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Q15067

- ACOX1_HUMAN

UniProt

Q15067 - ACOX1_HUMAN

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Protein

Peroxisomal acyl-coenzyme A oxidase 1

Gene

ACOX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs. Isoform 1 shows highest activity against medium-chain fatty acyl-CoAs and activity decreases with increasing chain length. Isoform 2 is active against a much broader range of substrates and shows activity towards very long-chain acyl-CoAs. Isoform 2 is twice as active as isoform 1 against 16-hydroxy-palmitoyl-CoA and is 25% more active against 1,16-hexadecanodioyl-CoA.2 Publications

Catalytic activityi

Acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2.

Cofactori

FAD.1 Publication

Kineticsi

  1. KM=73 µM for palmitoyl-CoA (isoform 1)1 Publication
  2. KM=90 µM for palmitoyl-CoA (isoform 2)1 Publication

pH dependencei

Optimum pH is 8.5 for isoform 1 and 7.5-8.5 for isoform 2.1 Publication

Temperature dependencei

Optimum temperature for isoform 1 at pH 7.5 is 40 degrees Celsius with no activity at 50 degrees Celsius. Optimum temperature for isoform 2 at pH 7.5 is 47.5 degrees Celsius with 57% activity retained at 50 degrees Celsius.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391FADBy similarity
Binding sitei178 – 1781FAD; via amide nitrogenBy similarity
Active sitei421 – 4211Proton acceptorBy similarity

GO - Molecular functioni

  1. acyl-CoA dehydrogenase activity Source: InterPro
  2. acyl-CoA oxidase activity Source: UniProtKB
  3. FAD binding Source: UniProtKB
  4. fatty acid binding Source: Ensembl
  5. flavin adenine dinucleotide binding Source: InterPro
  6. palmitoyl-CoA oxidase activity Source: UniProtKB
  7. PDZ domain binding Source: MGI
  8. protein N-terminus binding Source: UniProtKB
  9. receptor binding Source: UniProtKB

GO - Biological processi

  1. alpha-linolenic acid metabolic process Source: Reactome
  2. cellular lipid metabolic process Source: Reactome
  3. fatty acid beta-oxidation using acyl-CoA oxidase Source: BHF-UCL
  4. fatty acid oxidation Source: UniProtKB
  5. generation of precursor metabolites and energy Source: UniProtKB
  6. lipid homeostasis Source: UniProtKB
  7. lipid metabolic process Source: UniProtKB
  8. peroxisome fission Source: UniProtKB
  9. positive regulation of cholesterol homeostasis Source: UniProtKB
  10. prostaglandin metabolic process Source: UniProtKB
  11. small molecule metabolic process Source: Reactome
  12. spermatogenesis Source: Ensembl
  13. unsaturated fatty acid metabolic process Source: Reactome
  14. very long-chain fatty acid metabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:HS08589-MONOMER.
ReactomeiREACT_116145. PPARA activates gene expression.
REACT_121147. alpha-linolenic acid (ALA) metabolism.
REACT_17062. Beta-oxidation of very long chain fatty acids.
SABIO-RKQ15067.
UniPathwayiUPA00661.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal acyl-coenzyme A oxidase 1 (EC:1.3.3.6)
Short name:
AOX
Alternative name(s):
Palmitoyl-CoA oxidase
Straight-chain acyl-CoA oxidase
Short name:
SCOX
Gene namesi
Name:ACOX1
Synonyms:ACOX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:119. ACOX1.

Subcellular locationi

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. mitochondrion Source: Ensembl
  3. peroxisomal matrix Source: Reactome
  4. peroxisomal membrane Source: Ensembl
  5. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Involvement in diseasei

Adrenoleukodystrophy, pseudoneonatal (Pseudo-NALD) [MIM:264470]: A peroxisomal single-enzyme disorder of fatty acid beta-oxidation, resulting in clinical manifestations that remind neonatal adrenoleukodystrophy. Clinical features include mental retardation, leukodystrophy, seizures, mild hepatomegaly, hearing deficit. Pseudo-NALD is characterized by increased plasma levels of very-long chain fatty acids, due to decreased or absent peroxisome acyl-CoA oxidase activity. Peroxisomes are intact and functioning.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi264470. phenotype.
Orphaneti2971. Peroxisomal acyl-CoA oxidase deficiency.
PharmGKBiPA21.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 660660Peroxisomal acyl-coenzyme A oxidase 1PRO_0000204677Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261Phosphoserine2 Publications
Modified residuei89 – 891N6-succinyllysineBy similarity
Modified residuei90 – 901N6-succinyllysineBy similarity
Modified residuei216 – 2161N6-acetyllysineBy similarity
Modified residuei241 – 2411N6-succinyllysineBy similarity
Modified residuei255 – 2551N6-acetyllysine1 Publication
Modified residuei267 – 2671N6-acetyllysine1 Publication
Modified residuei272 – 2721N6-acetyllysineBy similarity
Modified residuei349 – 3491N6-succinyllysineBy similarity
Modified residuei437 – 4371N6-acetyllysine; alternate1 Publication
Modified residuei437 – 4371N6-succinyllysine; alternateBy similarity
Modified residuei446 – 4461N6-acetyllysine; alternateBy similarity
Modified residuei446 – 4461N6-succinyllysine; alternateBy similarity
Modified residuei500 – 5001N6-acetyllysine1 Publication
Modified residuei504 – 5041N6-acetyllysine1 Publication
Modified residuei512 – 5121N6-acetyllysine; alternateBy similarity
Modified residuei512 – 5121N6-succinyllysine; alternateBy similarity
Modified residuei542 – 5421N6-succinyllysineBy similarity
Modified residuei637 – 6371N6-acetyllysine; alternateBy similarity
Modified residuei637 – 6371N6-succinyllysine; alternateBy similarity
Modified residuei643 – 6431N6-succinyllysineBy similarity
Modified residuei651 – 6511N6-acetyllysineBy similarity
Modified residuei654 – 6541N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15067.
PaxDbiQ15067.
PeptideAtlasiQ15067.
PRIDEiQ15067.

PTM databases

PhosphoSiteiQ15067.

Expressioni

Tissue specificityi

Widely expressed with highest levels of isoform 1 and isoform 2 detected in testis. Isoform 1 is expressed at higher levels than isoform 2 in liver and kidney while isoform 2 levels are higher in brain, lung, muscle, white adipose tissue and testis. Levels are almost equal in heart.2 Publications

Gene expression databases

BgeeiQ15067.
CleanExiHS_ACOX1.
ExpressionAtlasiQ15067. baseline and differential.
GenevestigatoriQ15067.

Organism-specific databases

HPAiCAB021094.
HPA021192.
HPA021195.
HPA028759.

Interactioni

Protein-protein interaction databases

BioGridi106567. 18 interactions.
IntActiQ15067. 4 interactions.
MINTiMINT-4717708.
STRINGi9606.ENSP00000293217.

Structurei

3D structure databases

ProteinModelPortaliQ15067.
SMRiQ15067. Positions 1-654.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi658 – 6603Microbody targeting signal

Sequence similaritiesi

Belongs to the acyl-CoA oxidase family.Curated

Phylogenomic databases

eggNOGiCOG1960.
GeneTreeiENSGT00530000062919.
HOVERGENiHBG050451.
InParanoidiQ15067.
KOiK00232.
OMAiVHESYKH.
OrthoDBiEOG7D59MV.
PhylomeDBiQ15067.
TreeFamiTF300672.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProiIPR029320. Acyl-CoA_ox_N.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR012258. Acyl-CoA_oxidase.
IPR002655. Acyl-CoA_oxidase_C.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF01756. ACOX. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF14749. Acyl-CoA_ox_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000168. Acyl-CoA_oxidase. 1 hit.
SUPFAMiSSF47203. SSF47203. 2 hits.
SSF56645. SSF56645. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15067) [UniParc]FASTAAdd to Basket

Also known as: ACOX1a, SCOX-exon 3I

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

        10         20         30         40         50
MNPDLRRERD SASFNPELLT HILDGSPEKT RRRREIENMI LNDPDFQHED
60 70 80 90 100
LNFLTRSQRY EVAVRKSAIM VKKMREFGIA DPDEIMWFKK LHLVNFVEPV
110 120 130 140 150
GLNYSMFIPT LLNQGTTAQK EKWLLSSKGL QIIGTYAQTE MGHGTHLRGL
160 170 180 190 200
ETTATYDPET QEFILNSPTV TSIKWWPGGL GKTSNHAIVL AQLITKGKCY
210 220 230 240 250
GLHAFIVPIR EIGTHKPLPG ITVGDIGPKF GYDEIDNGYL KMDNHRIPRE
260 270 280 290 300
NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGEAA RALSKACTIA
310 320 330 340 350
IRYSAVRHQS EIKPGEPEPQ ILDFQTQQYK LFPLLATAYA FQFVGAYMKE
360 370 380 390 400
TYHRINEGIG QGDLSELPEL HALTAGLKAF TSWTANTGIE ACRMACGGHG
410 420 430 440 450
YSHCSGLPNI YVNFTPSCTF EGENTVMMLQ TARFLMKSYD QVHSGKLVCG
460 470 480 490 500
MVSYLNDLPS QRIQPQQVAV WPTMVDINSP ESLTEAYKLR AARLVEIAAK
510 520 530 540 550
NLQKEVIHRK SKEVAWNLTS VDLVRASEAH CHYVVVKLFS EKLLKIQDKA
560 570 580 590 600
IQAVLRSLCL LYSLYGISQN AGDFLQGSIM TEPQITQVNQ RVKELLTLIR
610 620 630 640 650
SDAVALVDAF DFQDVTLGSV LGRYDGNVYE NLFEWAKNSP LNKAEVHESY
660
KHLKSLQSKL
Length:660
Mass (Da):74,424
Last modified:February 20, 2007 - v3
Checksum:iD713768A47374EA1
GO
Isoform 2 (identifier: Q15067-2) [UniParc]FASTAAdd to Basket

Also known as: ACOX1b, SCOX-exon 3II

The sequence of this isoform differs from the canonical sequence as follows:
     90-131: KLHLVNFVEP...KWLLSSKGLQ → NFVHRGRPEP...RFFMPAWNLE

Show »
Length:660
Mass (Da):74,668
Checksum:i761C97B5043F9068
GO
Isoform 3 (identifier: Q15067-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: Missing.
     90-131: KLHLVNFVEP...KWLLSSKGLQ → NFVHRGRPEP...RFFMPAWNLE

Note: No experimental confirmation available.

