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UniProtKB - Q9UJM8 (HAOX1_HUMAN)

Entry version 181 (23 Feb 2022)
Sequence version 1 (01 May 2000)
Previous versions | rss
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Protein

2-Hydroxyacid oxidase 1

Gene

HAO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Broad substrate specificity (S)-2-hydroxy-acid oxidase that preferentially oxidizes glycolate (PubMed:10777549, PubMed:17669354, PubMed:18215067, PubMed:10978532).

The glyoxylate produced by the oxidation of glycolate can then be utilized by alanine-glyoxylate aminotransferase for the peroxisomal synthesis of glycine; this pathway appears to be an important step for the detoxification of glyoxylate which, if allowed to accumulate, may be metabolized to oxalate with formation of kidney stones (PubMed:10978532, PubMed:17669354).

Can also catalyze the oxidation of glyoxylate, and long chain hydroxyacids such as 2-hydroxyhexadecanoate and 2-hydroxyoctanoate, albeit with much lower catalytic efficiency (PubMed:10777549, PubMed:17669354, PubMed:18215067).

Active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCIP), but O2 is believed to be the physiological electron acceptor, leading to the production of H2O2 (PubMed:10777549, PubMed:17669354, PubMed:18215067, PubMed:10978532).

Is not active on L-lactate and 2-hydroxybutanoate (PubMed:10777549).

2 Publications4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FMN2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by its product oxalate (PubMed:17669354). Inhibited by high concentrations of dichlorophenolindophenol (DCIP) in vitro (PubMed:17669354).1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 3.6 sec(-1) for the oxidation of glycolate with DCIP as electron acceptor (at pH 7.0 and 37 degrees Celsius) (PubMed:17669354). kcat is 4.1 sec(-1) for the oxidation of glycolate with DCIP as electron acceptor (at pH 7.5 and 37 degrees Celsius) (PubMed:18215067). kcat is 0.7 sec(-1) for the oxidation of glyoxylate with DCIP as electron acceptor (at pH 7.5 and 37 degrees Celsius) (PubMed:18215067). kcat is 0.83 sec(-1) for the oxidation of glyoxylate with DCIP as electron acceptor (at pH 7.0 and 37 degrees Celsius) (PubMed:17669354). kcat is 0.46 sec(-1) for the oxidation of L-lactate with DCIP as electron acceptor (at pH 7.0 and 37 degrees Celsius) (PubMed:17669354). kcat is 0.11 sec(-1) for the oxidation of L-mandelate with DCIP as electron acceptor (at pH 7.0 and 37 degrees Celsius) (PubMed:17669354). Shows a higher catalytic efficiency for glycolate compared to glyoxylate (PubMed:17669354, PubMed:18215067).2 Publications
  1. KM=120 µM for glycolate (at pH 7.5, with DCIP as electron acceptor)1 Publication
  2. KM=141 µM for glycolate (at pH 7.5 and 37 degrees Celsius, with DCIP as electron acceptor)1 Publication
  3. KM=56 µM for glycolate (at pH 7.0 and 37 degrees Celsius, with DCIP as electron acceptor)1 Publication
  4. KM=40 µM for 2-hydroxy octanoate (at pH 7.5 and 37 degrees Celsius, with DCIP as electron acceptor)1 Publication
  5. KM=2200 µM for glyoxylate (at pH 7.5 and 37 degrees Celsius, with DCIP as electron acceptor)1 Publication
  6. KM=3400 µM for glyoxylate (at pH 7.0 and 37 degrees Celsius, with DCIP as electron acceptor)1 Publication
  7. KM=16.5 mM for L-lactate (at pH 7.0 and 37 degrees Celsius, with DCIP as electron acceptor)1 Publication
  8. KM=1.5 mM for L-mandelate (at pH 7.0 and 37 degrees Celsius, with DCIP as electron acceptor)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glycine biosynthesis

