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Nucleobindin-2 (NUCB2) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 is localized in neuronal perikarya and dendrites of mouse brain.

Syntaxin-binding protein 6 (STXBP6) binds components of the SNARE complex and takes part in regulating SNARE complex configuration. STXBP6 forms non-fusogenic complexes with SNAP25 and STX1A and modulates the formation of SNARE complexes and exocytosis.

Heterogeneous Nuclear Ribonucleoprotein K, also known as HNRNPK, is a part of the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). HNRNPK takes part in p53/TP53 reaction to DNA damage, acting at the level of both transcription activation and repression. HNRNPK is located in the nucleoplasm and has 3 repeats of KH domains which bind to RNAs.

SDCBP2 has two class II PDZ domains. PDZ domains assist protein-protein interactions by attaching to the cytoplasmic C-terminus of transmembrane proteins, and PDZ-containing proteins mediate cell signaling and the organization of protein complexes. SDCBP2 attaches to phosphatidylinositol 4, 5-bisphosphate (PIP2) and take part in nuclear PIP2 arrangement and cell division.

COL4A3BP is a kinase that particularly phosphorylates the N-terminal region of the non-collagenous domain of the alpha 3 chain of type IV collagen, recognized as the Goodpasture antigen that is the outcome of an autoimmune reaction directed at COL4A3BP. One isoform of COL4A3BP participates in ceramide intracellular transport.

MECP2 is the key modificator of eukaryotic genomes and has a crucial part in mammalian development.
Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 form a family of nuclear proteins linked by the existence in each of a methyl-CpG binding domain (MBD). Each one of these proteins, with the exception of MBD3, can bind specifically to methylated DNA. In addition, MECP2, MBD1 and MBD2 can inhibit transcription from methylated gene promoters. Unlike other MBD family members, MECP2 is X-linked and subject to X inactivation. MECP2 is expendable in stem cells, but is vital for embryonic development. MECP2 gene mutations are the cause of most cases of Rett syndrome, a progressive neurologic developmental disorder and one of the most common reasons of mental retardation in females.

MYCBP is a member of the AMY1 family. MYCBP (c-Myc binding protein) binds to the transactivation domain of c-Myc and stimulates the activation of E-box-dependent transcription. MYCBP translocates from the cytoplasm to the nucleus during S phase when increased expression of c-Myc occurs. MYCBP also associates with AKAP 149 and AKAP 84 in mitochondria of somatic cells and sperm, suggesting a role for MYCBP in spermatogenesis. MYCBP is highly expressed in the heart, placenta, pancreas, skeletal muscle and kidney. It is also present at low levels in the lung.

Growth Hormone Binding Protein or GHR, is a protein, part of the cytokine receptor superfamily. GHR binds to 2 receptors, therefore it enhances signal transduction via dimerization of receptors. In elevated levels, growth hormone operates as an antagonist due to high variance in the binding sites affinities. The antagonist operation can be embellished even more when the binding site is reduced its affinity.

Regulation Of Nuclear Pre-MRNA Domain Containing 1A (RPRD1A) is upregulated in cells overexpressing cyclin-dependent kinase inhibitor p15(INK4b) and may have a part in cell cycle regulation. RPRD1A interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and partakes in dephosphorylation of the CTD. RPRD1A May function as a negative regulator of cyclin-D1 (CCND1) and cyclin-E (CCNE1) in the cell cycle.

HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 (HERC5) is a member of the HERC family of ubiquitin ligases, found in a cluster of HERC family genes on chromosome 4. HERC5 is a protein with a HECT domain and 5 RCC1 repeats. The HERC5 protein localizes to the cytoplasm and perinuclear region and serves as an INF-induced E3 protein ligase that mediates ISGylation of protein targets. HERC5 exhibits antiviral activity towards HIV-1, influenza A virus and human papillomavirus. HERC5 is a major E3 ligase for ISG15 conjugation. HERC5 also serves as a positive regulator of innate antiviral response in cells induced by INF. Pro-inflammatory cytokines upregulate HERC5 in endothelial cells. HERC5 is physically connected with polyribosomes, broadly modifies recently synthesized proteins in a cotranslational fashion.

GHBP is a transmembrane receptor for growth hormone. Binding of growth hormone to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon three and has been well-characterized. Mutations in this gene have been associated with Laron syndrome, also known as the growth hormone insensitivity syndrome (GHIS), a disorder characterized by short stature. Other splice variants, including one encoding a soluble form of the protein (GHRtr), have been observed but have not been thoroughly characterized.

KLRB1 has an inhibitory role on natural killer (NK) cells cytotoxicity which are lymphocytes who facilitate cytotoxicity and secrete cytokines subsequent to immune stimulation. Some genes of the C-type lectin superfamily, like the rodent NKRP1 family of glycoproteins, are expressed by NK cells and take part in NK cell function regulation. KLRB1 holds an extracellular domain with a few characteristic motifs of C-type lectins, a transmembrane domain, and a cytoplasmic domain. Due to its external C terminus KLRB1 is considered to be a type II membrane protein.

