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Mouse CXCL16 is a nonELR motif including CXC chemokine with a transmembrane domain. Mouse CXCL16 cDNA encodes a 246 a.a. precursor protein with a putative 26 a.a. residue signal peptide, an 88 a.a. residue chemokine domain, an 87 a.a. residue mucinlike spacer region, a 22 a.a. residue transmembrane domain, and a 23 a.a. residue cytoplasmic tail.
CXCL16 induces a strong chemotactic response and calcium mobilization. Furthermore, CXCL16 acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis.
Mouse CXCL16 is generated by dendritic cells in lymphoid organ T cell zones as well as by cells in the splenic red pulp both as membranebound and soluble forms. CXCR6/Bonzo (STRL33 and TYMSTR) is the receptor for CXCL16. CXCL16 is expressed in the spleen, lymph nodes, and Peyer patches. It is also expressed in non-lymphoid tissues such as lung, kidney, small intestine, and thymus, with weak expression in heart and liver and no expression in brain and purified B- and T-cells.
CXCL16 deficiency is linked to breast cancer progression. In addition, CXCL16 is involved in immunological liver injury by regulating T lymphocyte infiltration in liver tissue. Furtheremore, CXCL16 has a distinctive role in the maintenance of cardiac allograft tolerance mediated by natural killer T cells. Moreover, CXCL16 has a significant role in not only the production of IFN-gamma by NKT cells, but also promotion of Th1-inclined immune responses mediated by NKT cells.

Cyclophilin-E is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. Cyclophilin-E contains a highly conserved cyclophilin domain in addition to a RNA-binding domain. Cyclophilin-E exhibits PPIase activity, protein folding activities and possess RNA-binding activity. Cyclophilin-E contains 2 RNA binding domains at the N-terminal region and a PPIase domain at the C-terminal region.

DCN1-like protein 2 (DCUN1D2) which contains one DCUN1 domain and 1 UBA-like domain, may have a role in the neddylation of cullins which regulate SCF-type ubiquitin ligase complexes. The gene encoding Dcun1D2 is located on human chromosome 13. Chromosome 13 contains major tumor suppressor genes, including BRCA2 and RB1, which are linked with breast cancer susceptibility and retinoblastoma, respectively.

Nucleosome Assembly Protein 1-Like 4 (NAP1L4) is a part of the nucleosome assembly protein (NAP) family which interacts with both core and linker histones. NAP1L4 plays a role as a histone chaperone due to his ability to shuttle between the cytoplasm and nucleus. NAP1L4 modulates transcriptional activation by target nuclear receptors. NAP1L4 is one of several located near the imprinted gene domain of 11p15.5 which is an important tumor-suppressor gene region.

DNTTIP1 binds DNA and increases the activity of terminal deoxynucleotidyltransferase (TDT or DNTT), a DNA polymerase which catalyzes the polymerization of DNA in the absence of a DNA template.

DPPA4 takes part in the conservation of active epigenetic status of target genes and prevents differentiation of embryonic cells into a primal ectoderm extraction.

SKP1 is a F-box enzyme which functions as a substrate recognition component of the SCF ubiquitin ligase complex which controls the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. SKP1 binds to proteins containing an F-box motif, such as cyclin F, S-phase kinase-associated protein 2, and other regulatory proteins involved in ubiquitin dependent proteolysis. SKP1 takes part in the control of beta-catenin levels and the activity of beta-catenin dependent TCF transcription factors. SKP1 serves as an adapter that links the F-box protein to CUL1 in the SCF complex.

ADP-ribosylation factor-like protein 5B (ARL5B) is a member of a family of proteins which are structurally similar to ADP-ribosylation factors. ARLs and ARFs belong to the RAS superfamily of regulatory GTPases. ARL5B is most closely related to ARL5, with which it shares 80% sequence identity. Furthermore, Human ARL5B shares 100% identity with mouse ARL8 and 71% identity with the Drosophila homolog.

a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

NME4 is a member of the NDK family. NME4 are ubiquitous enzymes which catalyze transfer of gamma-phosphates, using a phosphohistidine intermediate, between nucleoside and dioxynucleoside tri- and diphosphates. The enzymes are products of the nm23 gene family that include NME4. NME4 has a key part in the synthesis of nucleoside triphosphates other than ATP.

BAIAP2 is a ubiquitous regulator of the actin cytoskeleton. Controled by the Rho-family GTPases BAIAP2 facilitates filopodia development. BAIAP2 is expressed in the cytoplasm and binds small membrane-bound G-proteins to cytoplasmic effector proteins. BAIAP2 was identified as interacting with the dentatorubral-pallidoluysian atrophy gene, which is related to an autosomal dominant neurodegenerative disease.

NRTN belongs to the GDNF family of ligands, a distant member of the TGF-beta superfamily. NRTN, a ligand used to bind to GFRA2 receptors, signals through RET and a GPI-linked coreceptor, and promotes endurance of neuronal populations, controls the size of non-neuronal cell population such as haemopoietic cells and regulate the development and maintenance of the CNS. Mutation in NRTN results in Hirschsprung Disease.

