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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.

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.

Dyneins are multi-subunit, high molecular weight ATPases which cooperate with microtubules to create energy by altering the chemical energy of ATP into the mechanical energy of movement. DYNLL2 is a large protein complex made up of six different subunits and is in charge of a large number of intracellular movements to the minus ends of microtubules. DYNLL2 is an extremely conserved eukaryotic hub protein with dozens of binding partners and numerous roles other than being a subunit of dynein and myosin Va motor proteins.

V-maf Musculoaponeurotic Fibrosarcoma Oncogene F (MAFF) which is expressed in the term myometrium and kidney is a basic leucine zipper (bZIP) transcription factor which lacks a transactivation domain. MAFF is known to bind the US-2 DNA element and probably heterodimerizes along with other leucine zipper-containing proteins to enhance expression of the OTR gene throughout pregnancy period. MAFF also forms homodimers, and since it lacks a transactivation domain, the homodimer operates as a repressor of transcription.

Enfuvirtide also called human immunodeficiency fusion inhibitor blocks HIV’s ability to infect healthy CD4 cells. It can reduce the amount of HIV in the blood and increase the number of CD4 cells. Enfuvirtide operates by disrupting the HIV-1 molecular machinery at the final phase of fusion with the target cell, preventing uninfected cells from becoming infected. Enfuvirtide mimics components of the HIV-1 fusion apparatus and displace them, preventing normal fusion. HIV attaches to the host CD4+ cell receptor using the viral protein GP120; upon binding, GP120 deforms allowing the viral protein GP41 to insert itself into the host cell's plasma membrane. Entry inhibitors bind to GP41 preventing the formation of an entry pore for the capsid of the virus, keeping it out of the cell.

Human KIAA0513 is vastly expressed in the brain cortex, cerebellum, hippocampus, amygdala, pons and putamen. While the expression of KIAA0513 is high in neurons, KIAA0513 is also found in glial cells. In schizophrenic patients, higher levels are detected in the dorsolateral prefrontal cortex as compared to control patients.

Oncomodulin is a member of the superfamily of calmodulin proteins, otherwise known as the EF-hand proteins. It is a high-affinity calcium ion-binding protein. Oncomodulin is an oncodevelopmental protein which is found in early embryonic cells in the placenta and also in tumors.

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.

Mitochondrial Ribosome Recycling Factor (MRRF) is a member of the RRF family. MRRF attaches to the large ribosomal subunit in the cleft which has a peptidyl transferase center. MRRF controls the release of ribosome from messenger RNA at the termination of protein biosynthesis. Also, it may intensify the efficacy of translation by recycling ribosome from one round of translation to another.

SRP54 is a 54-kDa subunit of the signal recognition particle (SRP), a cytoplasmic ribonucleoprotein complex which leads the translocation of newly synthesized secretory proteins from the polysome to the endoplasmic reticulum. SRP is composed of six polypeptides and a tRNA-like molecule known as 7SL RNA. SRP54 is a GTP-binding protein that directly binds the signal sequences of nascent secretory and membrane proteins. Anti-SRP autoantibodies take place in patients with an autoimmune chronic muscle inflammation called polymyositis. These auto-antibodies predominantly recognize the SRP54 subunit and in addition are able to immunoprecipitate several of the SRP subunits and the RNA component. Nearly 5% of myositis patients are positive for anti-SRP autoantibodies, increasing to 18% in the subgroup of Jo-1 autoantibody-negative patients. The classic 'anti-SRP syndrome' is a severe form of polymyositis in which the myositic inflammation is acute and aggressive onset, with common myalgias and cardiac involvement. Normally there is a poor reaction to therapy with a 5-year survival rate of about 25%.

C8, a component of the complement system consists of three polypeptides C8A, C8B and C8G and takes part in the formation of Membrane Attack Complex (MAC). Patients with C8 deficiency are exposed to several bacteria infections. C8G, a member of the lipocalin family and calycin superfamily, is a secreted protein that can bind retinol. C8G is created in the liver, monocytes and fibroblast and has a role in clearing pathogens from an infected host.

KH homology domain containing 1-like, also known as KHDC1L is a member of the KHDC1 family.KHDC1L is a protein-coding gene; an important paralog of this gene is KHDC1.

