n-terminal

Dickkopf-1 (Dkk1), the founding and best-studied member of the Dkk family, functions as an antagonist of canonical Wnt/β-catenin. Dkk1 is considered to play a broad role in a variety of biological processes. DKK1 N terminal Domain Protein, Human, Recombinant (hFc & Avi) is expressed in HEK293 mammalian cells with C-hFc-Avi tag. The predicted molecular weight is 40.25 kDa and the accession number is O94907.

Dickkopf-1 (Dkk1), the founding and best-studied member of the Dkk family, functions as an antagonist of canonical Wnt/β-catenin. Dkk1 is considered to play a broad role in a variety of biological processes. DKK1 N terminal Domain Protein, Human, Recombinant (hFc & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-hFc-Avi tag. The predicted molecular weight is 40.25 kDa and the accession number is O94907.

Human protein N-terminal glutamine amidohydrolase (WDYHV1) is an enzyme that in humans is encoded by the WDYHV1 gene, belongs to the NTAQ1 family.WDYHV1 mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, which is an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. However,it does not act on substrates with internal or C-terminal glutamine andnon-glutamine residues in any position. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine.

May accelerate cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis. May orchestrate hematopoietic stem and progenitor cell emergence from the hemogenic endothelium, a type of specialized endothelium manifesting hematopoietic potential. YJEFN3-mediated cholesterol efflux activates endothelial SREBF2, the master transcription factor for cholesterol biosynthesis, which in turn transactivates NOTCH and promotes hematopoietic stem and progenitor cell emergence. May play a role in spermiogenesis and oogenesis.

METTL11A Protein, Human, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 25.5 kDa and the accession number is A0A024R8E4.

NOTCH2NLB Protein, Human, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 31.3 kDa and the accession number is P0DPK3.

NOTCH2NLB Protein, Human, Recombinant (E. coli, His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 34.9 kDa and the accession number is P0DPK3.

Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes (in vitro). Binds calcium ions. PITPNM3 Protein, Human, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 30.8 kDa and the accession number is Q9BZ71.

Scaffold protein for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic Functions as a cytoplasmic scaffold protein for the de novo synthesis of iron-sulfur clusters in the cytoplasm.

METTL11A Protein, Human, Recombinant (GST) is expressed in E. coli expression system with GST tag. The predicted molecular weight is 52.2 kDa and the accession number is A0A024R8E4.

NOTCH2NLA (Notch 2 N-Terminal Like A) is a Protein Coding gene. NOTCH2NL, human-specific paralogs of the NOTCH2 receptor, stood out for their ability to promote cortical progenitor maintenance. It belongs to the NOTCH family. NOTCH2NL promote the clonal expansion of human cortical progenitors, ultimately leading to higher neuronal output. At the molecular level, NOTCH2NL function by activating the Notch pathway through inhibition of cis Delta/Notch interactions. NOTCH2NL ectopic expression delays differentiation of neuronal progenitors, while deletion accelerates differentiation into cortical neurons. The emergence of human-specific NOTCH2NL genes may have contributed to the rapid evolution of the larger human neocortex, accompanied by loss of genomic stability at the 1q21.1 locus and resulting recurrent neurodevelopmental disorders.

Extracellular Matrix Metalloproteinase Inducer (EMMPRIN) belongs to the immunoglobulin superfamily, which has the homology to both the immunoglobulin V domain and MHC class II antigen β-chain. EMMPRIN is a transmembrane glycoprotein with different forms, resulting from different modes of glycosylation and N-terminal sequence variants. EMMPRIN can be expressed in breast cancer, oral squamous cell carcinoma, glioma, lymphoma, lung, bladder, and melanoma carcinomas cells. EMMPRIN promotes invasion, metastasis, growth, and survival of malignants cells, serves as a receptor for extracellular cyclophilinthe, may play a role in signal transduction.

