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Q15067 (ACOX1_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 acyl-coenzyme A oxidase 1

Short name=AOX
EC=1.3.3.6
Alternative name(s):
Palmitoyl-CoA oxidase
Straight-chain acyl-CoA oxidase
Short name=SCOX
Gene names
Name:ACOX1
Synonyms:ACOX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length660 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11 Ref.18

Catalytic activity

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

Cofactor

FAD. Ref.11

Pathway

Lipid metabolism; peroxisomal fatty acid beta-oxidation.

Subcellular location

Peroxisome.

Tissue specificity

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. Ref.11 Ref.14

Involvement in disease

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

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 (Ref.14).

Sequence similarities

Belongs to the acyl-CoA oxidase family.

Biophysicochemical properties

Kinetic parameters:

KM=73 µM for palmitoyl-CoA (isoform 1) Ref.11

KM=90 µM for palmitoyl-CoA (isoform 2)

pH dependence:

Optimum pH is 8.5 for isoform 1 and 7.5-8.5 for isoform 2.

Temperature dependence:

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.

Sequence caution

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

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentPeroxisome
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processalpha-linolenic acid metabolic process

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

fatty acid beta-oxidation using acyl-CoA oxidase

Inferred from mutant phenotype PubMed 18536048. Source: BHF-UCL

fatty acid oxidation

Inferred from genetic interaction Ref.14. Source: UniProtKB

generation of precursor metabolites and energy

Inferred from mutant phenotype Ref.2. Source: UniProtKB

lipid homeostasis

Inferred from direct assay Ref.14. Source: UniProtKB

lipid metabolic process

Inferred from direct assay Ref.4. Source: UniProtKB

peroxisome fission

Inferred from genetic interaction Ref.14. Source: UniProtKB

positive regulation of cholesterol homeostasis

Inferred from genetic interaction Ref.14. Source: UniProtKB

prostaglandin metabolic process

Inferred from mutant phenotype Ref.2. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

unsaturated fatty acid metabolic process

Traceable author statement. Source: Reactome

very long-chain fatty acid metabolic process

Inferred from mutant phenotype PubMed 18536048. Source: BHF-UCL

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: Ensembl

peroxisomal matrix

Traceable author statement. Source: Reactome

peroxisomal membrane

Inferred from electronic annotation. Source: Ensembl

peroxisome

Inferred from direct assay PubMed 17881773Ref.2Ref.4PubMed 8943006. Source: UniProtKB

   Molecular_functionFAD binding

Inferred from direct assay Ref.11. Source: UniProtKB

PDZ domain binding

Inferred from direct assay PubMed 23209302. Source: MGI

acyl-CoA dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

acyl-CoA oxidase activity

Inferred from direct assay Ref.4. Source: UniProtKB

fatty acid binding

Inferred from electronic annotation. Source: Ensembl

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

palmitoyl-CoA oxidase activity

Inferred from direct assay Ref.11. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 18281296. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 20178365. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15067-1)

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.
Isoform 2 (identifier: Q15067-2)

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
Isoform 3 (identifier: Q15067-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 660660Peroxisomal acyl-coenzyme A oxidase 1
PRO_0000204677

Regions

Motif658 – 6603Microbody targeting signal

Sites

Active site4211Proton acceptor By similarity
Binding site1391FAD By similarity
Binding site1781FAD; via amide nitrogen By similarity

Amino acid modifications

Modified residue261Phosphoserine Ref.10 Ref.12
Modified residue891N6-succinyllysine By similarity
Modified residue901N6-succinyllysine By similarity
Modified residue2161N6-acetyllysine By similarity
Modified residue2411N6-succinyllysine By similarity
Modified residue2551N6-acetyllysine Ref.13
Modified residue2671N6-acetyllysine Ref.13
Modified residue2721N6-acetyllysine By similarity
Modified residue3491N6-succinyllysine By similarity
Modified residue4371N6-acetyllysine; alternate Ref.13
Modified residue4371N6-succinyllysine; alternate By similarity
Modified residue4461N6-acetyllysine; alternate By similarity
Modified residue4461N6-succinyllysine; alternate By similarity
Modified residue5001N6-acetyllysine Ref.13
Modified residue5041N6-acetyllysine Ref.13
Modified residue5121N6-acetyllysine; alternate By similarity
Modified residue5121N6-succinyllysine; alternate By similarity
Modified residue5421N6-succinyllysine By similarity
Modified residue6371N6-acetyllysine; alternate By similarity
Modified residue6371N6-succinyllysine; alternate By similarity
Modified residue6431N6-succinyllysine By similarity
Modified residue6511N6-acetyllysine By similarity
Modified residue6541N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 3838Missing in isoform 3.
VSP_046129
Alternative sequence90 – 13142KLHLV…SKGLQ → NFVHRGRPEPLDLHLGMFLP TLLHQATAEQQERFFMPAWN LE in isoform 2 and isoform 3.
VSP_000146
Natural variant641Missing in pseudo-NALD. Ref.18
VAR_067040
Natural variant1011G → S.
Corresponds to variant rs3744032 [ dbSNP | Ensembl ].
VAR_048182
Natural variant1531T → I. Ref.9
Corresponds to variant rs17855420 [ dbSNP | Ensembl ].
VAR_030619
Natural variant1781G → C in pseudo-NALD. Ref.17 Ref.18
VAR_025789
Natural variant1841S → L in pseudo-NALD. Ref.18
VAR_067041
Natural variant2311G → V in pseudo-NALD. Ref.18
VAR_067042
Natural variant2781M → V in pseudo-NALD. Ref.17 Ref.18
VAR_025790
Natural variant3091Q → R in pseudo-NALD. Ref.18
VAR_067043
Natural variant3101S → P in pseudo-NALD. Ref.18
VAR_067044
Natural variant3121I → M. Ref.3 Ref.4 Ref.5 Ref.6 Ref.9
Corresponds to variant rs1135640 [ dbSNP | Ensembl ].
VAR_021529

