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Protein

Endothelin-converting enzyme 2

Gene

ECE2

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

Functioni

Converts big endothelin-1 to endothelin-1. Also involved in the processing of various neuroendocrine peptides, including neurotensin, angiotensin I, substance P, proenkephalin-derived peptides, and prodynorphin-derived peptides. May limit beta-amyloid peptide accumulation in brain. May also have methyltransferase activity.1 Publication

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Kineticsi

  1. KM=0.4 µM for big ET-11 Publication
  2. KM=1.4 µM for peptide E1 Publication
  3. KM=27.4 µM for bradykinin1 Publication
  4. KM=48.4 µM for dynorphin B1 Publication

pH dependencei

Optimum pH is 5.0-5.5. Inactive at neutral pH.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei30 – 301S-adenosyl-L-homocysteine1 Publication
Binding sitei41 – 411S-adenosyl-L-homocysteine; via amide nitrogen1 Publication
Binding sitei66 – 661S-adenosyl-L-homocysteine; via carbonyl oxygen1 Publication
Binding sitei130 – 1301S-adenosyl-L-homocysteine1 Publication
Metal bindingi720 – 7201Zinc; catalyticPROSITE-ProRule annotation
Active sitei721 – 7211PROSITE-ProRule annotation
Metal bindingi724 – 7241Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi780 – 7801Zinc; catalyticPROSITE-ProRule annotation
Active sitei784 – 7841Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: UniProtKB
  3. methyltransferase activity Source: UniProtKB-KW

GO - Biological processi

  1. brain development Source: UniProtKB
  2. cardioblast differentiation Source: UniProtKB
  3. cell-cell signaling Source: UniProtKB
  4. heart development Source: UniProtKB
  5. peptide hormone processing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Methyltransferase, Protease, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKO60344.

Protein family/group databases

MEROPSiM13.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Endothelin-converting enzyme 2
Short name:
ECE-2
Including the following 2 domains:
Methyltransferase-like region (EC:2.1.1.-)
Endothelin-converting enzyme 2 region (EC:3.4.24.71)
Gene namesi
Name:ECE2
Synonyms:KIAA0604
ORF Names:UNQ403/PRO740
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:13275. ECE2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 178178CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei179 – 19921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini200 – 883684LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasmic vesicle membrane Source: UniProtKB
  2. Golgi membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134886910.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 883883Endothelin-converting enzyme 2PRO_0000078223Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391Phosphotyrosine1 Publication
Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi384 – 3841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi429 – 4291N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiO60344.
PaxDbiO60344.
PRIDEiO60344.

PTM databases

PhosphoSiteiO60344.

Expressioni

Tissue specificityi

Expressed in brain. Strongly down-regulated in inferior parietal lobe from Alzheimer disease patients (at protein level).1 Publication

Gene expression databases

BgeeiO60344.
CleanExiHS_ECE2.
ExpressionAtlasiO60344. baseline and differential.
GenevestigatoriO60344.

Organism-specific databases

HPAiHPA043346.
HPA062215.

Interactioni

Protein-protein interaction databases

BioGridi115067. 10 interactions.
IntActiO60344. 3 interactions.
MINTiMINT-8417701.
STRINGi9606.ENSP00000384223.

Structurei

Secondary structure

1
883
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 213Combined sources
Helixi23 – 297Combined sources
Turni30 – 356Combined sources
Helixi45 – 528Combined sources
Helixi53 – 553Combined sources
Beta strandi62 – 654Combined sources
Helixi72 – 787Combined sources
Beta strandi84 – 896Combined sources
Helixi91 – 10010Combined sources
Turni101 – 1033Combined sources
Beta strandi108 – 1114Combined sources
Beta strandi124 – 1318Combined sources
Helixi132 – 1365Combined sources
Turni137 – 1393Combined sources
Helixi148 – 16114Combined sources
Helixi167 – 1693Combined sources
Beta strandi170 – 18112Combined sources
Helixi203 – 2097Combined sources
Helixi212 – 2143Combined sources
Beta strandi216 – 2216Combined sources
Beta strandi229 – 2313Combined sources
Helixi232 – 2343Combined sources
Beta strandi236 – 2438Combined sources
Helixi249 – 2557Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PXXX-ray1.30A19-255[»]
ProteinModelPortaliO60344.
SMRiO60344. Positions 19-161, 214-883.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60344.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 160160Methyltransferase-like regionAdd
BLAST
Regioni88 – 892S-adenosyl-L-homocysteine binding
Regioni113 – 1142S-adenosyl-L-homocysteine binding
Regioni200 – 883684Endothelin-converting enzyme 2 regionAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the methyltransferase superfamily.Curated
In the C-terminal section; belongs to the peptidase M13 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3590.
GeneTreeiENSGT00760000119162.
HOVERGENiHBG005554.
InParanoidiO60344.
KOiK01415.
OMAiYATHIWQ.
OrthoDBiEOG7PZRWQ.
PhylomeDBiO60344.
TreeFamiTF315192.

Family and domain databases

Gene3Di3.40.390.10. 2 hits.
3.40.50.150. 1 hit.
InterProiIPR029733. ECE2.
IPR024079. MetalloPept_cat_dom.
IPR013216. Methyltransf_11.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11733. PTHR11733. 1 hit.
PTHR11733:SF122. PTHR11733:SF122. 1 hit.
PfamiPF08241. Methyltransf_11. 1 hit.
PF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view]
PRINTSiPR00786. NEPRILYSIN.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: O60344-1) [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
MASPGAGRAP PELPERNCGY REVEYWDQRY QGAADSAPYD WFGDFSSFRA
60 70 80 90 100
LLEPELRPED RILVLGCGNS ALSYELFLGG FPNVTSVDYS SVVVAAMQAR
110 120 130 140 150
HAHVPQLRWE TMDVRKLDFP SASFDVVLEK GTLDALLAGE RDPWTVSSEG
160 170 180 190 200
VHTVDQVLSE VGFQKGTRQL LGSRTQLELV LAGASLLLAA LLLGCLVALG
210 220 230 240 250
VQYHRDPSHS TCLTEACIRV AGKILESLDR GVSPCEDFYQ FSCGGWIRRN
260 270 280 290 300
PLPDGRSRWN TFNSLWDQNQ AILKHLLENT TFNSSSEAEQ KTQRFYLSCL
310 320 330 340 350
QVERIEELGA QPLRDLIEKI GGWNITGPWD QDNFMEVLKA VAGTYRATPF
360 370 380 390 400
FTVYISADSK SSNSNVIQVD QSGLFLPSRD YYLNRTANEK VLTAYLDYME
410 420 430 440 450
ELGMLLGGRP TSTREQMQQV LELEIQLANI TVPQDQRRDE EKIYHKMSIS
460 470 480 490 500
ELQALAPSMD WLEFLSFLLS PLELSDSEPV VVYGMDYLQQ VSELINRTEP
510 520 530 540 550
SILNNYLIWN LVQKTTSSLD RRFESAQEKL LETLYGTKKS CVPRWQTCIS
560 570 580 590 600
NTDDALGFAL GSLFVKATFD RQSKEIAEGM ISEIRTAFEE ALGQLVWMDE
610 620 630 640 650
KTRQAAKEKA DAIYDMIGFP DFILEPKELD DVYDGYEISE DSFFQNMLNL
660 670 680 690 700
YNFSAKVMAD QLRKPPSRDQ WSMTPQTVNA YYLPTKNEIV FPAGILQAPF
710 720 730 740 750
YARNHPKALN FGGIGVVMGH ELTHAFDDQG REYDKEGNLR PWWQNESLAA
760 770 780 790 800
FRNHTACMEE QYNQYQVNGE RLNGRQTLGE NIADNGGLKA AYNAYKAWLR
810 820 830 840 850
KHGEEQQLPA VGLTNHQLFF VGFAQVWCSV RTPESSHEGL VTDPHSPARF
860 870 880
RVLGTLSNSR DFLRHFGCPV GSPMNPGQLC EVW
Length:883
Mass (Da):99,773
Last modified:November 24, 2008 - v4
Checksum:iEE1C0F4AA4C6B225
GO
Isoform B (identifier: O60344-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: MASPGAGRAP...GVHTVDQVLS → MNVALQELGA...VEGGASPDAM

Show »
Length:765
Mass (Da):86,470
Checksum:i89D1B831B5628694
GO
Isoform C (identifier: O60344-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: MASPGAGRAP...VHTVDQVLSE → MNVALQELGAGSN

Show »
Length:736
Mass (Da):83,322
Checksum:i77F14FE5AC80E187
GO
Isoform D (identifier: O60344-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     162-261: GFQKGTRQLL...LPDGRSRWNT → SRVLVPGGRF...HEDFLSAIQL
     262-883: Missing.

Show »
Length:255
Mass (Da):28,306
Checksum:i39389C81C0798805
GO
Isoform 2C (identifier: O60344-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: MASPGAGRAP...VHTVDQVLSE → MNVALQELGA...SISGLCSRTM

Show »
Length:811
Mass (Da):91,211
Checksum:i7379F7AFEA937FCE
GO

Sequence cautioni

The sequence AAL30386.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA25530.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti467 – 4671F → S in AAI42951 (PubMed:15489334).Curated
Sequence conflicti783 – 7831A → T in AAQ89362 (PubMed:12975309).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti101 – 1011H → Y.2 Publications
Corresponds to variant rs7633387 [ dbSNP | Ensembl ].
VAR_047752
Natural varianti571 – 5711R → Q.
Corresponds to variant rs35875049 [ dbSNP | Ensembl ].
VAR_037085

