CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002382
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heme oxygenase 1 
Protein Synonyms/Alias
 HO-1; HSP32 
Gene Name
 Hmox1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
149SGGQVLKKIAQKAMAacetylation[1]
153VLKKIAQKAMALPSSacetylation[1]
Reference
 [1] Mass spectrometric identification of lysine residues of heme oxygenase-1 that are involved in its interaction with NADPH-cytochrome P450 reductase.
 Higashimoto Y, Sugishima M, Sato H, Sakamoto H, Fukuyama K, Palmer G, Noguchi M.
 Biochem Biophys Res Commun. 2008 Mar 21;367(4):852-8. [PMID: 18194664
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. 
Sequence Annotation
 METAL 25 25 Iron (heme axial ligand).
 BINDING 18 18 Heme (By similarity).
 BINDING 134 134 Heme (By similarity).
 BINDING 183 183 Heme (By similarity).
 MOD_RES 229 229 Phosphoserine (By similarity).  
Keyword
 3D-structure; Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; Oxidoreductase; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 289 AA 
Protein Sequence
MERPQLDSMS QDLSEALKEA TKEVHIRAEN SEFMRNFQKG QVSREGFKLV MASLYHIYTA 60
LEEEIERNKQ NPVYAPLYFP EELHRRAALE QDMAFWYGPH WQEAIPYTPA TQHYVKRLHE 120
VGGTHPELLV AHAYTRYLGD LSGGQVLKKI AQKAMALPSS GEGLAFFTFP SIDNPTKFKQ 180
LYRARMNTLE MTPEVKHRVT EEAKTAFLLN IELFEELQAL LTEEHKDQSP SQTEFLRQRP 240
ASLVQDTTSA ETPRGKSQIS TSSSQTPLLR WVLTLSFLLA TVAVGIYAM 289 
Gene Ontology
 GO:0005901; C:caveola; IDA:RGD.
 GO:0005829; C:cytosol; IDA:RGD.
 GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IDA:RGD.
 GO:0020037; F:heme binding; IDA:RGD.
 GO:0004392; F:heme oxygenase (decyclizing) activity; IDA:BHF-UCL.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004630; F:phospholipase D activity; IDA:RGD.
 GO:0004871; F:signal transducer activity; IEA:Compara.
 GO:0001525; P:angiogenesis; IDA:RGD.
 GO:0071276; P:cellular response to cadmium ion; IEA:Compara.
 GO:0071456; P:cellular response to hypoxia; IEA:Compara.
 GO:0031670; P:cellular response to nutrient; IEP:RGD.
 GO:0034101; P:erythrocyte homeostasis; IEA:Compara.
 GO:0042167; P:heme catabolic process; IDA:RGD.
 GO:0006788; P:heme oxidation; TAS:RGD.
 GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:RGD.
 GO:0055072; P:iron ion homeostasis; IEA:Compara.
 GO:0043392; P:negative regulation of DNA binding; IDA:RGD.
 GO:0032764; P:negative regulation of mast cell cytokine production; IDA:RGD.
 GO:0043305; P:negative regulation of mast cell degranulation; IDA:RGD.
 GO:0010656; P:negative regulation of muscle cell apoptotic process; IDA:RGD.
 GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
 GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:RGD.
 GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:RGD.
 GO:0006644; P:phospholipid metabolic process; TAS:RGD.
 GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IEA:Compara.
 GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Compara.
 GO:0051260; P:protein homooligomerization; IEA:Compara.
 GO:0008217; P:regulation of blood pressure; IDA:RGD.
 GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IDA:BHF-UCL.
 GO:0043627; P:response to estrogen stimulus; IDA:RGD.
 GO:0042542; P:response to hydrogen peroxide; IDA:BHF-UCL.
 GO:0001666; P:response to hypoxia; IEP:RGD.
 GO:0035094; P:response to nicotine; IEA:Compara.
 GO:0007264; P:small GTPase mediated signal transduction; IDA:RGD.
 GO:0002246; P:wound healing involved in inflammatory response; IEA:Compara. 
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.