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Protein

Heme oxygenase 2

Gene

Hmox2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi44 – 441Iron (heme axial ligand)By similarity

GO - Molecular functioni

  1. heme oxygenase (decyclizing) activity Source: MGI
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. heme oxidation Source: InterPro
  2. response to hypoxia Source: MGI
  3. response to oxidative stress Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.99.3. 3474.
ReactomeiREACT_292451. Iron uptake and transport.
REACT_341594. Heme degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase 2 (EC:1.14.99.3)
Short name:
HO-2
Gene namesi
Name:Hmox2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:109373. Hmox2.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-SubCell
  2. membrane Source: MGI
  3. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 315314Heme oxygenase 2PRO_0000209692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO70252.
PaxDbiO70252.
PRIDEiO70252.

PTM databases

PhosphoSiteiO70252.

Expressioni

Gene expression databases

BgeeiO70252.
CleanExiMM_HMOX2.
ExpressionAtlasiO70252. baseline and differential.
GenevestigatoriO70252.

Interactioni

Protein-protein interaction databases

IntActiO70252. 3 interactions.
MINTiMINT-1847819.

Structurei

3D structure databases

SMRiO70252. Positions 29-247.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati263 – 2686HRM 1
Repeati280 – 2856HRM 2

Sequence similaritiesi

Belongs to the heme oxygenase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5398.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiO70252.
KOiK00510.
OMAiKKSHTMA.
PhylomeDBiO70252.
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]

Sequencei

Sequence statusi: Complete.

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

O70252-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSEVETSEG VDESEKNSMA PEKENHTKMA DLSELLKEGT KEAHDRAENT
60 70 80 90 100
QFVKDFLKGN IKKELFKLAT TALYFTYSAL EEEMDRNKDH PAFAPLYFPT
110 120 130 140 150
ELHRKAALIK DMKYFFGENW EEQVKCSEAA QKYVDRIHYV GQNEPELLVA
160 170 180 190 200
HAYTRYMGDL SGGQVLKKVA QRALKLPSTG EGTQFYLFEH VDNAQQFKQF
210 220 230 240 250
YRARMNALDL NLKTKERIVE EANKAFEYNM QIFSELDQAG SMLARETLED
260 270 280 290 300
GLPVHDGKGD IRKCPFYAAQ PDKGTLGGSN CPFQTTVAVL RKPSLQLILA
310
ASVALVAGLL AWYYM
Length:315
Mass (Da):35,739
Last modified:August 1, 1998 - v1
Checksum:iEA382EB2C7CED6D1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1743RAL → SSS in AAC82364 (PubMed:9795203).Curated
Sequence conflicti172 – 1743RAL → SSS in AAC82363 (PubMed:9795203).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029874 mRNA. Translation: AAC17981.1.
AF054670 mRNA. Translation: AAC82364.1.
AF054669 mRNA. Translation: AAC82363.1.
BC002011 mRNA. Translation: AAH02011.1.
CCDSiCCDS27924.1.
PIRiJC5149.
RefSeqiNP_001129538.1. NM_001136066.2.
NP_034573.2. NM_010443.2.
UniGeneiMm.272866.

Genome annotation databases

EnsembliENSMUST00000004172; ENSMUSP00000004172; ENSMUSG00000004070.
ENSMUST00000118885; ENSMUSP00000113110; ENSMUSG00000004070.
ENSMUST00000120232; ENSMUSP00000112397; ENSMUSG00000004070.
GeneIDi15369.
KEGGimmu:15369.
UCSCiuc007yag.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029874 mRNA. Translation: AAC17981.1.
AF054670 mRNA. Translation: AAC82364.1.
AF054669 mRNA. Translation: AAC82363.1.
BC002011 mRNA. Translation: AAH02011.1.
CCDSiCCDS27924.1.
PIRiJC5149.
RefSeqiNP_001129538.1. NM_001136066.2.
NP_034573.2. NM_010443.2.
UniGeneiMm.272866.

3D structure databases

SMRiO70252. Positions 29-247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO70252. 3 interactions.
MINTiMINT-1847819.

PTM databases

PhosphoSiteiO70252.

Proteomic databases

MaxQBiO70252.
PaxDbiO70252.
PRIDEiO70252.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004172; ENSMUSP00000004172; ENSMUSG00000004070.
ENSMUST00000118885; ENSMUSP00000113110; ENSMUSG00000004070.
ENSMUST00000120232; ENSMUSP00000112397; ENSMUSG00000004070.
GeneIDi15369.
KEGGimmu:15369.
UCSCiuc007yag.2. mouse.

Organism-specific databases

CTDi3163.
MGIiMGI:109373. Hmox2.

Phylogenomic databases

eggNOGiCOG5398.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiO70252.
KOiK00510.
OMAiKKSHTMA.
PhylomeDBiO70252.
TreeFamiTF314786.

Enzyme and pathway databases

BRENDAi1.14.99.3. 3474.
ReactomeiREACT_292451. Iron uptake and transport.
REACT_341594. Heme degradation.

Miscellaneous databases

NextBioi288002.
PROiO70252.
SOURCEiSearch...

Gene expression databases

BgeeiO70252.
CleanExiMM_HMOX2.
ExpressionAtlasiO70252. baseline and differential.
GenevestigatoriO70252.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of mouse heme oxygenase-2."
    Mount D.B.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CD-1.
  2. "The identification and expression of heme oxygenase-2 alternative transcripts in the mouse."
    Gibbs L., Willis D., Morgan M.J.
    Gene 221:171-177(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland.

Entry informationi

Entry nameiHMOX2_MOUSE
AccessioniPrimary (citable) accession number: O70252
Secondary accession number(s): O70626
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: April 1, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.