Q15067 (ACOX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	660 AA.
Sequence status	Complete.
Protein existence	Evidence 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 cids, 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 process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	alpha-linolenic acid 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 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 spermatogenesis Inferred from electronic annotation. Source: Compara very long-chain fatty acid metabolic process Inferred from mutant phenotype PubMed 18536048. Source: BHF-UCL
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara peroxisomal matrix Traceable author statement. Source: Reactome peroxisomal membrane Inferred from electronic annotation. Source: Compara
Molecular_function	FAD binding Inferred from direct assay Ref.11. Source: UniProtKB 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: Compara flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro palmitoyl-CoA oxidase activity Inferred from direct assay Ref.11. 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 660	660	Peroxisomal acyl-coenzyme A oxidase 1		PRO_0000204677
Regions
	Motif	658 – 660	3	Microbody targeting signal
Sites
	Active site	421	1	Proton acceptor By similarity
	Binding site	139	1	FAD By similarity
	Binding site	178	1	FAD; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	26	1	Phosphoserine Ref.10 Ref.12
	Modified residue	255	1	N6-acetyllysine Ref.13
	Modified residue	267	1	N6-acetyllysine Ref.13
	Modified residue	310	1	Phosphoserine By similarity
	Modified residue	437	1	N6-acetyllysine Ref.13
	Modified residue	500	1	N6-acetyllysine Ref.13
	Modified residue	504	1	N6-acetyllysine Ref.13
	Modified residue	643	1	N6-acetyllysine By similarity
	Modified residue	649	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 38	38	Missing in isoform 3.		VSP_046129
	Alternative sequence	90 – 131	42	KLHLV…SKGLQ → NFVHRGRPEPLDLHLGMFLP TLLHQATAEQQERFFMPAWN LE in isoform 2 and isoform 3.		VSP_000146
	Natural variant	64	1	Missing in pseudo-NALD. Ref.18		VAR_067040
	Natural variant	101	1	G → S. Corresponds to variant rs3744032 [ dbSNP | Ensembl ].		VAR_048182
	Natural variant	153	1	T → I. Ref.9 Corresponds to variant rs17855420 [ dbSNP | Ensembl ].		VAR_030619
	Natural variant	178	1	G → C in pseudo-NALD. Ref.17 Ref.18		VAR_025789
	Natural variant	184	1	S → L in pseudo-NALD. Ref.18		VAR_067041
	Natural variant	231	1	G → V in pseudo-NALD. Ref.18		VAR_067042
	Natural variant	278	1	M → V in pseudo-NALD. Ref.17 Ref.18		VAR_025790
	Natural variant	309	1	Q → R in pseudo-NALD. Ref.18		VAR_067043
	Natural variant	310	1	S → P in pseudo-NALD. Ref.18		VAR_067044
	Natural variant	312	1	I → M. Ref.3 Ref.4 Ref.5 Ref.6 Ref.9 Corresponds to variant rs1135640 [ dbSNP | Ensembl ].		VAR_021529
Experimental info
	Sequence conflict	27	1	P → L in CAA50574. Ref.3
	Sequence conflict	80	1	A → R in CAA50574. Ref.3
	Sequence conflict	84	1	E → D in CAD97622. Ref.6
	Sequence conflict	119	1	Q → E in AAB30019. Ref.4
	Sequence conflict	200	1	Y → H in AAA18595. Ref.2
	Sequence conflict	212 – 213	2	IG → NR in AAA19113. Ref.1
	Sequence conflict	212 – 213	2	IG → NR in AAA19114. Ref.1
	Sequence conflict	212 – 213	2	IG → NR in AAA18595. Ref.2
	Sequence conflict	264	1	T → P in AAA19113. Ref.1
	Sequence conflict	264	1	T → P in AAA19114. Ref.1
	Sequence conflict	264	1	T → P in AAA18595. Ref.2
	Sequence conflict	332	1	F → L in AAA18595. Ref.2
	Sequence conflict	449	1	C → R in AAA18595. Ref.2
	Sequence conflict	490	1	R → L in BAF85654. Ref.5
	Sequence conflict	531	1	C → L in AAA19113. Ref.1
	Sequence conflict	531	1	C → L in AAA19114. Ref.1
	Sequence conflict	531	1	C → L in AAA18595. Ref.2
	Sequence conflict	534 – 535	2	VV → GL in AAA19113. Ref.1
	Sequence conflict	534 – 535	2	VV → GL in AAA19114. Ref.1
	Sequence conflict	534 – 535	2	VV → GL in AAA18595. Ref.2
	Sequence conflict	615	1	V → A in CAA50574. Ref.3