This protein is involved in the pathway glycine biosynthesis, which is part of Amino-acid biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway glycine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei26GlyoxylateCombined sources1 Publication1
Binding sitei108FMNPROSITE-ProRule annotationCombined sources3 Publications1
Binding sitei130FMNPROSITE-ProRule annotationCombined sources2 Publications1
Binding sitei132GlyoxylateCombined sources1 Publication1
Binding sitei158FMNPROSITE-ProRule annotationCombined sources3 Publications1
Binding sitei167GlyoxylateCombined sources2 Publications1
Binding sitei236FMNPROSITE-ProRule annotationCombined sources3 Publications1
Binding sitei258FMNCombined sources3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei260Proton acceptorPROSITE-ProRule annotation1
Binding sitei260GlyoxylateCombined sources1 Publication1
Binding sitei263GlyoxylateCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi79 – 81FMNCombined sources2 Publications3
Nucleotide bindingi291 – 295FMNCombined sources3 Publications5
Nucleotide bindingi314 – 315FMNCombined sources3 Publications2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis
LigandFlavoprotein, FMN

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.1.3.15, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q9UJM8

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-389661, Glyoxylate metabolism and glycine degradation
R-HSA-9033241, Peroxisomal protein import

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q9UJM8

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		Q9UJM8

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00288

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
2-Hydroxyacid oxidase 11 Publication (EC:1.1.3.154 Publications)
Short name:
HAOX11 Publication
Alternative name(s):
Glycolate oxidase1 Publication
Short name:
GO1 Publication
Short name:
GOX1 Publication
Glyoxylate oxidase1 Publication (EC:1.2.3.53 Publications)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:HAO11 PublicationImported
Synonyms:GOX1Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 20

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:4809, HAO1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		605023, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9UJM8

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000101323

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Peroxisome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

DisGeNET

More...DisGeNETi		54363

Open Targets

More...OpenTargetsi		ENSG00000101323

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA29185

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9UJM8, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4229

Drug and drug target database

More...DrugBanki		DB07907, (2S)-2-HYDROXYOCTANOIC ACID
DB07060, 3-(INDOL-3-YL) LACTATE
DB03064, 3-Decyl-2,5-Dioxo-4-Hydroxy-3-Pyrroline
DB04374, 4-Carboxy-5-(1-Pentyl)Hexylsulfanyl-1,2,3-Triazole
DB06979, 5-(dodecylthio)-1H-1,2,3-triazole-4-carboxylic acid
DB02279, Benzoylformic Acid
DB03247, Flavin mononucleotide
DB15935, Lumasiran
DB02164, N-sulfo-flavin mononucleotide
DB03884, Phenylpyruvic acid

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		HAO1

Domain mapping of disease mutations (DMDM)

More...DMDMi		13124294

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002063181 – 3702-Hydroxyacid oxidase 1Add BLAST370

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei184N6-succinyllysineBy similarity1
Modified residuei194PhosphoserineBy similarity1
Modified residuei230PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9UJM8

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q9UJM8

PeptideAtlas

More...PeptideAtlasi		Q9UJM8

PRoteomics IDEntifications database

More...PRIDEi		Q9UJM8

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		84633

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9UJM8

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q9UJM8

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in liver.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000101323, Expressed in right lobe of liver and 27 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9UJM8, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9UJM8, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000101323, Tissue enriched (liver)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		119941, 4 interactors

Protein interaction database and analysis system

More...IntActi		Q9UJM8, 3 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000368066

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9UJM8

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9UJM8, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1370
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q9UJM8

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9UJM8

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 365FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd BLAST365

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi368 – 370Microbody targeting signalSequence analysis3

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0538, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000018717

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_020639_6_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9UJM8

Identification of Orthologs from Complete Genome Data

More...OMAi		FTRLMQT

Database of Orthologous Groups

More...OrthoDBi		879633at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9UJM8

TreeFam database of animal gene trees

More...TreeFami		TF313363

Family and domain databases

Conserved Domains Database

More...CDDi		cd02809, alpha_hydroxyacid_oxid_FMN, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.20.20.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013785, Aldolase_TIM
IPR012133, Alpha-hydoxy_acid_DH_FMN
IPR000262, FMN-dep_DH
IPR037396, FMN_HAD
IPR008259, FMN_hydac_DH_AS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01070, FMN_dh, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000138, Al-hdrx_acd_dh, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00557, FMN_HYDROXY_ACID_DH_1, 1 hit
PS51349, FMN_HYDROXY_ACID_DH_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q9UJM8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLPRLICIND YEQHAKSVLP KSIYDYYRSG ANDEETLADN IAAFSRWKLY 
        60         70         80         90        100
PRMLRNVAET DLSTSVLGQR VSMPICVGAT AMQRMAHVDG ELATVRACQS 
       110        120        130        140        150
LGTGMMLSSW ATSSIEEVAE AGPEALRWLQ LYIYKDREVT KKLVRQAEKM 
       160        170        180        190        200
GYKAIFVTVD TPYLGNRLDD VRNRFKLPPQ LRMKNFETST LSFSPEENFG 
       210        220        230        240        250
DDSGLAAYVA KAIDPSISWE DIKWLRRLTS LPIVAKGILR GDDAREAVKH 
       260        270        280        290        300
GLNGILVSNH GARQLDGVPA TIDVLPEIVE AVEGKVEVFL DGGVRKGTDV 
       310        320        330        340        350
LKALALGAKA VFVGRPIVWG LAFQGEKGVQ DVLEILKEEF RLAMALSGCQ 
       360        370
NVKVIDKTLV RKNPLAVSKI
Length:370
Mass (Da):40,924
Last modified:May 1, 2000 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC683C6F7CB5FD323
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF244134 mRNA Translation: AAF63219.1
AF231916 mRNA Translation: AAF40199.1
AL121739 mRNA Translation: CAB57329.1
AB024079 mRNA Translation: BAA82872.1
AL021879 Genomic DNA No translation available.
BC113665 mRNA Translation: AAI13666.1
BC113667 mRNA Translation: AAI13668.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS13100.1

NCBI Reference Sequences

More...RefSeqi		NP_060015.1, NM_017545.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000378789; ENSP00000368066; ENSG00000101323

Database of genes from NCBI RefSeq genomes

More...GeneIDi		54363

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:54363

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000378789.4; ENSP00000368066.3; NM_017545.3; NP_060015.1

UCSC genome browser

More...UCSCi		uc002wmw.2, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF244134 mRNA Translation: AAF63219.1
AF231916 mRNA Translation: AAF40199.1
AL121739 mRNA Translation: CAB57329.1
AB024079 mRNA Translation: BAA82872.1
AL021879 Genomic DNA No translation available.
BC113665 mRNA Translation: AAI13666.1
BC113667 mRNA Translation: AAI13668.1
CCDSiCCDS13100.1
RefSeqiNP_060015.1, NM_017545.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NZLX-ray1.35A1-370[»]
2RDTX-ray1.95A1-370[»]
2RDUX-ray1.65A1-370[»]
2RDWX-ray1.95A1-370[»]
2W0UX-ray2.84A/B/C/D1-370[»]
5QIBX-ray1.48A1-368[»]
5QICX-ray1.34A1-368[»]
5QIDX-ray1.45A1-368[»]
5QIEX-ray1.34A1-368[»]
5QIFX-ray1.20A1-368[»]
5QIGX-ray1.42A1-368[»]
5QIHX-ray1.33A1-368[»]
6GMBX-ray1.35A1-362[»]
6GMCX-ray1.20A1-362[»]
6W44X-ray1.64A1-368[»]
6W45X-ray1.70A1-368[»]
6W4CX-ray1.75A1-368[»]
7M2OX-ray2.07A1-370[»]
SMRiQ9UJM8
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi119941, 4 interactors
IntActiQ9UJM8, 3 interactors
STRINGi9606.ENSP00000368066

Chemistry databases

BindingDBiQ9UJM8
ChEMBLiCHEMBL4229
DrugBankiDB07907, (2S)-2-HYDROXYOCTANOIC ACID
DB07060, 3-(INDOL-3-YL) LACTATE
DB03064, 3-Decyl-2,5-Dioxo-4-Hydroxy-3-Pyrroline
DB04374, 4-Carboxy-5-(1-Pentyl)Hexylsulfanyl-1,2,3-Triazole
DB06979, 5-(dodecylthio)-1H-1,2,3-triazole-4-carboxylic acid
DB02279, Benzoylformic Acid
DB03247, Flavin mononucleotide
DB15935, Lumasiran
DB02164, N-sulfo-flavin mononucleotide
DB03884, Phenylpyruvic acid

PTM databases

iPTMnetiQ9UJM8
PhosphoSitePlusiQ9UJM8

Genetic variation databases

BioMutaiHAO1
DMDMi13124294

Proteomic databases

MassIVEiQ9UJM8
PaxDbiQ9UJM8
PeptideAtlasiQ9UJM8
PRIDEiQ9UJM8
ProteomicsDBi84633

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		8448, 398 antibodies from 32 providers

The DNASU plasmid repository

More...DNASUi		54363

Genome annotation databases

EnsembliENST00000378789; ENSP00000368066; ENSG00000101323
GeneIDi54363
KEGGihsa:54363
MANE-SelectiENST00000378789.4; ENSP00000368066.3; NM_017545.3; NP_060015.1
UCSCiuc002wmw.2, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		54363
DisGeNETi54363

GeneCards: human genes, protein and diseases

More...GeneCardsi		HAO1
HGNCiHGNC:4809, HAO1
HPAiENSG00000101323, Tissue enriched (liver)
MIMi605023, gene
neXtProtiNX_Q9UJM8
OpenTargetsiENSG00000101323
PharmGKBiPA29185
VEuPathDBiHostDB:ENSG00000101323

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0538, Eukaryota
GeneTreeiENSGT00390000018717
HOGENOMiCLU_020639_6_1_1
InParanoidiQ9UJM8
OMAiFTRLMQT
OrthoDBi879633at2759
PhylomeDBiQ9UJM8
TreeFamiTF313363

Enzyme and pathway databases

UniPathwayiUPA00288
BRENDAi1.1.3.15, 2681
PathwayCommonsiQ9UJM8
ReactomeiR-HSA-389661, Glyoxylate metabolism and glycine degradation
R-HSA-9033241, Peroxisomal protein import
SABIO-RKiQ9UJM8
SignaLinkiQ9UJM8

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		54363, 1 hit in 1032 CRISPR screens
EvolutionaryTraceiQ9UJM8

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		54363
PharosiQ9UJM8, Tchem

Protein Ontology

More...PROi		PR:Q9UJM8
RNActiQ9UJM8, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000101323, Expressed in right lobe of liver and 27 other tissues
ExpressionAtlasiQ9UJM8, baseline and differential
GenevisibleiQ9UJM8, HS

Family and domain databases

CDDicd02809, alpha_hydroxyacid_oxid_FMN, 1 hit
Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785, Aldolase_TIM
IPR012133, Alpha-hydoxy_acid_DH_FMN
IPR000262, FMN-dep_DH
IPR037396, FMN_HAD
IPR008259, FMN_hydac_DH_AS
PfamiView protein in Pfam
PF01070, FMN_dh, 1 hit
PIRSFiPIRSF000138, Al-hdrx_acd_dh, 1 hit
PROSITEiView protein in PROSITE
PS00557, FMN_HYDROXY_ACID_DH_1, 1 hit
PS51349, FMN_HYDROXY_ACID_DH_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHAOX1_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9UJM8
Secondary accession number(s): Q14CQ0, Q9UPZ0, Q9Y3I7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: February 23, 2022
This is version 181 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families
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