Insulin-Like Growth Factor-Binding Protein 5 (IGFBP-5) is a secreted protein that belongs to the insulin-like growth factor (IGF) binding proteins superfamily. Members of this family prolong the half-life of the IGFs. They have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. IGFBP-5 contains one IGFBP N-terminal domain and one thyroglobulin type-1 domain. IGFBP-5 is expressed by fibroblasts, myoblasts and Osteosarcoma. It is also present at lower levels in liver, kidney, and brain.

Angiopoietin-like 7 (ANGPTL7) is a secreted glycoprotein that is structurally related to the angiopoietins. Members of this protein family contain an N-terminal coiled coil domain and a C-terminal fibrinogen-like domain. ANGPTL7 shares 89% aa sequence identity with mouse and rat ANGPTL7. It is secreted as a 45-50kDa monomer that forms disulfide-linked homotrimers and tetramers via the coiled coil domain. ANGPTL7 is expressed in the corneal stroma, trabecular meshwork, and sclera and is elevated in glaucoma aqueous humor. Its production is up-regulated in trabecular meshwork cells by glucocorticoids and TGF-β and in cartilage by TNF-α. Overexpression of ANGPTL7 in trabecular meshwork cells inhibits the production of collagen and proteoglycans. When overexpressed in tumor cells it promotes collagen and proteoglycan deposition but inhibits tumor xenograft progression and tumor angiogenesis.

ACYP1, also known as Acylphosphatase-1, Acylphosphatase, erythrocyte isozyme, Acylphosphatase, organ-common type isozyme, Acylphosphate phosphohydrolase 1 and ACYPE, is a small cytosolic enzyme which catalyzes the hydrolysis of the carboxyl-phosphate bond of acylphosphates.ACYP1 is a protein which belongs to the acylphosphatase family and contains 1 fibrinogen C-terminal domain. Two isoenzymes have been isolated, called muscle acylphosphatase and erythrocyte acylphosphatase, on the basis of their tissue localization. This gene encodes the erythrocyte acylphosphatase isoenzyme. Alternatively spliced transcript variants that encode different proteins were identified through data analysis. Recombinant human ACYP1 protein was expressed in E. coli fused with HIS-tag at N-terminus.

L-Lactate Dehydrogenase A Chain (LDHA) is an enzyme that catalyzes the conversion of L-lactate and NAD+ to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA contains an N-terminal coenzyme binding region, a central catalytic site, and at least nine utilized Lys acetylation and two Tyr phosphorylation sites. LDHA belongs to the lactate dehydrogenase family, expressed predominantly in muscle tissue. LDHA mutations have been linked to exertional myoglobinuria.

Insulin-like growth factor I (IGF1) belongs to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mouse IGF-I is synthesized as two precursor isoforms with alternate N- and C-terminal propeptides. These isoforms are differentially expressed by various tissues. Mature mouse IGF-I shares 94% and 99% aa sequence identity with human and rat IGF-I, respectively, and exhibits cross-species activity. It shares 60% aa sequence identity with mature mouse IGF-II. IGF-I induces the proliferation, migration, and differentiation of a wide variety of cell types during development and postnatally. It plays an important role in muscle regeneration and tumor progression. IGF-I binds IGF-I R, IGF-II R, and the insulin receptor. IGF-I association with IGF binding proteins increases its plasma half-life and modulates its interactions with receptors.

Ezrin is expressed in cerebral cortex, basal ganglia, hippocampus, hypophysis, and optic nerve. The N-terminus of ezrin contains a FERM domain which is further subdivided into three subdomains. The C-terminus contain a ERM domain. As a member of the ERM protein family, Ezrin serves as an intermediate between the plasma membrane and the actin cytoskeleton. It plays a key role in cell surface structure adhesion, migration, and organization. Ezrin probably involved in connections of major cytoskeletal structures to the plasma membrane. The N-terminal FERM domain strongly binds sodium-hydrogen exchanger regulatory factor (NHERF) proteins (involving long-range allostery). The C-terminal binds to actin, phosphatidylinositol bis-phosphate (PIP2) and membrane proteins like CD44 and ICAM-2. In epithelial cells, Ezrin is required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, Ezrin is required for normal macropinocytosis.

Cryptic (CFC1) is a member of the epidermal growth factor (EGF)- Cripto, Frl-1, and Cryptic (CFC) family. It contains an EGF-like domain, and is glycosylated on its N-terminal during post-translational modification. Cryptic is identified as a NODAL coreceptor involved in the correct establishment of the left-right axis. It may play a role in mesoderm and/or neural patterning during gastrulation. The unnormal expression of this gene may causes a series of diseases such as HTX2, Transposition of the great arteries dextro-looped 2, and Conotruncal heart malformations.

Insulin-like growth factor-binding protein 7(IGFBP-7) is a secreted glycosylated protein that contains three protein domain modules. IGFBP7 contains an N-terminal IGFBP domain, followed by a Kazal-type serine proteinase inhibitor domain and a C-terminal immunoglobulin-like C2-type domain. Human and mouse IGFBP7 are highly homologous and share 94% aa sequence identity. It is expressed in many normal tissues and in cancer cells. It is abundantly expressed in high endothelial venules (HEVs) of blood vessels in the secondary lymphoid tissues. It binds IGF and insulin with very low affinity and has been shown to enhance the mitogenic actions of IGF and insulin. IGFBP7 also has IGF/insulin-independent activities. It interacts with heparan sulfate proteoglycans, type IV collagen, and specific chemokines. It supports weak cell adhesion, promotes cell spreading on type IV collagen, and stimulates the production of the potent vasodilator PGI2. It modulates tumor cell growth and has also been implicated in angiogenesis.

Coronin 6, a newly identified member of the coronin family, is highly enriched at adult NMJs and regulates AChR clustering via modulating the interaction between receptors and the actin cytoskeletal network. Coronins are a family of conserved actin-binding proteins originally identified in the actin-rich structure of the amoeba Dictyostelium discoideum . To date, seven members of coronins have been identified in mammals, and most exhibit tissue-specific distribution patterns. Coronin 6 is prominently expressed in adult muscle and enriched at the NMJ. Studies with cultured myotubes reveal that Coronin 6 regulates both agrin- and laminin-induced AChR clustering and is important for anchoring AChRs onto the actin cytoskeleton. Also, both the C-terminal region and a conserved Arg29 residue at the N terminus of Coronin 6 are essential for its actin-binding activity and stabilization of AChR–cytoskeleton linkage. Importantly, in vivo knockdown of Coronin 6 in mouse skeletal muscle fibers leads to destabilization of AChR clusters, which demonstrates that Coronin 6 is a critical regulator of AChR clustering at the postsynaptic region of the NMJs through modulating the receptor-anchored actin cytoskeleton. The human Coronin 6 has five isoforms produced by alternative splicing, and tissue-specific expression of these isoforms are unclear.

Lysine-tRNA ligase, also known as Lysyl-tRNA synthetase, LysRS, KARS and KIAA0070, belongs to the class-II aminoacyl-tRNA synthetase family. The N-terminal cytoplasmic domain (1-65) is a functional tRNA-binding domain, which is required for nuclear localization, is involved in the interaction with DARS, but has a repulsive role in the binding to EEF1A1. A central domain (208-259) is involved in homodimerization and is required for interaction with HIV-1 GAG and incorporation into virions. KARS catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Defects in KARS are the cause of Charcot-Marie-Tooth disease recessive intermediate type B (CMTRIB).

Cadherin-11 is a type II classical cadherin member of the cadherin superfamily of integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Cadherins interact with themselves in a homophilic manner in connecting cells, and thus contribute to the sorting of heterogeneous cell types. Cadherin-11 contains five cadherin domains and is mainly expressed in the brain. Mature cadherin proteins consists of a large N-terminal extracellular domain, a single membrane-spanning domain, and a small highly conserved C-terminal cytoplasmic domain. It is shown that Cadherin-11 is a viable molecular target for therapeutic intervention in Glioblastoma multiforme.

