About Products Protein Database Contact

HMOX1

Gene
HMOX1
Protein
Heme oxygenase 1
Organism
Gallus gallus
Length
296 amino acids
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.
Similarity
Belongs to the heme oxygenase family.
Mass
33.509 kDa
Sequence
METSQPHNAESMSQDLSELLKEATKEVHEQAENTPFMKNFQKGQVSLHEFKLVTASLYFIYSALEEEIERNKDNPVYAPVYFPMELHRKAALEKDLEYFYGSNWRAEIPCPEATQKYVERLHVVGKKHPELLVAHAYTRYLGDLSGGQVLKKIAQKALQLPSTGEGLAFFTFDGVSNATKFKQLYRSRMNALEMDHATKKRVLEEAKKAFLLNIQVFEALQKLVSKSQENGHAVQPKAELRTRSVNKSHENSPAAGKESERTSRMQADMLTTSPLVRWLLALGFIATTVAVGLFAM

Gene
Hmox1
Protein
Heme oxygenase 1
Organism
Rattus norvegicus
Length
289 amino acids
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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.
Similarity
Belongs to the heme oxygenase family.
Mass
33.006 kDa
Sequence
MERPQLDSMSQDLSEALKEATKEVHIRAENSEFMRNFQKGQVSREGFKLVMASLYHIYTALEEEIERNKQNPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEAIPYTPATQHYVKRLHEVGGTHPELLVAHAYTRYLGDLSGGQVLKKIAQKAMALPSSGEGLAFFTFPSIDNPTKFKQLYRARMNTLEMTPEVKHRVTEEAKTAFLLNIELFEELQALLTEEHKDQSPSQTEFLRQRPASLVQDTTSAETPRGKSQISTSSSQTPLLRWVLTLSFLLATVAVGIYAM

Gene
HMOX1
Protein
Heme oxygenase 1
Organism
Bos taurus
Length
289 amino acids
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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.
Similarity
Belongs to the heme oxygenase family.
Mass
32.94 kDa
Sequence
MERPQPDSSMPQDLSEALKEATKEVHTQAENAEFMKNFQKGELTQEGFKLVMASLYHIYVALEEEIERNKENPVYTPLYFPEELHRRASLEQDMAFWYGPRWQEAIPYTQATKRYVQRLQEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALNLPSSGEGLAFFTFPNIASATKFKQLYRSRMNTLEMTPEVRQRVLDEAKTAFLLNIQLFEELQGLLTQKAKDHDPLQAPELHRRAGSKVQDLAPTKASRGKPQPSVLSQAPLLRWVLTLSFLVATVAVGLYAM

Gene
Hmox1
Protein
Heme oxygenase 1
Organism
Mus musculus
Length
289 amino acids
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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.
Similarity
Belongs to the heme oxygenase family.
Mass
32.929 kDa
Sequence
MERPQPDSMPQDLSEALKEATKEVHIQAENAEFMKNFQKGQVSREGFKLVMASLYHIYTALEEEIERNKQNPVYAPLYFPEELHRRAALEQDMAFWYGPHWQEIIPCTPATQHYVKRLHEVGRTHPELLVAHAYTRYLGDLSGGQVLKKIAQKAMALPSSGEGLAFFTFPNIDSPTKFKQLYRARMNTLEMTPEVKHRVTEEAKTAFLLNIELFEELQVMLTEEHKDQSPSQMASLRQRPASLVQDTAPAETPRGKPQISTSSSQTPLLQWVLTLSFLLATVAVGIYAM

Gene
HMOX1
Protein
Heme oxygenase 1
Organism
Sus scrofa
Length
288 amino acids
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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.
Similarity
Belongs to the heme oxygenase family.
Mass
33.074 kDa
Sequence
MEHSQPNSMPQDLSEALKEATKEVHVQAENAEFMKNFQKGEVTREGFKLVMASLYHIYDALEEEIEHNKENPVYTPLYFPEELHRRAALEQDMAFWYGPRWQEAIPYTQATKRYVRRLQQVGRFEPELLVAHAYTRYMGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNVANATKFKQLYRSRMNTLEMTPEVKQRVLEEAKTAFLLNIQLFEEVQELLTQDTKDQRPSQASDIRKRAGSRVQDSTPVTTPRGKPQLSVLSQVPLIRWVLTLSFLVATVAMGLYAM

Gene
HMOX1
Protein
Heme oxygenase 1
Organism
Pongo abelii
Length
288 amino acids
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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.
Similarity
Belongs to the heme oxygenase family.
Mass
32.712 kDa
Sequence
MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTREGFKLVMASLYHIYVALEEEIEHNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALGLPSSGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRASNKAQDSAPVETPRGKTPLNTHSQAPLLRWVLTLSFLVATVAVGLYAM

Gene
HMOX1
Protein
Heme oxygenase 1
Organism
Homo sapiens
Length
288 amino acids
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. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.
Similarity
Belongs to the heme oxygenase family.
Mass
32.819 kDa
Sequence
MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVALEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHEVGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQLYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRASNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM