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HSPE1 | heat shock 10kDa protein 1 (chaperonin 10); Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (102 aa) | |||
BBS2 | Bardet-Biedl syndrome 2; The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of [...] (721 aa) | |||
CAD | carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase; This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase) (2225 aa) | |||
BBS4 | Bardet-Biedl syndrome 4; May be required for the dynein-mediated transport of pericentriolar proteins to the centrosome. Required for microtubule anchoring at the centrosome but not for microtubule nucleation. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane [...] (519 aa) | |||
SOD1 | superoxide dismutase 1, soluble; Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity) (154 aa) | |||
FARS2 | phenylalanyl-tRNA synthetase 2, mitochondrial; Catalyzes direct attachment of p-Tyr (Tyr) to tRNAPhe. Permits also, with a lower efficiency, the attachment of m-Tyr to tRNAPhe, thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins (451 aa) | |||
CCT6A | chaperonin containing TCP1, subunit 6A (zeta 1); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (531 aa) | |||
CCT5 | chaperonin containing TCP1, subunit 5 (epsilon); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (541 aa) | |||
CCT8 | chaperonin containing TCP1, subunit 8 (theta); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (548 aa) | |||
BBS5 | Bardet-Biedl syndrome 5; The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of [...] (341 aa) | |||
CCT3 | chaperonin containing TCP1, subunit 3 (gamma); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (545 aa) | |||
CCT2 | chaperonin containing TCP1, subunit 2 (beta); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (535 aa) | |||
MAT2A | methionine adenosyltransferase II, alpha; Catalyzes the formation of S-adenosylmethionine from methionine and ATP (By similarity) (395 aa) | |||
BBS1 | Bardet-Biedl syndrome 1; The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of [...] (593 aa) | |||
CCT6B | chaperonin containing TCP1, subunit 6B (zeta 2); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity) (530 aa) | |||
ACACB | acetyl-CoA carboxylase beta; ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions- biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase (2458 aa) | |||
ACACA | acetyl-CoA carboxylase alpha (2383 aa) | |||
CCT8L2 | chaperonin containing TCP1, subunit 8 (theta)-like 2; Possible molecular chaperone; assists the folding of proteins upon ATP hydrolysis (By similarity) (557 aa) | |||
MAT1A | methionine adenosyltransferase I, alpha; Catalyzes the formation of S-adenosylmethionine from methionine and ATP (By similarity) (395 aa) | |||
TTC8 | tetratricopeptide repeat domain 8 (515 aa) | |||
SOD3 | superoxide dismutase 3, extracellular; Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen (240 aa) | |||
BBS10 | Bardet-Biedl syndrome 10; Probable molecular chaperone. Assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Involved in adipogenic differentiation (723 aa) | |||
CCT4 | chaperonin containing TCP1, subunit 4 (delta); Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin (539 aa) | |||
CKAP5 | cytoskeleton associated protein 5; Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Promotes cytoplasmic microtubule nucleation and elongation. Plays a major role in organizing spindle poles (2032 aa) | |||
BBIP1 | BBSome interacting protein 1; Required for primary cilia assembly and BBSome stability. Regulates cytoplasmic microtubule stability and acetylation (103 aa) | |||
CCS | copper chaperone for superoxide dismutase; Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity) (274 aa) |