HAO1

Functionⁱ

Has 2-hydroxyacid oxidase activity. Most active on the 2-carbon substrate glycolate, but is also active on 2-hydroxy fatty acids, with high activity towards 2-hydroxy palmitate and 2-hydroxy octanoate.1 Publication

Catalytic activityⁱ

(S)-2-hydroxy acid + O₂ = 2-oxo acid + H₂O₂.1 Publication

Cofactorⁱ

FMNPROSITE-ProRule annotation1 Publication

Kineticsⁱ

K_M=
141 µM for glycolate
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design."
  Murray M.S., Holmes R.P., Lowther W.T.
  Biochemistry 47:2439-2449(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH FMN; GLYOXYLATE AND 4-CARBOXY-5-DODECYLSULFANYL-1,2,3-TRIAZOLE, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
K_M=
40 µM for 2-hydroxy octanoate
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design."
  Murray M.S., Holmes R.P., Lowther W.T.
  Biochemistry 47:2439-2449(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH FMN; GLYOXYLATE AND 4-CARBOXY-5-DODECYLSULFANYL-1,2,3-TRIAZOLE, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
K_M=
2200 µM for glyoxylate
1 Publication
Manual assertion based on experiment inⁱ
- Ref.8
  "Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design."
  Murray M.S., Holmes R.P., Lowther W.T.
  Biochemistry 47:2439-2449(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH FMN; GLYOXYLATE AND 4-CARBOXY-5-DODECYLSULFANYL-1,2,3-TRIAZOLE, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

Pathwayⁱ: glycolate degradation

This protein is involved in step 1 of the subpathway that synthesizes 3-phospho-D-glycerate from glycolate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:

Hydroxyacid oxidase 1 (HAO1)
no protein annotated in this organism
no protein annotated in this organism
no protein annotated in this organism

This subpathway is part of the pathway glycolate degradation, which is itself part of Organic acid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 3-phospho-D-glycerate from glycolate, the pathway glycolate degradation and in Organic acid metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	26	Substrate	1
Binding siteⁱ	108	FMNPROSITE-ProRule annotation3 Publications	1
Binding siteⁱ	130	FMNPROSITE-ProRule annotation3 Publications	1
Binding siteⁱ	132	FMNPROSITE-ProRule annotation3 Publications	1
Binding siteⁱ	132	Substrate	1
Binding siteⁱ	158	FMNPROSITE-ProRule annotation3 Publications	1
Binding siteⁱ	167	Substrate	1
Binding siteⁱ	236	FMNPROSITE-ProRule annotation3 Publications	1
Binding siteⁱ	258	FMNPROSITE-ProRule annotation3 Publications	1
Active siteⁱ	260	Proton acceptor	1
Binding siteⁱ	263	Substrate	1
Binding siteⁱ	315	FMNPROSITE-ProRule annotation3 Publications	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	291 – 315	FMNPROSITE-ProRule annotationAdd BLAST		25
Nucleotide bindingⁱ	291 – 295	FMN bindingPROSITE-ProRule annotation3 Publications		5

GO - Molecular functionⁱ

(S)-2-hydroxy-acid oxidase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 10777549
- 18215067
FMN binding
Source: UniProtKB
Inferred from direct assayⁱ
- 18215067
glycolate oxidase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 10777549
- 18215067
glyoxylate oxidase activity Source: Reactome
long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity Source: UniProtKB-EC
medium-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC
signaling receptor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 20178365
very-long-chain-(S)-2-hydroxy-acid oxidase activity Source: UniProtKB-EC

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular nitrogen compound metabolic process Source: Reactome
fatty acid alpha-oxidation
Source: UniProtKB
Inferred from direct assayⁱ
- 18215067
glycolate catabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 18215067
protein targeting to peroxisome Source: Reactome
response to oxidative stress Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Ligand	Flavoprotein, FMN

Enzyme and pathway databases

BRENDAⁱ	1.1.3.15 2681
Reactomeⁱ	R-HSA-389661 Glyoxylate metabolism and glycine degradation R-HSA-9033241 Peroxisomal protein import
SABIO-RKⁱ	Q9UJM8
UniPathwayⁱ	UPA00864;UER00830

