SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

E5RFU2

- E5RFU2_HUMAN

UniProt

E5RFU2 - E5RFU2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

Functioni

GO - Molecular functioni

  1. hydrolase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    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

    ArrayExpressiE5RFU2.
    BgeeiE5RFU2.

    Structurei

    3D structure databases

    ProteinModelPortaliE5RFU2.
    SMRiE5RFU2. Positions 2-516.

    Family & Domainsi

    Family and domain databases

    Gene3Di1.10.150.240. 1 hit.
    3.40.50.1000. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR011945. HAD-SF_ppase_IA/epoxid_hydro_N.
    IPR023198. PGP_dom2.
    [Graphical view]
    PfamiPF00561. Abhydrolase_1. 1 hit.
    PF13419. HAD_2. 1 hit.
    [Graphical view]
    PRINTSiPR00111. ABHYDROLASE.
    PR00413. HADHALOGNASE.
    SUPFAMiSSF53474. SSF53474. 1 hit.
    SSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR02247. HAD-1A3-hyp. 1 hit.
    TIGR01509. HAD-SF-IA-v3. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    E5RFU2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLRAAVFDL DGVLALPAVF GVLGRTEEAL ALPRGLLNDA FQKGGPEGAT    50
    TRLMKGEITL SQWIPLMEEN CRKCSETAKV CLPKNFSIKE IFDKAISARK 100
    INRPMLQAAL MLRKKGFTTA ILTNTWLDDR AERDGLAQLM CELKMHFDFL 150
    IESCQVGMVK PEPQIYKFLL DTLKASPSEV VFLDDIGANL KPARDLGMVT 200
    ILVQDTDTAL KELEKVTGIQ LLNTPAPLPT SCNPSDMSHG YVTVKIPALA 250
    QAGYRVLAMD MKGYGESSAP PEIEEYCMEV LCKEMVTFLD KLGLSQAVFI 300
    GHDWGGMLVW YMALFYPERV RAVASLNTPF IPANPNMSPL ESIKANPVFD 350
    YQLYFQEPGV AEAELEQNLS RTFKSLFRAS DESVLSMHKV CEAGGLFVNS 400
    PEEPSLSRMV TEEEIQFYVQ QFKKSGFRGP LNWYRNMERN WKWACKSLGR 450
    KILIPALMVT AEKDFVLVPQ MSQHMEDWIP HLKRGHIEDC GHWTQMDKPT 500
    EVNQILIKWL DSDARNPPVV SKM 523
    Length:523
    Mass (Da):58,855
    Last modified:February 8, 2011 - v1
    Checksum:iDD9880A21053CCB3
    GO

    Sequence databases

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

    Genome annotation databases

    EnsembliENST00000518379; ENSP00000427956; ENSG00000120915.

    Cross-referencesi

    Sequence databases

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

    3D structure databases

    ProteinModelPortali E5RFU2.
    SMRi E5RFU2. Positions 2-516.
    ModBasei Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000518379 ; ENSP00000427956 ; ENSG00000120915 .

    Organism-specific databases

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

    Miscellaneous databases

    NextBioi 35497854.

    Gene expression databases

    ArrayExpressi E5RFU2.
    Bgeei E5RFU2.

    Family and domain databases

    Gene3Di 1.10.150.240. 1 hit.
    3.40.50.1000. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR023214. HAD-like_dom.
    IPR006439. HAD-SF_hydro_IA.
    IPR011945. HAD-SF_ppase_IA/epoxid_hydro_N.
    IPR023198. PGP_dom2.
    [Graphical view ]
    Pfami PF00561. Abhydrolase_1. 1 hit.
    PF13419. HAD_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00111. ABHYDROLASE.
    PR00413. HADHALOGNASE.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    SSF56784. SSF56784. 1 hit.
    TIGRFAMsi TIGR02247. HAD-1A3-hyp. 1 hit.
    TIGR01509. HAD-SF-IA-v3. 1 hit.
    ProtoNeti Search...

    Publicationsi

    « Hide 'large scale' publications
    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 nameiE5RFU2_HUMAN
    AccessioniPrimary (citable) accession number: E5RFU2
    Entry historyi
    Integrated into UniProtKB/TrEMBL: February 8, 2011
    Last sequence update: February 8, 2011
    Last modified: June 11, 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 proteome

    External Data

    Dasty 3

    Similar proteinsi