HMOX1

Functionⁱ

Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase.UniRule annotation

Catalytic activityⁱ

heme b
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+ 3
O₂
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See the description of this molecule in ChEBI.
+ 3
reduced [NADPH—hemoprotein reductase]
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Search chemical reactions in Rhea for this molecule.
=
biliverdin IXα
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
CO
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
Fe²⁺
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H⁺
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See the description of this molecule in ChEBI.
+ 3
H₂O
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See the description of this molecule in ChEBI.
+ 3
oxidized [NADPH—hemoprotein reductase]
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Search chemical reactions in Rhea for this molecule.
UniRule annotation
Automatic assertion according to rulesⁱ
- PIRNR:PIRNR000343
ARBA annotation
Automatic assertion according to rulesⁱ
- ARBA:ARBA00001701
EC:
1.14.14.18
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
UniRule annotation
Automatic assertion according to rulesⁱ
- PIRNR:PIRNR000343
ARBA annotation
Automatic assertion according to rulesⁱ
- ARBA:ARBA00001701
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
heme b
zoom
+
3
O₂
+
3
reduced [NADPH—hemoprotein reductase]
FMNH₂
=
biliverdin IXα
zoom
+
CO
+
Fe²⁺
zoom
+
H⁺
+
3
H₂O
+
3
oxidized [NADPH—hemoprotein reductase]
FMN

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	18	HemeUniRule annotation	1
Metal bindingⁱ	25	Iron (heme axial ligand)UniRule annotation	1
Binding siteⁱ	134	HemeUniRule annotation	1
Binding siteⁱ	183	HemeUniRule annotation	1

GO - Molecular functionⁱ

enzyme binding Source: Ensembl
heme binding Source: Ensembl
heme oxygenase (decyclizing) activity Source: UniProtKB-UniRule
metal ion binding Source: UniProtKB-UniRule
phospholipase D activity Source: Ensembl

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

angiogenesis Source: Ensembl
cellular response to arsenic-containing substance Source: Ensembl
cellular response to cadmium ion Source: Ensembl
cellular response to cisplatin Source: Ensembl
cellular response to nutrient Source: Ensembl
heme catabolic process Source: Ensembl
heme oxidation Source: UniProtKB-UniRule
intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
liver regeneration Source: Ensembl
negative regulation of DNA binding Source: Ensembl
negative regulation of DNA-binding transcription factor activity Source: Ensembl
negative regulation of epithelial cell apoptotic process Source: Ensembl
negative regulation of macroautophagy Source: Ensembl
negative regulation of mast cell cytokine production Source: Ensembl
negative regulation of mast cell degranulation Source: Ensembl
negative regulation of muscle cell apoptotic process Source: Ensembl
negative regulation of neuron apoptotic process Source: Ensembl
negative regulation of vascular associated smooth muscle cell proliferation Source: Ensembl
positive regulation of angiogenesis Source: Ensembl
positive regulation of apoptotic process Source: Ensembl
positive regulation of macroautophagy Source: Ensembl
regulation of blood pressure Source: Ensembl
regulation of transcription from RNA polymerase II promoter in response to iron Source: Ensembl
regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: Ensembl
response to drug Source: Ensembl
response to estrogen Source: Ensembl
response to hydrogen peroxide Source: Ensembl
response to hypoxia Source: Ensembl
small GTPase mediated signal transduction Source: Ensembl

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	CyclinImported, OxidoreductaseARBA annotation
Ligand	HemeUniRule annotationARBA annotation, Iron, Metal-binding

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Heme oxygenaseUniRule annotation (EC:1.14.14.18UniRule annotation)
Gene namesⁱ	Name:HMOX1Imported ORF Names:hCG_40033Imported
Organismⁱ	Homo sapiens (Human)Imported
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

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000100292.16

EuPathDBⁱ

HostDB:ENSG00000100292.16

Subcellular locationⁱ

GO - Cellular component

Topology

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transmembraneⁱ	267 – 287	HelicalSequence analysisAdd BLAST		21

