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Q08426

- ECHP_HUMAN

UniProt

Q08426 - ECHP_HUMAN

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Protein
Peroxisomal bifunctional enzyme
Gene
EHHADH, ECHD
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 nitrogen By similarity
Sitei104 – 1041Important for catalytic activity By similarity
Sitei124 – 1241Important for catalytic activity By 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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 enzyme
PRO_0000109247Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381N6-succinyllysine By similarity
Modified residuei165 – 1651N6-acetyllysine; alternate1 Publication
Modified residuei165 – 1651N6-succinyllysine; alternate By similarity
Modified residuei171 – 1711N6-acetyllysine1 Publication
Modified residuei219 – 2191N6-acetyllysine; alternate By similarity
Modified residuei219 – 2191N6-succinyllysine; alternate By similarity
Modified residuei250 – 2501N6-acetyllysine By similarity
Modified residuei280 – 2801N6-succinyllysine By similarity
Modified residuei290 – 2901N6-succinyllysine By similarity
Modified residuei346 – 3461N6-acetyllysine1 Publication
Modified residuei350 – 3501N6-acetyllysine By similarity
Modified residuei464 – 4641N6-acetyllysine By similarity
Modified residuei532 – 5321N6-succinyllysine By similarity
Modified residuei577 – 5771N6-succinyllysine By similarity
Modified residuei584 – 5841N6-acetyllysine; alternate2 Publications
Modified residuei584 – 5841N6-succinyllysine; alternate By similarity
Modified residuei591 – 5911N6-acetyllysine; alternate By similarity
Modified residuei591 – 5911N6-succinyllysine; alternate By similarity
Modified residuei710 – 7101N6-acetyllysine; alternate By similarity
Modified residuei710 – 7101N6-succinyllysine; alternate By similarity
Modified residuei722 – 7221N6-succinyllysine By 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.1 Publication

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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 282282Enoyl-CoA hydratase / isomerase
Add
BLAST
Regioni283 – 5722903-hydroxyacyl-CoA dehydrogenase
Add
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.
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.

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

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.
VSP_042811Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti117 – 1171E → D in AAA53289. 1 Publication
Sequence conflicti656 – 6572WP → CA in AAA53289. 1 Publication
Sequence conflicti656 – 6572WP → CA in AAB19482. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 151 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

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