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Protein

Peroxisomal acyl-coenzyme A oxidase 1

Gene

Acox1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

FADBy similarity

Pathwayi: peroxisomal fatty acid beta-oxidation

This protein is involved in the pathway peroxisomal fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway peroxisomal fatty acid beta-oxidation and in Lipid metabolism.

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-MMU-2046106. alpha-linolenic acid (ALA) metabolism.
R-MMU-390247. Beta-oxidation of very long chain fatty acids.
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
Gene namesi
Name:Acox1
Synonyms:Acox, Paox
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1330812. Acox1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • membrane Source: MGI
  • mitochondrion Source: MGI
  • nucleolus Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • peroxisomal membrane Source: MGI
  • peroxisome Source: UniProtKB
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Disruption phenotypei

Severe microvesicular hepatic steatosis, sustained activation of Ppara, spontaneous massive peroxisome proliferation and eventual development of hepatocellular carcinomas.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 661661Peroxisomal acyl-coenzyme A oxidase 1PRO_0000204678Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei65 – 651N6-acetyllysineCombined sources
Modified residuei89 – 891N6-succinyllysineCombined sources
Modified residuei90 – 901N6-succinyllysineCombined sources
Modified residuei159 – 1591N6-succinyllysineCombined sources
Modified residuei216 – 2161N6-acetyllysineCombined sources
Modified residuei241 – 2411N6-succinyllysineCombined sources
Modified residuei255 – 2551N6-acetyllysineBy similarity
Modified residuei267 – 2671N6-acetyllysineCombined sources
Modified residuei272 – 2721N6-acetyllysineCombined sources
Modified residuei349 – 3491N6-succinyllysineCombined sources
Modified residuei437 – 4371N6-acetyllysine; alternateCombined sources
Modified residuei437 – 4371N6-succinyllysine; alternateCombined sources
Modified residuei446 – 4461N6-acetyllysine; alternateCombined sources
Modified residuei446 – 4461N6-succinyllysine; alternateCombined sources
Modified residuei500 – 5001N6-acetyllysineBy similarity
Modified residuei512 – 5121N6-acetyllysine; alternateCombined sources
Modified residuei512 – 5121N6-succinyllysine; alternateCombined sources
Modified residuei542 – 5421N6-succinyllysineCombined sources
Modified residuei637 – 6371N6-acetyllysine; alternateCombined sources
Modified residuei637 – 6371N6-succinyllysine; alternateCombined sources
Modified residuei643 – 6431N6-succinyllysineCombined sources
Modified residuei652 – 6521N6-acetyllysineCombined sources
Modified residuei655 – 6551N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9R0H0.
MaxQBiQ9R0H0.
PaxDbiQ9R0H0.
PRIDEiQ9R0H0.

PTM databases

iPTMnetiQ9R0H0.
PhosphoSiteiQ9R0H0.
SwissPalmiQ9R0H0.

Expressioni

Tissue specificityi

Highest levels of isoform 1 are found in liver and kidney while highest levels of isoform 2 are found in white adipose tissue. Isoform 1 is expressed at higher levels than isoform 2 in liver and kidney while isoform 2 is expressed at higher levels in brain, heart, lung, muscle, white adipose tissue and testis.1 Publication

Gene expression databases

BgeeiQ9R0H0.
CleanExiMM_ACOX1.
MM_PAOX.
ExpressionAtlasiQ9R0H0. baseline and differential.
GenevisibleiQ9R0H0. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9R0H0. 4 interactions.
MINTiMINT-1861412.
STRINGi10090.ENSMUSP00000063325.

Structurei

3D structure databases

ProteinModelPortaliQ9R0H0.
SMRiQ9R0H0. Positions 1-655.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi659 – 6613Microbody targeting signal

Sequence similaritiesi

Belongs to the acyl-CoA oxidase family.Curated

Phylogenomic databases

eggNOGiKOG0136. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00530000062919.
HOGENOMiHOG000181256.
HOVERGENiHBG050451.
InParanoidiQ9R0H0.
KOiK00232.
OMAiIRELGTH.
OrthoDBiEOG7D59MV.
TreeFamiTF300672.

Family and domain databases

Gene3Di1.10.540.10. 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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9R0H0-1) [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

        10         20         30         40         50
MNPDLRKERA AATFNPELIT HILDGSPENT RRRREIENLI LNDPDFQHED
60 70 80 90 100
YNFLTRSQRY EVAVKKSATM VKKMREFGIA DPEEIMWFKK LHMVNFVEPV
110 120 130 140 150
GLNYSMFIPT LLNQGTTAQQ EKWMHPSQEL QIIGTYAQTE MGHGTHLRGL
160 170 180 190 200
ETTATYDPKT QEFILNSPTV TSIKWWPGGL GKTSNHAIVL AQLITRGECY
210 220 230 240 250
GLHAFVVPIR EIGTHKPLPG ITVGDIGPKF GYEEMDNGYL KMDNYRIPRE
260 270 280 290 300
NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGSAA QSLSKACTIA
310 320 330 340 350
IRYSAVRRQS EIKRSEPEPQ ILDFQTQQYK LFPLLATAYA FHFLGRYIKE
360 370 380 390 400
TYMRINESIG QGDLSELPEL HALTAGLKAF TTWTANAGIE ECRMACGGHG
410 420 430 440 450
YSHSSGIPNI YVTFTPACTF EGENTVMMLQ TARFLMKIYD QVQSGKLVGG
460 470 480 490 500
MVSYLNDLPS QRIQPQQVAV WPTLVDINSL DSLTEAYKLR AARLVEIAAK
510 520 530 540 550
NLQAQVSHRK SKEVAWNLTS VDLVRASEAH CHYVTVKVFA DKLPKIQDRA
560 570 580 590 600
VQAVLRNLCL LYSLYGISQK GGDFLEGNII TGAQMSQVNS RILELLTVTR
610 620 630 640 650
PNAVALVDAF DFKDVTLGSV LGRYDGNVYE NLFEWAKKSP LNKTEVHESY
660
YKHLKPLQSK L
Length:661
Mass (Da):74,649
Last modified:July 27, 2011 - v5
Checksum:i4140DB77A4CE7BE6
GO
Isoform 2 (identifier: Q9R0H0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     90-133: KLHMVNFVEP...MHPSQELQII → NSVHRGHPEP...FMPAWNLEIT

Show »
Length:661
Mass (Da):74,718
Checksum:i537E816BDE686154
GO

Sequence cautioni

The sequence BAE41642.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221I → V in AAB62926 (PubMed:10672038).Curated
Sequence conflicti263 – 2631G → D in BAE41642 (PubMed:16141072).Curated
Sequence conflicti516 – 5161W → R in BAE41642 (PubMed:16141072).Curated
Sequence conflicti523 – 5231L → I in BAE41642 (PubMed:16141072).Curated
Sequence conflicti648 – 6481E → Q in AAB62926 (PubMed:10672038).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei90 – 13344KLHMV…ELQII → NSVHRGHPEPLDLHLGMFLP TLLHQATEEQQERFFMPAWN LEIT in isoform 2. 2 PublicationsVSP_042477Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006688 mRNA. Translation: AAB62926.1.
AB034914 mRNA. Translation: BAA86870.1.
AK040566 mRNA. Translation: BAC30628.1.
AK170217 mRNA. Translation: BAE41642.1. Different initiation.
AL669925, AL607108 Genomic DNA. Translation: CAM16380.1.
AL669925, AL607108 Genomic DNA. Translation: CAM16381.1.
AL607108, AL669925 Genomic DNA. Translation: CAM24036.1.
AL607108, AL669925 Genomic DNA. Translation: CAM24037.1.
CH466558 Genomic DNA. Translation: EDL34562.1.
CH466558 Genomic DNA. Translation: EDL34563.1.
BC056448 mRNA. Translation: AAH56448.1.
CCDSiCCDS25660.1. [Q9R0H0-2]
CCDS70354.1. [Q9R0H0-1]
RefSeqiNP_001258827.1. NM_001271898.1. [Q9R0H0-1]
NP_056544.2. NM_015729.3. [Q9R0H0-2]
UniGeneiMm.356689.

