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ALAD ALAD CPOX CPOX HMBS HMBS UROS UROS FECH FECH BLVRB BLVRB BLVRA BLVRA SLC25A38 SLC25A38 ABCB6 ABCB6 HMOX2 HMOX2 PPOX PPOX UROD UROD HMOX1 HMOX1 ENDOV ENDOV ENSBTAP00000067738 ENSBTAP00000067738
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
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gene fusions
gene co-occurrence
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ALADDelta-aminolevulinic acid dehydratase; Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity); Belongs to the ALAD family. (329 aa)
CPOXCoproporphyrinogen oxidase. (449 aa)
HMBSPorphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. (361 aa)
UROSUroporphyrinogen III synthase. (264 aa)
FECHFerrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. (416 aa)
BLVRBFlavin reductase (NADPH); Broad specificity oxidoreductase that catalyzes the NADPH- dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin and PQQ (pyrroloquinoline quinone). Contributes to heme catabolism and metabolizes linear tetrapyrroles. Can also reduce the complexed Fe(3+) iron to Fe(2+) in the presence of FMN and NADPH. In the liver, converts biliverdin to bilirubin. (206 aa)
BLVRABiliverdin reductase A; Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor; Belongs to the Gfo/Idh/MocA family. Biliverdin reductase subfamily. (296 aa)
SLC25A38Mitochondrial glycine transporter; Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the mitochondrial matrix. Required during erythropoiesis. Belongs to the mitochondrial carrier (TC 2.A.29) family. SLC25A38 subfamily. (306 aa)
ABCB6ATP binding cassette subfamily B member 6. (843 aa)
HMOX2Heme oxygenase 2. (334 aa)
PPOXProtoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. (477 aa)
URODUroporphyrinogen decarboxylase; Belongs to the uroporphyrinogen decarboxylase family. (367 aa)
HMOX1Heme oxygenase 1; 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. (302 aa)
ENDOVEndonuclease V. (399 aa)
ENSBTAP00000067738Uncharacterized protein. (156 aa)
Your Current Organism:
Bos taurus
NCBI taxonomy Id: 9913
Other names: B. taurus, Bos bovis, Bos primigenius taurus, Bovidae sp. Adi Nefas, bovine, cattle, cow, dairy cow, domestic cattle, domestic cow
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