Macrophage galactose N-acetyl-galactosamine-specific lectin 2(Mgl2), also known as CD301b, is a 38 kDa member that belongs to the C-type lectin family. Two MGL proteins are encoded by separate genes in the mouse, but share 91% amino acid (aa) identity in the extracellular domain (ECD). Only one MGL occurs in human and rat and this MGL is structurally more similar to mouse MGL1 than MGL2. However, human MGL and mouse MGL2 both bind specifically to terminal GalNAc residues, in contrast with mouse MGL1 which binds Lewis X. GalNAc recognition is likely to be important in dendritic cell-mediated tolerance to self-gangliosides as well as recognition of tumor antigens and parasite glycoproteins.

Four distinct genes encoding closely related FGF receptors, FGF R1-4, are known. All four genes for FGF Rs encode proteins with an N-terminal signal peptide, three immunoglobulin (Ig)-like domains, an acid‑box region containing a run of acidic residues between the IgI and IgII domains, a transmembrane domain and the split tyrosine-kinase domain.FGFR3 is tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts..

Venom dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. May process promelittin into its active form and/or modulate the chemotactic activity of immune cells after the insect sting. Venom dipeptidyl peptidase 4 Protein, Apis mellifera, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 36.4 kDa and the accession number is B2D0J4.

Probably mediates the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. HDT2 Protein, Arabidopsis thaliana, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 34.3 kDa and the accession number is Q56WH4.

Isoform VP2 is a structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or Vp3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly.; structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or Vp3 nuclear localization signal (shared C-terminus). Isoform VP3 plays a role in virion assembly within the nucleus. May participate in host cell lysis when associated with VP4.; Isoform VP4 is a viroporin inducing perforation of cellular membranes to trigger virus progeny release. Forms pores of 3 nm inner diameter. VP4 is expressed about 24 hours after the late structural proteins and is not incorporated into the mature virion.

Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). PBP1b Protein, E. coli, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 38.6 kDa and the accession number is P02919.

Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions. Peptide deformylase Protein, E. coli, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 35.2 kDa and the accession number is P0A6K3.

This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser. APEH Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 85.2 kDa and the accession number is P13798.

Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation. EIF4G1 Protein, Human, Recombinant (B2M & His & JD & Myc) is expressed in E. coli expression system with N-10xHis-B2M-JD and C-Myc tag. The predicted molecular weight is 46.6 kDa and the accession number is Q04637.

Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production in the terminal step of glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels. G6PC Protein, Human, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 17.1 kDa and the accession number is P35575.

Mast cell-specific receptor for basic secretagogues, i.e. cationic amphiphilic drugs, as well as endo- or exogenous peptides, consisting of a basic head group and a hydrophobic core. Recognizes and binds small molecules containing a cyclized tetrahydroisoquinoline (THIQ), such as non-steroidal neuromuscular blocking drugs (NMBDs), including tubocurarine and atracurium. In response to these compounds, mediates pseudo-allergic reactions characterized by histamine release, inflammation and airway contraction. Acts as a receptor for a number of other ligands, including peptides and alkaloids, such as cortistatin-14, proadrenomedullin N-terminal peptides PAMP-12 and, at lower extent, PAMP-20, antibacterial protein LL-37, PMX-53 peptide, beta-defensins, and complanadine A.

Factor that induces terminal differentiation of late-developing B-cells to immunoglobulin secreting cells. IL-5 Protein, Pig, Recombinant (E. coli, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 17.0 kDa and the accession number is Q9MYM5.

Factor that induces terminal differentiation of late-developing B-cells to immunoglobulin secreting cells. IL-5 Protein, Pig, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 15.0 kDa and the accession number is Q9MYM5.

Frizzled-1, also known as FZD1, belongs to theG-protein coupled receptor Fz/Smo family. FZD1 contains a signal peptide, a cysteine-rich domain in the N-terminal extracellular region, 7 transmembrane domains, and a C-terminal PDZ domain-binding motif. FZD1 is expressed in adult heart, placenta, lung, kidney, pancreas, prostate, and ovary and in fetal lung and kidney. Frizzled is a family of G protein-coupled receptor proteins that serve as receptors in the Wnt signaling pathway and other signaling pathways. When activated, Frizzled leads to activation of Dishevelled in the cytosol. Frizzled proteins and the genes encoding them have been identified in an array of animals, from sponges to humans. Frizzled proteins play key roles in governing cell polarity, embryonic development, formation of neural synapses, cell proliferation, and many other processes in developing and adult organisms. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes.