GHBP is a transmembrane receptor for growth hormone. Binding of growth hormone to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. A common alternate allele of this gene, called GHRd3, lacks exon three and has been well-characterized. Mutations in this gene have been associated with Laron syndrome, also known as the growth hormone insensitivity syndrome (GHIS), a disorder characterized by short stature. Other splice variants, including one encoding a soluble form of the protein (GHRtr), have been observed but have not been thoroughly characterized.

CCAAT/enhancer binding protein(C/EBP) a is a family of transcription factors that all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and that form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBPs differ significantly in their physiological functions and in their downstream target genes. For example, mice lacking C/EBPa die shortly after birth due to severe hypoglycemia and the absence of glycogen storage in liver, whereas knockout of C/EBPb causes defects in female reproduction.

CAMP Responsive Element Binding Protein 3-Like 2, also known as CREB3L2 belongs to the oasis bZIP transcription factor family. Members of this family are able to dimerize however from homodimers only. CREB3L2 is a transcriptional activator. Translocations between CREB3L2 on chromosome 7 and the gene fused in sarcoma on chromosome 16 can be found in some tumors. One disease which is associated with CREB3L2 is myxofibrosarcoma.

Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.

Centromere proteins are a group of proteins which form and/or mediate the function of centromeres, the central structures of chromosomes to which spindle fibers/microtubuli attach and pull the chromosomes apart in cell division. Currently, 9 centromere proteins are known and designated CENPA to CENP-I. Most of the centromere proteins are targets of autoantibodies, the anti-centromere antibodies.
CENPB is the most important of the centromeric autoantigens: it has a molecular weight of approx. 66 kDa and plays an important role in the formation of the centromeric chromatin. CENPB antibodies are present in the sera of up to 80% of patients with CREST syndrome.

RNA Binding Motif Protein 18 (RBM18) is comprised of one RNA recognition motif (RRM) domain.

TRIM21 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The 52 kDa Ro protein is part of the RoSSA ribonucleoprotein, which includes a single polypeptide and one of four small RNA molecules. The RoSSA particle localizes to both the cytoplasm and the nucleus. Ro/SSA interacts with autoantigens in patients with Sjogren syndrome and systemic lupus erythematosus. Ribonucleoprotein particle is composed of a single polypeptide and one of four small RNA molecules. The RoSSA is present in all mammalian cells studied but has no known function. At least 2 isoforms are present in nucleated and red blood cells, and tissue specific differences in Ro/SSA proteins were identified.

FABP6 also called ileal fatty acid binding protein, is part of the small family of highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABP6 cytosolic protein binds bile acid. FABP6 plays a role in fatty acid uptake, transport, and metabolism. FABP6 stimulates gastric acid and pepsinogen secretion. Seems to be able to bind to bile salts and bilirubins. FABP6 expression is restricted in the small intestine to the ileum where it is involved in the enterohepatic circulation of bile acids. Alternate transcription promoters generate 2 transcript variants, encoding a 128 aa and a 177 aa residue protein. Human FABP6 isoform 2 contains 128 amino acid residues and is acetylated on Ala2. FABP6 binds together fatty acids and bile acids and is directly involved in fatty acid transport and metabolism.

Calcium-binding protein 7 (CABP7) contains 2 EF-hand domains. CABP7 negatively regulates Golgi-to-plasma membrane trafficking by interacting with PI4KB and inhibiting its activity. The CaBP family of EF-hand containing small Ca (2+)-binding proteins has lately emerged as significant regulators of multiple targets essential to normal neuronal function in the mammalian central nervous system.

Recombinant Fatty Acid Binding Protein is a newly introduced plasma marker of acute myocardial infarction (AMI). The plasma kinetics of FABP (15kD) closely resemble those of myoglobin in that elevated plasma concentrations are found within 2 hours after AMI and return to normal generally within 18 to 24 hours. But the concentration of FABP in the skeletal muscle is 20 times lower than in cardiac tissue (for myoglobin the same content for cardiac and skeletal tissue), that makes FABP to be more cardiac specific than myoglobin. This makes FABP a useful biochemical marker for the early assessment or exclusion of AMI. FABP also appears to be a useful plasma marker for the estimation of myocardial infarct size.

CRCP is a ubiquitous coupling protein for the calcitonin gene-related peptide and adrenomedullin receptors. CRCP controls ligand sensitivity in several tissues and has DNA-directed RNA polymerase activity, catalytic activity and calcitonin receptor activity.

RDH12 is a member of the short-chain Dehydrogenases / Reductases (SDR) family. RDH12 is found generally in brain, stomach, eye, skeletal muscle and kidney. RDH12 is a NADPH-dependent retinal reductase whose main activity is toward 9-cis and all-trans-retinol. In addition, RDH12 takes part in the metabolism of short-chain aldehydes but does not display steroid dehydrogenase activity.