UniProt Accession

 HMOX2_HUMAN; P30519; A8MT35; D3DUD5; O60605 

Genbank Protein ID

 D21243; S34389; BT019788; AY771350; AC007606; CH471112; CH471112; BC002396; AF051306 

Genbank Nucleotide ID

 BAA04789.1; AAB22110.2; AAV38591.1; AAV28730.1; EAW85299.1; EAW85300.1; AAH02396.1; AAC05297.1 

Protein Name

 Heme oxygenase 2 

Protein Synonyms/Alias

 HO-2 

Gene Name

 HMOX2 

Gene Synonyms/Alias

 HO2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
24	KNSGALEKENQMRMA	ubiquitination	[1]
55	AENTQFVKDFLKGNI	ubiquitination	[1, 2, 3]
169	SGGQVLKKVAQRALK	ubiquitination	[1]
199	VDNAQQFKQLYRARM	ubiquitination	[1, 4, 5]
214	NALDLNMKTKERIVE	ubiquitination	[1, 5]
225	RIVEEANKAFEYNMQ	ubiquitination	[5]
259	GFPVHDGKGDMRKCP	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 

Functional Description

 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. 

Sequence Annotation

 REPEAT 264 269 HRM 1.
 REPEAT 281 286 HRM 2.
 METAL 45 45 Iron (heme axial ligand).
 MOD_RES 2 2 N-acetylserine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Metal-binding; Microsome; Oxidoreductase; Polymorphism; Reference proteome; Repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 316 AA 

Protein Sequence

Gene Ontology

 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0004392; F:heme oxygenase (decyclizing) activity; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
 GO:0042167; P:heme catabolic process; TAS:Reactome.
 GO:0006788; P:heme oxidation; IEA:InterPro.
 GO:0001666; P:response to hypoxia; IDA:UniProtKB.
 GO:0006979; P:response to oxidative stress; IEA:Compara.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0055085; P:transmembrane transport; TAS:Reactome. 

Interpro

 IPR002051; Haem_Oase.
 IPR016053; Haem_Oase-like.
 IPR016084; Haem_Oase-like_multi-hlx.
 IPR018207; Haem_oxygenase_CS. 

Pfam

 PF01126; Heme_oxygenase 

SMART

  

PROSITE

 PS00593; HEME_OXYGENASE 

PRINTS

 PR00088; HAEMOXYGNASE.