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Protein

Peroxisomal N(1)-acetyl-spermine/spermidine oxidase

Gene

PAOX

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

Functioni

Flavoenzyme which catalyzes the oxidation of N(1)-acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity: N(1)-acetylspermine = N(1)-acetylspermidine > N1,N(12)-diacylspermine >> spermine. Does not oxidize spermidine. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs.

Catalytic activityi

N(1)-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2.
N(1)-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2.
N1,N(12)-diacetylspermine + O2 + H2O = N(1)-acetylspermidine + 3-acetamidobutanal + H2O2.

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Pathwayi: spermine metabolism

This protein is involved in the pathway spermine metabolism, which is part of Amine and polyamine metabolism.
View all proteins of this organism that are known to be involved in the pathway spermine metabolism and in Amine and polyamine metabolism.

GO - Molecular functioni

GO - Biological processi

  • cellular nitrogen compound metabolic process Source: Reactome
  • oxidation-reduction process Source: GOC
  • polyamine biosynthetic process Source: Reactome
  • polyamine catabolic process Source: UniProtKB
  • polyamine metabolic process Source: Reactome
  • positive regulation of spermidine biosynthetic process Source: UniProtKB
  • putrescine biosynthetic process Source: UniProtKB
  • putrescine catabolic process Source: UniProtKB
  • small molecule metabolic process Source: Reactome
  • spermidine catabolic process Source: UniProtKB
  • spermine catabolic process Source: UniProtKB
  • xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.5.3.13. 2681.
ReactomeiR-HSA-141334. PAOs oxidise polyamines to amines.
R-HSA-351200. Interconversion of polyamines.
SABIO-RKQ6QHF9.
UniPathwayiUPA00826.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal N(1)-acetyl-spermine/spermidine oxidase (EC:1.5.3.13)
Alternative name(s):
Polyamine oxidase
Gene namesi
Name:PAOX
Synonyms:PAO
ORF Names:UNQ1923/PRO4398
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:20837. PAOX.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134907695.

Chemistry

ChEMBLiCHEMBL2105.

Polymorphism and mutation databases

DMDMi51316248.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 649649Peroxisomal N(1)-acetyl-spermine/spermidine oxidasePRO_0000099875Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ6QHF9.
PaxDbiQ6QHF9.
PRIDEiQ6QHF9.

PTM databases

PhosphoSiteiQ6QHF9.

Expressioni

Tissue specificityi

Widely expressed. Not detected in spleen. Expressed at lower level in neoplastic tissues.1 Publication

Inductioni

By polyamine analogs.

Gene expression databases

BgeeiQ6QHF9.
CleanExiHS_PAOX.
ExpressionAtlasiQ6QHF9. baseline and differential.
GenevisibleiQ6QHF9. HS.

Organism-specific databases

HPAiHPA047782.

Interactioni

Subunit structurei

Monomer.By similarity

GO - Molecular functioni

  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi128224. 1 interaction.
STRINGi9606.ENSP00000278060.

Chemistry

BindingDBiQ6QHF9.

Structurei

3D structure databases

ProteinModelPortaliQ6QHF9.
SMRiQ6QHF9. Positions 13-83, 181-637.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi647 – 6493Microbody targeting signalSequence analysis

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Curated

Phylogenomic databases

eggNOGiKOG0685. Eukaryota.
ENOG410XQW0. LUCA.
GeneTreeiENSGT00530000062888.
HOVERGENiHBG053499.
InParanoidiQ6QHF9.
KOiK00308.
OMAiGHSAFPH.
PhylomeDBiQ6QHF9.
TreeFamiTF318348.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 2 hits.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 3 hits.

Sequences (11)i

Sequence statusi: Complete.