NTAL participates in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. NTAL takes part in BCR (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these receptors and their associated kinases with distal intracellular events through the recruitment of GRB2.

TBCEL, is a factor that is in charge of the microtubule cytoskeleton in determining cell behavior. TBCEL plays a role as a regulator of tubulin stability. While widely expressed in testis, TBCEL is also present in several tissues at a much lower level. TBCEL comprises of seven LRR (leucine-rich) repeats, one LRRCT domain and one ubiquitin-like domain. The gene that translates TBCEL consists of 66,704 bases and maps to human chromosome 11q23.3. Chromosome 11 houses over 1,400 genes and consist of nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that map to chromosome 11.

Filamin is a large (270kd) dimeric actin crosslinking protein from a variety of sources, which helps to stabilize the 3D cortical actin network. The fundamental structure of filamin is well conserved and consists of an actin binding domain at the N-terminus followed by a C-terminal rod domain consisting of numerous repeat segments ranging from 4 in C. elegans to 24 in mammalian cells. Each repeat in the rod domain consists of roughly 100 residues and forms an immunoglobulin like fold. Such immunoglobulin folds have been found in a variety of proteins and are responsible for protein-protein interactions. Filamin Human actin-binding protein (ABP), aka filamin, crosslinks actin filaments into orthogonal networks in cortical cytoplasm and participates in the anchoring of membrane proteins for the actin cytoskeleton. Mammalian filamin interacts directly with at least 30 proteins such as transmembrane receptors, second messenger-associated proteins, protein kinases, phosphatases and cytoskeletal proteins and these interactions have been shown to require one or more of the repeat elements in the rod domain.

Thrombospondin-1 (TSP1) is a member of the Thrombospondin family and is encoded by the gene THBS1 which is a subunit of a disulfide-linked homotrimeric protein. Thrombospondin-1 is an adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Thrombospondin-1 can bind to fibrinogen, fibronectin, laminin, type V collagen and integrins alpha-V/beta-1. TSP1 has been shown to play roles in platelet aggregation, angiogenesis, and tumorigenesis. TSP1 has been shown to be a natural inhibitor of neovascularization and tumorigenesis in healthy tissue. TSP1 interacts with no less than 12 cell adhesion receptors, including CD36, av integrins, b1 integrins, syndecan, and integrin-associated protein (IAP or CD47). It also interacts with various proteases involved in angiogenesis, including plasminogen, matrix metalloproteinase, thrombin, cathepsin, and elastase. Positive and negative modulation of endothelial cell adhesion, motility, and growth are attributed to TSP1. Recently, thrombospondin-1 was found to bind to the reelin receptors, ApoER2 and VLDLR, in so doing affecting neuronal migration in the rostral migratory stream.

TIMP2 belongs to the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases that take part in degradation of the extracellular matrix. Besides having an inhibitory role against metalloproteinases, the encoded protein has a exclusive part among TIMP family members in its capability to directly suppress the proliferation of endothelial cells. Consequently, the encoded protein is crucial to the conservation of tissue homeostasis by suppressing the production of quiescent tissues as an answer to angiogenic factors, and by inhibiting protease activity in tissues undergoing renovation of the extracellular matrix.

KRAS is part of the small GTPase superfamily. A single amino acid substitution is accountable for an activating mutation. KRAS participates in various malignancies, including lung adenocarcinoma, mucinous adenoma, ductal carcinoma of the pancreas and colorectal carcinoma.

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.

TPT1 takes part in calcium binding and microtubule stabilization. TPT1 is an immunoglobulin E dependent histamine-releasing factor produced by lymphocytes of atopic children and present in biologic fluids of allergic patients. TPT1 protein is similar to p23, a protein of Ehrlich ascites tumor cells, synthesized in the exponentially growing tumor. TPT1 is similar with IgE-dependent histamine releasing factor. TPT1 has a cell housekeeping function. TPT1 is involved in spermatogenesis and acts as a calcium binding protein of the human placenta that regulates calcium handling in trophoblast cells.

Latexin enzyme is a carboxypeptidase A inhibitor that is highly expressed in the heart, prostate, ovary, kidney, pancrease, brain and colon. Latexin has no noticeable sequence resemblance with plant and parasite inhibitors, however it is related to a human putative tumor suppressor protein, TIG1. Latexin is down-regulated in the presenilin-1-deficient mouse brain, thus putatively playing a role in Alzheimer's disease.

PPP1R1A is an inhibitor of protein-phosphatase 1. IPP-1 protein plays important in hormonal control of glycogen metabolism. Hormones that elevate intracellular cAMP elevate IPP-1 activity. PPP1R1A activation caused cAMP to control over proteins that are not directly phosphorylated by PKA following a rise in intracellular calcium, IPP-1 is inactivated by calcineurin (PP2B). Multiple domains in IPP-1 target cellular PP1 complexes. PPP1R1A is a cellular regulator of eIF2 alpha phosphorylation.

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.

Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.