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E5RI53

- E5RI53_HUMAN

UniProt

E5RI53 - E5RI53_HUMAN

Protein
Submitted name:

Lipid-phosphate phosphatase

Gene

EPHX2

Organism
Homo sapiens (Human)
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli
  1. Functioni

    GO - Molecular functioni

    1. hydrolase activity Source: InterPro

    GO - Biological processi

    1. cholesterol homeostasis Source: Ensembl
    2. positive regulation of gene expression Source: Ensembl
    3. regulation of cholesterol metabolic process Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Submitted name:
    Lipid-phosphate phosphataseImported
    Gene namesi
    Name:EPHX2Imported
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:3402. EPHX2.

    Expressioni

    Gene expression databases

    ArrayExpressiE5RI53.
    BgeeiE5RI53.

    Structurei

    3D structure databases

    ProteinModelPortaliE5RI53.
    SMRiE5RI53. Positions 2-158.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Family and domain databases

    Gene3Di1.10.150.240. 1 hit.
    3.40.50.1000. 2 hits.
    InterProiIPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR023198. PGP_dom2.
    [Graphical view]
    PRINTSiPR00413. HADHALOGNASE.
    SUPFAMiSSF56784. SSF56784. 1 hit.

    Sequencei

    Sequence statusi: Fragment.

    E5RI53-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLRAAVFDL DGVLALPAVF GVLGRTEEAL ALPRGLLNDA FQKGGPEGAT    50
    TRLMKGEITL SQWIPLMEEN CRKCSETAKV CLPKNFSIKE IFDKAISARK 100
    INRPMLQAAL MLRKKGFTTA ILTNTWLDDR AERDGLAQLM CELKMHFDFL 150
    IESCQVGM 158
    Length:158
    Mass (Da):17,578
    Last modified:February 8, 2011 - v1
    Checksum:iAEC907FFEB2985D8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei158 – 1581Imported

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF311103 Genomic DNA. No translation available.

    Genome annotation databases

    EnsembliENST00000518328; ENSP00000430779; ENSG00000120915.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF311103 Genomic DNA. No translation available.

    3D structure databases

    ProteinModelPortali E5RI53.
    SMRi E5RI53. Positions 2-158.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000518328 ; ENSP00000430779 ; ENSG00000120915 .

    Organism-specific databases

    HGNCi HGNC:3402. EPHX2.
    GenAtlasi Search...

    Miscellaneous databases

    NextBioi 35498564.

    Gene expression databases

    ArrayExpressi E5RI53.
    Bgeei E5RI53.

    Family and domain databases

    Gene3Di 1.10.150.240. 1 hit.
    3.40.50.1000. 2 hits.
    InterProi IPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR023198. PGP_dom2.
    [Graphical view ]
    PRINTSi PR00413. HADHALOGNASE.
    SUPFAMi SSF56784. SSF56784. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Glockner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    4. Ensembl
      Submitted (JUL-2011) to UniProtKB
      Cited for: IDENTIFICATION.

    Entry informationi

    Entry nameiE5RI53_HUMAN
    AccessioniPrimary (citable) accession number: E5RI53
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 8, 2011
    Last sequence update: February 8, 2011
    Last modified: October 1, 2014
    This is version 24 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)
    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

    Caution

    The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3