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Protein

Heme oxygenase 1

Gene

Hmox1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.

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
Binding sitei18HemeBy similarity1
Metal bindingi25Iron (heme axial ligand)By similarity1
Binding sitei134HemeBy similarity1
Binding sitei183HemeBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processApoptosis
LigandHeme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.99.3 3474
ReactomeiR-MMU-189483 Heme degradation
R-MMU-917937 Iron uptake and transport

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase 1 (EC:1.14.14.18By similarity)
Short name:
HO-1
Alternative name(s):
P32 protein
Gene namesi
Name:Hmox1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:96163 Hmox1

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4434

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002096881 – 289Heme oxygenase 1Add BLAST289

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei229PhosphoserineBy similarity1
Modified residuei242PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP14901
PaxDbiP14901
PeptideAtlasiP14901
PRIDEiP14901

PTM databases

iPTMnetiP14901
PhosphoSitePlusiP14901
SwissPalmiP14901

Expressioni

Inductioni

Heme oxygenase 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, and endotoxin. It is also induced in macrophages, liver and the lungs upon infection with M.tuberculosis (at protein level). Data is conflicting as to whether macrophage induction is independent of the nitric oxide (NO) signaling pathway (PubMed:18400743), or dependent on NO (PubMed:18474359).2 Publications

Gene expression databases

BgeeiENSMUSG00000005413
CleanExiMM_HMOX1
ExpressionAtlasiP14901 baseline and differential
GenevisibleiP14901 MM

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

IntActiP14901, 3 interactors
MINTiP14901
STRINGi10090.ENSMUSP00000005548

Structurei

3D structure databases

ProteinModelPortaliP14901
SMRiP14901
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heme oxygenase family.Curated

Phylogenomic databases

eggNOGiKOG4480 Eukaryota
COG5398 LUCA
GeneTreeiENSGT00390000017673
HOGENOMiHOG000233221
HOVERGENiHBG005982
InParanoidiP14901
KOiK00510
OMAiKKSHTMA
OrthoDBiEOG091G0AS0
PhylomeDBiP14901
TreeFamiTF314786

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

Sequencei

Sequence statusi: Complete.

P14901-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERPQPDSMP QDLSEALKEA TKEVHIQAEN AEFMKNFQKG QVSREGFKLV
60 70 80 90 100
MASLYHIYTA LEEEIERNKQ NPVYAPLYFP EELHRRAALE QDMAFWYGPH
110 120 130 140 150
WQEIIPCTPA TQHYVKRLHE VGRTHPELLV AHAYTRYLGD LSGGQVLKKI
160 170 180 190 200
AQKAMALPSS GEGLAFFTFP NIDSPTKFKQ LYRARMNTLE MTPEVKHRVT
210 220 230 240 250
EEAKTAFLLN IELFEELQVM LTEEHKDQSP SQMASLRQRP ASLVQDTAPA
260 270 280
ETPRGKPQIS TSSSQTPLLQ WVLTLSFLLA TVAVGIYAM
Length:289
Mass (Da):32,929
Last modified:April 1, 1990 - v1
Checksum:i19DB0DCCD574044B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33203 mRNA Translation: AAA39872.1
X13356 mRNA Translation: CAA31732.1
X56824
, X56825, X56826, X56827 Genomic DNA Translation: CAA40159.1
BC010757 mRNA Translation: AAH10757.1
CCDSiCCDS22423.1
PIRiI48409
RefSeqiNP_034572.1, NM_010442.2
UniGeneiMm.276389

Genome annotation databases

EnsembliENSMUST00000005548; ENSMUSP00000005548; ENSMUSG00000005413
GeneIDi15368
KEGGimmu:15368
UCSCiuc009mhc.2 mouse

Similar proteinsi

Entry informationi

Entry nameiHMOX1_MOUSE
AccessioniPrimary (citable) accession number: P14901
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 23, 2018
This is version 154 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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