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S100B faintly binds calcium but binds zinc extremely strongly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. S100B binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction participates in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling.

SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

Dihydrofolate reductase (DHFR) is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, with NADPH as electron donor that can be converted to the kinds of tetrahydrofolate cofactors applied in 1-carbon transfer chemistry. DHFR converts dihydrofolate into tetrahydrofolate, which is a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and specific amino acids. Even though the functional DHFR gene is mapped to chromosome 5, numerous intronless processed pseudogenes or dihydrofolate reductase-like genes are identified on separate chromosomes.
DHFR deficiency is associated with megaloblastic anemia.
DHFR knockdown plays a role in the anticancer activity of 2-hydroxyoleic acid.
DHFR gene insertion/deletion polymorphism is linked to variation in serum and red blood cell folate concentrations in women.

ANXA3 is an inhibitor of phospholipase A2. ANXA3 possesses anti-coagulant properties. ANXA3 cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate. ANXA3 is part of the annexin family which are members of the calcium-dependent phospholipid-binding protein family that are involved in the regulation of cellular growth and in signal transduction pathways. ANXA3 takes part as an anti-coagulation factor.

DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development.

ANXA8 is part of the annexin family of evolutionarily conserved Ca2+ and phospholipid binding proteins. ANXA8 is an anticoagulant protein that functions as an indirect inhibitor of the thromboplastin-specific complex, which takes part in the blood coagulation cascade. Where co-expressed in the same tissues, ANXA8 is expressed at a 100-fold lower level than Annexin A5. Though, ANXA8 is preferentially expressed in acute promyelocytic leukemia (APL) cells which suggests its involvement in hematopoietic cell differentiation.

Dynein Axonemal Light Chain 1 (DNAL1) functions as a component of the outer dynein arms complex. DNAL1 acts as the molecular motor which supplies the force to move cilia in an ATP-dependent manner. DNAL1 is expressed in tissues with motile cilia or flagella and takes part in the movement of sperm flagella. Alternate splicing results in numerous transcript variants.

ADP-ribosylation factor 3 (ARF3) belongs to the human ARF gene family. This family encodes small guanine nucleotide-binding proteins which stimulate the ADP-ribosyltransferase activity of cholera toxin and have a role in vesicular trafficking and as activators of phospholipase D. ARF3 functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. ARF3 is involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. The ARF3 gene is comprised of 5 exons and 4 introns.

Diphthamide Biosynthesis 3 Pseudogene 1 also known as DPH3P1 may stand for a processed pseudogene of DPH3 since it lacks the exon/intron structurefound in the functional gene. Yet, DPH3P1 does contain an intact open reading frame, though its translation has not been established.

ARL11 (ADP-ribosylation factor-like protein 11) belongs to the ARF family of the Ras superfamily of small GTPases which are known to be involved in multiple regulatory pathways altered in human carcinogenesis. ARFs are highly conserved guanine nucleotide binding proteins which enhance the ADP-ribosyltransferase activity of choleratoxin. ARFs are important in eukaryotic vesicular trafficking pathways and they have a vital role in the activation of phospholipase D (PC-PLD). ARL11 is assumed to act as a tumor suppressor which may have a role in the regulation of apoptosis.

ADP-ribosylation factor-like 14 (ARL14) is a developmentally regulated member of the ADP-ribosylation factor/ARF-like protein (ARF/ARL) family of Ras-related GTPases. ARL14 is GTPase which recruits MYO1E to MHC class II-containing vesicles via the effector protein C11orf46/ARF7EP and thus controls the movement of these vesicles along the actin cytoskeleton in dendritic cells. MHC-II transport was controlled by the GTPase ARL14/ARF7, which recruits the motor myosin 1E via an effector protein ARF7EP.

NUDT10 belongs to the Nudix hydrolase family of pyrophosphatases. Nudix hydrolases contain a characteristic Nudix domain and are responsible for catalyzing the hydrolysis of nucleoside diphosphate derivatives. NUDT10 functions as a manganese-dependent polyphosphate phosphohydrolase with an optimum pH of 8.5. NUDT10 protein specifically metabolizes diadendosine-polyphosphates and, to a lesser extent, diphosphoinositol polyphosphates.

BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

BEN domain-containing protein 6 (BEND6) is a neural BEN-solo factor which shares many functional attributes with Drosophila Insensitive, a co-repressor for the Drosophila CSL factor. The BEND6 protein binds the mammalian CSL protein CBF1 and antagonizes Notch-dependent target activation. Furthermore, its association with Notch- and CBF1-regulated enhancers is stimulated by CBF1 and antagonized by activated Notch. In utero electroporation experiments demonstrated that ectopic BEND6 impeded Notch-mediated self-renewal of neocortical neural stem cells and promoted neurogenesis.

