Search results

COX Assembly Mitochondrial Protein 1(CMC1) is a member of the CMC family. CMC1 is required for mitochondrial cytochrome c oxidase (COX) assembly and respiration. CMC1 attaches copper and might be involved in copper trafficking and distribution to COX and SOD1.

PSME1 is an interferon gamma (IFNG) inducible proteasome activator essential for presentation of certain major histocompatibility (MHC) class I antigens. The PSME1 complex is an alternate proteasome activator which operates with no use of ubiquitin. The PSME1 complex is made out of two homologous subunits, alpha and beta, that functions in similar catalytic properties and is connected to a hexameric ring.

NAPA is part of the SNAP (Soluble NSF Attachment Protein) family. SNAPs, acting together with SNAREs (SNAP receptors) and the N-ethylmaleimide-sensitive fusion protein (NSF), are necessary for the fusion of transport vesicles to their objective membranes in synaptic transmission, intra-Golgi transport, endosome-to-endosome fusion and transcytotic vesicles-to-plasma membrane transport. NAPA is in charge of the binding of NSF and therefore the formation of a 20S fusion particle.

Synaptobrevin 2 which is an 18 kDa integral membrane protein localized to the cytoplasmic surface of synaptic vesicle, consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal. Synaptobrevin 2 is predominantly expressed in Langerhans islets and glomerular cells. The N-terminal domain of the protein (residues 1-89) forms a specific SNARE complex with the target membrane-associated t- or Q-SNAREs syntaxin 1 and SNAP-25.

CAPG is part of the gelsolin/villin family of actin-regulatory proteins. CAPG reversibly blocks the barbed ends of F-actin filaments in a Ca2+ and phosphoinositide-regulated method, though it does not separate preformed actin filaments. By capping the barbed ends of actin filaments, CAPG contributes to the control of actin-based motility in non-muscle cells. CAPG is involved in macrophage function. CAPG is involved in regulating cytoplasmic and/or nuclear structures via possible interactions with actin. CAPG binds DNA. CAPG lacks a nuclear export sequence present in structurally related proteins. CAPG is a tumor suppressor protein that plays a role in the tumorigenic progression of certain cancers. Dysregulated expression of CAPG was found in premalignant and malignant oral carcinogenesis.

GDNF promotes the survival and differentiation of minergic neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
GDNF enhances survival and morphological differentiation of minergic neurons and increases their high-affinity uptake.

ATG5 is a member of the autophagy-related (ATG) genes family. Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents. ATG5 protein is essential for autophagy. It conjugates to ATG12 and associates with isolation membrane to form autophagosomes. In addition ATG5 takes a vital part in the apoptotic process and it is expressed relatively late in the apoptotic process, downstream of caspase activity.

Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes and assist in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit (MRPL13 is a 39S subunit protein) and have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio is reversed. An additional difference between mammalian mitoribosomes and prokaryotic ribosomes is that the second contain a 5S rRNA. Among various species, the proteins comprising the mitoribosome differ greatly in sequence, and sometimes in biochemical properties, which prevents easy recognition by sequence homology.

CTNNBIP1 binds CTNNB1 and avoids interaction between CTNNB1 and TCF (T-cell transcription factor) family members. CTNNBIP1 is a negative regulator of the Wnt signaling pathway.

TIPIN is a member of the CSM3 family. TIPIN protein is essential for normal advancement of S-phase and vital for cell existence after DNA damage or replication stress. TIPIN is specifically necessary for the ATR - CHEK1 pathway in the replication checkpoint induced by ultraviolet light.

Mitochondrial Ribosomal Protein S23, also known as MRPS23 belongs to the mammalian mitochondrial ribosomal proteins which are encoded by nuclear genes and assist in proteinsynthesis inside the mitochondrion. Mitochondrial ribosomes consist of a small 28S subunit and a large 39S subunit. In addition, they have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio isreversed. An additional difference between mammalian mitoribosomes and prokaryotic ribosomes is that the lattercontain a 5S rRNA. Between different species, the proteins containing the mitoribosome differ very much in sequence, and occasionally in biochemical properties, which prevents easy recognition by sequence homology.

Musculoskeletal, Embryonic Nuclear Protein 1, also known as MUSTN1 is a member of the MUSTANG family. MUSTN1 is implicated in the development andregeneration of the musculoskeletal system.

Tribbles Pseudokinase 3, also known as TRIB3, is a putative protein kinase which is induced by the transcription factor NF-kappaB. In addition, TRIB3 is a negative regulator of NF-kappaB, and can as well sensitize cells to TNF- and TRAIL-induced apoptosis. Furthermore, TRIB3 is able to negatively regulate the cell survival serine-threonine kinase AKT1. One of the diseases which are associated with TRIB3 is anoxia.

Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.

Ubiquitin Carboxyl-Terminal Esterase L1 (UCHL1) is a part of a family whose products hydrolyze small C-terminal adducts of ubiquitin to create the ubiquitin monomer. UCHL1 is a part of the ubiquitin system, which regulates many biological activities. UCHL1 is a thiol protease that distinguishes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 binds to free monoubiquitin and avoids its degradation in lysosomes.

LSM5 also known as LSM5 Homolog, U6 Small Nuclear RNA Associated belongs to the Sm protein family. This family is identified in a variety of organisms based on sequence homology. Sm-like proteins contain the Sm sequence motif, which consists of 2 regions separated by a linker of variable length which folds as a loop. In addition, the Sm-like proteins are thought to create a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing. Among the diseases associated with LSM5 are spinal muscular atrophy, and muscular atrophy.

Though the exact role of MMACHC is unknown, its C-terminal region shows similarity to TonB, which is a bacterial protein involved in energy transduction for cobalamin (vitamin B12) uptake. Therefore, it is suggested that MMACHC may have a role in the binding and intracellular trafficking of cobalamin. MMACHC mutations are linked with methylmalonic aciduria and homocystinuria type cblC. MMACHC is widely expressed, it is expressed at higher level in the fetal liver, however it is also expressed in the spleen, lymph node, thymus and bone marrow. MMACHC is weakly or not expressed in the peripheral blood leukocytes.

Gametocyte Specific Factor 1 (GTSF1) is a member of the UPF0224 (FAM112) family and contains 1 CHHC-type zinc finger. A key paralog of the GTSF1 gene is GTSF1L.

Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2 also known as CAPZA2 belongs the F-actin capping protein alpha subunit family. It is the alpha subunit of the barbed-end actin binding protein Cap Z. By capping the barbed end of actin filaments, Cap Z regulates the growth of the actin filaments at the barbed end. Among the diseases associated with CAPZA2 are endocarditis, and cervicitis.

UCN119B is a member of the PDE6D/unc-119 family. UCN119B has a large number of photoreceptors of the retina. Additionaly, UCN119B has a strong homology with the C. elegans unc119 and is able to functionally complement the C. elegans unc119 mutation gene.

Smac/Diablo is a proapoptotic protein that increases caspase activation in the cytochrome c/Apaf-1/caspase-9 pathway by its binding to the inhibitor of apoptosis proteins (IAPs) and removing their inhibitory activity. Smac/Diablo is a mitochondrial protein which enters the cytosol when cells go through apoptosis, and it moderates the caspase inhibition of IAPs.
Smac/DIABLO expression is associated with the result of renal cell carcinoma.
Dimeric form of Smac/DIABLO implies that once expressed in the cell the protein has a little probability of dissociation and, thus, loss of function.
Survivin, Smac/DIABLO, & PKC-? play an important part in the inhibition of apoptosis by FGF-2 in human small cell lung cancer cells. Mitochondrial survivin associates with Smac/DIABLO, delaying its release. Decreased expression of Smac protein takes part in ovarian carcinogenesis and chemotherapeutic resistance. Smac/DIABLO plays a role in tumor cells during the pathway of apoptosis induction. SMAC protein is regulated by XIAP and degraded by proteasome. SMAC protein takes part inleukemic cell apoptosis.
Smac is released during stress-induced apoptosis in multiple myeloma cells.

TOR1A which is a member of the AAA family of adenosine triphosphatases (ATPases) is associated to the Clp protease/heat shock family and is expressed highly in the substantia nigra pars compacta.TOR1A functions as a molecular chaperone assisting in the suitable folding of secreted and/or membrane proteins. Mutations in TOR1A result in the autosomal dominant disorder, torsion dystonia one.

Connective Tissue Growth Factor is a part of the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF, Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: tumorigenesis,fibrosis and vascular ailments. Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
The full length protein consists of 4 modules: Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.

Muted homolog (MUTED) is a component of the BLOC-1 complex, a complex which is necessary for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. The BLOC-1 complex is needed to steer membrane protein cargos into vesicles assembled at cell bodies for release into neurites and nerve terminals. In addition, this complex, along with SNARE proteins, is suggested to be involved in neurite extension. MUTED also interacts with pallidin, dystrobrevin binding protein 1 and CNO/cappuccino. MUTED is ubiquitously expressed with higher levels in the brain, bone marrow, kidney, and liver and lower levels in the skeletal muscle.