Show »
Length:622
Mass (Da):70,136
Checksum:iFE52A881C050EB78
GO

Sequence cautioni

The sequence CAD97622.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271P → L in CAA50574. (PubMed:8040306)Curated
Sequence conflicti80 – 801A → R in CAA50574. (PubMed:8040306)Curated
Sequence conflicti84 – 841E → D in CAD97622. (PubMed:17974005)Curated
Sequence conflicti119 – 1191Q → E in AAB30019. (PubMed:8117268)Curated
Sequence conflicti200 – 2001Y → H in AAA18595. (PubMed:7876265)Curated
Sequence conflicti212 – 2132IG → NR in AAA19113. (PubMed:8159712)Curated
Sequence conflicti212 – 2132IG → NR in AAA19114. (PubMed:8159712)Curated
Sequence conflicti212 – 2132IG → NR in AAA18595. (PubMed:7876265)Curated
Sequence conflicti264 – 2641T → P in AAA19113. (PubMed:8159712)Curated
Sequence conflicti264 – 2641T → P in AAA19114. (PubMed:8159712)Curated
Sequence conflicti264 – 2641T → P in AAA18595. (PubMed:7876265)Curated
Sequence conflicti332 – 3321F → L in AAA18595. (PubMed:7876265)Curated
Sequence conflicti449 – 4491C → R in AAA18595. (PubMed:7876265)Curated
Sequence conflicti490 – 4901R → L in BAF85654. (PubMed:14702039)Curated
Sequence conflicti531 – 5311C → L in AAA19113. (PubMed:8159712)Curated
Sequence conflicti531 – 5311C → L in AAA19114. (PubMed:8159712)Curated
Sequence conflicti531 – 5311C → L in AAA18595. (PubMed:7876265)Curated
Sequence conflicti534 – 5352VV → GL in AAA19113. (PubMed:8159712)Curated
Sequence conflicti534 – 5352VV → GL in AAA19114. (PubMed:8159712)Curated
Sequence conflicti534 – 5352VV → GL in AAA18595. (PubMed:7876265)Curated
Sequence conflicti615 – 6151V → A in CAA50574. (PubMed:8040306)Curated
Sequence conflicti650 – 6501Y → YH in AAB30019. (PubMed:8117268)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti64 – 641Missing in pseudo-NALD. 1 Publication
VAR_067040
Natural varianti101 – 1011G → S.
Corresponds to variant rs3744032 [ dbSNP | Ensembl ].
VAR_048182
Natural varianti153 – 1531T → I.1 Publication
Corresponds to variant rs17855420 [ dbSNP | Ensembl ].
VAR_030619
Natural varianti178 – 1781G → C in pseudo-NALD. 2 Publications
VAR_025789
Natural varianti184 – 1841S → L in pseudo-NALD. 1 Publication
VAR_067041
Natural varianti231 – 2311G → V in pseudo-NALD. 1 Publication
VAR_067042
Natural varianti278 – 2781M → V in pseudo-NALD. 2 Publications
VAR_025790
Natural varianti309 – 3091Q → R in pseudo-NALD. 1 Publication
VAR_067043
Natural varianti310 – 3101S → P in pseudo-NALD. 1 Publication
VAR_067044
Natural varianti312 – 3121I → M.5 Publications
Corresponds to variant rs1135640 [ dbSNP | Ensembl ].
VAR_021529

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3838Missing in isoform 3. 1 PublicationVSP_046129Add
BLAST
Alternative sequencei90 – 13142KLHLV…SKGLQ → NFVHRGRPEPLDLHLGMFLP TLLHQATAEQQERFFMPAWN LE in isoform 2 and isoform 3. 4 PublicationsVSP_000146Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U03268
, U03254, U03255, U03256, U03258, U03259, U03260, U03261, U03263, U03264, U03265, U03266, U03267 Genomic DNA. Translation: AAA19113.1.
U03268
, U03254, U03255, U03257, U03258, U03259, U03260, U03261, U03263, U03264, U03265, U03266, U03267 Genomic DNA. Translation: AAA19114.1.
U07866 mRNA. Translation: AAA18595.1.
X71440 mRNA. Translation: CAA50574.1.
S69189 mRNA. Translation: AAB30019.2.
AK291793 mRNA. Translation: BAF84482.1.
AK292965 mRNA. Translation: BAF85654.1.
AK296409 mRNA. Translation: BAG59073.1.
BX537380 mRNA. Translation: CAD97622.1. Different initiation.
AC040980 Genomic DNA. No translation available.
AC087289 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89351.1.
BC008767 mRNA. Translation: AAH08767.1.
BC010425 mRNA. Translation: AAH10425.1.
CCDSiCCDS11734.1. [Q15067-2]
CCDS11735.1. [Q15067-1]
PIRiA54942.
B54942.
I38095.
RefSeqiNP_001171968.1. NM_001185039.1. [Q15067-3]
NP_004026.2. NM_004035.6. [Q15067-2]
NP_009223.2. NM_007292.5. [Q15067-1]
UniGeneiHs.464137.