Methionine aminopeptidase 1D, also known as MAP1D, is a member of the peptidase M24A family. N-terminal methionine removal is an important cellular process required for proper biological activity, subcellular localization, and eventual degradation of many proteins. The enzymes that catalyze this reaction are called Methionine aminopeptidases (MAPs). MAP1D is overexpressed in colon cancer cell lines and colon tumors as compared to normal tissues (at protein level). Downregulation of MAP1D expression by shRNA in HCT-116 colon carcinoma cells reduces anchorage-independent growth in soft agar. MAP1D binds two cobalt ions per subunit. The true nature of the physiological cofactor is under debate. MAP1D is also active with zinc, manganese, or divalent ions. MAP1D removes the amino-terminal methionine from nascent proteins. It may also play an important role in colon tumorigenesis.

Carbohydrate sulfotransferase 15, also known as N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase, GalNAc4S-6ST, B-cell RAG-associated gene protein, CHST15 and BRAG, is a single-pass type II membrane protein which belongs to thesulfotransferase 1 family. CHST15 / BRAG is expressed in B-cell-enriched tissues but not in fetal or adult thymus. It is expressed in fetal and adult spleen, lymph node, tonsil, bone marrow and peripheral leukocytes. It is not expressed in T-cells. In pro-B, pre-B, and mature B-cell lines, it colocalizes with RAG1. CHST15 / BRAG is a sulfotransferase that transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms chondroitin sulfate E containing GlcA-GalNAc(4,6-SO4) repeating units. It also transfers sulfate to a unique non-reducing terminal sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. CHST15 / BRAG may also act as a B-cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B-cell development and / or regulation of B-cell-specific RAG expression.

CNTNAP2/CASPR2 is a member of the neurexin family which functions in the vertebrate nervous system as cell adhesion molecules and receptors. This protein, like other neurexin proteins, contains epidermal growth factor repeats and laminin G domains. In addition, it includes an F5/8 type C domain, discoidin/neuropilin- and fibrinogen-like domains, thrombospondin N-terminal-like domains and a putative PDZ binding site. CNTNAP2/CASPR2 is localized at the juxtaparanodes of myelinated axons, and mediates interactions between neurons and glia during nervous system development and is also involved in localization of potassium channels within differentiating axons. This protein encoding gene is directly bound and regulated by forkhead box protein P2 (FOXP2), a transcription factor related to speech and language development. This gene has been implicated in multiple neurodevelopmental disorders, including Gilles de la Tourette syndrome, schizophrenia, epilepsy, autism, ADHD and mental retardation. CNTNAP2/CASPR2 may play a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibers. CNTNAP2/CASPR2 Seems to demarcate the juxtaparanodal region of the axo-glial junction.

Glutathione S-transferase Mu 2, also known as GST class-mu 2, GSTM2-2, and GSTM2, is a cytoplasm protein that belongs to the GST superfamily and Mu family. GSTM2 / GST4 contains one GST C-terminal domain and one GST N-terminal domain. The glutathione S-transferases (GSTs) are a multigene family of enzymes largely involved in the detoxification of chemicals. Eight distinct classes of the soluble cytoplasmic mammalian glutathione S-transferases have been identified: alpha, kappa, mu, omega, pi, sigma, theta, and zeta. Butyrate, an important luminal component produced from the fermentation of dietary fibers, is an efficient inducer of GSTs and especially of GSTM2. Butyrate may act chemoprotective by increasing detoxification capabilities in the colon mucosa.

