriction Source: BHF-UCL
  14. substance P catabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM13.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Endothelin-converting enzyme 1 (EC:3.4.24.71)
Short name:
ECE-1
Gene namesi
Name:ECE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3146. ECE1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6868Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei69 – 8921Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini90 – 770681Extracellular Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. early endosome Source: BHF-UCL
  2. endosome Source: BHF-UCL
  3. external side of plasma membrane Source: BHF-UCL
  4. extracellular vesicular exosome Source: UniProt
  5. integral component of membrane Source: BHF-UCL
  6. intrinsic component of endosome membrane Source: BHF-UCL
  7. lysosomal membrane Source: UniProtKB
  8. perinuclear region of cytoplasm Source: BHF-UCL
  9. plasma membrane Source: BHF-UCL
  10. vesicle Source: BHF-UCL
  11. Weibel-Palade body Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Hirschsprung disease cardiac defects and autonomic dysfunction (HSCRCDAD) [MIM:613870]: A disorder characterized by skip-lesions Hirschsprung disease, craniofacial abnormalities and other dysmorphic features, cardiac defects including ductus arteriosus, small subaortic ventricular septal defect, small atrial septal defect, and autonomic dysfunction.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti754 – 7541R → C in HSCRCDAD. 1 Publication
Corresponds to variant rs3026906 [ dbSNP | Ensembl ].
VAR_026747

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi428 – 4281C → S: Abolishes dimerization. 1 Publication

Keywords - Diseasei

Disease mutation, Hirschsprung disease

Organism-specific databases

MIMi613870. phenotype.
Orphaneti388. Hirschsprung disease.
PharmGKBiPA27594.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 770770Endothelin-converting enzyme 1PRO_0000078220Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Phosphothreonine1 Publication
Glycosylationi166 – 1661N-linked (GlcNAc...)2 Publications
Glycosylationi187 – 1871N-linked (GlcNAc...) Reviewed prediction
Glycosylationi210 – 2101N-linked (GlcNAc...)3 Publications
Glycosylationi270 – 2701N-linked (GlcNAc...)1 Publication
Glycosylationi316 – 3161N-linked (GlcNAc...)1 Publication
Glycosylationi362 – 3621N-linked (GlcNAc...)1 Publication
Glycosylationi383 – 3831N-linked (GlcNAc...)1 Publication
Disulfide bondi428 – 428Interchain
Glycosylationi539 – 5391N-linked (GlcNAc...) Reviewed prediction
Glycosylationi632 – 6321N-linked (GlcNAc...) Reviewed prediction
Glycosylationi651 – 6511N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP42892.
PaxDbiP42892.
PRIDEiP42892.

PTM databases

PhosphoSiteiP42892.

Expressioni

Tissue specificityi

All isoforms are expressed in umbilical vein endothelial cells, polynuclear neutrophils, fibroblasts, atrium cardiomyocytes and ventricles. Isoforms A, B and C are also expressed in placenta, lung, heart, adrenal gland and phaeochromocytoma; isoforms A and C in liver, testis and small intestine; isoform B, C and D in endothelial cells and umbilical vein smooth muscle cells; isoforms C and D in saphenous vein cells, and isoform C in kidney.2 Publications

Gene expression databases

ArrayExpressiP42892.
BgeeiP42892.
GenevestigatoriP42892.

Organism-specific databases

HPAiHPA001490.
HPA013616.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

Protein-protein interaction databases

BioGridi108218. 16 interactions.
IntActiP42892. 3 interactions.