Genome annotation databases

EnsembliENST00000293217; ENSP00000293217; ENSG00000161533. [Q15067-2]
ENST00000301608; ENSP00000301608; ENSG00000161533. [Q15067-1]
GeneIDi51.
KEGGihsa:51.
UCSCiuc002jqe.3. human. [Q15067-2]
uc002jqf.3. human. [Q15067-1]

Polymorphism databases

DMDMi126302511.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U03268
, U03254 , U03255 , U03256 , U03258 , U03259 , U03260 , U03261 , U03263 , U03264 , U03265 , U03266 , U03267 Genomic DNA. Translation: AAA19113.1 .
U03268
, U03254 , U03255 , U03257 , U03258 , U03259 , U03260 , U03261 , U03263 , U03264 , U03265 , U03266 , U03267 Genomic DNA. Translation: AAA19114.1 .
U07866 mRNA. Translation: AAA18595.1 .
X71440 mRNA. Translation: CAA50574.1 .
S69189 mRNA. Translation: AAB30019.2 .
AK291793 mRNA. Translation: BAF84482.1 .
AK292965 mRNA. Translation: BAF85654.1 .
AK296409 mRNA. Translation: BAG59073.1 .
BX537380 mRNA. Translation: CAD97622.1 . Different initiation.
AC040980 Genomic DNA. No translation available.
AC087289 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89351.1 .
BC008767 mRNA. Translation: AAH08767.1 .
BC010425 mRNA. Translation: AAH10425.1 .
CCDSi CCDS11734.1. [Q15067-2 ]
CCDS11735.1. [Q15067-1 ]
PIRi A54942.
B54942.
I38095.
RefSeqi NP_001171968.1. NM_001185039.1. [Q15067-3 ]
NP_004026.2. NM_004035.6. [Q15067-2 ]
NP_009223.2. NM_007292.5. [Q15067-1 ]
UniGenei Hs.464137.

3D structure databases

ProteinModelPortali Q15067.
SMRi Q15067. Positions 1-654.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106567. 18 interactions.
IntActi Q15067. 4 interactions.
MINTi MINT-4717708.
STRINGi 9606.ENSP00000293217.

Chemistry

DrugBanki DB03147. Flavin adenine dinucleotide.

PTM databases

PhosphoSitei Q15067.

Polymorphism databases

DMDMi 126302511.

Proteomic databases

MaxQBi Q15067.
PaxDbi Q15067.
PeptideAtlasi Q15067.
PRIDEi Q15067.

Protocols and materials databases

DNASUi 51.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000293217 ; ENSP00000293217 ; ENSG00000161533 . [Q15067-2 ]
ENST00000301608 ; ENSP00000301608 ; ENSG00000161533 . [Q15067-1 ]
GeneIDi 51.
KEGGi hsa:51.
UCSCi uc002jqe.3. human. [Q15067-2 ]
uc002jqf.3. human. [Q15067-1 ]

Organism-specific databases

CTDi 51.
GeneCardsi GC17M073937.
HGNCi HGNC:119. ACOX1.
HPAi CAB021094.
HPA021192.
HPA021195.
HPA028759.
MIMi 264470. phenotype.
609751. gene.
neXtProti NX_Q15067.
Orphaneti 2971. Peroxisomal acyl-CoA oxidase deficiency.
PharmGKBi PA21.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1960.
GeneTreei ENSGT00530000062919.
HOVERGENi HBG050451.
InParanoidi Q15067.
KOi K00232.
OMAi VHESYKH.
OrthoDBi EOG7D59MV.
PhylomeDBi Q15067.
TreeFami TF300672.

Enzyme and pathway databases

UniPathwayi UPA00661 .
BioCyci MetaCyc:HS08589-MONOMER.
Reactomei REACT_116145. PPARA activates gene expression.
REACT_121147. alpha-linolenic acid (ALA) metabolism.
REACT_17062. Beta-oxidation of very long chain fatty acids.
SABIO-RK Q15067.

Miscellaneous databases

ChiTaRSi ACOX1. human.
GeneWikii ACOX1.
GenomeRNAii 51.
NextBioi 199.
PROi Q15067.
SOURCEi Search...