Cyclin-dependent kinase inhibitors (CDKIs) are proteins that bind to and inhibit the activity of CDKs. Two major classes of CDK inhibitors have been identified. The p16 family (p15, p16, p18 and p19) binds to and inhibits the activities of CDK4 and CDK6. The p21 family (p21, p27, p28 and p57) can bind to broad range of CDK-cyclin complexes and inhibit their activities. CDKIs are capable of suppressing growth, and several lines of evidence strongly suggest that at least some CDKIs may be tumor suppressor proteins.

PCBD1 enzyme takes part in phenylalanine hydroxylation. PCBD1 deficiency results in hyperphenylalaninemia. PCBD1 enzyme controls the homodimerization of HNF1. PCBD1 takes part in tetrahydrobiopterin biosynthesis. PCBD1 prevents the formation of 7-pterins and accelerate the formation of quinonoid-BH2. PCBD1 is a coactivator for HNF1A-dependent transcription.

Calcium-binding protein 39-like (CAB39L), is analogous to MO25 and located in the serum of virtually half of all patients diagnosed with acute monocytic leukemia. CAB39L plays a role in carcinogenesis. Furthermore, LKB1 activity raises upon the binding of a regulatory complex consisting of the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase and the CAB39L.

Peroxisomal Biogenesis Factor 26 (PEX26) which is a part of the peroxin-26 gene family is probably required for protein import into peroxisomes. PEX26 attaches PEX1 and PEX6 to peroxisome membranes to form heteromeric AAA ATPase complexes needed for the import of proteins into peroxisomes. Deficiencies in this gene are the cause of peroxisome biogenesis disorder complementation group 8. PBD is a group of peroxisomal disorders evolving from a failure of protein import into the peroxisomal membrane or matrix.

Transferrin receptor protein 1 (TFRC) is required for iron delivery from transferring to cells. The TFRC protein is a transmembrane glycoprotein comprised of 2 disulfide-linked monomers joined by 2 disulfide bonds. Each monomer will bind one holo-transferrin molecule producing an iron-Tf-TfR complex which enters the cell by endocytosis.

Furin is a member of the peptidase S8 family. Furin signifies the ubiquitous endoprotease activity within constitutive secretory pathwaysas well as capable of cleavage at the RX (K/R) R consensus motif.Furin is considered to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 as well as gp140 and might take part in tumor progression. Among the diseases associated with FURIN are dementia, familial british and plague.

Adiponectin (247amino acids) is adipocyte complement-related protein of 30 kDa and exclusively expressed in differentiated adipocytes. APM-1 (Acrp30 Mouse) is a member of the complement factor C1q family and consists of signal sequence, Non-homologous sequence, collagen domain and domain (gAcrp30).
Adiponectin expression is reduced in a variety of obese and insulin-resistant states in human, monkeys and mice. Injection of Acrp30 Mouse (247aa) or gAcrp30 (globular domain) lowers serum glucose and free fatty acid level in mice.

Tubby-related protein 1 (TULP1) belongs to the TULP family of 4 proteins (TUB and TULP1, -2, and -3), categorized structurally by the highly conserved C-terminal half of the protein. Tubby-like gene family (TULPs) members are found in plants, vertebrates, and invertebrates and encode proteins of unknown function. TULP proteins share a conserved C-terminal region of roughly 200 amino acid residues. In the retina, TULP1 is observed exclusively in the photoreceptor cells, localizing predominantly in the inner segments and connecting cilium and to a lesser degree in the perinuclear cytoplasm and synaptic termini. TULP1 gene mutations are linked with retinitis pigmentosa.

Geminin is a 25 kDa nuclear protein, which inhibits DNA replication and is degraded during the mitotic phase of the cell cycle. Geminin controls replication by binding to the licensing factor Cdt1, and is involved in neural differentiation. In addition, Geminin directly interacts with Six3 and Hox homeodomain proteins during embryogenesis and inhibits their functions. Geminin can also promote DNA replication. Geminin has 2 roles in 2 different stages of the cell cycle: Geminin is a negative regulator of DNA replication during the “S phase” of the cell cycle. Inhibition of Geminin during the “S phase” (by RNAi) results in an additional round of replication of portions of the genome. During the “M phase” of the cell cycle (mitosis) Geminin stabilizes the replication factor Cdt1 promoting DNA replication during the next cell cycle. Moreover, inhibition of Geminin during mitosis (by RNAi) causes destabilization of Cdt1 protein and impairment of DNA replication during the next cell cycle. Geminin thus guarantees that only one round of replication occurs during each cell cycle. It was discovered that Geminin is overexpressed in a number of malignancies and cancer cell lines. This maintains the concept that Geminin has also a positive role in DNA replication and cell cycle progression. Geminin accumulates through S, G2 and M phases of the cell cycle but is absent during the G1 phase. During the metaphase/anaphase transition of mitosis Geminin levels decrease.