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Blvra Blvra Hmox2 Hmox2 Hmox1 Hmox1 Por Por Tmem14c Tmem14c Sfxn1 Sfxn1 Ftmt Ftmt Abcb6 Abcb6 Urod Urod Uros Uros Abcb7 Abcb7 Slc25a38 Slc25a38 Slc25a28 Slc25a28 Slc25a37 Slc25a37 Blvrb Blvrb Cpox Cpox Ppox Ppox Abcb10 Abcb10 Hmbs Hmbs Flvcr1 Flvcr1 Endov Endov Alad Alad Slc48a1 Slc48a1 Fech Fech
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
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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. (295 aa)
Hmox2Heme oxygenase 2; 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. (315 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. (289 aa)
PorNADPH--cytochrome P450 reductase; This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5; In the N-terminal section; belongs to the flavodoxin family. (678 aa)
Tmem14cTransmembrane protein 14C; Required for normal heme biosynthesis; Belongs to the TMEM14 family. (114 aa)
Sfxn1Sideroflexin-1; Mitochondrial serine transporter that mediates transport of serine into mitochondria, an important step of the one-carbon metabolism pathway (By similarity). Mitochondrial serine is converted to glycine and formate, which then exits to the cytosol where it is used to generate the charged folates that serve as one-carbon donors (By similarity). Transports both D-serine and L-serine (By similarity). Also able to transport other amino-acids, such as alanine (By similarity). May be indirectly involved in the transport of a component required for iron utilization into or out [...] (322 aa)
FtmtFerritin, mitochondrial; Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (By similarity); Belongs to the ferritin family. (237 aa)
Abcb6ATP-binding cassette sub-family B member 6, mitochondrial; Binds heme and porphyrins and functions in their ATP- dependent uptake into the mitochondria. Plays a crucial role in heme synthesis. (842 aa)
UrodUroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. (367 aa)
UrosUroporphyrinogen-III synthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of porphyrins. Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell such as methionine synthesis (vitamin B12) or oxygen transport (heme) (By similarity). Belongs to the uroporphyrinogen-III synthase family. (265 aa)
Abcb7ATP-binding cassette sub-family B member 7, mitochondrial; Could be involved in the transport of heme from the mitochondria to the cytosol. Plays a central role in the maturation of cytosolic iron-sulfur (Fe/S) cluster-containing proteins. (752 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. (326 aa)
Slc25a28Mitoferrin-2; Mitochondrial iron transporter that mediates iron uptake. Probably required for heme synthesis of hemoproteins and Fe-S cluster assembly in non-erythroid cells. The iron delivered into the mitochondria, presumably as Fe(2+), is then probably delivered to ferrochelatase to catalyze Fe(2+) incorporation into protoprophyrin IX to make heme (Probable); Belongs to the mitochondrial carrier (TC 2.A.29) family. (364 aa)
Slc25a37Mitoferrin-1; Mitochondrial iron transporter that specifically mediates iron uptake in developing erythroid cells, thereby playing an essential role in heme biosynthesis. The iron delivered into the mitochondria, presumably as Fe(2+), is then probably delivered to ferrochelatase to catalyze Fe(2+) incorporation into protoprophyrin IX to make heme. (338 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)
CpoxOxygen-dependent coproporphyrinogen-III oxidase, mitochondrial; Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- IX (By similarity). (443 aa)
PpoxProtoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX. (477 aa)
Abcb10ATP-binding cassette sub-family B member 10, mitochondrial; May mediate critical mitochondrial transport functions related to heme biosynthesis; Belongs to the ABC transporter superfamily. ABCB family. Mitochondrial peptide exporter (TC 3.A.1.212) subfamily. (715 aa)
HmbsPorphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps; Belongs to the HMBS family. (361 aa)
Flvcr1Feline leukemia virus subgroup C receptor-related protein 1; [Isoform 1]: Heme transporter that exports cytoplasmic heme. It can also export coproporphyrin and protoporphyrin IX, which are both intermediate products in the heme biosynthetic pathway. Does not export bilirubin. Heme export depends on the presence of HPX and is required to maintain intracellular free heme balance, protecting cells from heme toxicity. Heme export provides protection from heme or ferrous iron toxicities in liver, brain, sensory neurons and during erythtopoiesis, a process in which heme synthesis intensifies [...] (560 aa)
EndovEndonuclease V; Endoribonuclease that specifically cleaves inosine-containing RNAs: cleaves RNA at the second phosphodiester bond 3' to inosine. Has strong preference for single-stranded RNAs (ssRNAs) toward double- stranded RNAs (dsRNAs). Cleaves mRNAs and tRNAs containing inosine. Also able to cleave structure-specific dsRNA substrates containing the specific sites 5'-IIUI-3' and 5'-UIUU-3'. Inosine is present in a number of RNAs following editing; the function of inosine-specific endoribonuclease is still unclear: it could either play a regulatory role in edited RNAs, or be involved [...] (338 aa)
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. (330 aa)
Slc48a1Heme transporter HRG1; Heme transporter that regulates intracellular heme availability through the endosomal or lysosomal compartment. Belongs to the HRG family. (146 aa)
FechFerrochelatase, mitochondrial; Catalyzes the ferrous insertion into protoporphyrin IX. (422 aa)
Your Current Organism:
Mus musculus
NCBI taxonomy Id: 10090
Other names: LK3 transgenic mice, M. musculus, Mus sp. 129SV, house mouse, mouse, nude mice, transgenic mice
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