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P30519 (HMOX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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

Protoheme + 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 316315Heme oxygenase 2
PRO_0000209691

Regions

Repeat264 – 2696HRM 1
Repeat281 – 2866HRM 2

Sites

Metal binding451Iron (heme axial ligand)

Amino acid modifications

Modified residue21N-acetylserine Ref.8 Ref.10

Natural variations

Natural variant1371R → Q. Ref.4
Corresponds to variant rs17884623 [ dbSNP | Ensembl ].
VAR_021067
Natural variant1461P → L. Ref.4
Corresponds to variant rs17880805 [ dbSNP | Ensembl ].
VAR_021068

Experimental info

Sequence conflict165 – 1662QV → KC in AAC05297. Ref.9
Sequence conflict2221Missing in AAB22110. Ref.2
Sequence conflict2761Missing in AAB22110. Ref.2
Sequence conflict281 – 2888SCPFRTAM → LSLPTSY in AAB22110. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P30519 [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

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] [Europe PMC] [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] [Europe PMC] [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 sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[8]Bienvenut W.V., Bilsland A.E., Keith W.N.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-17; 30-38; 48-59; 138-168; 206-214 AND 219-246, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon carcinoma and Ovarian carcinoma.
[9]Follett J., Ahn J.-Y.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-166.
Tissue: Intestine.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-264, HEME-BINDING SITE.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
AF051306 mRNA. Translation: AAC05297.1.
PIRI60119.
S21700.
RefSeqNP_001120676.1. NM_001127204.1.
NP_001120677.1. NM_001127205.1.
NP_001120678.1. NM_001127206.2.
NP_001273196.1. NM_001286267.1.
NP_001273197.1. NM_001286268.1.
NP_001273198.1. NM_001286269.1.
NP_001273199.1. NM_001286270.1.
NP_001273200.1. NM_001286271.1.
NP_002125.3. NM_002134.3.
UniGeneHs.284279.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q32X-ray2.40A/B1-264[»]
2QPPX-ray2.61A/B1-264[»]
2RGZX-ray2.61A/B1-264[»]
ProteinModelPortalP30519.
SMRP30519. Positions 30-248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109406. 31 interactions.
IntActP30519. 34 interactions.
MINTMINT-1384587.
STRING9606.ENSP00000219700.

Chemistry

DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP30519.

Polymorphism databases

DMDM1170328.

Proteomic databases

PaxDbP30519.
PRIDEP30519.

Protocols and materials databases

DNASU3163.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000219700; ENSP00000219700; ENSG00000103415.
ENST00000398595; ENSP00000381595; ENSG00000103415.
ENST00000406590; ENSP00000385100; ENSG00000103415.
ENST00000414777; ENSP00000391637; ENSG00000103415.
ENST00000458134; ENSP00000394103; ENSG00000103415.
ENST00000570646; ENSP00000459214; ENSG00000103415.
GeneID3163.
KEGGhsa:3163.
UCSCuc002cwq.4. human.

Organism-specific databases

CTD3163.
GeneCardsGC16P004524.
HGNCHGNC:5014. HMOX2.
HPACAB025464.
HPA040611.
MIM141251. gene.
neXtProtNX_P30519.
PharmGKBPA29342.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5398.
HOGENOMHOG000233221.
HOVERGENHBG005982.
InParanoidP30519.
KOK00510.
OMAKKSHTMA.
PhylomeDBP30519.
TreeFamTF314786.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP30519.
BgeeP30519.
CleanExHS_HMOX2.
GenevestigatorP30519.

Family and domain databases

Gene3D1.20.910.10. 1 hit.
InterProIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
PANTHERPTHR10720. PTHR10720. 1 hit.
PfamPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFPIRSF000343. Haem_Oase. 1 hit.
PRINTSPR00088. HAEMOXYGNASE.
SUPFAMSSF48613. SSF48613. 1 hit.
PROSITEPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHMOX2. human.
EvolutionaryTraceP30519.
GeneWikiHMOX2.
GenomeRNAi3163.
NextBio12542.
PMAP-CutDBP30519.
PROP30519.
SOURCESearch...

Entry information

Entry nameHMOX2_HUMAN
AccessionPrimary (citable) accession number: P30519
Secondary accession number(s): A8MT35, D3DUD5, O60605
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

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