Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Heme oxygenase 2

Gene

HMOX2

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

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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.

Catalytic activityi

Protoheme + 3 [reduced NADPH--hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH--hemoprotein reductase] + 3 H2O.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi45Iron (heme axial ligand)1

GO - Molecular functioni

  • heme binding Source: GO_Central
  • heme oxygenase (decyclizing) activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS02501-MONOMER.
BRENDAi1.14.99.3. 2681.
ReactomeiR-HSA-189483. Heme degradation.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-917937. Iron uptake and transport.
SIGNORiP30519.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase 2 (EC:1.14.14.18By similarity)
Short name:
HO-2
Gene namesi
Name:HMOX2
Synonyms:HO2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:5014. HMOX2.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: Reactome
  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Microsome

Pathology & Biotechi

Organism-specific databases

DisGeNETi3163.
OpenTargetsiENSG00000103415.
ENSG00000277424.
PharmGKBiPA29342.

Chemistry databases

ChEMBLiCHEMBL2546.

Polymorphism and mutation databases

BioMutaiHMOX2.
DMDMi1170328.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00002096912 – 316Heme oxygenase 2Add BLAST315

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei2PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP30519.
MaxQBiP30519.
PaxDbiP30519.
PeptideAtlasiP30519.
PRIDEiP30519.

PTM databases

iPTMnetiP30519.
PhosphoSitePlusiP30519.
SwissPalmiP30519.

Miscellaneous databases

PMAP-CutDBP30519.

Expressioni

Inductioni

Heme oxygenase 2 activity is non-inducible.

Gene expression databases

BgeeiENSG00000103415.
CleanExiHS_HMOX2.
ExpressionAtlasiP30519. baseline and differential.
GenevisibleiP30519. HS.

Organism-specific databases

HPAiCAB025464.
HPA040611.

Interactioni

Protein-protein interaction databases

BioGridi109406. 53 interactors.
DIPiDIP-53564N.
IntActiP30519. 45 interactors.
MINTiMINT-1384587.
STRINGi9606.ENSP00000219700.

Structurei

Secondary structure

1316
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi33 – 40Combined sources8
Helixi42 – 49Combined sources8
Helixi52 – 58Combined sources7
Helixi64 – 87Combined sources24
Turni88 – 90Combined sources3
Turni92 – 94Combined sources3
Helixi95 – 97Combined sources3
Helixi100 – 103Combined sources4
Helixi106 – 117Combined sources12
Helixi121 – 124Combined sources4
Helixi129 – 144Combined sources16
Helixi146 – 148Combined sources3
Helixi149 – 175Combined sources27
Helixi185 – 187Combined sources3
Helixi195 – 208Combined sources14
Helixi213 – 238Combined sources26
Turni243 – 247Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Q32X-ray2.40A/B1-264[»]
2QPPX-ray2.61A/B1-264[»]
2RGZX-ray2.61A/B1-264[»]
4WMHX-ray2.50A31-237[»]
ProteinModelPortaliP30519.
SMRiP30519.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30519.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati264 – 269HRM 16
Repeati281 – 286HRM 26

Sequence similaritiesi

Belongs to the heme oxygenase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4480. Eukaryota.
COG5398. LUCA.
GeneTreeiENSGT00390000017673.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiP30519.
KOiK00510.
PhylomeDBiP30519.
TreeFamiTF314786.

Family and domain databases

Gene3Di1.20.910.10. 1 hit.
InterProiIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
PANTHERiPTHR10720. PTHR10720. 1 hit.
PfamiPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFiPIRSF000343. Haem_Oase. 1 hit.
PRINTSiPR00088. HAEMOXYGNASE.
SUPFAMiSSF48613. SSF48613. 1 hit.
PROSITEiPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

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

Isoform 1 (identifier: P30519-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN
60 70 80 90 100
TQFVKDFLKG NIKKELFKLA TTALYFTYSA LEEEMERNKD HPAFAPLYFP
110 120 130 140 150
MELHRKEALT KDMEYFFGEN WEEQVQCPKA AQKYVERIHY IGQNEPELLV
160 170 180 190 200
AHAYTRYMGD LSGGQVLKKV AQRALKLPST GEGTQFYLFE NVDNAQQFKQ
210 220 230 240 250
LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA GSTLARETLE
260 270 280 290 300
DGFPVHDGKG DMRKCPFYAA EQDKGALEGS SCPFRTAMAV LRKPSLQFIL
310
AAGVALAAGL LAWYYM
Length:316
Mass (Da):36,033
Last modified:November 1, 1995 - v2
Checksum:iBF4B6A341F1A81AC
GO
Isoform 2 (identifier: P30519-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.

Show »
Length:287
Mass (Da):32,837
Checksum:iE03CE816D6C72A30
GO

Sequence cautioni

The sequence W38932 differs from that shown. Reason: Frameshift at position 82.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti107E → T in W38932 (Ref. 8) Curated1
Sequence conflicti165 – 166QV → KC in AAC05297 (Ref. 10) Curated2
Sequence conflicti222Missing in AAB22110 (PubMed:1575508).Curated1
Sequence conflicti276Missing in AAB22110 (PubMed:1575508).Curated1
Sequence conflicti281 – 288SCPFRTAM → LSLPTSY in AAB22110 (PubMed:1575508).Curated8

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021067137R → Q.1 PublicationCorresponds to variant rs17884623dbSNPEnsembl.1
Natural variantiVAR_021068146P → L.1 PublicationCorresponds to variant rs17880805dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0550311 – 29Missing in isoform 2. 1 PublicationAdd BLAST29

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21243 mRNA. Translation: BAA04789.1.
S34389 mRNA. Translation: AAB22110.2.
BT019788 mRNA. Translation: AAV38591.1.
AY771350 Genomic DNA. Translation: AAV28730.1.
AC007606 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85299.1.
CH471112 Genomic DNA. Translation: EAW85300.1.
BC002396 mRNA. Translation: AAH02396.1.
W38932 mRNA. No translation available.
AF051306 mRNA. Translation: AAC05297.1.
CCDSiCCDS10517.1. [P30519-1]
CCDS66931.1. [P30519-2]
PIRiI60119.
S21700.
RefSeqiNP_001120676.1. NM_001127204.1. [P30519-1]
NP_001120677.1. NM_001127205.1. [P30519-1]
NP_001120678.1. NM_001127206.2. [P30519-1]
NP_001273196.1. NM_001286267.1.
NP_001273197.1. NM_001286268.1. [P30519-1]
NP_001273198.1. NM_001286269.1. [P30519-1]
NP_001273199.1. NM_001286270.1. [P30519-1]
NP_001273200.1. NM_001286271.1. [P30519-2]
NP_002125.3. NM_002134.3. [P30519-1]
XP_016878685.1. XM_017023196.1. [P30519-1]
XP_016878686.1. XM_017023197.1. [P30519-1]
UniGeneiHs.284279.

Genome annotation databases

EnsembliENST00000219700; ENSP00000219700; ENSG00000103415. [P30519-1]
ENST00000398595; ENSP00000381595; ENSG00000103415. [P30519-1]
ENST00000406590; ENSP00000385100; ENSG00000103415. [P30519-1]
ENST00000414777; ENSP00000391637; ENSG00000103415. [P30519-1]
ENST00000458134; ENSP00000394103; ENSG00000103415. [P30519-1]
ENST00000570646; ENSP00000459214; ENSG00000103415. [P30519-1]
ENST00000575120; ENSP00000460926; ENSG00000103415. [P30519-2]
ENST00000612525; ENSP00000481295; ENSG00000277424. [P30519-1]
ENST00000615778; ENSP00000484422; ENSG00000277424. [P30519-1]
ENST00000619528; ENSP00000484423; ENSG00000103415. [P30519-1]
ENST00000619913; ENSP00000484467; ENSG00000103415. [P30519-1]
ENST00000620445; ENSP00000478785; ENSG00000277424. [P30519-1]
ENST00000621065; ENSP00000481811; ENSG00000277424. [P30519-1]
ENST00000622146; ENSP00000483319; ENSG00000277424. [P30519-1]
ENST00000631540; ENSP00000487673; ENSG00000277424. [P30519-1]
ENST00000631677; ENSP00000488579; ENSG00000277424. [P30519-1]
ENST00000632458; ENSP00000488880; ENSG00000277424. [P30519-1]
ENST00000633319; ENSP00000488769; ENSG00000277424. [P30519-2]
GeneIDi3163.
KEGGihsa:3163.
UCSCiuc002cwq.5. human. [P30519-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21243 mRNA. Translation: BAA04789.1.
S34389 mRNA. Translation: AAB22110.2.
BT019788 mRNA. Translation: AAV38591.1.
AY771350 Genomic DNA. Translation: AAV28730.1.
AC007606 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85299.1.
CH471112 Genomic DNA. Translation: EAW85300.1.
BC002396 mRNA. Translation: AAH02396.1.
W38932 mRNA. No translation available.
AF051306 mRNA. Translation: AAC05297.1.
CCDSiCCDS10517.1. [P30519-1]
CCDS66931.1. [P30519-2]
PIRiI60119.
S21700.
RefSeqiNP_001120676.1. NM_001127204.1. [P30519-1]
NP_001120677.1. NM_001127205.1. [P30519-1]
NP_001120678.1. NM_001127206.2. [P30519-1]
NP_001273196.1. NM_001286267.1.
NP_001273197.1. NM_001286268.1. [P30519-1]
NP_001273198.1. NM_001286269.1. [P30519-1]
NP_001273199.1. NM_001286270.1. [P30519-1]
NP_001273200.1. NM_001286271.1. [P30519-2]
NP_002125.3. NM_002134.3. [P30519-1]
XP_016878685.1. XM_017023196.1. [P30519-1]
XP_016878686.1. XM_017023197.1. [P30519-1]
UniGeneiHs.284279.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Q32X-ray2.40A/B1-264[»]
2QPPX-ray2.61A/B1-264[»]
2RGZX-ray2.61A/B1-264[»]
4WMHX-ray2.50A31-237[»]
ProteinModelPortaliP30519.
SMRiP30519.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109406. 53 interactors.
DIPiDIP-53564N.
IntActiP30519. 45 interactors.
MINTiMINT-1384587.
STRINGi9606.ENSP00000219700.