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 160160MASPG…QVLSE → MNVALQELGAGSNMVEYKRA TLRDEDAPETPVEGGASPDA MEVGKGASPFSPGPSPGMTP GTPRSSGLFWRVTCPHLRSI SGLCSRTM in isoform 2C. 1 PublicationVSP_039176Add
BLAST
Alternative sequencei1 – 160160MASPG…QVLSE → MNVALQELGAGSN in isoform C. 3 PublicationsVSP_005509Add
BLAST
Alternative sequencei1 – 159159MASPG…DQVLS → MNVALQELGAGSNMVEYKRA TLRDEDAPETPVEGGASPDA M in isoform B. 2 PublicationsVSP_005508Add
BLAST
Alternative sequencei162 – 261100GFQKG…SRWNT → SRVLVPGGRFISMTSAAPHF RTRHYAQAYYGWSLRHATYG SGFHFHLYLMHKGGKLSVAQ LALGAQILSPPRPPTSPCFL QDSDHEDFLSAIQL in isoform D. 1 PublicationVSP_029333Add
BLAST
Alternative sequencei262 – 883622Missing in isoform D. 1 PublicationVSP_029334Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF428263 mRNA. Translation: AAL30386.1. Different initiation.
AF428264 mRNA. Translation: AAL30387.1.
AF192531 mRNA. Translation: AAG28399.1.
AF521189 mRNA. Translation: AAM77664.1.
AB011176 mRNA. Translation: BAA25530.2. Different initiation.
AY359003 mRNA. Translation: AAQ89362.1.
AC061705 Genomic DNA. No translation available.
AC078797 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78277.1.
BC005835 mRNA. Translation: AAH05835.1.
BC012449 mRNA. Translation: AAH12449.1.
BC069005 mRNA. Translation: AAH69005.1.
BC142950 mRNA. Translation: AAI42951.1.
CCDSiCCDS3255.1. [O60344-4]
CCDS3256.2. [O60344-1]
CCDS33899.1. [O60344-3]
CCDS43179.1. [O60344-5]
CCDS46969.1. [O60344-2]
RefSeqiNP_001032401.1. NM_001037324.2. [O60344-3]
NP_001093590.1. NM_001100120.1. [O60344-5]
NP_001093591.1. NM_001100121.1. [O60344-2]
NP_055508.3. NM_014693.3. [O60344-1]
NP_115707.2. NM_032331.3. [O60344-4]
UniGeneiHs.146161.

Genome annotation databases

EnsembliENST00000324557; ENSP00000314295; ENSG00000145194. [O60344-4]
ENST00000357474; ENSP00000350066; ENSG00000145194. [O60344-5]
ENST00000359140; ENSP00000352052; ENSG00000145194. [O60344-3]
ENST00000402825; ENSP00000384223; ENSG00000145194. [O60344-1]
ENST00000404464; ENSP00000385846; ENSG00000145194. [O60344-2]
GeneIDi9718.
KEGGihsa:9718.
UCSCiuc003fnh.4. human. [O60344-4]
uc003fni.4. human. [O60344-1]
uc003fnk.4. human. [O60344-3]
uc003fnl.4. human. [O60344-5]
uc003fnm.4. human. [O60344-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF428263 mRNA. Translation: AAL30386.1. Different initiation.
AF428264 mRNA. Translation: AAL30387.1.
AF192531 mRNA. Translation: AAG28399.1.
AF521189 mRNA. Translation: AAM77664.1.
AB011176 mRNA. Translation: BAA25530.2. Different initiation.
AY359003 mRNA. Translation: AAQ89362.1.
AC061705 Genomic DNA. No translation available.
AC078797 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW78277.1.
BC005835 mRNA. Translation: AAH05835.1.
BC012449 mRNA. Translation: AAH12449.1.
BC069005 mRNA. Translation: AAH69005.1.
BC142950 mRNA. Translation: AAI42951.1.
CCDSiCCDS3255.1. [O60344-4]
CCDS3256.2. [O60344-1]
CCDS33899.1. [O60344-3]
CCDS43179.1. [O60344-5]
CCDS46969.1. [O60344-2]
RefSeqiNP_001032401.1. NM_001037324.2. [O60344-3]
NP_001093590.1. NM_001100120.1. [O60344-5]
NP_001093591.1. NM_001100121.1. [O60344-2]
NP_055508.3. NM_014693.3. [O60344-1]
NP_115707.2. NM_032331.3. [O60344-4]
UniGeneiHs.146161.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PXXX-ray1.30A19-255[»]
ProteinModelPortaliO60344.
SMRiO60344. Positions 19-161, 214-883.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115067. 10 interactions.
IntActiO60344. 3 interactions.
MINTiMINT-8417701.
STRINGi9606.ENSP00000384223.