The protein kinase A holoenzyme is a heterotetramer composed of two types of subunits: Catalytic and Regulatory. The Catalyticsubunit contains the enzyme's active site. It also contains a domain that binds ATP and a domain that binds the regulatory subunit. The Regulatory subunit consists oftwo molecules which bind one another in an anti-parallel orientation to form a homodimer; for type I subunits- this binding is covalent via disulfide bonds. This subunit also has has two domains that bind cyclic AMP, a domain that interacts with a catalytic subunit, and an "auto-inhibitory" domain that serves as a substrate or pseudosubstrate for the catalytic subunit. Regulatory subunits may also have biologic activity distinct from their role in modulating catalytic subunit activity. Regulatory subunits exist in two major forms, RI and RII, with each form having two subtypes designated alpha and beta. Each of the four isotypes of the regulatory subunit is encoded by a different gene. In addition, three isotypes of the catalytic subunit have been identified (alpha, beta and gamma). The different isotypes tend to have different distributions within cells and among tissues. Type I enzymes inhabit cytoplasmic, soluble fractions of the cell, whereas type II enzymes tend to associate with cellular membranes.

Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake and stimulated by insulin.

Secreted frizzled-related protein 4 (SFRP4) belongs to the SFRP family which contains a cysteine-rich domain homologous to the putative Wnt-binding site of Frizzled proteins. SFRPs serve as soluble modulators of Wnt signaling. SFRP4 may serve as a regulator of adult uterine morphology and function. SFRP4 increases apoptosis during ovulation possibly via modulation of FZ1/FZ4/WNT4 signaling. SFRP4 also has phosphaturic effects by specifically inhibiting sodium-dependent phosphate uptake. SFRP4 is expressed in proliferative endometrium and several types of ovarian, endometrial and Brest tumors. SFRP4 is expressed in mesenchymal cells and in cardiomyocytes. SFRP4 expression in ventricular myocardium correlates with apoptosis related gene expression. SFRP4 is up-regulated in failing myocardium.

IGFBP5 is a member of the insulin-like growth factor binding protein (IGFBP) family and encodes a protein with an IGFBP domain and a thyroglobulin type-I domain. The protein forms a ternary complex with insulin-like growth factor acid-labile subunit (IGFALS) and either insulin-like growth factor (IGF) I or II. In this form, it circulates in the plasma, prolonging the half-life of IGFs and altering their interaction with cell surface receptors. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

IGF-2 is a member of the insulin family of polypeptide growth factors that is involved in development and growth. It is an imprinted gene and is expressed only from the paternally inherited allele. It is a candidate gene for eating disorders. There is a read-through, INS-IGF2, which aligns to this gene at the 3' region and to the upstream INS gene at the 5' region. Two alternatively spliced transcript variants encoding the same protein have been found for this gene.

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.

Dysbindin domain-containing protein 1 (DBNDD1) is a member of the dysbindin family.

Retinitis pigmentosa 9 (RP9) is assumed to be a target protein for the PIM1 kinase. The RP9 protein may have some roles in B-cell proliferation in association with PIM1. RP9 can be bound and phosphorylated by the protooncogene PIM1 product, a serine/threonine protein kinase. RP9 localizes in nuclear speckles containing the splicing factors, and has a part in pre-mRNA splicing. RP9 gene mutations result in autosomal dominant retinitis pigmentosa-9.

Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

Melanoma Antigen Family A 8, also known as MAGEA8 belongs to the MAGE gene family, which includes twelve known genes, of which six are expressed in tumors. Furthermore, the MAGE genes were at first isolated from different kinds of tumors, and according to their virtually exclusive tumor-specific expression in adult tissues, they have been used as targets for cancer immunotherapy.

Intrinsic Factor is a member of the cobalamin transport protein family. It encodes a glycoprotein secreted by parietal cells of the gastric mucosa and is required for adequate absorption of vitamin B12 in the terminal ileum. Vitamin B12 is essential for erythrocyte maturation and mutations in the Intrinsic Factor may lead to congenital pernicious anemia. Upon entry into the stomach, vitamin B12 binds to one of two B12 binding proteins present in the gastric fluid. In the less acidic environment of the small intestine, these proteins dissociate from the vitamin, allowing it to bind to intrinsic factor and enter the portal circulation through a receptor in the ileal mucosa specific for the B12-intrinsic factor complex.

ARF4 belongs to the ARF gene family whose members encode 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. The ARF proteins include five ARF proteins and eleven ARF-like proteins and constitute one family of the RAS superfamily. They are classified as class I, class II and class III; the ARF4 gene is a class II member. The members of each class share a common gene organization. The ARF4 gene spans approximately 12kb and contains 6 exons and 5 introns. The ARF4 gene is the most divergent member of the human ARFs.