Structurei

Secondary structure

1
770
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi102 – 11413
Turni121 – 1233
Helixi125 – 13612
Beta strandi144 – 1474
Helixi148 – 16417
Helixi173 – 18614
Helixi189 – 1946
Helixi197 – 2059
Helixi220 – 22910
Beta strandi235 – 24410
Beta strandi247 – 25610
Beta strandi261 – 2644
Helixi266 – 2694
Turni270 – 2734
Helixi277 – 29115
Helixi297 – 31721
Helixi321 – 3244
Helixi327 – 3304
Beta strandi332 – 3354
Helixi336 – 3427
Helixi348 – 3558
Beta strandi366 – 3705
Helixi372 – 38413
Helixi387 – 40216
Helixi403 – 4053
Helixi408 – 41811
Helixi434 – 45522
Helixi458 – 47922
Helixi487 – 49913
Beta strandi501 – 5066
Helixi508 – 5114
Helixi513 – 5208
Helixi530 – 54617
Turni547 – 5504
Beta strandi568 – 5703
Turni571 – 5744
Beta strandi575 – 5795
Helixi580 – 5823
Turni585 – 5873
Helixi594 – 5996
Helixi601 – 61111
Helixi617 – 6193
Helixi632 – 64918
Beta strandi653 – 6586
Turni661 – 6644
Helixi665 – 68925
Beta strandi696 – 6983
Helixi702 – 71312
Beta strandi716 – 7183
Helixi720 – 72910
Helixi735 – 74410
Helixi747 – 7537

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DWBX-ray2.38A101-770[»]
ProteinModelPortaliP42892.
SMRiP42892. Positions 101-770.

Miscellaneous databases

EvolutionaryTraceiP42892.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M13 family.

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3590.
HOVERGENiHBG005554.
InParanoidiP42892.
KOiK01415.
OMAiQVVTAHY.
OrthoDBiEOG7PZRWQ.
PhylomeDBiP42892.
TreeFamiTF315192.

Family and domain databases

Gene3Di3.40.390.10. 2 hits.
InterProiIPR024079. MetalloPept_cat_dom.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view]
PANTHERiPTHR11733. PTHR11733. 1 hit.
PfamiPF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view]
PRINTSiPR00786. NEPRILYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform B (identifier: P42892-1) [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

MRGVWPPPVS ALLSALGMST YKRATLDEED LVDSLSEGDA YPNGLQVNFH    50
SPRSGQRCWA ARTQVEKRLV VLVVLLAAGL VACLAALGIQ YQTRSPSVCL 100
SEACVSVTSS ILSSMDPTVD PCHDFFSYAC GGWIKANPVP DGHSRWGTFS 150
NLWEHNQAII KHLLENSTAS VSEAERKAQV YYRACMNETR IEELRAKPLM 200
ELIERLGGWN ITGPWAKDNF QDTLQVVTAH YRTSPFFSVY VSADSKNSNS 250
NVIQVDQSGL GLPSRDYYLN KTENEKVLTG YLNYMVQLGK LLGGGDEEAI 300
RPQMQQILDF ETALANITIP QEKRRDEELI YHKVTAAELQ TLAPAINWLP 350
FLNTIFYPVE INESEPIVVY DKEYLEQIST LINTTDRCLL NNYMIWNLVR 400
KTSSFLDQRF QDADEKFMEV MYGTKKTCLP RWKFCVSDTE NNLGFALGPM 450
FVKATFAEDS KSIATEIILE IKKAFEESLS TLKWMDEETR KSAKEKADAI 500
YNMIGYPNFI MDPKELDKVF NDYTAVPDLY FENAMRFFNF SWRVTADQLR 550
KAPNRDQWSM TPPMVNAYYS PTKNEIVFPA GILQAPFYTR SSPKALNFGG 600
IGVVVGHELT HAFDDQGREY DKDGNLRPWW KNSSVEAFKR QTECMVEQYS 650
NYSVNGEPVN GRHTLGENIA DNGGLKAAYR AYQNWVKKNG AEHSLPTLGL 700
TNNQLFFLGF AQVWCSVRTP ESSHEGLITD PHSPSRFRVI GSLSNSKEFS 750
EHFRCPPGSP MNPPHKCEVW 770
Length:770
Mass (Da):87,164
Last modified:October 1, 1996 - v2
Checksum:iDD88A59748B22F80
GO
Isoform A (identifier: P42892-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: MRGVWPPPVS...LSEGDAYPNG → MPLQGLGLQRNPFLQGKRGPGLTSSPPLLPPS

Show »
Length:758
Mass (Da):85,808
Checksum:i4768314E789DFF96
GO
Isoform C (identifier: P42892-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MRGVWPPPVSALLSALG → M

Show »
Length:754
Mass (Da):85,562
Checksum:iA16E45032B03029D
GO
Isoform D (identifier: P42892-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MRGVWPPPVSALLSALG → MEALRESVLHLALQ

Show »
Length:767
Mass (Da):87,022
Checksum:i09B58AF5A63882F4
GO

Sequence cautioni

The sequence CAA84548.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAX35820.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti341 – 3411T → I.1 Publication
Corresponds to variant rs1076669 [ dbSNP | Ensembl ].
VAR_011972
Natural varianti630 – 6301W → R.
Corresponds to variant rs2229451 [ dbSNP | Ensembl ].
VAR_054007
Natural varianti754 – 7541R → C in HSCRCDAD. 1 Publication
Corresponds to variant rs3026906 [ dbSNP | Ensembl ].
VAR_026747

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4444MRGVW…AYPNG → MPLQGLGLQRNPFLQGKRGP GLTSSPPLLPPS in isoform A. VSP_005502Add
BLAST
Alternative sequencei1 – 1717MRGVW…LSALG → M in isoform C. VSP_005504Add
BLAST
Alternative sequencei1 – 1717MRGVW…LSALG → MEALRESVLHLALQ in isoform D. VSP_005503Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D49471 mRNA. Translation: BAA08442.1.
D43698 mRNA. Translation: BAA07800.1.
X91922
, X91923, X91924, X91925, X91926, X91927, X91928, X91929, X91930, X91931, X91932, X91933, X91934, X91935, X91936, X91937, X91938, X91939 Genomic DNA. Translation: CAA63015.1.
X91923
, X91924, X91925, X91926, X91927, X91928, X91929, X91930, X91931, X91932, X91933, X91934, X91935, X91936, X91937, X91938, X91939 Genomic DNA. Translation: CAA63016.1.
AB031742 mRNA. Translation: BAA83687.1.
AK290656 mRNA. Translation: BAF83345.1.
AK304167 mRNA. Translation: BAG65053.1.
AY953519 Genomic DNA. Translation: AAX35820.1. Sequence problems.
AL031005 Genomic DNA. Translation: CAI20195.1.
AL031005, AL031728 Genomic DNA. Translation: CAI20192.1.
AL031005, AL031728 Genomic DNA. Translation: CAI20194.1.
AL031728 Genomic DNA. Translation: CAB52285.2.
AL031728, AL031005 Genomic DNA. Translation: CAI19064.1.
CH471134 Genomic DNA. Translation: EAW94959.1.
CH471134 Genomic DNA. Translation: EAW94964.1.
BC117256 mRNA. Translation: AAI17257.1.
BC126257 mRNA. Translation: AAI26258.1.
AJ130828 mRNA. Translation: CAB46443.1.
X98272 mRNA. Translation: CAA66922.1.
Z35307 mRNA. Translation: CAA84548.1. Different initiation.
AF018034 Genomic DNA. Translation: AAD21221.1.
CCDSiCCDS215.1. [P42892-1]
CCDS44081.1. [P42892-3]
CCDS44082.1. [P42892-4]
CCDS44083.1. [P42892-2]
PIRiJC2521.
JC4136.
RefSeqiNP_001106818.1. NM_001113347.1. [P42892-2]
NP_001106819.1. NM_001113348.1. [P42892-3]
NP_001106820.1. NM_001113349.1. [P42892-4]
NP_001388.1. NM_001397.2. [P42892-1]
XP_006710461.1. XM_006710398.1.
UniGeneiHs.195080.

Genome annotation databases

EnsembliENST00000264205; ENSP00000264205; ENSG00000117298. [P42892-4]
ENST00000357071; ENSP00000349581; ENSG00000117298. [P42892-2]
ENST00000374893; ENSP00000364028; ENSG00000117298. [P42892-1]
ENST00000415912; ENSP00000405088; ENSG00000117298. [P42892-3]
GeneIDi1889.
KEGGihsa:1889.
UCSCiuc001bei.2. human. [P42892-4]
uc001bej.2. human. [P42892-2]
uc001bek.2. human. [P42892-1]
uc001bem.2. human. [P42892-3]