Keywords - Cellular componentⁱ

Membrane

Pathology & Biotechⁱ

Organism-specific databases

PharmGKBⁱ	PA29341

PharmGKBⁱ

PA29341

PTM / Processingⁱ

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q6FH11

MaxQBⁱ

Q6FH11

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000100292, Expressed in layer of synovial tissue and 191 other tissues
ExpressionAtlasⁱ	Q6FH11, baseline and differential

Interactionⁱ

GO - Molecular functionⁱ

enzyme binding Source: Ensembl

Complete GO annotation on QuickGO ...

Chemistry databases

BindingDBⁱ	Q6FH11

BindingDBⁱ

Q6FH11

Structureⁱ

3D structure databases

SMRⁱ	Q6FH11
ModBaseⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	223 – 260	DisorderedSequence analysisAdd BLAST		38

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	227 – 248	PolarSequence analysisAdd BLAST		22

Sequence similaritiesⁱ

Belongs to the heme oxygenase family.UniRule annotationARBA annotation

Keywords - Domainⁱ

Transmembrane, Transmembrane helixSequence analysis

Phylogenomic databases

HOGENOMⁱ	CLU_057050_0_0_1
OMAⁱ	KKSHTMA
Database of Orthologous Groups More...OrthoDBⁱ	1424194at2759

Family and domain databases

Gene3Dⁱ	1.20.910.10, 1 hit
InterProⁱ	View protein in InterPro IPR002051, Haem_Oase IPR016053, Haem_Oase-like IPR016084, Haem_Oase-like_multi-hlx IPR018207, Haem_oxygenase_CS
PANTHERⁱ	PTHR10720, PTHR10720, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01126, Heme_oxygenase, 1 hit
PIRSFⁱ	PIRSF000343, Haem_Oase, 1 hit
PRINTSⁱ	PR00088, HAEMOXYGNASE
SUPFAMⁱ	SSF48613, SSF48613, 1 hit
PROSITEⁱ	View protein in PROSITE PS00593, HEME_OXYGENASE, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q6FH11-1 [UniParc]FASTA Add to basket

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        10         20         30         40         50
MERPQPDSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV 
        60         70         80         90        100
MASLYHIYVA LEEEIERNKE SPVFAPVYFP EELHRKAALE QDLAFWYGPR 
       110        120        130        140        150
WQEVIPYTPA MQRYVKRLHE VGRTEPELLV AHAYTRYLGD LSGGQVLKKI 
       160        170        180        190        200
AQKALDLPSS GEGLAFFTFP NIASATKFKQ LYRSRMNSLE MTPAVRQRVI 
       210        220        230        240        250
EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA SNKVQDSAPV 
       260        270        280 
ETPRGKPPLN TRSQAPLLRW VLTLSFLVAT VAVGLYAM

Length:288

Mass (Da):32,819

Last modified:May 10, 2005 - v1

Checksum:ⁱAB47827778694064

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BT019785 mRNA Translation: AAV38588.1 CR541945 mRNA Translation: CAG46743.1 CR541968 mRNA Translation: CAG46766.1 CH471095 Genomic DNA Translation: EAW60059.1
NCBI Reference Sequences More...RefSeqⁱ	NP_002124.1, NM_002133.2

Genome annotation databases

GeneIDⁱ	3162
KEGGⁱ	hsa:3162
UCSC genome browser More...UCSCⁱ	uc003ant.3, human

Protein	Similar proteins		Species	Score	Length	Source
Q6FH11	Heme oxygenase 1	)	HUMAN		288	UniRef100_P09601
Heme oxygenase (biliverdin-producing)		PANTR		311
Heme oxygenase (biliverdin-producing)		PANPA		311
Heme oxygenase		PANTR		288
HMOX1 (Fragment)		HUMAN		42
+4

