HEM14 protein (Saccharomyces cerevisiae) - STRING interaction network
"HEM14" - Protoporphyrinogen oxidase, a mitochondrial enzyme that catalyzes the seventh step in the heme biosynthetic pathway, converting protoporphyrinogen IX to protoporphyrin IX in Saccharomyces cerevisiae
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
HEM14Protoporphyrinogen oxidase, a mitochondrial enzyme that catalyzes the seventh step in the heme biosynthetic pathway, converting protoporphyrinogen IX to protoporphyrin IX; inhibited by diphenyl ether-type herbicides; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX (539 aa)    
Predicted Functional Partners:
Coproporphyrinogen III oxidase, an oxygen requiring enzyme that catalyzes the sixth step in the heme biosynthetic pathway; transcription is repressed by oxygen and heme (via Rox1p and Hap1p); 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) (328 aa)
Ferrochelatase, a mitochondrial inner membrane protein, catalyzes the insertion of ferrous iron into protoporphyrin IX, the eighth and final step in the heme biosynthetic pathway; Catalyzes the ferrous insertion into protoporphyrin IX (393 aa)
Porphobilinogen deaminase, catalyzes the conversion of 4-porphobilinogen to hydroxymethylbilane, the third step in heme biosynthesis; localizes to the cytoplasm and nucleus; expression is regulated by Hap2p-Hap3p, but not by levels of heme; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps (327 aa)
Uroporphyrinogen decarboxylase, catalyzes the fifth step in the heme biosynthetic pathway; localizes to both the cytoplasm and nucleus; a hem12 mutant has phenotypes similar to patients with porphyria cutanea tarda; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III (362 aa)
Aminolevulinate dehydratase, a homo-octameric enzyme, catalyzes the conversion of 5-aminolevulinate to porphobilinogen, the second step in heme biosynthesis; enzymatic activity is zinc-dependent; localizes to the cytoplasm and nucleus; 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 (342 aa)
Uroporphyrinogen III synthase, catalyzes the conversion of hydroxymethylbilane to uroporphyrinogen III, the fourth step in heme biosynthesis; deficiency in the human homolog can result in the disease congenital erythropoietic porphyria; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III (275 aa)
5-aminolevulinate synthase, catalyzes the first step in the heme biosynthetic pathway; an N-terminal signal sequence is required for localization to the mitochondrial matrix; expression is regulated by Hap2p-Hap3p; Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis (548 aa)
Alpha subunit of the F1 sector of mitochondrial F1F0 ATP synthase, which is a large, evolutionarily conserved enzyme complex required for ATP synthesis; phosphorylated; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and [...] (545 aa)
Catalytic subunit of the mitochondrial inner membrane i-AAA protease complex, which is responsible for degradation of unfolded or misfolded mitochondrial gene products; mutation causes an elevated rate of mitochondrial turnover; Catalytic subunit of the mitochondrial inner membrane i- AAA protease supercomplex required for mitochondrial inner membrane protein turnover. The protease is probably ATP-dependent. Important to maintain the integrity of the mitochondrial compartment. Required both for the degradation of unassembled subunit 2 of cytochrome c oxidase (COX2) and for efficient as [...] (747 aa)
Multidrug transporter of the major facilitator superfamily, required for resistance to quinidine, ketoconazole, fluconazole, and barban; Multidrug resistance transporter involved in resistance and adaptation to quinidine and ketoconazole (563 aa)
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
Server load: low (3%) [HD]