Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q08426

- ECHP_HUMAN

UniProt

Q08426 - ECHP_HUMAN

Protein

Peroxisomal bifunctional enzyme

Gene

EHHADH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (10 Feb 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.
    (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.
    (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

    Enzyme regulationi

    Enzyme activity enhanced by acetylation.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei101 – 1011Substrate; via amide nitrogenBy similarity
    Sitei104 – 1041Important for catalytic activityBy similarity
    Sitei124 – 1241Important for catalytic activityBy similarity

    GO - Molecular functioni

    1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB
    2. coenzyme binding Source: InterPro
    3. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-EC
    4. enoyl-CoA hydratase activity Source: UniProtKB
    5. enzyme binding Source: UniProtKB
    6. receptor binding Source: UniProtKB

    GO - Biological processi

    1. fatty acid beta-oxidation Source: UniProtKB
    2. internal protein amino acid acetylation Source: UniProtKB

    Keywords - Molecular functioni

    Isomerase, Lyase, Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03720-MONOMER.
    RETL1328306-WGS:GSTH-5129-MONOMER.
    SABIO-RKQ08426.
    UniPathwayiUPA00659.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal bifunctional enzyme
    Short name:
    PBE
    Short name:
    PBFE
    Including the following 2 domains:
    Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase (EC:4.2.1.17, EC:5.3.3.8)
    3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
    Gene namesi
    Name:EHHADH
    Synonyms:ECHD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:3247. EHHADH.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Ensembl
    3. intracellular membrane-bounded organelle Source: HPA
    4. mitochondrion Source: Ensembl
    5. nucleus Source: HPA
    6. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Involvement in diseasei

    Fanconi renotubular syndrome 3 (FRTS3) [MIM:615605]: A disease due to a generalized dysfunction of the proximal kidney tubule resulting in decreased solute and water reabsorption. Patients have polydipsia and polyuria with phosphaturia, glycosuria and aminoaciduria. They may develop hypophosphatemic rickets or osteomalacia, acidosis and a tendency toward dehydration. Some eventually develop renal insufficiency.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31E → K in FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells. 1 Publication
    VAR_070949

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi165 – 1651K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584. 1 Publication
    Mutagenesisi171 – 1711K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584. 1 Publication
    Mutagenesisi346 – 3461K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584. 1 Publication
    Mutagenesisi584 – 5841K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi615605. phenotype.
    Orphaneti300. Bifunctional enzyme deficiency.
    3337. Primary Fanconi syndrome.
    PharmGKBiPA27682.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 723723Peroxisomal bifunctional enzymePRO_0000109247Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381N6-succinyllysineBy similarity
    Modified residuei165 – 1651N6-acetyllysine; alternate1 Publication
    Modified residuei165 – 1651N6-succinyllysine; alternateBy similarity
    Modified residuei171 – 1711N6-acetyllysine1 Publication
    Modified residuei219 – 2191N6-acetyllysine; alternateBy similarity
    Modified residuei219 – 2191N6-succinyllysine; alternateBy similarity
    Modified residuei250 – 2501N6-acetyllysineBy similarity
    Modified residuei280 – 2801N6-succinyllysineBy similarity
    Modified residuei290 – 2901N6-succinyllysineBy similarity
    Modified residuei346 – 3461N6-acetyllysine1 Publication
    Modified residuei350 – 3501N6-acetyllysineBy similarity
    Modified residuei464 – 4641N6-acetyllysineBy similarity
    Modified residuei532 – 5321N6-succinyllysineBy similarity
    Modified residuei577 – 5771N6-succinyllysineBy similarity
    Modified residuei584 – 5841N6-acetyllysine; alternate2 Publications
    Modified residuei584 – 5841N6-succinyllysine; alternateBy similarity
    Modified residuei591 – 5911N6-acetyllysine; alternateBy similarity
    Modified residuei591 – 5911N6-succinyllysine; alternateBy similarity
    Modified residuei710 – 7101N6-acetyllysine; alternateBy similarity
    Modified residuei710 – 7101N6-succinyllysine; alternateBy similarity
    Modified residuei722 – 7221N6-succinyllysineBy similarity

    Post-translational modificationi

    Acetylated, leading to enhanced enzyme activity. Acetylation is enhanced by up to 80% after treatment either with trichostin A (TSA) or with nicotinamide (NAM) with highest increase on Lys-346. Acetylation and enzyme activity increased by about 1.5% on addition of fatty acids.2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ08426.
    PaxDbiQ08426.
    PRIDEiQ08426.

    PTM databases

    PhosphoSiteiQ08426.

