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Q08426 (ECHP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal bifunctional enzyme

Short name=PBE
Short name=PBFE

Including the following 2 domains:

  1. Enoyl-CoA hydratase/3,2-trans-enoyl-CoA isomerase
    EC=4.2.1.17
    EC=5.3.3.8
  2. 3-hydroxyacyl-CoA dehydrogenase
    EC=1.1.1.35
Gene names
Name:EHHADH
Synonyms:ECHD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length723 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(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 regulation

Enzyme activity enhanced by acetylation. Ref.11

Pathway

Lipid metabolism; fatty acid beta-oxidation.

Subunit structure

Monomer.

Subcellular location

Peroxisome.

Tissue specificity

Liver and kidney. Strongly expressed in the terminal segments of the proximal tubule. Lower amounts seen in the brain. Ref.1 Ref.13

Post-translational modification

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. Ref.11

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Miscellaneous

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

Sequence similarities

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.

In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandNAD
   Molecular functionIsomerase
Lyase
Oxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid beta-oxidation

Non-traceable author statement Ref.1. Source: UniProtKB

internal protein amino acid acetylation

Inferred from direct assay Ref.11. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from electronic annotation. Source: Ensembl

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

peroxisome

Inferred from direct assay Ref.8PubMed 2895531PubMed 9053548. Source: UniProtKB

   Molecular_function3-hydroxyacyl-CoA dehydrogenase activity

Non-traceable author statement Ref.1. Source: UniProtKB

coenzyme binding

Inferred from electronic annotation. Source: InterPro

dodecenoyl-CoA delta-isomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

enoyl-CoA hydratase activity

Non-traceable author statement Ref.1. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 16781659. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q08426-1)

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.
Isoform 2 (identifier: Q08426-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 723723Peroxisomal bifunctional enzyme
PRO_0000109247

Regions

Region1 – 282282Enoyl-CoA hydratase / isomerase
Region283 – 5722903-hydroxyacyl-CoA dehydrogenase
Motif721 – 7233Microbody targeting signal

Sites

Binding site1011Substrate; via amide nitrogen By similarity
Site1041Important for catalytic activity By similarity
Site1241Important for catalytic activity By similarity

Amino acid modifications

Modified residue381N6-succinyllysine By similarity
Modified residue1651N6-acetyllysine; alternate Ref.11
Modified residue1651N6-succinyllysine; alternate By similarity
Modified residue1711N6-acetyllysine Ref.11
Modified residue2191N6-acetyllysine; alternate By similarity
Modified residue2191N6-succinyllysine; alternate By similarity
Modified residue2501N6-acetyllysine By similarity
Modified residue2801N6-succinyllysine By similarity
Modified residue2901N6-succinyllysine By similarity
Modified residue3461N6-acetyllysine Ref.11
Modified residue3501N6-acetyllysine By similarity
Modified residue4641N6-acetyllysine By similarity
Modified residue5321N6-succinyllysine By similarity
Modified residue5771N6-succinyllysine By similarity
Modified residue5841N6-acetyllysine; alternate Ref.10 Ref.11
Modified residue5841N6-succinyllysine; alternate By similarity
Modified residue5911N6-acetyllysine; alternate By similarity
Modified residue5911N6-succinyllysine; alternate By similarity
Modified residue7101N6-acetyllysine; alternate By similarity
Modified residue7101N6-succinyllysine; alternate By similarity
Modified residue7221N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 9696Missing in isoform 2.
VSP_042811
Natural variant31E → 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. Ref.13
VAR_070949
Natural variant401V → G. Ref.1
Corresponds to variant rs1062551 [ dbSNP | Ensembl ].
VAR_054329
Natural variant411I → R. Ref.1
Corresponds to variant rs1062552 [ dbSNP | Ensembl ].
VAR_054330
Natural variant751T → I. Ref.1
Corresponds to variant rs1062553 [ dbSNP | Ensembl ].
VAR_047132
Natural variant2741A → T. Ref.3
Corresponds to variant rs2302819 [ dbSNP | Ensembl ].
VAR_047133
Natural variant3251A → G. Ref.1
Corresponds to variant rs1062555 [ dbSNP | Ensembl ].
VAR_054331
Natural variant5981K → T. Ref.1 Ref.8
Corresponds to variant rs1042437 [ dbSNP | Ensembl ].
VAR_054332
Natural variant6061T → P. Ref.1 Ref.8
Corresponds to variant rs1042438 [ dbSNP | Ensembl ].
VAR_047134
Natural variant6851Q → K.
Corresponds to variant rs11919970 [ dbSNP | Ensembl ].
VAR_047135
Natural variant7151L → S.
Corresponds to variant rs11927618 [ dbSNP | Ensembl ].
VAR_047136

