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PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.

Anaphase-promoting complex subunit 13 (ANAPC13) is a component of the anaphase promoting complex, which is a large ubiquitin-protein ligase that controls cell cycle progression by regulating the degradation of cell cycle regulators such as B-type cyclins. The ANAPC13 protein is evolutionarily conserved and is essential for the integrity and ubiquitin ligase activity of the anaphase promoting complex.

Hydroxylysine Kinase, also known as HYKK, is a Protein Coding gene. HYKK which is a part of the aminoglycoside phosphotransferase family catalyzes the GTPdependent phosphorylation of 5-hydroxy-L-lysine.

AMRC10 is a protein which contains an armadillo repeat and transmembrane domain. Upregulation of the AMRC10 gene has a role in hepatocellular carcinoma. AMRC10 decreases the transcriptional activity of the tumor suppressor protein p53 through direct interaction with the DNA-binding domain of p53, moreover it might play a role in cell growth and survival.

AURKA (Aurora Kinase A) belongs to the mitotic serine/threonine kinases family. AURKA is a cell cycle-regulated kinase which may be involved in microtubule formation and/or stabilization at the spindle pole during chromosome segregation. AURKA is found at the centrosome in interphase cells and at the spindle poles in mitosis. Since the AURKA expression is cell-cycle regulated, it is low in G1/S, it accumulates during G2/M, and it decreases rapidly after. AURKA is involved in important processes during mitosis and meiosis whose proper function is essential for healthy cell proliferation. In addition, AURKA plays an essential role in tumourigenesis and is overexpressed in various types of cancers. AURKA is strongly expressed in the testis, colon, ovarian, prostate, neuroblastoma, breast and cervical cancer cell lines and weakly in skeletal muscle, thymus and spleen. AURKA interacts with its substrates BORA and ARHGEF2, as well as with TACC1 and CPEB1.
Defects in the AURKA gene cause numerical centrosome aberrations including aneuploidy. AURKA overexpression has been linked to chromosomal instability in colorectal cancer. AURKA expression may have a prognostic significance in ovarian carcinoma.

BAALC gene is found in patients with acute myeloid leukemia and is conserved among mammals and is not found in lower organisms. Tissues which express BAALC develop from the neuroectoderm. BAALC is located both in the membrane and in the cytoplasma, it exists as multiple alternatively spliced isoform. BAALC is expressed by hematopoetic and neural cells, BAALC interacts with CaMKII? and is involved in synaptic function at postsynaptic lipid rafts. Overexpression of BAALC concomitant forecast adverse clinical outcome and defines a significant risk factor in cytogenetically normal acute myeloid leukemia (AML).

Neurexophilin 1 (NXPH1) is a part of the neurexophilin family which encodes a secreted protein with a variable N terminal domain, an extremely conserved, N-glycosylated central domain, a short linker region, and a cysteine-rich Cterminal domain. NXPH1 shapes a very tight complex with alpha neurexins, a group of proteins which promote adhesion among dendrites and axons.

The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. This cytokine is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of this cytokine is reported to be related to asthma or hypereosinophilic syndromes. The receptor of this cytokine is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). This gene, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. This cytokine, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.

PEA15 (Phospho-enriched protein in astrocytes 15kDa) is a death effector domain (DED)-containing protein mainly expressed in the central nervous system, principally in astrocytes. PEA15 is implicated in the regulation of various cellular processes including apoptosis, proliferation, glucose transport, adhesion and migration. Increased PEA15 levels have an affect tumorigenesis and cancer progression, therefore it is overexpressed in breast cancers and gliomas as well as in type 2 diabetes. PEA15 blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. PEA15 also inhibits RPS6KA3 activities by holding it in the cytoplasm. In addition, PEA15 inhibits both TNFRSF6 and TNFRSF1A mediated CASP8 activity and apoptosis.
PEA15 is ubiquitously expressed. PEA15 is most abundant in tissues such as the heart, brain, muscle and adipose tissue which use glucose as an energy source. Lower PEA15 expression is in glucose-producing tissues. Higher levels of PEA15 expression are found in tissues from individuals with type 2 diabetes than in controls.
PEA15 expression is a significant prognostic marker in ovarian cancer.