    Expressioni

    Tissue specificityi

    Liver and kidney. Strongly expressed in the terminal segments of the proximal tubule. Lower amounts seen in the brain.2 Publications

    Gene expression databases

    ArrayExpressiQ08426.
    BgeeiQ08426.
    CleanExiHS_EHHADH.
    GenevestigatoriQ08426.

    Organism-specific databases

    HPAiHPA036401.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi108282. 2 interactions.
    IntActiQ08426. 4 interactions.
    STRINGi9606.ENSP00000231887.

    Structurei

    3D structure databases

    ProteinModelPortaliQ08426.
    SMRiQ08426. Positions 1-717.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 282282Enoyl-CoA hydratase / isomeraseAdd
    BLAST
    Regioni283 – 5722903-hydroxyacyl-CoA dehydrogenaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi721 – 7233Microbody targeting signal

    Sequence similaritiesi

    In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.Curated
    In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG1250.
    HOGENOMiHOG000261347.
    HOVERGENiHBG104990.
    InParanoidiQ08426.
    KOiK07514.
    OMAiLKMRKQH.
    OrthoDBiEOG725DH0.
    PhylomeDBiQ08426.
    TreeFamiTF316708.

    Family and domain databases

    Gene3Di1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 1 hit.
    InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR013328. DH_multihelical.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00725. 3HCDH. 2 hits.
    PF02737. 3HCDH_N. 1 hit.
    PF00378. ECH. 1 hit.
    [Graphical view]
    SUPFAMiSSF48179. SSF48179. 2 hits.
    SSF52096. SSF52096. 1 hit.
    PROSITEiPS00067. 3HCDH. 1 hit.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q08426-1) [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

    MAEYTRLHNA LALIRLRNPP VNAISTTLLR DIKEGLQKAV IDHTIKAIVI    50
    CGAEGKFSAG ADIRGFSAPR TFGLTLGHVV DEIQRNEKPV VAAIQGMAFG 100
    GGLELALGCH YRIAHAEAQV GLPEVTLGLL PGARGTQLLP RLTGVPAALD 150
    LITSGRRILA DEALKLGILD KVVNSDPVEE AIRFAQRVSD QPLESRRLCN 200
    KPIQSLPNMD SIFSEALLKM RRQHPGCLAQ EACVRAVQAA VQYPYEVGIK 250
    KEEELFLYLL QSGQARALQY AFFAERKANK WSTPSGASWK TASARPVSSV 300
    GVVGLGTMGR GIVISFARAR IPVIAVDSDK NQLATANKMI TSVLEKEASK 350
    MQQSGHPWSG PKPRLTSSVK ELGGVDLVIE AVFEEMSLKK QVFAELSAVC 400
    KPEAFLCTNT SALDVDEIAS STDRPHLVIG THFFSPAHVM KLLEVIPSQY 450
    SSPTTIATVM NLSKKIKKIG VVVGNCFGFV GNRMLNPYYN QAYFLLEEGS 500
    KPEEVDQVLE EFGFKMGPFR VSDLAGLDVG WKSRKGQGLT GPTLLPGTPA 550
    RKRGNRRYCP IPDVLCELGR FGQKTGKGWY QYDKPLGRIH KPDPWLSKFL 600
    SRYRKTHHIE PRTISQDEIL ERCLYSLINE AFRILGEGIA ASPEHIDVVY 650
    LHGYGWPRHK GGPMFYASTV GLPTVLEKLQ KYYRQNPDIP QLEPSDYLKK 700
    LASQGNPPLK EWQSLAGSPS SKL 723
    Length:723
    Mass (Da):79,495
    Last modified:February 10, 2009 - v3
    Checksum:iFC3B44B030A7BCBD
    GO
    Isoform 2 (identifier: Q08426-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-96: Missing.

