Nodes:
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 Size
small nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
second shell of interactors
Edges:
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
Others
textmining
co-expression
protein homology
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Your Input:
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 | COX15 | cytochrome c oxidase assembly homolog 15 (yeast); May be involved in the biosynthesis of heme A (410 aa) | ||
 | UQCRC1 | ubiquinol-cytochrome c reductase core protein I; This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This protein may mediate formation of the complex between cytochromes c and c1 (480 aa) | ||
 | CAT | catalase; Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells (527 aa) | ||
 | PMPCB | peptidase (mitochondrial processing) beta; Cleaves presequences (transit peptides) from mitochondrial protein precursors (By similarity) (489 aa) | ||
 | SCO2 | SCO2 cytochrome c oxidase assembly protein; Acts as a copper chaperone, transporting copper to the Cu(A) site on the cytochrome c oxidase subunit II (COX2) (266 aa) | ||
 | SCO1 | SCO1 cytochrome c oxidase assembly protein; Thought to play a role in cellular copper homeostasis, mitochondrial redox signaling or insertion of copper into the active site of COX (301 aa) | ||
 | COQ9 | coenzyme Q9 homolog (S. cerevisiae); Involved in the biosynthesis of coenzyme Q (By similarity) (318 aa) | ||
 | UQCRC2 | ubiquinol-cytochrome c reductase core protein II; This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. The core protein 2 is required for the assembly of the complex (453 aa) | ||
 | COX11 | cytochrome c oxidase assembly homolog 11 (yeast); Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I (By similarity) (276 aa) | ||
 | UQCRFS1 | ubiquinol-cytochrome c reductase, Rieske iron-sulfur polypeptide 1; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis (274 aa) | ||
 | CYCS | cytochrome c, somatic; Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain (By similarity) (105 aa) | ||
 | CYC1 | cytochrome c-1; This is the heme-containing component of the cytochrome b-c1 complex, which accepts electrons from Rieske protein and transfers electrons to cytochrome c in the mitochondrial respiratory chain (325 aa) | ||
 | KLK5 | kallikrein-related peptidase 5; May be involved in desquamation (293 aa) | ||
 | NDUFA4 | NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 4, 9kDa; Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (81 aa) | ||
 | MT-CO1 | mitochondrially encoded cytochrome c oxidase I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B (By similarity) (513 aa) | ||
 | MT-CYB | mitochondrially encoded cytochrome b; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis (By similarity) (380 aa) | ||
 | MT-CO2 | mitochondrially encoded cytochrome c oxidase II; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1 (By similarity) (227 aa) | ||
 | MT-CO3 | mitochondrially encoded cytochrome c oxidase III; Subunits I, II and III form the functional core of the enzyme complex (By similarity) (261 aa) | ||
 | DCLRE1A | DNA cross-link repair 1A; May be required for DNA interstrand cross-link repair. Also required for checkpoint mediated cell cycle arrest in early prophase in response to mitotic spindle poisons (1040 aa) | ||
 | LACE1 | lactation elevated 1 (481 aa) | ||
 | DCLRE1B | DNA cross-link repair 1B; 5’-3’ exonuclease that plays a central role in telomere maintenance and protection during S-phase. Participates in the protection of telomeres against non-homologous end-joining (NHEJ)- mediated repair, thereby ensuring that telomeres do not fuse. Plays a key role in telomeric loop (T loop) formation by being recruited by TERF2 at the leading end telomeres and by processing leading-end telomeres immediately after their replication via its exonuclease activity- generates 3’ single-stranded overhang at the leading end telomeres avoiding blunt leading-end telomer [...] (532 aa) | ||
 | CTH | cystathionase (cystathionine gamma-lyase); Catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure. Acts as a cysteine-protein sulfhydrase by mediating sulfhydration [...] (405 aa) | ||
 | PMPCA | peptidase (mitochondrial processing) alpha; Cleaves presequences (transit peptides) from mitochondrial protein precursors (By similarity) (525 aa) | ||
 | ENSG00000248919 | ATP5J2-PTCD1 readthrough (749 aa) | ||
 | PTCD1 | pentatricopeptide repeat domain 1; Mitochondrial protein implicated in negative regulation of leucine tRNA levels, as well as negative regulation of mitochondria-encoded proteins and COX activity. Affects also the 3’ processing of mitochondrial tRNAs (749 aa) | ||
 | ENSG00000269383 | Uncharacterized protein; Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain (By similarity) (100 aa) | ||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
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