POU5F1 is a homeodomain transcription factor of the POU family, expressed in embryonic stem (ES) cells and embryonic carcinoma (EC) cells.POU5F1 is significantly involved in the signaling pathway for maintaining self-renewal and pluripotency of ES cells. POU5F1 has 2 distinct DNA binding domains which independently bind half-sites of the canonical octamer motif. This flexibility allows POU5F1 to bind with distinct DNA motifs by forming heterodimers with other transcription factors or by forming homodimers in several conformations. Human POU5F1 contains a 75aa POU specific (POUS) domain and a 60aa POU-Homeo-(POUH) domain connected by a linker region. The Human POU5F1 specifically interacts with Octamer motif ATGCAAAT. In addition, 2 proline-rich domains in the N-terminal and C-terminal regions are vital for POU5F1 transactivation. POU5F1 regulates a number of target genes and has been shown to work jointly with other transcription factors including Sox2 as well as Nanog to sustain stem cell potency and self-renewal.

Galectins are a family of animal lectins with an affinity for beta-galactosides. This family has at least 14 identified members. Galectins share similarities in the CRD (the carbohydrate recognition domain). Galectins are synthesized as cytosolic proteins. Though localized principally in the cytoplasm and lacking a classical signal peptide, galectins can also be stimulated to secretion by non-classical pathways or alternatively targeted to the nucleus. Galectins are involved in modulating cell-cell and cell-matrix interactions. Galectin-8 is a tandem-repeat-type member of the galectin family, consisting of 2 CRDs attached by a linker peptide. Galectin-8 is greatly expressed in lung carcinomas, a number of forms of prostate carcinomas, in addition to other tumor cells. Galectin-8 attaches to a subset of cell surface integrins to modulate ECM-integrin interactions. Once immobilized, Galectin-8 promotes cell adhesion by ligation and clustering of cell surface integrin receptors. On the other hand, as a soluble ligand, Galectin-8 can inhibit cell adhesion.

Excess adiposity is the most important risk in the development of insulin resistance and type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-?, and IL-6, that modulate insulin sensitivity and appear to play an important role in the pathogenesis of insulin resistance, diabetes, dyslipidemia, inflammation, and atherosclerosis. However, the mechanisms by which fat tissue induces insulin resistance and the role of adipocytokines in the pathogenesis of T2DM have not been well established.
Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It has been postulated to play a role in innate immunity.
Visfatin exerts insulin-mimetic effects that are dose-dependent and quantitatively similar to those of insulin in stimulating muscle and adipocyte glucose transport, and in inhibiting hepatocyte glucose production. Intravenous injection of recombinant visfatin in mice decreased plasma glucose in a dose-dependent fashion. In keeping with its insulin-mimetic effects, visfatin was as effective as insulin in reducing hyperglycemia in insulin-deficient diabetic mice. Visfatin was also found to be bound to and activate insulin receptor, causing receptor phosphorylation and the activation of downstream signaling molecules. However, visfatin and insulin did not compete for binding to the insulin receptor, indicating that the two proteins were recognized by different regions of the receptor. Thus, visfatin might play a role in glucose homeostasis and dysregulation in biosynthesis or signal transduction, and might contribute to the pathogenesis of diabetes.

Vitronectin (VTN) which is a part of the pexin family is a cell adhesion and spreading factor found in serum and tissues. VTN interacts with glycosaminoglycans and proteoglycans. VTN inhibits the membrane-damaging effect of the terminal cytolytic complement pathway and binds to numerous serpin serine protease inhibitors. Scientists have been noticed an over expression of VTN, integrins and plasminogen in migrating cells during wound healing.

Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity. Steppan et al. have suggested that resistin suppresses the ability to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

Non-Metastatic Cells 2 or NME2, is a protein, that acts as a nucleoside diphosphate kinase. This protein is of a heterodimeric structure and has 152 aa A & B polypeptide chains that builds the whole protein. Erythrocyte NDP kinase beta subunit has an identical structure to NME2. NDP kinases linked to nucleoside triphosphates synthesis and it appears as though NME2 takes part in regulating signal transduction.

