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Protein

Hydroxyacid oxidase 2

Gene

HAO2

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

Functioni

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

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061FMNPROSITE-ProRule annotation
Binding sitei128 – 1281FMNPROSITE-ProRule annotation
Binding sitei130 – 1301SubstratePROSITE-ProRule annotation
Binding sitei156 – 1561FMNPROSITE-ProRule annotation
Binding sitei165 – 1651SubstratePROSITE-ProRule annotation
Binding sitei222 – 2221FMNPROSITE-ProRule annotation
Active sitei246 – 2461Proton acceptorPROSITE-ProRule annotation
Binding sitei249 – 2491SubstratePROSITE-ProRule annotation
Binding sitei301 – 3011FMNPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi277 – 30125FMNPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • (S)-2-hydroxy-acid oxidase activity Source: UniProtKB
  • FMN binding Source: InterPro
  • long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity Source: UniProtKB
  • medium-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC
  • receptor binding Source: UniProtKB
  • very-long-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC

GO - Biological processi

  • fatty acid oxidation Source: UniProtKB
  • mandelate metabolic process Source: Ensembl
  • protein homooligomerization Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Flavoprotein, FMN

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxyacid oxidase 2 (EC:1.1.3.15)
Short name:
HAOX2
Alternative name(s):
(S)-2-hydroxy-acid oxidase, peroxisomal
Cell growth-inhibiting gene 16 protein
Long chain alpha-hydroxy acid oxidase
Long-chain L-2-hydroxy acid oxidase
Gene namesi
Name:HAO2
Synonyms:HAOX2
ORF Names:GIG16
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4810. HAO2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: Ensembl
  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29186.

Polymorphism and mutation databases

BioMutaiHAO2.
DMDMi13124287.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 351350Hydroxyacid oxidase 2PRO_0000206320Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei178 – 1781Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9NYQ3.
PRIDEiQ9NYQ3.

PTM databases

PhosphoSiteiQ9NYQ3.

Expressioni

Tissue specificityi

Liver and kidney.

Gene expression databases

BgeeiQ9NYQ3.
CleanExiHS_HAO2.
ExpressionAtlasiQ9NYQ3. baseline and differential.
GenevisibleiQ9NYQ3. HS.

Organism-specific databases

HPAiHPA045773.

Interactioni

Subunit structurei

Homotetramer or homooctamer.By similarity

Protein-protein interaction databases

BioGridi119356. 1 interaction.
IntActiQ9NYQ3. 1 interaction.
STRINGi9606.ENSP00000316339.

Structurei

3D structure databases

ProteinModelPortaliQ9NYQ3.
SMRiQ9NYQ3. Positions 3-348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 351350FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi349 – 3513Microbody targeting signalSequence Analysis

Sequence similaritiesi

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.PROSITE-ProRule annotation
Contains 1 FMN hydroxy acid dehydrogenase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1304.
GeneTreeiENSGT00390000018717.
HOGENOMiHOG000217463.
HOVERGENiHBG051881.
InParanoidiQ9NYQ3.
KOiK11517.
OMAiEGPEMSL.
PhylomeDBiQ9NYQ3.
TreeFamiTF313363.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: Q9NYQ3-1) [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
MSLVCLTDFQ AHAREQLSKS TRDFIEGGAD DSITRDDNIA AFKRIRLRPR
60 70 80 90 100
YLRDVSEVDT RTTIQGEEIS APICIAPTGF HCLVWPDGEM STARAAQAAG
110 120 130 140 150
ICYITSTFAS CSLEDIVIAA PEGLRWFQLY VHPDLQLNKQ LIQRVESLGF
160 170 180 190 200
KALVITLDTP VCGNRRHDIR NQLRRNLTLT DLQSPKKGNA IPYFQMTPIS
210 220 230 240 250
TSLCWNDLSW FQSITRLPII LKGILTKEDA ELAVKHNVQG IIVSNHGGRQ
260 270 280 290 300
LDEVLASIDA LTEVVAAVKG KIEVYLDGGV RTGNDVLKAL ALGAKCIFLG
310 320 330 340 350
RPILWGLACK GEHGVKEVLN ILTNEFHTSM ALTGCRSVAE INRNLVQFSR

L
Length:351
Mass (Da):38,839
Last modified:October 1, 2000 - v1
Checksum:i7330DE44E282947D
GO
Isoform 2 (identifier: Q9NYQ3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEDKMWSECEGPEM

Note: No experimental confirmation available.
Show »
Length:364
Mass (Da):40,391
Checksum:i13F52C5D431E8B2E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801F → Y in AAF14000 (Ref. 2) Curated
Sequence conflicti292 – 2943LGA → HED in AAF14000 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151E → K.
Corresponds to variant rs34638261 [ dbSNP | Ensembl ].
VAR_049087
Natural varianti221 – 2211L → M.
Corresponds to variant rs6661625 [ dbSNP | Ensembl ].
VAR_049088

