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O60344

- ECE2_HUMAN

UniProt

O60344 - ECE2_HUMAN

Protein

Endothelin-converting enzyme 2

Gene

ECE2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 4 (25 Nov 2008)
      Previous versions | rss
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    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

    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

    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: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:13275. ECE2.

    Subcellular locationi

    GO - Cellular componenti

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

    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

    ArrayExpressiO60344.
    BgeeiO60344.
    CleanExiHS_ECE2.
    GenevestigatoriO60344.

    Organism-specific databases

    HPAiHPA043346.

    Interactioni

    Protein-protein interaction databases

    BioGridi115067. 4 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 – 213
    Helixi23 – 297
    Turni30 – 356
    Helixi45 – 528
    Helixi53 – 553
    Beta strandi62 – 654
    Helixi72 – 787
    Beta strandi84 – 896
    Helixi91 – 10010
    Turni101 – 1033
    Beta strandi108 – 1114
    Beta strandi124 – 1318
    Helixi132 – 1365
    Turni137 – 1393
    Helixi148 – 16114
    Helixi167 – 1693
    Beta strandi170 – 18112
    Helixi203 – 2097
    Helixi212 – 2143
    Beta strandi216 – 2216
    Beta strandi229 – 2313
    Helixi232 – 2343
    Beta strandi236 – 2438
    Helixi249 – 2557

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiO60344.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 178178CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini200 – 883684LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei179 – 19921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    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.
    HOVERGENiHBG005554.
    InParanoidiO60344.
    KOiK01415.
    OMAiINTTWFL.
    OrthoDBiEOG7PZRWQ.
    PhylomeDBiO60344.
    TreeFamiTF315192.

    Family and domain databases

    Gene3Di3.40.390.10. 2 hits.
    3.40.50.150. 1 hit.
    InterProiIPR024079. MetalloPept_cat_dom.
    IPR013216. Methyltransf_11.
    IPR000718. Peptidase_M13.
    IPR018497. Peptidase_M13_C.
    IPR008753. Peptidase_M13_N.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PANTHERiPTHR11733. PTHR11733. 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. Align

    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

    MASPGAGRAP PELPERNCGY REVEYWDQRY QGAADSAPYD WFGDFSSFRA    50
    LLEPELRPED RILVLGCGNS ALSYELFLGG FPNVTSVDYS SVVVAAMQAR 100
    HAHVPQLRWE TMDVRKLDFP SASFDVVLEK GTLDALLAGE RDPWTVSSEG 150
    VHTVDQVLSE VGFQKGTRQL LGSRTQLELV LAGASLLLAA LLLGCLVALG 200
    VQYHRDPSHS TCLTEACIRV AGKILESLDR GVSPCEDFYQ FSCGGWIRRN 250
    PLPDGRSRWN TFNSLWDQNQ AILKHLLENT TFNSSSEAEQ KTQRFYLSCL 300
    QVERIEELGA QPLRDLIEKI GGWNITGPWD QDNFMEVLKA VAGTYRATPF 350
    FTVYISADSK SSNSNVIQVD QSGLFLPSRD YYLNRTANEK VLTAYLDYME 400
    ELGMLLGGRP TSTREQMQQV LELEIQLANI TVPQDQRRDE EKIYHKMSIS 450
    ELQALAPSMD WLEFLSFLLS PLELSDSEPV VVYGMDYLQQ VSELINRTEP 500
    SILNNYLIWN LVQKTTSSLD RRFESAQEKL LETLYGTKKS CVPRWQTCIS 550
    NTDDALGFAL GSLFVKATFD RQSKEIAEGM ISEIRTAFEE ALGQLVWMDE 600
    KTRQAAKEKA DAIYDMIGFP DFILEPKELD DVYDGYEISE DSFFQNMLNL 650
    YNFSAKVMAD QLRKPPSRDQ WSMTPQTVNA YYLPTKNEIV FPAGILQAPF 700
    YARNHPKALN FGGIGVVMGH ELTHAFDDQG REYDKEGNLR PWWQNESLAA 750
    FRNHTACMEE QYNQYQVNGE RLNGRQTLGE NIADNGGLKA AYNAYKAWLR 800
    KHGEEQQLPA VGLTNHQLFF VGFAQVWCSV RTPESSHEGL VTDPHSPARF 850
    RVLGTLSNSR DFLRHFGCPV GSPMNPGQLC EVW 883
    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.
    The sequence BAA25530.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS3255.1. [O60344-4 ]
    CCDS3256.2. [O60344-1 ]
    CCDS33899.1. [O60344-3 ]
    CCDS43179.1. [O60344-5 ]
    CCDS46969.1. [O60344-2 ]
    RefSeqi NP_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 ]
    UniGenei Hs.146161.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PXX X-ray 1.30 A 19-255 [» ]
    ProteinModelPortali O60344.
    SMRi O60344. Positions 19-161, 214-883.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115067. 4 interactions.
    IntActi O60344. 3 interactions.
    MINTi MINT-8417701.
    STRINGi 9606.ENSP00000384223.

    Chemistry

    BindingDBi O60344.
    ChEMBLi CHEMBL5890.

    Protein family/group databases

    MEROPSi M13.003.

    PTM databases

    PhosphoSitei O60344.

    Proteomic databases

    MaxQBi O60344.
    PaxDbi O60344.
    PRIDEi O60344.

    Protocols and materials databases

    DNASUi 9718.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324557 ; ENSP00000314295 ; ENSG00000145194 . [O60344-4 ]
    ENST00000357474 ; ENSP00000350066 ; ENSG00000145194 . [O60344-5 ]
    ENST00000359140 ; ENSP00000352052 ; ENSG00000145194 . [O60344-3 ]
    ENST00000402825 ; ENSP00000384223 ; ENSG00000145194 . [O60344-1 ]
    ENST00000404464 ; ENSP00000385846 ; ENSG00000145194 . [O60344-2 ]
    GeneIDi 9718.
    KEGGi hsa:9718.
    UCSCi uc003fnh.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

    CTDi 9718.
    GeneCardsi GC03P183967.
    H-InvDB HIX0003914.
    HGNCi HGNC:13275. ECE2.
    HPAi HPA043346.
    MIMi 610145. gene.
    neXtProti NX_O60344.
    PharmGKBi PA134886910.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3590.
    HOVERGENi HBG005554.
    InParanoidi O60344.
    KOi K01415.
    OMAi INTTWFL.
    OrthoDBi EOG7PZRWQ.
    PhylomeDBi O60344.
    TreeFami TF315192.

    Enzyme and pathway databases

    SABIO-RK O60344.

    Miscellaneous databases

    EvolutionaryTracei O60344.
    GenomeRNAii 9718.
    NextBioi 36537.
    PROi O60344.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60344.
    Bgeei O60344.
    CleanExi HS_ECE2.
    Genevestigatori O60344.

    Family and domain databases

    Gene3Di 3.40.390.10. 2 hits.
    3.40.50.150. 1 hit.
    InterProi IPR024079. MetalloPept_cat_dom.
    IPR013216. Methyltransf_11.
    IPR000718. Peptidase_M13.
    IPR018497. Peptidase_M13_C.
    IPR008753. Peptidase_M13_N.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    PANTHERi PTHR11733. PTHR11733. 1 hit.
    Pfami PF08241. Methyltransf_11. 1 hit.
    PF01431. Peptidase_M13. 1 hit.
    PF05649. Peptidase_M13_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00786. NEPRILYSIN.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 141 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