| Tag | Content |
|---|
| CPLM ID | CPLM-005214 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Heme oxygenase 2 |
Protein Synonyms/Alias | HO-2 |
Gene Name | Hmox2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 37 | ADLSELLKEGTKEAH | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
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 263 268 HRM 1.
REPEAT 280 285 HRM 2.
METAL 44 44 Iron (heme axial ligand) (By similarity).
MOD_RES 2 2 N-acetylserine (By similarity). |
Keyword | Acetylation; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Metal-binding; Microsome; Oxidoreductase; Reference proteome; Repeat. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 315 AA |
Protein Sequence | MSSEVETSEG VDESENNSTA PEKENHTKMA DLSELLKEGT KEAHDRAENT QFVKDFLKGN 60
IKKELFKLAT TALYFTYSAL EEEMDRNKDH PAFAPLYFPT ELHRKEALIK DMEYFFGENW 120
EEQVKCSEAA QKYVDRIHYV GQNEPELLVA HAYTRYMGDL SGGQVLKKVA QRALKLPSTG 180
EGTQFYLFEH VDNAQQFKQF YRARMNALDL SMKTKERIVE EANKAFEYNM QIFSELDQAG 240
SMLTKETLED GLPVHDGKGD VRKCPFYAAQ PDKGTLGGSN CPFRTAMAVL RKPSLQLILA 300
ASVALVAGLL AWYYM 315 |
Gene Ontology | GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. GO:0005886; C:plasma membrane; IEA:Compara. GO:0004392; F:heme oxygenase (decyclizing) activity; IDA:RGD. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006788; P:heme oxidation; TAS:RGD. GO:0001666; P:response to hypoxia; IEA:Compara. GO:0006979; P:response to oxidative stress; IDA:RGD. |
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Pfam | |
SMART | |
PROSITE | |
PRINTS | |