	Sequence conflict	650	1	Y → YH in AAB30019. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (ACOX1a) (SCOX-exon 3I) [UniParc]. Last modified February 20, 2007. Version 3. Checksum: D713768A47374EA1	FASTA	660	74,424
	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
	Isoform 2 (ACOX1b) (SCOX-exon 3II) [UniParc]. Checksum: 761C97B5043F9068	FASTA	660	74,668
	10 20 30 40 50 60 MNPDLRRERD SASFNPELLT HILDGSPEKT RRRREIENMI LNDPDFQHED LNFLTRSQRY 70 80 90 100 110 120 EVAVRKSAIM VKKMREFGIA DPDEIMWFKN FVHRGRPEPL DLHLGMFLPT LLHQATAEQQ 130 140 150 160 170 180 ERFFMPAWNL EIIGTYAQTE 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
	Isoform 3 [UniParc]. Checksum: FE52A881C050EB78	FASTA	622	70,136
	10 20 30 40 50 60 MILNDPDFQH EDLNFLTRSQ RYEVAVRKSA IMVKKMREFG IADPDEIMWF KNFVHRGRPE 70 80 90 100 110 120 PLDLHLGMFL PTLLHQATAE QQERFFMPAW NLEIIGTYAQ TEMGHGTHLR GLETTATYDP 130 140 150 160 170 180 ETQEFILNSP TVTSIKWWPG GLGKTSNHAI VLAQLITKGK CYGLHAFIVP IREIGTHKPL 190 200 210 220 230 240 PGITVGDIGP KFGYDEIDNG YLKMDNHRIP RENMLMKYAQ VKPDGTYVKP LSNKLTYGTM 250 260 270 280 290 300 VFVRSFLVGE AARALSKACT IAIRYSAVRH QSEIKPGEPE PQILDFQTQQ YKLFPLLATA 310 320 330 340 350 360 YAFQFVGAYM KETYHRINEG IGQGDLSELP ELHALTAGLK AFTSWTANTG IEACRMACGG 370 380 390 400 410 420 HGYSHCSGLP NIYVNFTPSC TFEGENTVMM LQTARFLMKS YDQVHSGKLV CGMVSYLNDL 430 440 450 460 470 480 PSQRIQPQQV AVWPTMVDIN SPESLTEAYK LRAARLVEIA AKNLQKEVIH RKSKEVAWNL 490 500 510 520 530 540 TSVDLVRASE AHCHYVVVKL FSEKLLKIQD KAIQAVLRSL CLLYSLYGIS QNAGDFLQGS 550 560 570 580 590 600 IMTEPQITQV NQRVKELLTL IRSDAVALVD AFDFQDVTLG SVLGRYDGNV YENLFEWAKN 610 620 SPLNKAEVHE SYKHLKSLQS KL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00296907. IPI00477729. IPI00984655.
PIR	A54942. B54942. I38095.
RefSeq	NP_001171968.1. NM_001185039.1. NP_004026.2. NM_004035.6. NP_009223.2. NM_007292.5.
UniGene	Hs.464137.
3D structure databases
ProteinModelPortal	Q15067.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15067. 4 interactions.
STRING	9606.ENSP00000293217.
PTM databases
PhosphoSite	Q15067.
Polymorphism databases
DMDM	126302511.
Proteomic databases
PaxDb	Q15067.
PeptideAtlas	Q15067.
PRIDE	Q15067.
Protocols and materials databases
DNASU	51.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000293217; ENSP00000293217; ENSG00000161533. ENST00000301608; ENSP00000301608; ENSG00000161533. ENST00000537812; ENSP00000441257; ENSG00000161533. ENST00000539791; ENSP00000446392; ENSG00000161533.
GeneID	51.
KEGG	hsa:51.
UCSC	uc002jqe.3. human. uc002jqf.3. human.
Organism-specific databases
CTD	51.
GeneCards	GC17M073937.
HGNC	HGNC:119. ACOX1.
HPA	CAB021094. HPA021192. HPA021195. HPA028759.
MIM	264470. phenotype. 609751. gene.
neXtProt	NX_Q15067.
Orphanet	2971. Peroxisomal acyl-CoA oxidase deficiency.
PharmGKB	PA21.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1960.
HOVERGEN	HBG050451.
KO	K00232.
OMA	QGSIMTE.
OrthoDB	EOG4KWJSB.
PhylomeDB	Q15067.
Enzyme and pathway databases
BioCyc	MetaCyc:HS08589-MONOMER.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00661.
Gene expression databases
ArrayExpress	Q15067.
Bgee	Q15067.
CleanEx	HS_ACOX1.
Genevestigator	Q15067.
GermOnline	ENSG00000161533. Homo sapiens.
Family and domain databases
Gene3D	1.10.540.10. 1 hit. 2.40.110.10. 1 hit.
InterPro	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. [Graphical view]
PANTHER	PTHR10909:SF11. PTHR10909:SF11. 1 hit.
Pfam	PF01756. ACOX. 1 hit. PF02770. Acyl-CoA_dh_M. 1 hit. [Graphical view]
PIRSF	PIRSF000168. Acyl-CoA_oxidase. 1 hit.
SUPFAM	SSF56645. AcylCoA_dehyd_NM. 1 hit. SSF47203. AcylCoADH_C_like. 2 hits.
ProtoNet	Search...
Other
ChiTaRS	ACOX1. human.
GenomeRNAi	51.
NextBio	199.
SOURCE	Search...

Entry information

Entry name

ACOX1_HUMAN

Accession

Primary (citable) accession number: Q15067
Secondary accession number(s): A8K6X8 , 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:	May 1, 2013
This is version 139 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.