This entry describes 11 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 9 (identifier: Q6QHF9-1) [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
MESTGSVGEA PGGPRVLVVG GGIAGLGAAQ RLCGHSAFPH LRVLEATARA
60 70 80 90 100
GGRIRSERCF GGVVEVGAHW IHGPSRGNPV FQLAAEYGLL GEKELSQENQ
110 120 130 140 150
LVETGGHVGL PSVSYASSGT SVSLQLVAEM ATLFYGLIDQ TREFLHAAET
160 170 180 190 200
PVPSVGEYLK KEIGQHVARL CGHSAFPHLR VLEATARAGG RIRSERCFGG
210 220 230 240 250
VVEVGAHWIH GPSRGNPVFQ LAAEYGLLGE KELSQENQLV ETGGHVGLPS
260 270 280 290 300
VSYASSGASV SLQLVAEMAT LFYGLIDQTR EFLHAAETPV PSVGEYLKKE
310 320 330 340 350
IGQHVAGWTE DEETRKLKLA VLNSFFNLEC CVSGTHSMDL VALAPFGEYT
360 370 380 390 400
VLPGLDCTFS KGYQGLTNCM MAALPEDTVV FEKPVKTIHW NGSFQEAAFP
410 420 430 440 450
GETFPVSVEC EDGDRFPAHH VIVTVPLGFL REHLDTFFDP PLPAEKAEAI
460 470 480 490 500
RKIGFGTNNK IFLEFEEPFW EPDCQLIQLV WEDTSPLEDA APELQDAWFR
510 520 530 540 550
KLIGFVVLPA FASVHVLCGF IAGLESEFME TLSDEEVLLC LTQVLRRVTG
560 570 580 590 600
NPRLPAPKSV LRSRWHSAPY TRGSYSYVAV GSTGGDLDLL AQPLPADGAG
610 620 630 640
AQLQILFAGE ATHRTFYSTT HGALLSGWRE ADRLLSLWAP QVQQPRPRL
Length:649
Mass (Da):70,290
Last modified:January 23, 2007 - v3
Checksum:iD332E2AA7242F609
GO
Isoform 1 (identifier: Q6QHF9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     31-168: Missing.

Show »
Length:511
Mass (Da):55,513
Checksum:iBF1A6E43AA09965A
GO
Isoform 3 (identifier: Q6QHF9-6) [UniParc]FASTAAdd to basket

Also known as: 7

The sequence of this isoform differs from the canonical sequence as follows:
     62-69: GVVEVGAH → AIKDSQTA
     70-649: Missing.

Show »
Length:69
Mass (Da):6,917
Checksum:i6479901AFA86F3BC
GO
Isoform 4 (identifier: Q6QHF9-5) [UniParc]FASTAAdd to basket

Also known as: 2

The sequence of this isoform differs from the canonical sequence as follows:
     31-168: Missing.
     429-463: FLREHLDTFFDPPLPAEKAEAIRKIGFGTNNKIFL → LSTFSVGSLPDLSLSSWRLCRMKKYFCVSPKCSGE
     464-649: Missing.

Show »
Length:325
Mass (Da):34,706
Checksum:i9F461E2A9F42C661
GO
Isoform 5 (identifier: Q6QHF9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     31-168: Missing.
     550-649: GNPRLPAPKS...PQVQQPRPRL → APDPVCGGSH...SFLLTDFSLA

Show »
Length:486
Mass (Da):51,963
Checksum:i8F044535B0B0296E
GO
Isoform 6 (identifier: Q6QHF9-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-80: GGVVEVGAHWIHGPSRGNPV → RVSRTHKLHDGRPAGGHCSF
     81-649: Missing.

Show »
Length:80
Mass (Da):8,245
Checksum:i6C6D2D32475F8713
GO
Isoform 8 (identifier: Q6QHF9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     31-168: Missing.
     435-482: Missing.

Show »
Length:463
Mass (Da):49,861
Checksum:iD898B10BD2B29076
GO
Isoform 10 (identifier: Q6QHF9-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     73-489: Missing.

Show »
Length:232
Mass (Da):24,784
Checksum:iB99A956DE69468B8
GO
Isoform 11 (identifier: Q6QHF9-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-267: Missing.
     338-649: MDLVALAPFG...PQVQQPRPRL → TGLCCRDGGR...QPTLFHPCRG

Show »
Length:112
Mass (Da):12,203
Checksum:i2C6A7B68E8D6B5EF
GO
Isoform 12 (identifier: Q6QHF9-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     23-83: IAGLGAAQRL...PSRGNPVFQL → SSRSCLRGKP...QPTLFHPCRG
     84-649: Missing.