Polymorphism databases

DMDMi1706563.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D49471 mRNA. Translation: BAA08442.1 .
D43698 mRNA. Translation: BAA07800.1 .
X91922
, X91923 , X91924 , X91925 , X91926 , X91927 , X91928 , X91929 , X91930 , X91931 , X91932 , X91933 , X91934 , X91935 , X91936 , X91937 , X91938 , X91939 Genomic DNA. Translation: CAA63015.1 .
X91923
, X91924 , X91925 , X91926 , X91927 , X91928 , X91929 , X91930 , X91931 , X91932 , X91933 , X91934 , X91935 , X91936 , X91937 , X91938 , X91939 Genomic DNA. Translation: CAA63016.1 .
AB031742 mRNA. Translation: BAA83687.1 .
AK290656 mRNA. Translation: BAF83345.1 .
AK304167 mRNA. Translation: BAG65053.1 .
AY953519 Genomic DNA. Translation: AAX35820.1 . Sequence problems.
AL031005 Genomic DNA. Translation: CAI20195.1 .
AL031005 , AL031728 Genomic DNA. Translation: CAI20192.1 .
AL031005 , AL031728 Genomic DNA. Translation: CAI20194.1 .
AL031728 Genomic DNA. Translation: CAB52285.2 .
AL031728 , AL031005 Genomic DNA. Translation: CAI19064.1 .
CH471134 Genomic DNA. Translation: EAW94959.1 .
CH471134 Genomic DNA. Translation: EAW94964.1 .
BC117256 mRNA. Translation: AAI17257.1 .
BC126257 mRNA. Translation: AAI26258.1 .
AJ130828 mRNA. Translation: CAB46443.1 .
X98272 mRNA. Translation: CAA66922.1 .
Z35307 mRNA. Translation: CAA84548.1 . Different initiation.
AF018034 Genomic DNA. Translation: AAD21221.1 .
CCDSi CCDS215.1. [P42892-1 ]
CCDS44081.1. [P42892-3 ]
CCDS44082.1. [P42892-4 ]
CCDS44083.1. [P42892-2 ]
PIRi JC2521.
JC4136.
RefSeqi NP_001106818.1. NM_001113347.1. [P42892-2 ]
NP_001106819.1. NM_001113348.1. [P42892-3 ]
NP_001106820.1. NM_001113349.1. [P42892-4 ]
NP_001388.1. NM_001397.2. [P42892-1 ]
XP_006710461.1. XM_006710398.1.
UniGenei Hs.195080.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3DWB X-ray 2.38 A 101-770 [» ]
ProteinModelPortali P42892.
SMRi P42892. Positions 101-770.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108218. 16 interactions.
IntActi P42892. 3 interactions.

Chemistry

BindingDBi P42892.
ChEMBLi CHEMBL4791.
GuidetoPHARMACOLOGYi 1615.

Protein family/group databases

MEROPSi M13.002.

PTM databases

PhosphoSitei P42892.

Polymorphism databases

DMDMi 1706563.

Proteomic databases

MaxQBi P42892.
PaxDbi P42892.
PRIDEi P42892.

Protocols and materials databases

DNASUi 1889.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264205 ; ENSP00000264205 ; ENSG00000117298 . [P42892-4 ]
ENST00000357071 ; ENSP00000349581 ; ENSG00000117298 . [P42892-2 ]
ENST00000374893 ; ENSP00000364028 ; ENSG00000117298 . [P42892-1 ]
ENST00000415912 ; ENSP00000405088 ; ENSG00000117298 . [P42892-3 ]
GeneIDi 1889.
KEGGi hsa:1889.
UCSCi uc001bei.2. human. [P42892-4 ]
uc001bej.2. human. [P42892-2 ]
uc001bek.2. human. [P42892-1 ]
uc001bem.2. human. [P42892-3 ]

Organism-specific databases

CTDi 1889.
GeneCardsi GC01M021543.
GeneReviewsi ECE1.
H-InvDB HIX0159964.
HGNCi HGNC:3146. ECE1.
HPAi HPA001490.
HPA013616.
MIMi 600423. gene.
613870. phenotype.
neXtProti NX_P42892.
Orphaneti 388. Hirschsprung disease.
PharmGKBi PA27594.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3590.
HOVERGENi HBG005554.
InParanoidi P42892.
KOi K01415.
OMAi QVVTAHY.
OrthoDBi EOG7PZRWQ.
PhylomeDBi P42892.
TreeFami TF315192.

Miscellaneous databases

ChiTaRSi ECE1. human.
EvolutionaryTracei P42892.
GeneWikii Endothelin_converting_enzyme_1.
GenomeRNAii 1889.
NextBioi 7703.
PROi P42892.
SOURCEi Search...