Protein	Similar proteins		Species	Score	Length	Source
Q6FH11	Heme oxygenase 1	)	HUMAN		288	UniRef90_P09601
Heme oxygenase (biliverdin-producing)		PANTR		311
Heme oxygenase (biliverdin-producing)		PANPA		311
Heme oxygenase (biliverdin-producing)		CERAT		311
Heme oxygenase (biliverdin-producing)		MANLE		311
+15

Protein	Similar proteins		Species	Score	Length	Source
Q6FH11	Heme oxygenase 1	)	HUMAN		288	UniRef50_P09601
Heme oxygenase (biliverdin-producing)		PANTR		311
Heme oxygenase (biliverdin-producing)		PANPA		311
Heme oxygenase (biliverdin-producing)		MANLE		311
Heme oxygenase (biliverdin-producing)		CERAT		311
+34

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BT019785 mRNA Translation: AAV38588.1 CR541945 mRNA Translation: CAG46743.1 CR541968 mRNA Translation: CAG46766.1 CH471095 Genomic DNA Translation: EAW60059.1
RefSeqⁱ	NP_002124.1, NM_002133.2

3D structure databases

SMRⁱ	Q6FH11
ModBaseⁱ	Search...

Chemistry databases

BindingDBⁱ	Q6FH11

BindingDBⁱ

Q6FH11

Proteomic databases

MaxQBⁱ	Q6FH11

MaxQBⁱ

Q6FH11

Protocols and materials databases

Antibodypediaⁱ	266, 1070 antibodies
The DNASU plasmid repository More...DNASUⁱ	3162

Genome annotation databases

GeneIDⁱ	3162
KEGGⁱ	hsa:3162
UCSCⁱ	uc003ant.3, human

Organism-specific databases

CTDⁱ	3162
EuPathDBⁱ	HostDB:ENSG00000100292.16
PharmGKBⁱ	PA29341

Phylogenomic databases

HOGENOMⁱ	CLU_057050_0_0_1
OMAⁱ	KKSHTMA
OrthoDBⁱ	1424194at2759

Miscellaneous databases

BioGRID-ORCSⁱ	3162, 7 hits in 854 CRISPR screens
ChiTaRSⁱ	HMOX1, human
GenomeRNAiⁱ	3162

Gene expression databases

Bgeeⁱ	ENSG00000100292, Expressed in layer of synovial tissue and 191 other tissues
ExpressionAtlasⁱ	Q6FH11, baseline and differential

Family and domain databases

Gene3Dⁱ	1.20.910.10, 1 hit
InterProⁱ	View protein in InterPro IPR002051, Haem_Oase IPR016053, Haem_Oase-like IPR016084, Haem_Oase-like_multi-hlx IPR018207, Haem_oxygenase_CS
PANTHERⁱ	PTHR10720, PTHR10720, 1 hit
Pfamⁱ	View protein in Pfam PF01126, Heme_oxygenase, 1 hit
PIRSFⁱ	PIRSF000343, Haem_Oase, 1 hit
PRINTSⁱ	PR00088, HAEMOXYGNASE
SUPFAMⁱ	SSF48613, SSF48613, 1 hit
PROSITEⁱ	View protein in PROSITE PS00593, HEME_OXYGENASE, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	Q6FH11_HUMAN
Accessionⁱ	Q6FH11Primary (citable) accession number: Q6FH11
Entry historyⁱ	Integrated into UniProtKB/TrEMBL:	May 10, 2005
	Last sequence update:	May 10, 2005
	Last modified:	December 2, 2020
	This is version 124 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Unreviewed (UniProtKB/TrEMBL)
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.

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UniProtKB - Q6FH11 (Q6FH11_HUMAN)

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Heme oxygenase

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<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 <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

Sites

<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

<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

Cytosol

Endoplasmic reticulum

Nucleus

Plasma Membrane

Other locations

Topology

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

<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

Proteomic 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

<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

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

3D structure 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

Region

Compositional bias

<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

Keywords - Domaini

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

Chemistry databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic 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

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