    Show »
    Length:627
    Mass (Da):69,154
    Checksum:iF1F1A30F0E89ED98
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti117 – 1171E → D in AAA53289. (PubMed:8188243)Curated
    Sequence conflicti656 – 6572WP → CA in AAA53289. (PubMed:8188243)Curated
    Sequence conflicti656 – 6572WP → CA in AAB19482. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31E → K in FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells. 1 Publication
    VAR_070949
    Natural varianti40 – 401V → G.1 Publication
    Corresponds to variant rs1062551 [ dbSNP | Ensembl ].
    VAR_054329
    Natural varianti41 – 411I → R.1 Publication
    Corresponds to variant rs1062552 [ dbSNP | Ensembl ].
    VAR_054330
    Natural varianti75 – 751T → I.1 Publication
    Corresponds to variant rs1062553 [ dbSNP | Ensembl ].
    VAR_047132
    Natural varianti274 – 2741A → T.1 Publication
    Corresponds to variant rs2302819 [ dbSNP | Ensembl ].
    VAR_047133
    Natural varianti325 – 3251A → G.1 Publication
    Corresponds to variant rs1062555 [ dbSNP | Ensembl ].
    VAR_054331
    Natural varianti598 – 5981K → T.2 Publications
    Corresponds to variant rs1042437 [ dbSNP | Ensembl ].
    VAR_054332
    Natural varianti606 – 6061T → P.2 Publications
    Corresponds to variant rs1042438 [ dbSNP | Ensembl ].
    VAR_047134
    Natural varianti685 – 6851Q → K.
    Corresponds to variant rs11919970 [ dbSNP | Ensembl ].
    VAR_047135
    Natural varianti715 – 7151L → S.
    Corresponds to variant rs11927618 [ dbSNP | Ensembl ].
    VAR_047136

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9696Missing in isoform 2. 1 PublicationVSP_042811Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07077 mRNA. Translation: AAA53289.1.
    AJ427345
    , AJ427346, AJ427347, AJ427348, AJ427349, AJ427350, AJ427351 Genomic DNA. Translation: CAD22483.1.
    AK291798 mRNA. Translation: BAF84487.1.
    AK223460 mRNA. Translation: BAD97180.1.
    AK301521 mRNA. Translation: BAG63025.1.
    AC007934 Genomic DNA. No translation available.
    AC128680 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78229.1.
    CH471052 Genomic DNA. Translation: EAW78230.1.
    BC038948 mRNA. Translation: AAH38948.1.
    BC110460 mRNA. Translation: AAI10461.1.
    S50245 mRNA. Translation: AAB19482.1.
    CCDSiCCDS33901.1. [Q08426-1]
    CCDS54694.1. [Q08426-2]
    PIRiA49613.
    RefSeqiNP_001159887.1. NM_001166415.1. [Q08426-2]
    NP_001957.2. NM_001966.3. [Q08426-1]
    UniGeneiHs.429879.

    Genome annotation databases

    EnsembliENST00000231887; ENSP00000231887; ENSG00000113790. [Q08426-1]
    ENST00000456310; ENSP00000387746; ENSG00000113790. [Q08426-2]
    GeneIDi1962.
    KEGGihsa:1962.
    UCSCiuc003fpf.3. human. [Q08426-1]

    Polymorphism databases

    DMDMi223590229.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L07077 mRNA. Translation: AAA53289.1 .
    AJ427345
    , AJ427346 , AJ427347 , AJ427348 , AJ427349 , AJ427350 , AJ427351 Genomic DNA. Translation: CAD22483.1 .
    AK291798 mRNA. Translation: BAF84487.1 .
    AK223460 mRNA. Translation: BAD97180.1 .
    AK301521 mRNA. Translation: BAG63025.1 .
    AC007934 Genomic DNA. No translation available.
    AC128680 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78229.1 .
    CH471052 Genomic DNA. Translation: EAW78230.1 .
    BC038948 mRNA. Translation: AAH38948.1 .
    BC110460 mRNA. Translation: AAI10461.1 .
    S50245 mRNA. Translation: AAB19482.1 .
    CCDSi CCDS33901.1. [Q08426-1 ]
    CCDS54694.1. [Q08426-2 ]
    PIRi A49613.
    RefSeqi NP_001159887.1. NM_001166415.1. [Q08426-2 ]
    NP_001957.2. NM_001966.3. [Q08426-1 ]
    UniGenei Hs.429879.

    3D structure databases

    ProteinModelPortali Q08426.
    SMRi Q08426. Positions 1-717.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108282. 2 interactions.
    IntActi Q08426. 4 interactions.
    STRINGi 9606.ENSP00000231887.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei Q08426.

    Polymorphism databases

    DMDMi 223590229.

    Proteomic databases

    MaxQBi Q08426.
    PaxDbi Q08426.
    PRIDEi Q08426.