Cytohesin-interacting protein, also known as CYTIP contains 2 leucine zipper domains as well as a putative C-terminal nuclear targeting signal. However, CYTIP does not contain any hydrophobic regions. In addition, CYTIP is expressed weakly in resting NK and T cells. It also modulates the activation of ARF genes by CYTH1.

Vesicle-trafficking protein SEC22b precursor (SEC22B) is a member of the synaptobrevin family. SEC22B forms a complex with SNARE and it is believed to have a role in the ER-Golgi protein trafficking. SEC22B has a strong similarity to the mouse and Chinese hamster proteins.

SERPINA1 is secreted and is a serine protease inhibitor which its targets include elastase, plasmin, collagenase, thrombin, leucocytic proteases, trypsin, chymotrypsin, and plasminogen activator. Defects in SERPINA1 gene can cause emphysema or liver disease. Antral SERPINA1 expression is particularly induced by H. pylori infection. lung and prostate cancers have shown a significant increase in SERPINA1 serum levels compared with healthy controls though breast cancers did not show a significant change. SERPINA1 is an endogenous inhibitor of serine proteases and inhibits the catalytic domain of human recombinant matriptase in vitro. Rise in SERPINA1 occurs as an acute phase response to tissue necrosis and inflammation. mutations in SERPINA1 and SLC11A1 genes change the balance between elastase produced by leukocytes during phagocytosis.

SERPINH1 is part of the serpin superfamily of serine proteinase inhibitors. SEPINH1 expression is induced by heat shock. HSP47 localizes to the endoplasmic reticulum lumen and binds collagen therefore it is a molecular chaperone which takes part in the maturation of collagen molecules, facilitating the folding and assembly of procollagen molecules, retaining unfolded molecules within the ER, and assisting the transport of correctly folded-molecules from the ER to Golgi apparatus. Autoantibodies to HSP47 protein have been found in rheumatoid arthritis. SERPINH1 binds specifically to collagen and acts as a chaperone in the biosynthetic pathway of collagen.

NCK1 is an adapter protein which binds with tyrosine-phosphorylated growth factor receptors or their cellular substrates. NCK1 maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. NCK1 is involved in the DNA damage response, for efficient activation of downstream effectors, such as that of CHEK2. NCK1 is one of the signaling and transforming proteins containing Src homology 2 and 3 (SH2 and SH3) domains. NCK1 is located in the cytoplasm and is an adaptor protein that participates in transducing signals from receptor tyrosine kinases to downstream signal recipients such as RAS.

Dynein Axonemal Light Intermediate Chain1 also known as DNALI1 belongs to the inner dynein arm light chain family. DNALI1 take a dynamic role in flagellar motility. DNALI1 is the human homolog of the Chlamydomonas inner dynein arm gene, p28. The exactfunction of DNALI1 is not known yet, on the other hand, it is a potential candidate for immotile cilia syndrome. In addition it has been found that the following diseases: primary ciliary dyskinesia, and huntington's disease have been associated with DNALI1. Ultrastructural defects of the inner dynein arms are seen in patients with ICS. Immotile mutant strains ofChlamydomonas, biflagellated algae, show similar defects.

60S ribosome subunit biogenesis protein NIP7 homolog (NIP7) belongs to NIP7 family and contains 1 PUA domain. NIP7 interacts with pre-ribosome complex and may bind to RNA. NIP7 is vital for proper 27S pre-rRNA processing and 60S ribosome subunit assembly.

EEF1A1 is an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible forthe enzymatic release of aminoacyl tRNAs to the ribosome. EEF1A1 is expressed in brain, placenta, lung, liver, kidney, and pancreas, and the other isoform (alpha 2) is expressed in brain, heart and skeletal muscle. EEF1A1 is recognized as an autoantigen in 66% of patients with Felty syndrome. EEF1A1 has multiple copies on numerous chromosomes, part of them, if not all, symbolize different pseudogenes. Among the diseases associated with EEF1A1 are tinea nigra and andcervical cancer.