Show »
Length:83
Mass (Da):8,695
Checksum:i9775DE41FD8D7693
GO
Isoform 13 (identifier: Q6QHF9-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     14-45: PRVLVVGGGIAGLGAAQRLCGHSAFPHLRVLE → GHGPRRGPHPLGALLRWRGGGGRALDPWALPG
     46-649: Missing.

Show »
Length:45
Mass (Da):4,499
Checksum:iA3DFC1D1AEA13C12
GO

Sequence cautioni

Isoform 6 : The sequence AAS64377.1 differs from that shown. Reason: Frameshift at position 26. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231I → M in AAS64378 (Ref. 2) Curated
Sequence conflicti40 – 401H → Q in AAS64378 (Ref. 2) Curated
Sequence conflicti186 – 1861A → T in AAS64379 (Ref. 2) Curated
Sequence conflicti214 – 2141R → Q in AAN40706 (PubMed:12660232).Curated
Sequence conflicti223 – 2231A → V in AAN40706 (PubMed:12660232).Curated
Sequence conflicti376 – 3761E → G in AAS64376 (Ref. 2) Curated
Sequence conflicti396 – 3961E → K in AAS64373 (Ref. 2) Curated
Sequence conflicti502 – 5021L → F in AAS64381 (Ref. 2) Curated
Sequence conflicti506 – 5061V → G in AAN40706 (PubMed:12660232).Curated
Sequence conflicti551 – 5511N → S in AAS64379 (Ref. 2) Curated
Isoform 5 (identifier: Q6QHF9-4)
Sequence conflicti457 – 4571Q → E in AAS64376 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 267267Missing in isoform 11. 1 PublicationVSP_011247Add
BLAST
Alternative sequencei14 – 4532PRVLV…LRVLE → GHGPRRGPHPLGALLRWRGG GGRALDPWALPG in isoform 13. 1 PublicationVSP_011261Add
BLAST
Alternative sequencei23 – 8361IAGLG…PVFQL → SSRSCLRGKPHIARFTPRRT GLCCRDGWRPTASSVCGPRR CSSPGRGSSWAQPTLFHPCR G in isoform 12. 1 PublicationVSP_011259Add
BLAST
Alternative sequencei31 – 168138Missing in isoform 1, isoform 5, isoform 4 and isoform 8. 4 PublicationsVSP_011249Add
BLAST
Alternative sequencei46 – 649604Missing in isoform 13. 1 PublicationVSP_011262Add
BLAST
Alternative sequencei61 – 8020GGVVE…RGNPV → RVSRTHKLHDGRPAGGHCSF in isoform 6. 1 PublicationVSP_011248Add
BLAST
Alternative sequencei62 – 698GVVEVGAH → AIKDSQTA in isoform 3. 1 PublicationVSP_011250
Alternative sequencei70 – 649580Missing in isoform 3. 1 PublicationVSP_011251Add
BLAST
Alternative sequencei73 – 489417Missing in isoform 10. 1 PublicationVSP_011252Add
BLAST
Alternative sequencei81 – 649569Missing in isoform 6. 1 PublicationVSP_011256Add
BLAST
Alternative sequencei84 – 649566Missing in isoform 12. 1 PublicationVSP_011260Add
BLAST
Alternative sequencei338 – 649312MDLVA…PRPRL → TGLCCRDGGRPTASSVCGPR RCSSPGRGSSWAQPTLFHPC RG in isoform 11. 1 PublicationVSP_011253Add
BLAST
Alternative sequencei429 – 46335FLREH…NKIFL → LSTFSVGSLPDLSLSSWRLC RMKKYFCVSPKCSGE in isoform 4. 1 PublicationVSP_011255Add
BLAST
Alternative sequencei435 – 48248Missing in isoform 8. 1 PublicationVSP_011254Add
BLAST
Alternative sequencei464 – 649186Missing in isoform 4. 1 PublicationVSP_011257Add
BLAST
Alternative sequencei550 – 649100GNPRL…PRPRL → APDPVCGGSHTSHVLLHDAR GSAVGMEGGRPPPQSVGPAG AAAQAQALAGPSLLCSTRVG GRLGPSFLLTDFSLA in isoform 5. 1 PublicationVSP_011258Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF226657 mRNA. Translation: AAN40706.1.
AF312698 mRNA. Translation: AAO63265.1.
AY541513 mRNA. Translation: AAS64373.1.
AY541514 mRNA. Translation: AAS64374.1.
AY541515 mRNA. Translation: AAS64375.1.
AY541516 mRNA. Translation: AAS64376.1.
AY541517 mRNA. Translation: AAS64377.1. Frameshift.
AY541518 mRNA. Translation: AAS64378.1.
AY541519 mRNA. Translation: AAS64379.1.
AY541520 mRNA. Translation: AAS64380.1.
AY541521 mRNA. Translation: AAS64381.1.
AY541522 mRNA. Translation: AAS64382.1.
AY541523 mRNA. Translation: AAS64383.1.
AY541524 mRNA. Translation: AAS64384.1.
AY358418 mRNA. Translation: AAQ88784.1.
AL360181 Genomic DNA. Translation: CAH70287.1.
CH471211 Genomic DNA. Translation: EAW61340.1.
CH471211 Genomic DNA. Translation: EAW61341.1.
CH471211 Genomic DNA. Translation: EAW61344.1.
BC032778 mRNA. Translation: AAH32778.1.
AL834535 mRNA. Translation: CAD39191.1.
CCDSiCCDS7682.1. [Q6QHF9-4]
CCDS7683.1. [Q6QHF9-2]
CCDS7684.1. [Q6QHF9-5]
RefSeqiNP_690875.1. NM_152911.3. [Q6QHF9-2]
NP_997010.1. NM_207127.2. [Q6QHF9-5]
NP_997011.1. NM_207128.2. [Q6QHF9-4]
UniGeneiHs.501578.