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Hydroxyacid oxidase 1 (EC:1.1.3.15) Short name: HAOX1 Alternative name(s): Glycolate oxidase Short name: GOX
Gene namesⁱ	Name:HAO1 Synonyms:GOX1, HAOX1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 20

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000101323.4
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:4809 HAO1
MIMⁱ	605023 gene
neXtProtⁱ	NX_Q9UJM8

Keywords - Cellular componentⁱ

Peroxisome

Pathology & Biotechⁱ

Organism-specific databases

DisGeNET More...DisGeNETⁱ	54363
Open Targets More...OpenTargetsⁱ	ENSG00000101323
PharmGKBⁱ	PA29185

Chemistry databases

ChEMBLⁱ	CHEMBL4229
Drug and drug target database More...DrugBankⁱ	DB07907 (2S)-2-HYDROXYOCTANOIC ACID DB07060 3-(INDOL-3-YL) LACTATE DB03884 3-Phenylpyruvic Acid DB02279 Benzoylformic Acid DB02164 N-Sulfo-Flavin Mononucleotide DB03247 Riboflavin Monophosphate

Polymorphism and mutation databases

BioMutaⁱ	HAO1
DMDMⁱ	13124294

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000206318	1 – 370	Hydroxyacid oxidase 1Add BLAST		370

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	184	N6-succinyllysineBy similarity	1
Modified residueⁱ	194	PhosphoserineBy similarity	1
Modified residueⁱ	230	PhosphoserineCombined sources	1

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

EPDⁱ	Q9UJM8
PaxDbⁱ	Q9UJM8
PeptideAtlas More...PeptideAtlasⁱ	Q9UJM8
PRIDEⁱ	Q9UJM8
ProteomicsDBⁱ	84633

PTM databases

iPTMnetⁱ	Q9UJM8
PhosphoSitePlusⁱ	Q9UJM8

Expressionⁱ

Tissue specificityⁱ

Liver.

Gene expression databases

Bgeeⁱ	ENSG00000101323 Expressed in 15 organ(s), highest expression level in right lobe of liver
CleanExⁱ	HS_HAO1
ExpressionAtlasⁱ	Q9UJM8 baseline and differential
Genevisibleⁱ	Q9UJM8 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA049552

HPAⁱ

HPA049552

Interactionⁱ

GO - Molecular functionⁱ

signaling receptor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 20178365

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	119941, 4 interactors
IntActⁱ	Q9UJM8, 1 interactor
STRINGⁱ	9606.ENSP00000368066

Chemistry databases

BindingDBⁱ

Q9UJM8

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	8 – 18	Combined sources	11
Helixⁱ	21 – 28	Combined sources	8
Helixⁱ	35 – 46	Combined sources	12
Beta strandⁱ	47 – 49	Combined sources	3
Beta strandⁱ	64 – 66	Combined sources	3
Beta strandⁱ	69 – 77	Combined sources	9
Helixⁱ	83 – 85	Combined sources	3
Helixⁱ	90 – 101	Combined sources	12
Beta strandⁱ	104 – 107	Combined sources	4
Helixⁱ	115 – 121	Combined sources	7
Beta strandⁱ	125 – 131	Combined sources	7
Beta strandⁱ	134 – 136	Combined sources	3
Helixⁱ	137 – 149	Combined sources	13
Beta strandⁱ	155 – 158	Combined sources	4
Helixⁱ	168 – 172	Combined sources	5
Turnⁱ	189 – 193	Combined sources	5
Helixⁱ	204 – 212	Combined sources	9
Helixⁱ	219 – 228	Combined sources	10
Beta strandⁱ	233 – 238	Combined sources	6
Helixⁱ	241 – 249	Combined sources	9
Beta strandⁱ	254 – 257	Combined sources	4
Helixⁱ	260 – 262	Combined sources	3
Helixⁱ	271 – 282	Combined sources	12
Beta strandⁱ	285 – 293	Combined sources	9
Helixⁱ	297 – 305	Combined sources	9
Beta strandⁱ	309 – 314	Combined sources	6
Helixⁱ	315 – 347	Combined sources	33
Helixⁱ	352 – 354	Combined sources	3
Helixⁱ	357 – 359	Combined sources	3
Beta strandⁱ	360 – 362	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	Q9UJM8
SMRⁱ	Q9UJM8
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