Gene expression databases

Bgeei Q15067.
CleanExi HS_ACOX1.
ExpressionAtlasi Q15067. baseline and differential.
Genevestigatori Q15067.

Family and domain databases

Gene3Di 1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProi IPR029320. Acyl-CoA_ox_N.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR012258. Acyl-CoA_oxidase.
IPR002655. Acyl-CoA_oxidase_C.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view ]
Pfami PF01756. ACOX. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF14749. Acyl-CoA_ox_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000168. Acyl-CoA_oxidase. 1 hit.
SUPFAMi SSF47203. SSF47203. 2 hits.
SSF56645. SSF56645. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of the human peroxisomal acyl-CoA oxidase gene: organization, promoter analysis, and chromosomal localization."
    Varanasi U., Chu R., Chu S., Espinosa R., Lebeau M.M., Reddy J.K.
    Proc. Natl. Acad. Sci. U.S.A. 91:3107-3111(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
  2. "Overexpression and characterization of the human peroxisomal acyl-CoA oxidase in insect cells."
    Chu R., Varanasi U., Chu S., Lin Y., Usuda N., Rao M.S., Reddy J.K.
    J. Biol. Chem. 270:4908-4915(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. "Large deletion of the peroxisomal acyl-CoA oxidase gene in pseudoneonatal adrenoleukodystrophy."
    Fourner B., Saudubray J.-M., Benichou B., Lyonnet S., Munnich A., Clevers H., Poll-The B.T.
    J. Clin. Invest. 94:526-531(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT MET-312, INVOLVEMENT IN PSEUDO-NALD.
    Tissue: Liver.
  4. "Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase."
    Aoyama T., Tsushima K., Souri M., Kamijo T., Suzuki Y., Shimozawa N., Orii T., Hashimoto T.
    Biochem. Biophys. Res. Commun. 198:1113-1118(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-312.
    Tissue: Liver.
  5. "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; 2 AND 3), VARIANT MET-312.
    Tissue: Placenta, Thalamus and Trachea.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT MET-312.
    Tissue: Retina.
  7. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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 2), VARIANTS ILE-153 AND MET-312.
    Tissue: Colon and Eye.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Biochemical characterization of two functional human liver acyl-CoA oxidase isoforms 1a and 1b encoded by a single gene."
    Oaxaca-Castillo D., Andreoletti P., Vluggens A., Yu S., van Veldhoven P.P., Reddy J.K., Cherkaoui-Malki M.
    Biochem. Biophys. Res. Commun. 360:314-319(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-255; LYS-267; LYS-437; LYS-500 AND LYS-504, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: TISSUE SPECIFICITY, REVERSAL OF ACOX1 NULL PHENOTYPE IN MOUSE.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: VARIANTS PSEUDO-NALD CYS-178 AND VAL-278.
  17. "Clinical, biochemical, and mutational spectrum of peroxisomal acyl-coenzyme A oxidase deficiency."
    Ferdinandusse S., Denis S., Hogenhout E.M., Koster J., van Roermund C.W., Ijlst L., Moser A.B., Wanders R.J., Waterham H.R.
    Hum. Mutat. 28:904-912(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PSEUDO-NALD VAL-64 DEL; CYS-178; LEU-184; VAL-231; VAL-278; ARG-309 AND PRO-310, FUNCTION.

Entry informationi

Entry nameiACOX1_HUMAN
AccessioniPrimary (citable) accession number: Q15067
Secondary accession number(s): A8K6X8
, A8KAA0, B4DK61, F5GYQ8, Q12863, Q15068, Q15101, Q16131, Q7Z3W5, Q9UD31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 20, 2007
Last modified: October 29, 2014
This is version 154 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

Isoform 1 and isoform 2 can reverse the Acox1 null phenotype in mouse which is characterized by severe microvesicular hepatic steatosis, sustained activation of Ppara, spontaneous massive peroxisome proliferation and eventual development of hepatocellular carcinomas. Isoform 2 is more effective in reversal of the phenotype than isoform 1 (PubMed:20195242).1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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