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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

    • metal ion binding Source: UniProtKB-KW
    • metalloendopeptidase activity Source: UniProtKB
    • methyltransferase activity Source: UniProtKB-KW

    GO - Biological processi

    • brain development Source: UniProtKB
    • cardioblast differentiation Source: UniProtKB
    • cell-cell signaling Source: UniProtKB
    • heart development Source: UniProtKB
    • 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

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

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134886910.

    Polymorphism and mutation databases

    BioMutaiECE2.

    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.
    GenevisibleiO60344. HS.

    Organism-specific databases

    HPAiHPA043346.
    HPA062215.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SYNE4Q8N2053EBI-3906484,EBI-7131783

    Protein-protein interaction databases

    BioGridi115067. 10 interactions.
    IntActiO60344. 4 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 25, 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. 4 interactions.
    MINTiMINT-8417701.
    STRINGi9606.ENSP00000384223.

    Chemistry

    BindingDBiO60344.
    ChEMBLiCHEMBL5890.

    Protein family/group databases

    MEROPSiM13.003.

    PTM databases

    PhosphoSiteiO60344.

    Polymorphism and mutation databases

    BioMutaiECE2.

    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.
    GenevisibleiO60344. HS.

    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(2001) [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 (JUN-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(1998) [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(2006) [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(2004) [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(2003) [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(2005) [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(2007) [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(2009) [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 30, 2000
    Last sequence update: November 25, 2008
    Last modified: June 24, 2015
    This is version 148 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.