Experimental info

Sequence conflict271P → L in CAA50574. Ref.3
Sequence conflict801A → R in CAA50574. Ref.3
Sequence conflict841E → D in CAD97622. Ref.6
Sequence conflict1191Q → E in AAB30019. Ref.4
Sequence conflict2001Y → H in AAA18595. Ref.2
Sequence conflict212 – 2132IG → NR in AAA19113. Ref.1
Sequence conflict212 – 2132IG → NR in AAA19114. Ref.1
Sequence conflict212 – 2132IG → NR in AAA18595. Ref.2
Sequence conflict2641T → P in AAA19113. Ref.1
Sequence conflict2641T → P in AAA19114. Ref.1
Sequence conflict2641T → P in AAA18595. Ref.2
Sequence conflict3321F → L in AAA18595. Ref.2
Sequence conflict4491C → R in AAA18595. Ref.2
Sequence conflict4901R → L in BAF85654. Ref.5
Sequence conflict5311C → L in AAA19113. Ref.1
Sequence conflict5311C → L in AAA19114. Ref.1
Sequence conflict5311C → L in AAA18595. Ref.2
Sequence conflict534 – 5352VV → GL in AAA19113. Ref.1
Sequence conflict534 – 5352VV → GL in AAA19114. Ref.1
Sequence conflict534 – 5352VV → GL in AAA18595. Ref.2
Sequence conflict6151V → A in CAA50574. Ref.3
Sequence conflict6501Y → YH in AAB30019. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ACOX1a) (SCOX-exon 3I) [UniParc].

Last modified February 20, 2007. Version 3.
Checksum: D713768A47374EA1

FASTA66074,424
        10         20         30         40         50         60 
MNPDLRRERD SASFNPELLT HILDGSPEKT RRRREIENMI LNDPDFQHED LNFLTRSQRY 

        70         80         90        100        110        120 
EVAVRKSAIM VKKMREFGIA DPDEIMWFKK LHLVNFVEPV GLNYSMFIPT LLNQGTTAQK 

       130        140        150        160        170        180 
EKWLLSSKGL QIIGTYAQTE MGHGTHLRGL ETTATYDPET QEFILNSPTV TSIKWWPGGL 

       190        200        210        220        230        240 
GKTSNHAIVL AQLITKGKCY GLHAFIVPIR EIGTHKPLPG ITVGDIGPKF GYDEIDNGYL 

       250        260        270        280        290        300 
KMDNHRIPRE NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGEAA RALSKACTIA 

       310        320        330        340        350        360 
IRYSAVRHQS EIKPGEPEPQ ILDFQTQQYK LFPLLATAYA FQFVGAYMKE TYHRINEGIG 

       370        380        390        400        410        420 
QGDLSELPEL HALTAGLKAF TSWTANTGIE ACRMACGGHG YSHCSGLPNI YVNFTPSCTF 

       430        440        450        460        470        480 
EGENTVMMLQ TARFLMKSYD QVHSGKLVCG MVSYLNDLPS QRIQPQQVAV WPTMVDINSP 

       490        500        510        520        530        540 
ESLTEAYKLR AARLVEIAAK NLQKEVIHRK SKEVAWNLTS VDLVRASEAH CHYVVVKLFS 

       550        560        570        580        590        600 
EKLLKIQDKA IQAVLRSLCL LYSLYGISQN AGDFLQGSIM TEPQITQVNQ RVKELLTLIR 

       610        620        630        640        650        660 
SDAVALVDAF DFQDVTLGSV LGRYDGNVYE NLFEWAKNSP LNKAEVHESY KHLKSLQSKL 

« Hide

Isoform 2 (ACOX1b) (SCOX-exon 3II) [UniParc].

Checksum: 761C97B5043F9068
Show »

FASTA66074,668
Isoform 3 [UniParc].