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MEDKMWSECEGPEM in isoform 2. 1 PublicationVSP_055095

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF231917 mRNA. Translation: AAF40200.1.
AF203975 mRNA. Translation: AAF14000.1.
AY513277 mRNA. Translation: AAT08030.1.
AK298289 mRNA. Translation: BAG60549.1.
AL139346 Genomic DNA. No translation available.
AL359553 Genomic DNA. Translation: CAC19798.1.
CH471122 Genomic DNA. Translation: EAW56698.1.
CH471122 Genomic DNA. Translation: EAW56699.1.
BC020863 mRNA. Translation: AAH20863.1.
CCDSiCCDS901.1. [Q9NYQ3-1]
RefSeqiNP_001005783.2. NM_001005783.2. [Q9NYQ3-2]
NP_057611.1. NM_016527.3. [Q9NYQ3-1]
UniGeneiHs.659767.

Genome annotation databases

EnsembliENST00000325945; ENSP00000316339; ENSG00000116882. [Q9NYQ3-1]
ENST00000361035; ENSP00000354314; ENSG00000116882. [Q9NYQ3-2]
ENST00000622548; ENSP00000483507; ENSG00000116882. [Q9NYQ3-1]
GeneIDi51179.
KEGGihsa:51179.
UCSCiuc001ehq.1. human. [Q9NYQ3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF231917 mRNA. Translation: AAF40200.1.
AF203975 mRNA. Translation: AAF14000.1.
AY513277 mRNA. Translation: AAT08030.1.
AK298289 mRNA. Translation: BAG60549.1.
AL139346 Genomic DNA. No translation available.
AL359553 Genomic DNA. Translation: CAC19798.1.
CH471122 Genomic DNA. Translation: EAW56698.1.
CH471122 Genomic DNA. Translation: EAW56699.1.
BC020863 mRNA. Translation: AAH20863.1.
CCDSiCCDS901.1. [Q9NYQ3-1]
RefSeqiNP_001005783.2. NM_001005783.2. [Q9NYQ3-2]
NP_057611.1. NM_016527.3. [Q9NYQ3-1]
UniGeneiHs.659767.

3D structure databases

ProteinModelPortaliQ9NYQ3.
SMRiQ9NYQ3. Positions 3-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119356. 1 interaction.
IntActiQ9NYQ3. 1 interaction.
STRINGi9606.ENSP00000316339.

Chemistry

BindingDBiQ9NYQ3.
ChEMBLiCHEMBL2169732.

PTM databases

PhosphoSiteiQ9NYQ3.

Polymorphism and mutation databases

BioMutaiHAO2.
DMDMi13124287.

Proteomic databases

PaxDbiQ9NYQ3.
PRIDEiQ9NYQ3.

Protocols and materials databases

DNASUi51179.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000325945; ENSP00000316339; ENSG00000116882. [Q9NYQ3-1]
ENST00000361035; ENSP00000354314; ENSG00000116882. [Q9NYQ3-2]
ENST00000622548; ENSP00000483507; ENSG00000116882. [Q9NYQ3-1]
GeneIDi51179.
KEGGihsa:51179.
UCSCiuc001ehq.1. human. [Q9NYQ3-1]

Organism-specific databases

CTDi51179.
GeneCardsiGC01P119913.
HGNCiHGNC:4810. HAO2.
HPAiHPA045773.
MIMi605176. gene.
neXtProtiNX_Q9NYQ3.
PharmGKBiPA29186.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1304.
GeneTreeiENSGT00390000018717.
HOGENOMiHOG000217463.
HOVERGENiHBG051881.
InParanoidiQ9NYQ3.
KOiK11517.
OMAiEGPEMSL.
PhylomeDBiQ9NYQ3.
TreeFamiTF313363.

Miscellaneous databases

ChiTaRSiHAO2. human.
GenomeRNAii51179.
NextBioi54141.
PROiQ9NYQ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NYQ3.
CleanExiHS_HAO2.
ExpressionAtlasiQ9NYQ3. baseline and differential.
GenevisibleiQ9NYQ3. HS.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORM 1).
  3. "Identification of a human cell growth inhibiting gene."
    Kim J.W.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "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] (ISOFORM 2).
    Tissue: Kidney.
  5. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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: Kidney.
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHAOX2_HUMAN
AccessioniPrimary (citable) accession number: Q9NYQ3
Secondary accession number(s): Q2TU86, Q5QP00, Q9UJS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 121 of the entry and version 1 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.