Q9UJM8

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	1 – 365	FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd BLAST		365

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	368 – 370	Microbody targeting signalSequence analysis		3

Sequence similaritiesⁱ

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

Phylogenomic databases

eggNOGⁱ	KOG0538 Eukaryota COG1304 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000018717
HOGENOMⁱ	HOG000217463
HOVERGENⁱ	HBG051881
InParanoidⁱ	Q9UJM8
KEGG Orthology (KO) More...KOⁱ	K11517
OMAⁱ	KSVYDYY
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0ADA
PhylomeDBⁱ	Q9UJM8
TreeFamⁱ	TF313363

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd02809 alpha_hydroxyacid_oxid_FMN, 1 hit
Gene3Dⁱ	3.20.20.70, 1 hit
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
PIRSFⁱ	PIRSF000138 Al-hdrx_acd_dh, 1 hit
PROSITEⁱ	View protein in PROSITE PS00557 FMN_HYDROXY_ACID_DH_1, 1 hit PS51349 FMN_HYDROXY_ACID_DH_2, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q9UJM8-1 [UniParc]FASTA Add 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

Checksum:ⁱC683C6F7CB5FD323

GO

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS13100.1
NCBI Reference Sequences More...RefSeqⁱ	NP_060015.1, NM_017545.2
UniGeneⁱ	Hs.193640

Genome annotation databases

Ensemblⁱ	ENST00000378789; ENSP00000368066; ENSG00000101323
GeneIDⁱ	54363
KEGGⁱ	hsa:54363
UCSC genome browser More...UCSCⁱ	uc002wmw.2 human

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9UJM8	Hydroxyacid oxidase (Glycolate oxidase) 1, isoform CRA_a		HUMAN		370	UniRef100_Q9UJM8
HAO1 isoform 2		PANTR		370
Uncharacterized protein		PANPA		370
UPI0000E9BBCC		HUMAN		392
UPI000DE7BDAF		HUMAN		369
+2

Protein	Similar proteins		Species	Score	Length	Source
Q9UJM8	Hydroxyacid oxidase (Glycolate oxidase) 1, isoform CRA_a		HUMAN		370	UniRef90_Q9UJM8
HAO1 isoform 2		PANTR		370
Uncharacterized protein		PANPA		370
Uncharacterized protein		MACMU		409
Uncharacterized protein		CERAT		409
+32

Protein	Similar proteins		Species	Score	Length	Source
Q9UJM8	Hydroxyacid oxidase 1		MOUSE		370	UniRef50_Q9UJM8
Hydroxyacid oxidase (Glycolate oxidase) 1, isoform CRA_a		HUMAN		370
HAO1 isoform 2		PANTR		370
Uncharacterized protein		PANPA		370
Uncharacterized protein		CERAT		409
+139

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
CCDSⁱ	CCDS13100.1
RefSeqⁱ	NP_060015.1, NM_017545.2
UniGeneⁱ	Hs.193640

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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2NZL	X-ray	1.35	A	1-370	[»]
	2RDT	X-ray	1.95	A	1-370	[»]
	2RDU	X-ray	1.65	A	1-370	[»]
	2RDW	X-ray	1.95	A	1-370	[»]
	2W0U	X-ray	2.84	A/B/C/D	1-370	[»]
	5QIB	X-ray	1.48	A	1-368	[»]
	5QIC	X-ray	1.34	A	1-368	[»]
	5QID	X-ray	1.45	A	1-368	[»]
	5QIE	X-ray	1.34	A	1-368	[»]
	5QIF	X-ray	1.20	A	1-368	[»]
	5QIG	X-ray	1.42	A	1-368	[»]
	5QIH	X-ray	1.33	A	1-368	[»]
	6GMB	X-ray	1.35	A	1-362	[»]
	6GMC	X-ray	1.20	A	1-362	[»]
ProteinModelPortalⁱ	Q9UJM8
SMRⁱ	Q9UJM8
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	119941, 4 interactors
IntActⁱ	Q9UJM8, 1 interactor
STRINGⁱ	9606.ENSP00000368066

Chemistry databases

BindingDBⁱ	Q9UJM8
ChEMBLⁱ	CHEMBL4229
DrugBankⁱ	DB07907 (2S)-2-HYDROXYOCTANOIC ACID DB07060 3-(INDOL-3-YL) LACTATE DB03884 3-Phenylpyruvic Acid DB02279 Benzoylformic Acid DB02164 N-Sulfo-Flavin Mononucleotide DB03247 Riboflavin Monophosphate

PTM databases

iPTMnetⁱ	Q9UJM8
PhosphoSitePlusⁱ	Q9UJM8

Polymorphism and mutation databases

BioMutaⁱ	HAO1
DMDMⁱ	13124294

Proteomic databases

EPDⁱ	Q9UJM8
PaxDbⁱ	Q9UJM8
PeptideAtlasⁱ	Q9UJM8
PRIDEⁱ	Q9UJM8
ProteomicsDBⁱ	84633

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	54363
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000378789; ENSP00000368066; ENSG00000101323
GeneIDⁱ	54363
KEGGⁱ	hsa:54363
UCSCⁱ	uc002wmw.2 human

Organism-specific databases

CTDⁱ	54363
DisGeNETⁱ	54363
EuPathDBⁱ	HostDB:ENSG00000101323.4
GeneCardsⁱ	HAO1
HGNCⁱ	HGNC:4809 HAO1
HPAⁱ	HPA049552
MIMⁱ	605023 gene
neXtProtⁱ	NX_Q9UJM8
OpenTargetsⁱ	ENSG00000101323
PharmGKBⁱ	PA29185
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0538 Eukaryota COG1304 LUCA
GeneTreeⁱ	ENSGT00390000018717
HOGENOMⁱ	HOG000217463
HOVERGENⁱ	HBG051881
InParanoidⁱ	Q9UJM8
KOⁱ	K11517
OMAⁱ	KSVYDYY
OrthoDBⁱ	EOG091G0ADA
PhylomeDBⁱ	Q9UJM8
TreeFamⁱ	TF313363

Enzyme and pathway databases

UniPathwayⁱ	UPA00864;UER00830
BRENDAⁱ	1.1.3.15 2681
Reactomeⁱ	R-HSA-389661 Glyoxylate metabolism and glycine degradation R-HSA-9033241 Peroxisomal protein import
SABIO-RKⁱ	Q9UJM8

Miscellaneous databases

EvolutionaryTraceⁱ	Q9UJM8
GenomeRNAiⁱ	54363
Protein Ontology More...PROⁱ	PR:Q9UJM8
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000101323 Expressed in 15 organ(s), highest expression level in right lobe of liver
CleanExⁱ	HS_HAO1
ExpressionAtlasⁱ	Q9UJM8 baseline and differential
Genevisibleⁱ	Q9UJM8 HS

Family and domain databases

CDDⁱ	cd02809 alpha_hydroxyacid_oxid_FMN, 1 hit
Gene3Dⁱ	3.20.20.70, 1 hit
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
Pfamⁱ	View protein in Pfam PF01070 FMN_dh, 1 hit
PIRSFⁱ	PIRSF000138 Al-hdrx_acd_dh, 1 hit
PROSITEⁱ	View protein in PROSITE PS00557 FMN_HYDROXY_ACID_DH_1, 1 hit PS51349 FMN_HYDROXY_ACID_DH_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	HAOX1_HUMAN
Accessionⁱ	Q9UJM8Primary (citable) accession number: Q9UJM8 Secondary accession number(s): Q14CQ0, Q9UPZ0, Q9Y3I7
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
	Last sequence update:	May 1, 2000
	Last modified:	November 7, 2018
	This is version 161 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways
Human chromosome 20
Human chromosome 20: entries, gene names and cross-references to MIM
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9UJM8 (HAOX1_HUMAN)

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Hydroxyacid oxidase 1

Select a section on the left to see content.

<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

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glycolate degradation

Sites

Regions

<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

GO - Biological processi

Enzyme and pathway databases

<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

Organism-specific databases

<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

Peroxisome

Cytosol

Peroxisome

Keywords - Cellular componenti

<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

Chemistry databases

Polymorphism and mutation databases

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<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

Gene expression databases

Organism-specific databases

<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

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<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

3D structure databases

Miscellaneous databases

<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

Motif

<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

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<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 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

Documents

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Functionⁱ

Kineticsⁱ

Pathwayⁱ: glycolate degradation

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