Genome annotation databases

EnsembliENST00000278060; ENSP00000278060; ENSG00000148832. [Q6QHF9-2]
ENST00000356306; ENSP00000348654; ENSG00000148832. [Q6QHF9-5]
ENST00000357296; ENSP00000349847; ENSG00000148832. [Q6QHF9-4]
ENST00000476834; ENSP00000432737; ENSG00000148832. [Q6QHF9-6]
ENST00000480071; ENSP00000435514; ENSG00000148832. [Q6QHF9-5]
ENST00000483211; ENSP00000434550; ENSG00000148832. [Q6QHF9-6]
ENST00000529585; ENSP00000432517; ENSG00000148832. [Q6QHF9-6]
GeneIDi196743.
KEGGihsa:196743.
UCSCiuc001lmv.5. human. [Q6QHF9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF226657 mRNA. Translation: AAN40706.1.
AF312698 mRNA. Translation: AAO63265.1.
AY541513 mRNA. Translation: AAS64373.1.
AY541514 mRNA. Translation: AAS64374.1.
AY541515 mRNA. Translation: AAS64375.1.
AY541516 mRNA. Translation: AAS64376.1.
AY541517 mRNA. Translation: AAS64377.1. Frameshift.
AY541518 mRNA. Translation: AAS64378.1.
AY541519 mRNA. Translation: AAS64379.1.
AY541520 mRNA. Translation: AAS64380.1.
AY541521 mRNA. Translation: AAS64381.1.
AY541522 mRNA. Translation: AAS64382.1.
AY541523 mRNA. Translation: AAS64383.1.
AY541524 mRNA. Translation: AAS64384.1.
AY358418 mRNA. Translation: AAQ88784.1.
AL360181 Genomic DNA. Translation: CAH70287.1.
CH471211 Genomic DNA. Translation: EAW61340.1.
CH471211 Genomic DNA. Translation: EAW61341.1.
CH471211 Genomic DNA. Translation: EAW61344.1.
BC032778 mRNA. Translation: AAH32778.1.
AL834535 mRNA. Translation: CAD39191.1.
CCDSiCCDS7682.1. [Q6QHF9-4]
CCDS7683.1. [Q6QHF9-2]
CCDS7684.1. [Q6QHF9-5]
RefSeqiNP_690875.1. NM_152911.3. [Q6QHF9-2]
NP_997010.1. NM_207127.2. [Q6QHF9-5]
NP_997011.1. NM_207128.2. [Q6QHF9-4]
UniGeneiHs.501578.

