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E5RI53

- E5RI53_HUMAN

UniProt

E5RI53 - E5RI53_HUMAN

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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

GO - Biological processi

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

ArrayExpressiE5RI53.
BgeeiE5RI53.

Structurei

3D structure databases

ProteinModelPortaliE5RI53.
SMRiE5RI53. Positions 2-158.

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

Non-terminal residue

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

« 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 nameiE5RI53_HUMAN
AccessioniPrimary (citable) accession number: E5RI53
Entry historyi
Integrated into UniProtKB/TrEMBL: February 8, 2011
Last sequence update: February 8, 2011
Last modified: June 11, 2014
This is version 23 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

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