Gene expression databases

ArrayExpressi P42892.
Bgeei P42892.
Genevestigatori P42892.

Family and domain databases

Gene3Di 3.40.390.10. 2 hits.
InterProi IPR024079. MetalloPept_cat_dom.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view ]
PANTHERi PTHR11733. PTHR11733. 1 hit.
Pfami PF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view ]
PRINTSi PR00786. NEPRILYSIN.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of a human endothelin converting enzyme in renal adenocarcinoma (ACHN) cells producing endothelin-2."
    Yorimitsu K., Moroi K., Inagaki N., Saito T., Masuda Y., Masaki T., Seino S., Kimura S.
    Biochem. Biophys. Res. Commun. 208:721-727(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
  3. "Organization of the gene encoding the human endothelin-converting enzyme (ECE-1)."
    Valdenaire O., Rohrbacher E., Mattei M.-G.
    J. Biol. Chem. 270:29794-29798(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B).
    Tissue: Placenta.
  4. "Human endothelin-converting enzyme-1c."
    Takayanagi R.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
    Tissue: Umbilical vein endothelial cell.
  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 B).
    Tissue: Trachea.
  6. NIEHS SNPs program
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-341.
  7. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Tissue: Brain.
  10. "A fourth isoform of endothelin-converting enzyme (ECE-1) is generated from an additional promoter."
    Valdenaire O., Lepailleur-Enouf D., Egidy G., Thouard A., Barret A., Vranckx R., Tougard C., Michel J.-B.
    Eur. J. Biochem. 264:341-349(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-132 (ISOFORM D), TISSUE SPECIFICITY.
  11. "Human endothelin-converting enzyme (ECE-1): three isoforms with distinct subcellular localizations."
    Schweizer A., Valdenaire O., Nelboeck P., Deuschle U., Dumas Milne Edwards J.B., Stumpf J.G., Loeffler B.-M.
    Biochem. J. 328:871-877(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-103 (ISOFORM C), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Umbilical vein endothelial cell.
  12. "Molecular characterization of human and bovine endothelin converting enzyme (ECE-1)."
    Schmidt M., Kroeger B., Jacob E., Seulberger H., Subkowski T., Otter R., Meyer T., Schmalzing G., Hillen H.
    FEBS Lett. 356:238-243(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-770 (ISOFORM B).
    Tissue: Placenta.
  13. "Characterization of the human endothelin converting enzyme-1 gene (ECE-1): genomic structure and chromosomal localization."
    Flowers M.A., Tai S.C., Baluyut C.A., Cheung A.H., Kau C.L., Wong G.K.T., Marsden P.A.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 713-770.
  14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
    Lewandrowski U., Moebius J., Walter U., Sickmann A.
    Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-210.
    Tissue: Platelet.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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-166; ASN-210; ASN-270 AND ASN-316.
    Tissue: Liver.
  18. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-166; ASN-210; ASN-362 AND ASN-383.
    Tissue: Leukemic T-cell.
  19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Structure of human endothelin-converting enzyme I complexed with phosphoramidon."
    Schulz H., Dale G.E., Karimi-Nejad Y., Oefner C.
    J. Mol. Biol. 385:178-187(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 101-770 OF MUTANT SER-428 IN COMPLEX WITH ZINC IONS AND PHOSPHORAMIDON, COFACTOR, SUBUNIT, MUTAGENESIS OF CYS-428.
  22. "A loss-of-function mutation in the endothelin-converting enzyme 1 (ECE-1) associated with Hirschsprung disease, cardiac defects, and autonomic dysfunction."
    Hofstra R.M.W., Valdenaire O., Arch E., Osinga J., Kroes H., Loffler B.-M., Hamosh A., Meijers C., Buys C.H.C.M.
    Am. J. Hum. Genet. 64:304-308(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HSCRCDAD CYS-754.

Entry informationi

Entry nameiECE1_HUMAN
AccessioniPrimary (citable) accession number: P42892
Secondary accession number(s): A8K3P1
, B4E291, Q14217, Q17RN5, Q2Z2K8, Q58GE7, Q5THM5, Q5THM7, Q5THM8, Q9UJQ6, Q9UPF4, Q9UPM4, Q9Y501
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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