3D structure databases

ProteinModelPortaliQ6QHF9.
SMRiQ6QHF9. Positions 13-83, 181-637.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128224. 1 interaction.
STRINGi9606.ENSP00000278060.

Chemistry

BindingDBiQ6QHF9.
ChEMBLiCHEMBL2105.

PTM databases

PhosphoSiteiQ6QHF9.

Polymorphism and mutation databases

DMDMi51316248.

Proteomic databases

MaxQBiQ6QHF9.
PaxDbiQ6QHF9.
PRIDEiQ6QHF9.

Protocols and materials databases

DNASUi196743.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000278060; ENSP00000278060; ENSG00000148832. [Q6QHF9-2]
ENST00000356306; ENSP00000348654; ENSG00000148832. [Q6QHF9-5]
ENST00000357296; ENSP00000349847; ENSG00000148832. [Q6QHF9-4]
ENST00000476834; ENSP00000432737; ENSG00000148832. [Q6QHF9-6]
ENST00000480071; ENSP00000435514; ENSG00000148832. [Q6QHF9-5]
ENST00000483211; ENSP00000434550; ENSG00000148832. [Q6QHF9-6]
ENST00000529585; ENSP00000432517; ENSG00000148832. [Q6QHF9-6]
GeneIDi196743.
KEGGihsa:196743.
UCSCiuc001lmv.5. human. [Q6QHF9-1]

Organism-specific databases

CTDi196743.
GeneCardsiPAOX.
HGNCiHGNC:20837. PAOX.
HPAiHPA047782.
MIMi615853. gene.
neXtProtiNX_Q6QHF9.
PharmGKBiPA134907695.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0685. Eukaryota.
ENOG410XQW0. LUCA.
GeneTreeiENSGT00530000062888.
HOVERGENiHBG053499.
InParanoidiQ6QHF9.
KOiK00308.
OMAiGHSAFPH.
PhylomeDBiQ6QHF9.
TreeFamiTF318348.

Enzyme and pathway databases

UniPathwayiUPA00826.
BRENDAi1.5.3.13. 2681.
ReactomeiR-HSA-141334. PAOs oxidise polyamines to amines.
R-HSA-351200. Interconversion of polyamines.
SABIO-RKQ6QHF9.

Miscellaneous databases

GeneWikiiPAOX.
GenomeRNAii196743.
NextBioi89545.
PROiQ6QHF9.
SOURCEiSearch...

Gene expression databases

BgeeiQ6QHF9.
CleanExiHS_PAOX.
ExpressionAtlasiQ6QHF9. baseline and differential.
GenevisibleiQ6QHF9. HS.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 2 hits.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N(1)-acetylated polyamine oxidase."
    Wu T., Yankovskaya V., McIntire W.S.
    J. Biol. Chem. 278:20514-20525(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "Polyamine oxidase."
    Wang Y., Murray-Stewart T., Hacker A., Casero R.A. Jr.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6; 8; 9; 10; 11; 12 AND 13).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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 1).
    Tissue: Brain.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 364-649 (ISOFORM 9).
    Tissue: Testis.
  8. "Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion."
    Vujcic S., Liang P., Diegelman P., Kramer D.L., Porter C.W.
    Biochem. J. 370:19-28(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION, TISSUE SPECIFICITY.
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPAOX_HUMAN
AccessioniPrimary (citable) accession number: Q6QHF9
Secondary accession number(s): D3DXI6
, Q5VWY0, Q6QHF5, Q6QHF6, Q6QHF7, Q6QHF8, Q6QHG0, Q6QHG1, Q6QHG2, Q6QHG3, Q6QHG4, Q6QHG5, Q6QHG6, Q86WP9, Q8N555, Q8NCX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 120 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

Oxidizes N(1)-acetylated polyamines on the exo-side of their N(4)-amino groups. Plant PAO oxidizes spermine on the endo-side of the N(4)-nitrogen (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. 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.