    Protocols and materials databases

    DNASUi 1962.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000231887 ; ENSP00000231887 ; ENSG00000113790 . [Q08426-1 ]
    ENST00000456310 ; ENSP00000387746 ; ENSG00000113790 . [Q08426-2 ]
    GeneIDi 1962.
    KEGGi hsa:1962.
    UCSCi uc003fpf.3. human. [Q08426-1 ]

    Organism-specific databases

    CTDi 1962.
    GeneCardsi GC03M184908.
    HGNCi HGNC:3247. EHHADH.
    HPAi HPA036401.
    MIMi 607037. gene.
    615605. phenotype.
    neXtProti NX_Q08426.
    Orphaneti 300. Bifunctional enzyme deficiency.
    3337. Primary Fanconi syndrome.
    PharmGKBi PA27682.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1250.
    HOGENOMi HOG000261347.
    HOVERGENi HBG104990.
    InParanoidi Q08426.
    KOi K07514.
    OMAi LKMRKQH.
    OrthoDBi EOG725DH0.
    PhylomeDBi Q08426.
    TreeFami TF316708.

    Enzyme and pathway databases

    UniPathwayi UPA00659 .
    BioCyci MetaCyc:HS03720-MONOMER.
    RETL1328306-WGS:GSTH-5129-MONOMER.
    SABIO-RK Q08426.

    Miscellaneous databases

    GenomeRNAii 1962.
    NextBioi 7961.
    PROi Q08426.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q08426.
    Bgeei Q08426.
    CleanExi HS_EHHADH.
    Genevestigatori Q08426.

    Family and domain databases

    Gene3Di 1.10.1040.10. 2 hits.
    3.40.50.720. 1 hit.
    3.90.226.10. 1 hit.
    InterProi IPR006180. 3-OHacyl-CoA_DH_CS.
    IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
    IPR006108. 3HC_DH_C.
    IPR008927. 6-PGluconate_DH_C-like.
    IPR029045. ClpP/crotonase-like_dom.
    IPR001753. Crotonase_core_superfam.
    IPR013328. DH_multihelical.
    IPR018376. Enoyl-CoA_hyd/isom_CS.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00725. 3HCDH. 2 hits.
    PF02737. 3HCDH_N. 1 hit.
    PF00378. ECH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48179. SSF48179. 2 hits.
    SSF52096. SSF52096. 1 hit.
    PROSITEi PS00067. 3HCDH. 1 hit.
    PS00166. ENOYL_COA_HYDRATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of the human peroxisomal enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme and localization to chromosome 3q26.3-3q28: a free left Alu Arm is inserted in the 3' noncoding region."
      Hoefler G., Forstner M., McGuinness M.C., Hulla W., Hiden M., Krisper P., Kenner L., Ried T., Lengauer C., Zechner R., Moser H.W., Chen G.L.
      Genomics 19:60-67(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANTS GLY-40; ARG-41; ILE-75; GLY-325; THR-598 AND PRO-606.
      Tissue: Liver.
    2. "Structural organization of gene for human peroxisomal enoyl-CoA hydratase/L-3-hydroxyacyl-CoA dehydrogenase: L-bifunctional enzyme (L-PBE)."
      Cherkaoui-Malki M., Surapureddi S., Yeldandi A.V., Rao S.M., Zhu Y., Reddy J.K.
      Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT THR-274.
      Tissue: Placenta.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Kidney.
    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].
    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] (ISOFORM 1).
      Tissue: Uterus.
    8. "Import of human bifunctional enzyme into peroxisomes of human hepatoma cells in vitro."
      Chen G.L., Balfe A., Erwa W., Hoefler G., Gaertner J., Aikawa J., Chen W.W.
      Biochem. Biophys. Res. Commun. 178:1084-1091(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 502-723 (ISOFORMS 1/2), VARIANTS THR-598 AND PRO-606.
      Tissue: Liver.
    9. "Peroxisomal beta-oxidation enzyme proteins in adrenoleukodystrophy: distinction between X-linked adrenoleukodystrophy and neonatal adrenoleukodystrophy."
      Chen W.W., Watkins P.A., Osumi T., Hashimoto T., Moser H.W.
      Proc. Natl. Acad. Sci. U.S.A. 84:1425-1428(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH PERIXOSOMAL DISORDERS.
    10. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-584, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: ACETYLATION AT LYS-165; LYS-171; LYS-346 AND LYS-584, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-165; LYS-171; LYS-346 AND LYS-584.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: VARIANT FRTS3 LYS-3, CHARACTERIZATION OF VARIANT FRTS3 LYS-3, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiECHP_HUMAN
    AccessioniPrimary (citable) accession number: Q08426
    Secondary accession number(s): A8K6Y3
    , B4DWG3, D3DNU0, Q58EZ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 152 of the entry and version 3 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

    Miscellaneous

    Absent in patients suffering with peroxisomal disorders such as Zellweger syndrome, neonatal adrenoleukodystrophy and infantile Refsum disease.

    Keywords - Technical termi

    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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3