AFG3 ATPase family member 3-like 2 (S. cerevisiae); ATP-dependent protease which is essential for axonal development (By similarity)

YME1-like 1 (S. cerevisiae); Putative ATP-dependent protease which plays a role in mitochondrial protein metabolism. Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins. Requires to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1). Seems to act in the processing of OPA1

adaptor-related protein complex 1, beta 1 subunit; Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules

adaptor-related protein complex 3, beta 1 subunit; Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required [...]

adaptor-related protein complex 1, beta 1 subunit; Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules

adaptor-related protein complex 4, beta 1 subunit; Subunit of novel type of clathrin- or non-clathrin- associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system

adaptor-related protein complex 2, beta 1 subunit; Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin- coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as [...]

adaptor-related protein complex 3, beta 1 subunit; Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required [...]

adaptor-related protein complex 2, beta 1 subunit; Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin- coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as [...]

adaptor-related protein complex 4, beta 1 subunit; Subunit of novel type of clathrin- or non-clathrin- associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system

adaptor-related protein complex 3, beta 1 subunit; Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required [...]

adaptor-related protein complex 1, beta 1 subunit; Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules

adaptor-related protein complex 3, beta 1 subunit; Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required [...]

adaptor-related protein complex 2, beta 1 subunit; Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin- coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as [...]

adaptor-related protein complex 3, beta 1 subunit; Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required [...]

adaptor-related protein complex 4, beta 1 subunit; Subunit of novel type of clathrin- or non-clathrin- associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system

adaptor-related protein complex 4, beta 1 subunit; Subunit of novel type of clathrin- or non-clathrin- associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system

adaptor-related protein complex 1, beta 1 subunit; Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules

adaptor-related protein complex 4, beta 1 subunit; Subunit of novel type of clathrin- or non-clathrin- associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system

adaptor-related protein complex 2, beta 1 subunit; Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin- coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as [...]

adaptor-related protein complex 4, beta 1 subunit; Subunit of novel type of clathrin- or non-clathrin- associated protein coat involved in targeting proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system

adaptor-related protein complex 3, beta 1 subunit; Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required [...]

cytochrome b5 reductase 4; NADH-cytochrome b5 reductase involved in endoplasmic reticulum stress response pathway. Plays a critical role in protecting pancreatic beta-cells against oxidant stress, possibly by protecting the cell from excess buildup of reactive oxygen species (ROS). Reduces a variety of substrates in vitro, such as cytochrome c, feericyanide and methemoglobin

stearoyl-CoA desaturase (delta-9-desaturase)

cytochrome b5 reductase 4; NADH-cytochrome b5 reductase involved in endoplasmic reticulum stress response pathway. Plays a critical role in protecting pancreatic beta-cells against oxidant stress, possibly by protecting the cell from excess buildup of reactive oxygen species (ROS). Reduces a variety of substrates in vitro, such as cytochrome c, feericyanide and methemoglobin

stearoyl-CoA desaturase 5; Fatty acid delta-9-desaturase that introduces a double bond in fatty acyl-coenzyme A at the delta-9 position

cytochrome b5 reductase 4; NADH-cytochrome b5 reductase involved in endoplasmic reticulum stress response pathway. Plays a critical role in protecting pancreatic beta-cells against oxidant stress, possibly by protecting the cell from excess buildup of reactive oxygen species (ROS). Reduces a variety of substrates in vitro, such as cytochrome c, feericyanide and methemoglobin

ubiquitin A-52 residue ribosomal protein fusion product 1

IMP1 inner mitochondrial membrane peptidase-like (S. cerevisiae); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO

IMP2 inner mitochondrial membrane peptidase-like (S. cerevisiae); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO

IMP1 inner mitochondrial membrane peptidase-like (S. cerevisiae); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO

signal peptidase complex subunit 1 homolog (S. cerevisiae); Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity)

IMP1 inner mitochondrial membrane peptidase-like (S. cerevisiae); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO

signal peptidase complex subunit 3 homolog (S. cerevisiae); Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity)

IMP1 inner mitochondrial membrane peptidase-like (S. cerevisiae); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO

YME1-like 1 (S. cerevisiae); Putative ATP-dependent protease which plays a role in mitochondrial protein metabolism. Ensures cell proliferation, maintains normal cristae morphology and complex I respiration activity, promotes antiapoptotic activity and protects mitochondria from the accumulation of oxidatively damaged membrane proteins. Requires to control the accumulation of nonassembled respiratory chain subunits (NDUFB6, OX4 and ND1). Seems to act in the processing of OPA1

IMP2 inner mitochondrial membrane peptidase-like (S. cerevisiae); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO

IMP1 inner mitochondrial membrane peptidase-like (S. cerevisiae); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO

IMP2 inner mitochondrial membrane peptidase-like (S. cerevisiae); Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO

signal peptidase complex subunit 1 homolog (S. cerevisiae); Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity)