CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002804
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Heme oxygenase 1 
Protein Synonyms/Alias
 HO-1 
Gene Name
 HMOX1 
Gene Synonyms/Alias
 HO; HO1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
18QDLSEALKEATKEVHacetylation[1]
18QDLSEALKEATKEVHubiquitination[2]
39EFMRNFQKGQVTRDGacetylation[3]
39EFMRNFQKGQVTRDGubiquitination[2]
69EEEIERNKESPVFAPubiquitination[2]
86FPEELHRKAALEQDLubiquitination[2, 4]
148LSGGQVLKKIAQKALubiquitination[2, 4]
153VLKKIAQKALDLPSSubiquitination[2, 4]
177PNIASATKFKQLYRSubiquitination[2, 4]
179IASATKFKQLYRSRMubiquitination[2]
243LRQRASNKVQDSAPVubiquitination[2, 4, 5]
256PVETPRGKPPLNTRSubiquitination[2, 4]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [2] 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]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] 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]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
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.
 BINDING 134 134 Heme.
 BINDING 183 183 Heme.
 MOD_RES 229 229 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 288 AA 
Protein Sequence
MERPQPDSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA 60
LEEEIERNKE SPVFAPVYFP EELHRKAALE QDLAFWYGPR WQEVIPYTPA MQRYVKRLHE 120
VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQ 180
LYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA 240
SNKVQDSAPV ETPRGKPPLN TRSQAPLLRW VLTLSFLVAT VAVGLYAM 288 
Gene Ontology
 GO:0005901; C:caveola; IEA:Compara.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0005615; C:extracellular space; TAS:BHF-UCL.
 GO:0005730; C:nucleolus; IEA:Compara.
 GO:0005634; C:nucleus; ISS:BHF-UCL.
 GO:0019899; F:enzyme binding; ISS:BHF-UCL.
 GO:0020037; F:heme binding; IDA:BHF-UCL.
 GO:0004392; F:heme oxygenase (decyclizing) activity; IMP:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004630; F:phospholipase D activity; IEA:Compara.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0004871; F:signal transducer activity; IMP:UniProtKB.
 GO:0001525; P:angiogenesis; TAS:BHF-UCL.
 GO:0008219; P:cell death; ISS:BHF-UCL.
 GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
 GO:0071276; P:cellular response to cadmium ion; IEA:Compara.
 GO:0071456; P:cellular response to hypoxia; IEP:UniProtKB.
 GO:0031670; P:cellular response to nutrient; IEA:Compara.
 GO:0001935; P:endothelial cell proliferation; TAS:BHF-UCL.
 GO:0034101; P:erythrocyte homeostasis; IMP:BHF-UCL.
 GO:0007588; P:excretion; IC:BHF-UCL.
 GO:0042167; P:heme catabolic process; IDA:BHF-UCL.
 GO:0006788; P:heme oxidation; IDA:BHF-UCL.
 GO:0007243; P:intracellular protein kinase cascade; TAS:BHF-UCL.
 GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Compara.
 GO:0034383; P:low-density lipoprotein particle clearance; TAS:BHF-UCL.
 GO:0043392; P:negative regulation of DNA binding; IEA:Compara.
 GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:BHF-UCL.
 GO:0002686; P:negative regulation of leukocyte migration; TAS:BHF-UCL.
 GO:0032764; P:negative regulation of mast cell cytokine production; IEA:Compara.
 GO:0043305; P:negative regulation of mast cell degranulation; IEA:Compara.
 GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Compara.
 GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IEA:Compara.
 GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:UniProtKB.
 GO:0045766; P:positive regulation of angiogenesis; IEA:Compara.
 GO:0045080; P:positive regulation of chemokine biosynthetic process; TAS:BHF-UCL.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
 GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:UniProtKB.
 GO:0045909; P:positive regulation of vasodilation; IC:BHF-UCL.
 GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
 GO:0045765; P:regulation of angiogenesis; TAS:BHF-UCL.
 GO:0008217; P:regulation of blood pressure; IEA:Compara.
 GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; ISS:BHF-UCL.
 GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; ISS:BHF-UCL.
 GO:0043627; P:response to estrogen stimulus; IEA:Compara.
 GO:0042542; P:response to hydrogen peroxide; ISS:BHF-UCL.
 GO:0035094; P:response to nicotine; IDA:BHF-UCL.
 GO:0007264; P:small GTPase mediated signal transduction; IEA:Compara.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0014806; P:smooth muscle hyperplasia; TAS:BHF-UCL.
 GO:0055085; P:transmembrane transport; TAS:Reactome.
 GO:0002246; P:wound healing involved in inflammatory response; IMP:BHF-UCL. 
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.