Experimental info

Mutagenesis1651K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584. Ref.11
Mutagenesis1711K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584. Ref.11
Mutagenesis3461K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584. Ref.11
Mutagenesis5841K → Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346. Ref.11
Sequence conflict1171E → D in AAA53289. Ref.1
Sequence conflict656 – 6572WP → CA in AAA53289. Ref.1
Sequence conflict656 – 6572WP → CA in AAB19482. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 10, 2009. Version 3.
Checksum: FC3B44B030A7BCBD

FASTA72379,495
        10         20         30         40         50         60 
MAEYTRLHNA LALIRLRNPP VNAISTTLLR DIKEGLQKAV IDHTIKAIVI CGAEGKFSAG 

        70         80         90        100        110        120 
ADIRGFSAPR TFGLTLGHVV DEIQRNEKPV VAAIQGMAFG GGLELALGCH YRIAHAEAQV 

       130        140        150        160        170        180 
GLPEVTLGLL PGARGTQLLP RLTGVPAALD LITSGRRILA DEALKLGILD KVVNSDPVEE 

       190        200        210        220        230        240 
AIRFAQRVSD QPLESRRLCN KPIQSLPNMD SIFSEALLKM RRQHPGCLAQ EACVRAVQAA 

       250        260        270        280        290        300 
VQYPYEVGIK KEEELFLYLL QSGQARALQY AFFAERKANK WSTPSGASWK TASARPVSSV 

       310        320        330        340        350        360 
GVVGLGTMGR GIVISFARAR IPVIAVDSDK NQLATANKMI TSVLEKEASK MQQSGHPWSG 

       370        380        390        400        410        420 
PKPRLTSSVK ELGGVDLVIE AVFEEMSLKK QVFAELSAVC KPEAFLCTNT SALDVDEIAS 

       430        440        450        460        470        480 
STDRPHLVIG THFFSPAHVM KLLEVIPSQY SSPTTIATVM NLSKKIKKIG VVVGNCFGFV 

       490        500        510        520        530        540 
GNRMLNPYYN QAYFLLEEGS KPEEVDQVLE EFGFKMGPFR VSDLAGLDVG WKSRKGQGLT 

       550        560        570        580        590        600 
GPTLLPGTPA RKRGNRRYCP IPDVLCELGR FGQKTGKGWY QYDKPLGRIH KPDPWLSKFL 

       610        620        630        640        650        660 
SRYRKTHHIE PRTISQDEIL ERCLYSLINE AFRILGEGIA ASPEHIDVVY LHGYGWPRHK 

       670        680        690        700        710        720 
GGPMFYASTV GLPTVLEKLQ KYYRQNPDIP QLEPSDYLKK LASQGNPPLK EWQSLAGSPS 


SKL 

« Hide

Isoform 2 [UniParc].

Checksum: F1F1A30F0E89ED98
Show »

FASTA62769,154

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Regulation of cellular metabolism by protein lysine acetylation."
Zhao S., Xu W., Jiang W., Yu W., Lin Y., Zhang T., Yao J., Zhou L., Zeng Y., Li H., Li Y., Shi J., An W., Hancock S.M., He F., Qin L., Chin J., Yang P. expand/collapse author list , Chen X., Lei Q., Xiong Y., Guan K.L.
Science 327:1000-1004(2010) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Mistargeting of peroxisomal EHHADH and inherited renal Fanconi's syndrome."
Klootwijk E.D., Reichold M., Helip-Wooley A., Tolaymat A., Broeker C., Robinette S.L., Reinders J., Peindl D., Renner K., Eberhart K., Assmann N., Oefner P.J., Dettmer K., Sterner C., Schroeder J., Zorger N., Witzgall R., Reinhold S.W. expand/collapse author list , Stanescu H.C., Bockenhauer D., Jaureguiberry G., Courtneidge H., Hall A.M., Wijeyesekera A.D., Holmes E., Nicholson J.K., O'Brien K., Bernardini I., Krasnewich D.M., Arcos-Burgos M., Izumi Y., Nonoguchi H., Jia Y., Reddy J.K., Ilyas M., Unwin R.J., Gahl W.A., Warth R., Kleta R.
N. Engl. J. Med. 370:129-138(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FRTS3 LYS-3, CHARACTERIZATION OF VARIANT FRTS3 LYS-3, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07077 mRNA. Translation: AAA53289.1.
AJ427345 expand/collapse EMBL AC list , 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.
CCDSCCDS33901.1. [Q08426-1]
CCDS54694.1. [Q08426-2]
PIRA49613.
RefSeqNP_001159887.1. NM_001166415.1. [Q08426-2]
NP_001957.2. NM_001966.3. [Q08426-1]
UniGeneHs.429879.

3D structure databases

ProteinModelPortalQ08426.
SMRQ08426. Positions 1-717.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108282. 2 interactions.
IntActQ08426. 4 interactions.
STRING9606.ENSP00000231887.

Chemistry

DrugBankDB00157. NADH.

PTM databases

PhosphoSiteQ08426.

Polymorphism databases

DMDM223590229.

Proteomic databases

MaxQBQ08426.
PaxDbQ08426.
PRIDEQ08426.

Protocols and materials databases

DNASU1962.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000231887; ENSP00000231887; ENSG00000113790. [Q08426-1]
ENST00000456310; ENSP00000387746; ENSG00000113790. [Q08426-2]
GeneID1962.
KEGGhsa:1962.
UCSCuc003fpf.3. human. [Q08426-1]

Organism-specific databases

CTD1962.
GeneCardsGC03M184908.
HGNCHGNC:3247. EHHADH.
HPAHPA036401.
MIM607037. gene.
615605. phenotype.
neXtProtNX_Q08426.
Orphanet300. Bifunctional enzyme deficiency.
3337. Primary Fanconi syndrome.
PharmGKBPA27682.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1250.
HOGENOMHOG000261347.
HOVERGENHBG104990.
InParanoidQ08426.
KOK07514.
OMALKMRKQH.
OrthoDBEOG725DH0.
PhylomeDBQ08426.
TreeFamTF316708.

Enzyme and pathway databases

BioCycMetaCyc:HS03720-MONOMER.
RETL1328306-WGS:GSTH-5129-MONOMER.
SABIO-RKQ08426.
UniPathwayUPA00659.

Gene expression databases

ArrayExpressQ08426.
BgeeQ08426.
CleanExHS_EHHADH.
GenevestigatorQ08426.

Family and domain databases

Gene3D1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProIPR006180. 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]
PfamPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
PROSITEPS00067. 3HCDH. 1 hit.
PS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi1962.
NextBio7961.
PROQ08426.
SOURCESearch...

Entry information

Entry nameECHP_HUMAN
AccessionPrimary (citable) accession number: Q08426
Secondary accession number(s): A8K6Y3 expand/collapse secondary AC list , B4DWG3, D3DNU0, Q58EZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: February 10, 2009
Last modified: July 9, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM