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Protein

Heme oxygenase 1

Gene

HMOX1

Organism
Bos taurus (Bovine)
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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.By similarity

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 sitei19HemeBy similarity1
Metal bindingi26Iron (heme axial ligand)By similarity1
Binding sitei135HemeBy similarity1
Binding sitei184HemeBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.99.3. 908.
ReactomeiR-BTA-189483. Heme degradation.
R-BTA-917937. Iron uptake and transport.
SABIO-RKQ5E9F2.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase 1 (EC:1.14.14.18By similarity)
Short name:
HO-1
Gene namesi
Name:HMOX1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1255146.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002096861 – 289Heme oxygenase 1Add BLAST289

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei243PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5E9F2.
PRIDEiQ5E9F2.

Expressioni

Gene expression databases

BgeeiENSBTAG00000015582.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000020701.

Structurei

3D structure databases

ProteinModelPortaliQ5E9F2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heme oxygenase family.Curated

Phylogenomic databases

eggNOGiKOG4480. Eukaryota.
COG5398. LUCA.
GeneTreeiENSGT00390000017673.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiQ5E9F2.
KOiK00510.
OMAiTKKAHTM.
OrthoDBiEOG091G0AS0.
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]
PRINTSiPR00088. HAEMOXYGNASE.
SUPFAMiSSF48613. SSF48613. 1 hit.
PROSITEiPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5E9F2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERPQPDSSM PQDLSEALKE ATKEVHTQAE NAEFMKNFQK GELTQEGFKL
60 70 80 90 100
VMASLYHIYV ALEEEIERNK ENPVYTPLYF PEELHRRASL EQDMAFWYGP
110 120 130 140 150
RWQEAIPYTQ ATKRYVQRLQ EVGRTEPELL VAHAYTRYLG DLSGGQVLKK
160 170 180 190 200
IAQKALNLPS SGEGLAFFTF PNIASATKFK QLYRSRMNTL EMTPEVRQRV
210 220 230 240 250
LDEAKTAFLL NIQLFEELQG LLTQKAKDHD PLQAPELHRR AGSKVQDLAP
260 270 280
TKASRGKPQP SVLSQAPLLR WVLTLSFLVA TVAVGLYAM
Length:289
Mass (Da):32,940
Last modified:March 15, 2005 - v1
Checksum:i8EAEA06BCCA4B96C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti28Q → E AA sequence (PubMed:1700666).Curated1
Sequence conflicti100P → PH AA sequence (PubMed:1700666).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020968 mRNA. Translation: AAX08985.1.
BC102105 mRNA. Translation: AAI02106.4.
PIRiS13265.
RefSeqiNP_001014912.1. NM_001014912.1.
UniGeneiBt.4001.

Genome annotation databases

EnsembliENSBTAT00000020701; ENSBTAP00000020701; ENSBTAG00000015582.
GeneIDi513221.
KEGGibta:513221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT020968 mRNA. Translation: AAX08985.1.
BC102105 mRNA. Translation: AAI02106.4.
PIRiS13265.
RefSeqiNP_001014912.1. NM_001014912.1.
UniGeneiBt.4001.

3D structure databases

ProteinModelPortaliQ5E9F2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000020701.

Chemistry databases

ChEMBLiCHEMBL1255146.

Proteomic databases

PaxDbiQ5E9F2.
PRIDEiQ5E9F2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000020701; ENSBTAP00000020701; ENSBTAG00000015582.
GeneIDi513221.
KEGGibta:513221.

Organism-specific databases

CTDi3162.

Phylogenomic databases

eggNOGiKOG4480. Eukaryota.
COG5398. LUCA.
GeneTreeiENSGT00390000017673.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiQ5E9F2.
KOiK00510.
OMAiTKKAHTM.
OrthoDBiEOG091G0AS0.
TreeFamiTF314786.

Enzyme and pathway databases

BRENDAi1.14.99.3. 908.
ReactomeiR-BTA-189483. Heme degradation.
R-BTA-917937. Iron uptake and transport.
SABIO-RKQ5E9F2.

Gene expression databases

BgeeiENSBTAG00000015582.

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]
PRINTSiPR00088. HAEMOXYGNASE.
SUPFAMiSSF48613. SSF48613. 1 hit.
PROSITEiPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHMOX1_BOVIN
AccessioniPrimary (citable) accession number: Q5E9F2
Secondary accession number(s): Q3ZCK7, Q7M338
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 15, 2005
Last modified: November 30, 2016
This is version 87 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, Direct protein sequencing, Reference proteome

Documents

  1. 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.