Chemistry databases

ChEMBLiCHEMBL2546.

PTM databases

iPTMnetiP30519.
PhosphoSitePlusiP30519.
SwissPalmiP30519.

Polymorphism and mutation databases

BioMutaiHMOX2.
DMDMi1170328.

Proteomic databases

EPDiP30519.
MaxQBiP30519.
PaxDbiP30519.
PeptideAtlasiP30519.
PRIDEiP30519.

Protocols and materials databases

DNASUi3163.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219700; ENSP00000219700; ENSG00000103415. [P30519-1]
ENST00000398595; ENSP00000381595; ENSG00000103415. [P30519-1]
ENST00000406590; ENSP00000385100; ENSG00000103415. [P30519-1]
ENST00000414777; ENSP00000391637; ENSG00000103415. [P30519-1]
ENST00000458134; ENSP00000394103; ENSG00000103415. [P30519-1]
ENST00000570646; ENSP00000459214; ENSG00000103415. [P30519-1]
ENST00000575120; ENSP00000460926; ENSG00000103415. [P30519-2]
ENST00000612525; ENSP00000481295; ENSG00000277424. [P30519-1]
ENST00000615778; ENSP00000484422; ENSG00000277424. [P30519-1]
ENST00000619528; ENSP00000484423; ENSG00000103415. [P30519-1]
ENST00000619913; ENSP00000484467; ENSG00000103415. [P30519-1]
ENST00000620445; ENSP00000478785; ENSG00000277424. [P30519-1]
ENST00000621065; ENSP00000481811; ENSG00000277424. [P30519-1]
ENST00000622146; ENSP00000483319; ENSG00000277424. [P30519-1]
ENST00000631540; ENSP00000487673; ENSG00000277424. [P30519-1]
ENST00000631677; ENSP00000488579; ENSG00000277424. [P30519-1]
ENST00000632458; ENSP00000488880; ENSG00000277424. [P30519-1]
ENST00000633319; ENSP00000488769; ENSG00000277424. [P30519-2]
GeneIDi3163.
KEGGihsa:3163.
UCSCiuc002cwq.5. human. [P30519-1]

Organism-specific databases

CTDi3163.
DisGeNETi3163.
GeneCardsiHMOX2.
HGNCiHGNC:5014. HMOX2.
HPAiCAB025464.
HPA040611.
MIMi141251. gene.
neXtProtiNX_P30519.
OpenTargetsiENSG00000103415.
ENSG00000277424.
PharmGKBiPA29342.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4480. Eukaryota.
COG5398. LUCA.
GeneTreeiENSGT00390000017673.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiP30519.
KOiK00510.
PhylomeDBiP30519.
TreeFamiTF314786.

Enzyme and pathway databases

BioCyciZFISH:HS02501-MONOMER.
BRENDAi1.14.99.3. 2681.
ReactomeiR-HSA-189483. Heme degradation.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-917937. Iron uptake and transport.
SIGNORiP30519.

Miscellaneous databases

ChiTaRSiHMOX2. human.
EvolutionaryTraceiP30519.
GeneWikiiHMOX2.
GenomeRNAii3163.
PMAP-CutDBP30519.
PROiP30519.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000103415.
CleanExiHS_HMOX2.
ExpressionAtlasiP30519. baseline and differential.
GenevisibleiP30519. HS.

Family and domain databases

Gene3Di1.20.910.10. 1 hit.
InterProiIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
PANTHERiPTHR10720. PTHR10720. 1 hit.
PfamiPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFiPIRSF000343. Haem_Oase. 1 hit.
PRINTSiPR00088. HAEMOXYGNASE.
SUPFAMiSSF48613. SSF48613. 1 hit.
PROSITEiPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHMOX2_HUMAN
AccessioniPrimary (citable) accession number: P30519
Secondary accession number(s): A8MT35
, D3DUD5, I3L430, O60605
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 169 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.