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Reviewed, UniProtKB/Swiss-Prot P30519 (HMOX2_HUMAN)

Last modified June 16, 2009. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Heme oxygenase 2
      Short name=HO-2
    EC=1.14.99.3
Gene names
Name: HMOX2
Synonyms: HO2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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 activity

Heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.

Subcellular location

Microsome. Endoplasmic reticulum.

Induction

Heme oxygenase 2 activity is non-inducible.

Sequence similarities

Belongs to the heme oxygenase family.

Contains 2 HRM (heme regulatory motif) repeats.

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Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Microsome
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processheme oxidation

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

response to hypoxia

Inferred from direct assay. Source: UniProtKB

   Cellular componentendoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

microsome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay. Source: UniProtKB

   Molecular functionelectron carrier activity Ref.2

Inferred from direct assay. Source: UniProtKB

heme oxygenase (decyclizing) activity Ref.2

Inferred from direct assay. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316Heme oxygenase 2
PRO_0000209691

Regions

Repeat264 – 2696HRM 1
Repeat281 – 2866HRM 2

Sites

Metal binding451Iron (heme axial ligand)

Natural variations

Natural variant1371R → Q: dbSNP rs17884623. Ref.4
VAR_021067
Natural variant1461P → L: dbSNP rs17880805. Ref.4
VAR_021068

Experimental info

Sequence conflict165 – 1662QV → KC in AAC05297. Ref.6
Sequence conflict2221Missing in AAB22110. Ref.2
Sequence conflict2761Missing Ref.2
Sequence conflict281 – 2888SCPFRTAM → LSLPTSY Ref.2

Secondary structure

1 ................................ 316
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P30519-1 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: BF4B6A341F1A81AC

FASTA31636,033
        10         20         30         40         50         60 
MSAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN TQFVKDFLKG 

        70         80         90        100        110        120 
NIKKELFKLA TTALYFTYSA LEEEMERNKD HPAFAPLYFP MELHRKEALT KDMEYFFGEN 

       130        140        150        160        170        180 
WEEQVQCPKA AQKYVERIHY IGQNEPELLV AHAYTRYMGD LSGGQVLKKV AQRALKLPST 

       190        200        210        220        230        240 
GEGTQFYLFE NVDNAQQFKQ LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA 

       250        260        270        280        290        300 
GSTLARETLE DGFPVHDGKG DMRKCPFYAA EQDKGALEGS SCPFRTAMAV LRKPSLQFIL 

       310 
AAGVALAAGL LAWYYM

« Hide

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References

« Hide 'large scale' references
[1]"Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2."
Ishikawa K.
J. Biol. Chem. 270:6345-6350(1995) [PubMed: 7890772] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal."
McCoubrey W.K. Jr., Ewing J.F., Maines M.D.
Arch. Biochem. Biophys. 295:13-20(1992) [PubMed: 1575508] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]NIEHS SNPs program
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-137 AND LEU-146.
[5]"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(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[6]Follett J., Ahn J.-Y.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-166.
Tissue: Intestine.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]"Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2."
Bianchetti C.M., Yi L., Ragsdale S.W., Phillips G.N. Jr.
J. Biol. Chem. 282:37624-37631(2007) [PubMed: 17965015] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-264, HEME-BINDING SITE.
+Additional computationally mapped references.

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Web resources

NIEHS-SNPs

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Cross-references

Sequence databases

D21243 mRNA. Translation: BAA04789.1.
S34389 mRNA. Translation: AAB22110.2.
BT019788 mRNA. Translation: AAV38591.1.
AY771350 Genomic DNA. Translation: AAV28730.1.
BC002396 mRNA. Translation: AAH02396.1.
AF051306 mRNA. Translation: AAC05297.1.
IPIIPI00026824.
PIRI60119.
S21700.
RefSeqNP_001120676.1.
NP_001120677.1.
NP_001120678.1.
NP_002125.3.
UniGeneHs.284279

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2Q32X-ray2.40A/B1-264[»]
2QPPX-ray2.61A/B1-264[»]
2RGZX-ray2.61A/B1-264[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP30519. 9 interactions.

Proteomic databases

PRIDEP30519.

Genome annotation databases

EnsemblENSG00000103415. Homo sapiens. [Contig view]
GeneID3163.
KEGGhsa:3163.

Organism-specific databases

GeneCardsGC16P004466.
H-InvDBHIX0012784.
HGNCHGNC:5014. HMOX2.
MIM141251. gene.
PharmGKBPA29342.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP30519.
HOVERGENP30519.
OMAP30519. REGTKKS.

Enzyme and pathway databases

BRENDA1.14.99.3. 247.

Gene expression databases

ArrayExpressP30519.
BgeeP30519.
CleanExHS_HMOX2.
GermOnlineENSG00000103415. Homo sapiens.

Family and domain databases

InterProIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
Gene3DG3DSA:1.20.910.10. Haem_Oase-like_multi-hlx. 1 hit.
PANTHERPTHR10720. Haem_Oase. 1 hit.
PfamPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFPIRSF000343. Haem_Oase. 1 hit.
PRINTSPR00088. HAEMOXYGNASE.
PROSITEPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00157. NADH.
NextBio12542.
PMAP-CutDBP30519.
SOURCESearch...

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Entry information

Entry nameHMOX2_HUMAN
AccessionPrimary (citable) accession number: P30519
Secondary accession number(s): O60605
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents