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Reviewed, UniProtKB/Swiss-Prot Q9NYQ3 (HAOX2_HUMAN)

Last modified October 13, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Hydroxyacid oxidase 2
      Short name=HAOX2
    EC=1.1.3.15
Alternative name(s):
    (S)-2-hydroxy-acid oxidase, peroxisomal
    Long chain alpha-hydroxy acid oxidase
    Long-chain L-2-hydroxy acid oxidase
Gene names
Name: HAO2
Synonyms: HAOX2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Catalyzes the oxidation of L-alpha-hydroxy acids as well as, more slowly, that of L-alpha-amino acids.

Catalytic activity

(S)-2-hydroxy acid + O2 = 2-oxo acid + H2O2.

Cofactor

FMN.

Subunit structure

Homotetramer or homooctamer By similarity.

Subcellular location

Peroxisome.

Tissue specificity

Liver and kidney.

Sequence similarities

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.

Contains 1 FMN hydroxy acid dehydrogenase domain.

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Ontologies

Keywords
   Cellular componentPeroxisome
   Coding sequence diversityPolymorphism
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfatty acid alpha-oxidation Ref.1

Traceable author statement. Source: UniProtKB

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome Ref.1

Traceable author statement. Source: UniProtKB

   Molecular function(S)-2-hydroxy-acid oxidase activity Ref.1

Traceable author statement. Source: UniProtKB

FMN binding

Inferred from electronic annotation. Source: InterPro

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 351351Hydroxyacid oxidase 2
PRO_0000206320

Regions

Domain1 – 351351FMN hydroxy acid dehydrogenase
Nucleotide binding277 – 30125FMN By similarity
Motif349 – 3513Microbody targeting signal Potential

Sites

Active site2461Proton acceptor By similarity
Binding site1061FMN By similarity
Binding site1281FMN By similarity
Binding site1301Substrate By similarity
Binding site1561FMN By similarity
Binding site1651Substrate By similarity
Binding site2221FMN By similarity
Binding site2491Substrate Potential

Natural variations

Natural variant151E → K: dbSNP rs34638261.
VAR_049087
Natural variant2211L → M: dbSNP rs6661625.
VAR_049088

Experimental info

Sequence conflict801F → Y in AAF14000. Ref.2
Sequence conflict292 – 2943LGA → HED in AAF14000. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q9NYQ3-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 7330DE44E282947D

FASTA35138,839
        10         20         30         40         50         60 
MSLVCLTDFQ AHAREQLSKS TRDFIEGGAD DSITRDDNIA AFKRIRLRPR YLRDVSEVDT 

        70         80         90        100        110        120 
RTTIQGEEIS APICIAPTGF HCLVWPDGEM STARAAQAAG ICYITSTFAS CSLEDIVIAA 

       130        140        150        160        170        180 
PEGLRWFQLY VHPDLQLNKQ LIQRVESLGF KALVITLDTP VCGNRRHDIR NQLRRNLTLT 

       190        200        210        220        230        240 
DLQSPKKGNA IPYFQMTPIS TSLCWNDLSW FQSITRLPII LKGILTKEDA ELAVKHNVQG 

       250        260        270        280        290        300 
IIVSNHGGRQ LDEVLASIDA LTEVVAAVKG KIEVYLDGGV RTGNDVLKAL ALGAKCIFLG 

       310        320        330        340        350 
RPILWGLACK GEHGVKEVLN ILTNEFHTSM ALTGCRSVAE INRNLVQFSR L

« Hide

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References

« Hide 'large scale' references
[1]"Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases."
Jones J.M., Morrell J.C., Gould S.J.
J. Biol. Chem. 275:12590-12597(2000) [PubMed: 10777549] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human long-chain L-2-hydroxy acid oxidase."
Spielbauer B., Conzelmann E.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF231917 mRNA. Translation: AAF40200.1.
AF203975 mRNA. Translation: AAF14000.1.
AL359553 Genomic DNA. Translation: CAC19798.1.
BC020863 mRNA. Translation: AAH20863.1.
IPIIPI00021109.
RefSeqNP_001005783.1.
NP_057611.1.
UniGeneHs.659767

3D structure databases

HSSPHSSP built from PDB template 1GOX based on UniProtKB P05414.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9NYQ3.

PTM databases

PhosphoSiteQ9NYQ3.

Proteomic databases

PRIDEQ9NYQ3.

Genome annotation databases

EnsemblENST00000325945; ENSP00000316339; ENSG00000116882; Homo sapiens. [Genome view]
ENST00000361035; ENSP00000354314; ENSG00000116882; Homo sapiens. [Genome view]
ENST00000369420; ENSP00000358428; ENSG00000116882; Homo sapiens. [Genome view]
ENST00000457318; ENSP00000393955; ENSG00000116882; Homo sapiens. [Genome view]
GeneID51179.
KEGGhsa:51179.
UCSCuc001ehq.1. human.

Organism-specific databases

CTD51179.
GeneCardsGC01P119623.
H-InvDBHIX0000947.
HGNCHGNC:4810. HAO2.
MIM605176. gene.
PharmGKBPA29186.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9NYQ3.
HOVERGENQ9NYQ3.

Enzyme and pathway databases

BRENDA1.1.3.15. 247.

Gene expression databases

ArrayExpressQ9NYQ3.
BgeeQ9NYQ3.
CleanExHS_HAO2.
GenevestigatorQ9NYQ3.
GermOnlineENSG00000116882. Homo sapiens.

Family and domain databases

InterProIPR012133. a-Hydoxy_acid_DH_FMN.
IPR013785. Aldolase_TIM.
IPR000262. FMN-dep_DH.
IPR017934. FMN-dep_OHA_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PfamPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio54141.
SOURCESearch...

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Entry information

Entry nameHAOX2_HUMAN
AccessionPrimary (citable) accession number: Q9NYQ3
Secondary accession number(s): Q9UJS6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: October 13, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents