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Protein

Heme oxygenase 1

Gene

HMOX1

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

Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei18Heme1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi25Iron (heme axial ligand)1
Binding sitei134Heme1
Binding sitei183Heme1

<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

  • enzyme binding Source: BHF-UCL
  • heme binding Source: BHF-UCL
  • heme oxygenase (decyclizing) activity Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • phospholipase D activity Source: Ensembl
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

<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 processApoptosis
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS02027-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
1.14.99.3 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-189483 Heme degradation
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-917937 Iron uptake and transport

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P09601

<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_and_taxonomy_section">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:
Heme oxygenase 1 (EC:1.14.14.18By similarity)
Short name:
HO-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:HMOX1
Synonyms:HO, HO1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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 22

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000100292.16

Human Gene Nomenclature Database

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HGNCi
HGNC:5013 HMOX1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
141250 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P09601

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Heme oxygenase 1 deficiency (HMOX1D)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.
See also OMIM:614034

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi140D → A: Inactive as a heme oxygenase but active as a peroxidase. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
3162

MalaCards human disease database

More...
MalaCardsi
HMOX1
MIMi614034 phenotype

Open Targets

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OpenTargetsi
ENSG00000100292

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29341

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2823

Drug and drug target database

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DrugBanki
DB07342 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone
DB02468 12-Phenylheme
DB03906 2-Phenylheme
DB02073 Biliverdine Ix Alpha
DB01942 Formic Acid
DB00157 NADH
DB04912 Stannsoporfin
DB04803 Verdoheme
DB00163 Vitamin E

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1441

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
HMOX1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
123446

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002096871 – 288Heme oxygenase 1Add BLAST288

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 residuei229PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P09601

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P09601

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

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PaxDbi
P09601

PeptideAtlas

More...
PeptideAtlasi
P09601

PRoteomics IDEntifications database

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PRIDEi
P09601

ProteomicsDB human proteome resource

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ProteomicsDBi
52249

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P09601

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

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PhosphoSitePlusi
P09601

<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

Expressed at higher levels in renal cancer tissue than in normal tissue (at protein level).1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Heme oxygenase 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, endotoxin, oxidizing agents and UVA.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000100292 Expressed in 174 organ(s), highest expression level in layer of synovial tissue

CleanEx database of gene expression profiles

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CleanExi
HS_HMOX1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P09601 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P09601 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB017444
HPA000635

<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_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
POT1Q9NUX52EBI-2806151,EBI-752420

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
109405, 37 interactors

Protein interaction database and analysis system

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IntActi
P09601, 32 interactors

Molecular INTeraction database

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MINTi
P09601

STRING: functional protein association networks

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STRINGi
9606.ENSP00000216117

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P09601

<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

1288
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N3UX-ray2.58A/B1-233[»]
1N45X-ray1.50A/B1-233[»]
1NI6X-ray2.10A/B/C/D1-224[»]
1OYKX-ray2.59A/B1-233[»]
1OYLX-ray1.59A/B1-233[»]
1OZEX-ray2.19A/B1-233[»]
1OZLX-ray1.58A/B1-233[»]
1OZRX-ray1.74A/B1-233[»]
1OZWX-ray1.55A/B1-233[»]
1S13X-ray2.29A/B1-233[»]
1S8CX-ray2.19A/B/C/D1-233[»]
1T5PX-ray2.11A/B1-233[»]
1TWNX-ray2.20A/B1-233[»]
1TWRX-ray2.10A/B1-233[»]
1XJZX-ray1.88A/B1-233[»]
1XK0X-ray2.18A/B1-233[»]
1XK1X-ray2.08A/B1-233[»]
1XK2X-ray2.20A/B1-233[»]
1XK3X-ray2.08A/B1-233[»]
3CZYX-ray1.54A/B1-233[»]
3HOKX-ray2.19A/B1-233[»]
3K4FX-ray2.17A/B1-233[»]
3TGMX-ray2.85A/B1-233[»]
4WD4X-ray2.95A/B/C/D1-288[»]
5BTQX-ray2.08A/B1-233[»]
6EHAX-ray2.00A/B1-288[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P09601

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

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SMRi
P09601

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P09601

<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

<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 heme oxygenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4480 Eukaryota
COG5398 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000017673

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233221

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG005982

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P09601

KEGG Orthology (KO)

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KOi
K00510

Identification of Orthologs from Complete Genome Data

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OMAi
KKSHTMA

Database of Orthologous Groups

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OrthoDBi
1424194at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P09601

TreeFam database of animal gene trees

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TreeFami
TF314786

Family and domain databases

Conserved Domains Database

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CDDi
cd00232 HemeO, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.910.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002051 Haem_Oase
IPR016053 Haem_Oase-like
IPR016084 Haem_Oase-like_multi-hlx
IPR018207 Haem_oxygenase_CS

The PANTHER Classification System

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PANTHERi
PTHR10720 PTHR10720, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF01126 Heme_oxygenase, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF000343 Haem_Oase, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00088 HAEMOXYGNASE

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48613 SSF48613, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00593 HEME_OXYGENASE, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P09601-1 [UniParc]FASTAAdd to basket
« Hide
        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:July 1, 1989 - 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:iAB47827778694064
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B1AHA8B1AHA8_HUMAN
Heme oxygenase 1
HMOX1
187Annotation score:

Annotation score:1 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0191657D → H1 PublicationCorresponds to variant dbSNP:rs2071747Ensembl.1
Natural variantiVAR_022156106P → L. Corresponds to variant dbSNP:rs9282702Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X06985 mRNA Translation: CAA30045.1
CR456505 mRNA Translation: CAG30391.1
AY460337 Genomic DNA Translation: AAR23262.1
Z82244 Genomic DNA No translation available.
M23041 mRNA Translation: AAA50403.1
X14782 Genomic DNA Translation: CAA32886.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS13914.1

Protein sequence database of the Protein Information Resource

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PIRi
S00325

NCBI Reference Sequences

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RefSeqi
NP_002124.1, NM_002133.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.517581
Hs.727017

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000216117; ENSP00000216117; ENSG00000100292

Database of genes from NCBI RefSeq genomes

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GeneIDi
3162

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3162

Keywords - Coding sequence diversityi

Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06985 mRNA Translation: CAA30045.1
CR456505 mRNA Translation: CAG30391.1
AY460337 Genomic DNA Translation: AAR23262.1
Z82244 Genomic DNA No translation available.
M23041 mRNA Translation: AAA50403.1
X14782 Genomic DNA Translation: CAA32886.1
CCDSiCCDS13914.1
PIRiS00325
RefSeqiNP_002124.1, NM_002133.2
UniGeneiHs.517581
Hs.727017

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N3UX-ray2.58A/B1-233[»]
1N45X-ray1.50A/B1-233[»]
1NI6X-ray2.10A/B/C/D1-224[»]
1OYKX-ray2.59A/B1-233[»]
1OYLX-ray1.59A/B1-233[»]
1OZEX-ray2.19A/B1-233[»]
1OZLX-ray1.58A/B1-233[»]
1OZRX-ray1.74A/B1-233[»]
1OZWX-ray1.55A/B1-233[»]
1S13X-ray2.29A/B1-233[»]
1S8CX-ray2.19A/B/C/D1-233[»]
1T5PX-ray2.11A/B1-233[»]
1TWNX-ray2.20A/B1-233[»]
1TWRX-ray2.10A/B1-233[»]
1XJZX-ray1.88A/B1-233[»]
1XK0X-ray2.18A/B1-233[»]
1XK1X-ray2.08A/B1-233[»]
1XK2X-ray2.20A/B1-233[»]
1XK3X-ray2.08A/B1-233[»]
3CZYX-ray1.54A/B1-233[»]
3HOKX-ray2.19A/B1-233[»]
3K4FX-ray2.17A/B1-233[»]
3TGMX-ray2.85A/B1-233[»]
4WD4X-ray2.95A/B/C/D1-288[»]
5BTQX-ray2.08A/B1-233[»]
6EHAX-ray2.00A/B1-288[»]
ProteinModelPortaliP09601
SMRiP09601
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109405, 37 interactors
IntActiP09601, 32 interactors
MINTiP09601
STRINGi9606.ENSP00000216117

Chemistry databases

BindingDBiP09601
ChEMBLiCHEMBL2823
DrugBankiDB07342 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone
DB02468 12-Phenylheme
DB03906 2-Phenylheme
DB02073 Biliverdine Ix Alpha
DB01942 Formic Acid
DB00157 NADH
DB04912 Stannsoporfin
DB04803 Verdoheme
DB00163 Vitamin E
GuidetoPHARMACOLOGYi1441

PTM databases

iPTMnetiP09601
PhosphoSitePlusiP09601

Polymorphism and mutation databases

BioMutaiHMOX1
DMDMi123446

Proteomic databases

EPDiP09601
jPOSTiP09601
PaxDbiP09601
PeptideAtlasiP09601
PRIDEiP09601
ProteomicsDBi52249

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
3162
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216117; ENSP00000216117; ENSG00000100292
GeneIDi3162
KEGGihsa:3162

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
3162
DisGeNETi3162
EuPathDBiHostDB:ENSG00000100292.16

GeneCards: human genes, protein and diseases

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GeneCardsi
HMOX1
HGNCiHGNC:5013 HMOX1
HPAiCAB017444
HPA000635
MalaCardsiHMOX1
MIMi141250 gene
614034 phenotype
neXtProtiNX_P09601
OpenTargetsiENSG00000100292
PharmGKBiPA29341

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4480 Eukaryota
COG5398 LUCA
GeneTreeiENSGT00390000017673
HOGENOMiHOG000233221
HOVERGENiHBG005982
InParanoidiP09601
KOiK00510
OMAiKKSHTMA
OrthoDBi1424194at2759
PhylomeDBiP09601
TreeFamiTF314786

Enzyme and pathway databases

BioCyciMetaCyc:HS02027-MONOMER
BRENDAi1.14.99.3 2681
ReactomeiR-HSA-189483 Heme degradation
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-917937 Iron uptake and transport
SIGNORiP09601

Miscellaneous databases

EvolutionaryTraceiP09601

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
HMOX1

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

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GenomeRNAii
3162

Protein Ontology

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PROi
PR:P09601

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000100292 Expressed in 174 organ(s), highest expression level in layer of synovial tissue
CleanExiHS_HMOX1
ExpressionAtlasiP09601 baseline and differential
GenevisibleiP09601 HS

Family and domain databases

CDDicd00232 HemeO, 1 hit
Gene3Di1.20.910.10, 1 hit
InterProiView protein in InterPro
IPR002051 Haem_Oase
IPR016053 Haem_Oase-like
IPR016084 Haem_Oase-like_multi-hlx
IPR018207 Haem_oxygenase_CS
PANTHERiPTHR10720 PTHR10720, 1 hit
PfamiView protein in Pfam
PF01126 Heme_oxygenase, 1 hit
PIRSFiPIRSF000343 Haem_Oase, 1 hit
PRINTSiPR00088 HAEMOXYGNASE
SUPFAMiSSF48613 SSF48613, 1 hit
PROSITEiView protein in PROSITE
PS00593 HEME_OXYGENASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiHMOX1_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: P09601
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 16, 2019
This is version 196 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, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
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