Genome annotation databases

EnsembliENSMUST00000066587; ENSMUSP00000063325; ENSMUSG00000020777. [Q9R0H0-2]
ENSMUST00000072948; ENSMUSP00000072717; ENSMUSG00000020777. [Q9R0H0-1]
GeneIDi11430.
KEGGimmu:11430.
UCSCiuc007mkj.2. mouse. [Q9R0H0-1]
uc007mkl.2. mouse. [Q9R0H0-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006688 mRNA. Translation: AAB62926.1.
AB034914 mRNA. Translation: BAA86870.1.
AK040566 mRNA. Translation: BAC30628.1.
AK170217 mRNA. Translation: BAE41642.1. Different initiation.
AL669925, AL607108 Genomic DNA. Translation: CAM16380.1.
AL669925, AL607108 Genomic DNA. Translation: CAM16381.1.
AL607108, AL669925 Genomic DNA. Translation: CAM24036.1.
AL607108, AL669925 Genomic DNA. Translation: CAM24037.1.
CH466558 Genomic DNA. Translation: EDL34562.1.
CH466558 Genomic DNA. Translation: EDL34563.1.
BC056448 mRNA. Translation: AAH56448.1.
CCDSiCCDS25660.1. [Q9R0H0-2]
CCDS70354.1. [Q9R0H0-1]
RefSeqiNP_001258827.1. NM_001271898.1. [Q9R0H0-1]
NP_056544.2. NM_015729.3. [Q9R0H0-2]
UniGeneiMm.356689.

3D structure databases

ProteinModelPortaliQ9R0H0.
SMRiQ9R0H0. Positions 1-655.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9R0H0. 4 interactions.
MINTiMINT-1861412.
STRINGi10090.ENSMUSP00000063325.

PTM databases

iPTMnetiQ9R0H0.
PhosphoSiteiQ9R0H0.
SwissPalmiQ9R0H0.

Proteomic databases

EPDiQ9R0H0.
MaxQBiQ9R0H0.
PaxDbiQ9R0H0.
PRIDEiQ9R0H0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066587; ENSMUSP00000063325; ENSMUSG00000020777. [Q9R0H0-2]
ENSMUST00000072948; ENSMUSP00000072717; ENSMUSG00000020777. [Q9R0H0-1]
GeneIDi11430.
KEGGimmu:11430.
UCSCiuc007mkj.2. mouse. [Q9R0H0-1]
uc007mkl.2. mouse. [Q9R0H0-2]

Organism-specific databases

CTDi51.
MGIiMGI:1330812. Acox1.

Phylogenomic databases

eggNOGiKOG0136. Eukaryota.
COG1960. LUCA.
GeneTreeiENSGT00530000062919.
HOGENOMiHOG000181256.
HOVERGENiHBG050451.
InParanoidiQ9R0H0.
KOiK00232.
OMAiIRELGTH.
OrthoDBiEOG7D59MV.
TreeFamiTF300672.

Enzyme and pathway databases

UniPathwayiUPA00661.
ReactomeiR-MMU-2046106. alpha-linolenic acid (ALA) metabolism.
R-MMU-390247. Beta-oxidation of very long chain fatty acids.

Miscellaneous databases

ChiTaRSiAcox1. mouse.
NextBioi278708.
PROiQ9R0H0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R0H0.
CleanExiMM_ACOX1.
MM_PAOX.
ExpressionAtlasiQ9R0H0. baseline and differential.
GenevisibleiQ9R0H0. MM.

Family and domain databases

Gene3Di1.10.540.10. 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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and analysis of tissue-specific expression of mouse peroxisomal straight-chain acyl-CoA oxidase."
    Nohammer C., El-Shabrawi Y., Schauer S., Hiden M., Berger J., Forss-Petter S., Winter E., Eferl R., Zechner R., Hoefler G.
    Eur. J. Biochem. 267:1254-1260(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Saibara T., Adachi K.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Liver.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J and NOD.
    Tissue: Dendritic cell and Thymus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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).
    Strain: C57BL/6J.
    Tissue: Brain.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.
  8. Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-89; LYS-90; LYS-159; LYS-241; LYS-349; LYS-437; LYS-446; LYS-512; LYS-542; LYS-637; LYS-643 AND LYS-655, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-65; LYS-216; LYS-267; LYS-272; LYS-437; LYS-446; LYS-512; LYS-637 AND LYS-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACOX1_MOUSE
AccessioniPrimary (citable) accession number: Q9R0H0
Secondary accession number(s): A2A850
, O35616, Q3TDG0, Q8BYC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 138 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.