Chemistry

BindingDBiO60344.
ChEMBLiCHEMBL5890.

Protein family/group databases

MEROPSiM13.003.

PTM databases

PhosphoSiteiO60344.

Proteomic databases

MaxQBiO60344.
PaxDbiO60344.
PRIDEiO60344.

Protocols and materials databases

DNASUi9718.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000324557; ENSP00000314295; ENSG00000145194. [O60344-4]
ENST00000357474; ENSP00000350066; ENSG00000145194. [O60344-5]
ENST00000359140; ENSP00000352052; ENSG00000145194. [O60344-3]
ENST00000402825; ENSP00000384223; ENSG00000145194. [O60344-1]
ENST00000404464; ENSP00000385846; ENSG00000145194. [O60344-2]
GeneIDi9718.
KEGGihsa:9718.
UCSCiuc003fnh.4. human. [O60344-4]
uc003fni.4. human. [O60344-1]
uc003fnk.4. human. [O60344-3]
uc003fnl.4. human. [O60344-5]
uc003fnm.4. human. [O60344-2]

Organism-specific databases

CTDi9718.
GeneCardsiGC03P183967.
H-InvDBHIX0003914.
HGNCiHGNC:13275. ECE2.
HPAiHPA043346.
HPA062215.
MIMi610145. gene.
neXtProtiNX_O60344.
PharmGKBiPA134886910.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3590.
GeneTreeiENSGT00760000119162.
HOVERGENiHBG005554.
InParanoidiO60344.
KOiK01415.
OMAiYATHIWQ.
OrthoDBiEOG7PZRWQ.
PhylomeDBiO60344.
TreeFamiTF315192.

Enzyme and pathway databases

SABIO-RKO60344.

Miscellaneous databases

ChiTaRSiECE2. human.
EvolutionaryTraceiO60344.
GenomeRNAii9718.
NextBioi36537.
PROiO60344.
SOURCEiSearch...

Gene expression databases

BgeeiO60344.
CleanExiHS_ECE2.
ExpressionAtlasiO60344. baseline and differential.
GenevestigatoriO60344.

Family and domain databases

Gene3Di3.40.390.10. 2 hits.
3.40.50.150. 1 hit.
InterProiIPR029733. ECE2.
IPR024079. MetalloPept_cat_dom.
IPR013216. Methyltransf_11.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11733. PTHR11733. 1 hit.
PTHR11733:SF122. PTHR11733:SF122. 1 hit.
PfamiPF08241. Methyltransf_11. 1 hit.
PF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view]
PRINTSiPR00786. NEPRILYSIN.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human endothelin converting enzyme-2 (ECE2): characterization of mRNA species and chromosomal localization."
    Lorenzo M.-N., Khan R.Y., Wang Y., Tai S.C., Chan G.C., Cheung A.H., Marsden P.A.
    Biochim. Biophys. Acta 1522:46-52(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), NUCLEOTIDE SEQUENCE [MRNA] OF 13-883 (ISOFORM A).
  2. "Human endothelin-converting enzyme-2C (ECE-2C): a new ECE-2 variant."
    Funke-Kaiser H., Scheuch K., Behrouzi T., Synowitz M., Draheim N., Schwaneberg B., Thomas A., Zollmann F.S., Paul M., Orzechowski H.D.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2C).
    Tissue: Thalamus.
  3. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
  5. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TYR-101.
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C AND D), VARIANT TYR-101.
    Tissue: Lung and Ovary.
  8. "Characterization of endothelin-converting enzyme-2. Implication for a role in the nonclassical processing of regulatory peptides."
    Mzhavia N., Pan H., Che F.-Y., Fricker L.D., Devi L.A.
    J. Biol. Chem. 278:14704-14711(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  9. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Alterations in immunological and neurological gene expression patterns in Alzheimer's disease tissues."
    Weeraratna A.T., Kalehua A., Deleon I., Bertak D., Maher G., Wade M.S., Lustig A., Becker K.G., Wood W. III, Walker D.G., Beach T.G., Taub D.D.
    Exp. Cell Res. 313:450-461(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "An intact SAM-dependent methyltransferase fold is encoded by the human endothelin-converting enzyme-2 gene."
    Tempel W., Wu H., Dombrovsky L., Zeng H., Loppnau P., Zhu H., Plotnikov A.N., Bochkarev A.
    Proteins 74:789-793(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 19-161 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.

Entry informationi

Entry nameiECE2_HUMAN
AccessioniPrimary (citable) accession number: O60344
Secondary accession number(s): A5PLK8
, Q6NTG7, Q6UW36, Q8NFD7, Q96NX3, Q96NX4, Q9BRZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2000
Last sequence update: November 24, 2008
Last modified: March 3, 2015
This is version 146 of the entry and version 4 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, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.