Checksum: FE52A881C050EB78
Show »

FASTA62270,136

References

« Hide 'large scale' references
[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. 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; 2 AND 3), VARIANT MET-312.
Tissue: Placenta, Thalamus and Trachea.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Reversal of mouse Acyl-CoA oxidase 1 (ACOX1) null phenotype by human ACOX1b isoform."
Vluggens A., Andreoletti P., Viswakarma N., Jia Y., Matsumoto K., Kulik W., Khan M., Huang J., Guo D., Yu S., Sarkar J., Singh I., Rao M.S., Wanders R.J., Reddy J.K., Cherkaoui-Malki M.
Lab. Invest. 90:696-708(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, REVERSAL OF ACOX1 NULL PHENOTYPE IN MOUSE.
[15]Erratum
Vluggens A., Andreoletti P., Viswakarma N., Jia Y., Matsumoto K., Kulik W., Khan M., Huang J., Guo D., Yu S., Sarkar J., Singh I., Rao M.S., Wanders R.J., Reddy J.K., Cherkaoui-Malki M.
Lab. Invest. 90:808-808(2010)
[16]"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].
[17]"Peroxisomal acyl-CoA oxidase deficiency."
Suzuki Y., Iai M., Kamei A., Tanabe Y., Chida S., Yamaguchi S., Zhang Z., Takemoto Y., Shimozawa N., Kondo N.
J. Pediatr. 140:128-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSEUDO-NALD CYS-178 AND VAL-278.
[18]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03268 expand/collapse EMBL AC list , U03254, U03255, U03256, U03258, U03259, U03260, U03261, U03263, U03264, U03265, U03266, U03267 Genomic DNA. Translation: AAA19113.1.
U03268 expand/collapse EMBL AC list , 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.
CCDSCCDS11734.1. [Q15067-2]
CCDS11735.1. [Q15067-1]
PIRA54942.
B54942.
I38095.
RefSeqNP_001171968.1. NM_001185039.1. [Q15067-3]
NP_004026.2. NM_004035.6. [Q15067-2]
NP_009223.2. NM_007292.5. [Q15067-1]
UniGeneHs.464137.

3D structure databases

ProteinModelPortalQ15067.
SMRQ15067. Positions 1-654.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106567. 11 interactions.
IntActQ15067. 4 interactions.
MINTMINT-4717708.
STRING9606.ENSP00000293217.

PTM databases

PhosphoSiteQ15067.

Polymorphism databases

DMDM126302511.

Proteomic databases

MaxQBQ15067.
PaxDbQ15067.
PeptideAtlasQ15067.
PRIDEQ15067.

Protocols and materials databases

DNASU51.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000293217; ENSP00000293217; ENSG00000161533. [Q15067-2]
ENST00000301608; ENSP00000301608; ENSG00000161533. [Q15067-1]
ENST00000537812; ENSP00000441257; ENSG00000161533. [Q15067-3]
GeneID51.
KEGGhsa:51.
UCSCuc002jqe.3. human. [Q15067-2]
uc002jqf.3. human. [Q15067-1]

Organism-specific databases

CTD51.
GeneCardsGC17M073937.
HGNCHGNC:119. ACOX1.
HPACAB021094.
HPA021192.
HPA021195.
HPA028759.
MIM264470. phenotype.
609751. gene.
neXtProtNX_Q15067.
Orphanet2971. Peroxisomal acyl-CoA oxidase deficiency.
PharmGKBPA21.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1960.
HOVERGENHBG050451.
KOK00232.
OMAVHESYKH.
OrthoDBEOG7D59MV.
PhylomeDBQ15067.
TreeFamTF300672.

Enzyme and pathway databases

BioCycMetaCyc:HS08589-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00661.

Gene expression databases

ArrayExpressQ15067.
BgeeQ15067.
CleanExHS_ACOX1.
GenevestigatorQ15067.

Family and domain databases

Gene3D1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProIPR029320. 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]
PfamPF01756. ACOX. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF14749. Acyl-CoA_ox_N. 1 hit.
[Graphical view]
PIRSFPIRSF000168. Acyl-CoA_oxidase. 1 hit.
SUPFAMSSF47203. SSF47203. 2 hits.
SSF56645. SSF56645. 1 hit.
ProtoNetSearch...

Other

ChiTaRSACOX1. human.
GeneWikiACOX1.
GenomeRNAi51.
NextBio199.
PROQ15067.
SOURCESearch...

Entry information

Entry nameACOX1_HUMAN
AccessionPrimary (citable) accession number: Q15067
Secondary accession number(s): A8K6X8 expand/collapse secondary AC list , A8KAA0, B4DK61, F5GYQ8, Q12863, Q15068, Q15101, Q16131, Q7Z3W5, Q9UD31
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 20, 2007
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 17

Human chromosome 17: entries, gene names and cross-references to MIM