LGALS3 (Galectin 3) is a Protein Coding gene. This gene encodes a member of the galectin family of carbohydrate-binding proteins. The encoded protein is characterized by an N-terminal proline-rich tandem repeat domain and a single C-terminal carbohydrate recognition domain. LGALS3 is a beta-galactoside-binding lectin and plays a role in numerous cellular functions including apoptosis, innate immunity, cell adhesion, and T-cell regulation. LGALS3 has an important role in tumor progression through inhibition of apoptosis. LGALS3 expression is associated with neoplastic transformation and with differentiation of monocytes to macrophages. Elevated expression of LGALS3 has been demonstrated in the synovium of rheumatoid arthritis (RA). Diseases associated with LGALS3 include Follicular Adenoma and Papillary Carcinoma.

Izumo is a sperm membrane protein that plays a key role in the fusion in the mouse. It has an Immunoglobulin (Ig) domain and an N-terminal domain for which neither the functions nor homologous sequences are known. Up to now, there four members has an N-terminal domain with significant homology to the N-terminal domain of Izumo. We call this domain the Izumo domain. The four proteins are Izumo 1, 2, 3, and 4. Izumo domain possesses the ability to form dimers, whereas the transmembrane domain or the cytoplasmic domain, or both of Izumo 1 are required for the formation of multimers of a higher order. Izumo 1-3 are transmembrane proteins expressed specifically in the testis, and Izumo 4 is a soluble protein expressed in the testis and other tissues. Izumo 1, 3, and 4 formed protein complexes on sperm, Izumo 1 forming several larger complexes, and Izumo 3 and 4 forming a single larger complex. Izumo1 is essential for sperm-egg plasma membrane binding and fusion.

Calumenin belongs to the CREC family. It contains 6 EF-hand domains. Calumenin is expressed in skeletal muscle (at protein level). Calumenin interacts with GGCX and RYR1 in the presence of calcium ions, but not in the presence of EDTA. Calumenin is Involved in regulation of vitamin K-dependent carboxylation of multiple N-terminal glutamate residues. It seems to inhibit gamma-carboxylase GGCX. Calumenin also binds 7 calcium ions with a low affinity and may modulate calcium release from the sarcoplasmic reticulum.

Mitogen-activated protein kinase 9 (MAPK9), also well known as c-Jun N-terminal kinase (JNK2), is a member of the MAP kinase subfamily belonging to the protein kinase superfamily. MAPK9 responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating some transcription factors, such as c-Jun and ATF2. The crystal structure of human JNK2 complexed with an indazole inhibitor by applying a high-throughput protein engineering and surface-site mutagenesis approach. A novel conformation of the activation loop is observed, which is not compatible with its phosphorylation by upstream kinases. This activation inhibitory conformation of JNK2 is stabilized by the MAP kinase insert that interacts with the activation loop in an induced-fit manner. It suggests that the MAP kinase insert of JNK2 plays a role in the regulation of JNK2 activation, possibly by interacting with intracellular binding partners. JNK2 deficiency leads to reduced c-Jun degradation, thereby augmenting c-Jun levels and cellular proliferation, and suggests that JNK2 is a negative regulator of cellular proliferation in multiple cell types. JNK2 prevents replicative stress by coordinating cell cycle progression and DNA damage repair mechanisms. JNK2 blocks the ubiquitination of tumor suppressor p53, and thus increases the stability of p53 in nonstressed cells. JNK2 negatively regulates antigen-specific CD8+ T cell expansion and effector function, and thus selectively blocking JNK2 in CD8+ T cells may potentially enhance the anti-tumor immune response. Lack of JNK2 expression was associated with higher tumor aneuploidy and reduced DNA damage response. Additionally, the JNK2 protein could be a novel therapeutic target in dry eye disease and may provide a novel target for the prevention of vascular disease and atherosclerosis.

ACK1 (also known as ACK, TNK2, or activated Cdc42 kinase) is a structurally unique non-receptor tyrosine kinase that is expressed in diverse cell types. This downstream effector of CDC42 mediates CDC42-dependent cell migration via phosphorylation of BCAR1. The ACK1 protein may be involved in a regulatory mechanism that sustains the GTP-bound active form of Cdc42Hs and which is directly linked to a tyrosine phosphorylation signal transduction pathway. ACK1 integrates signals from plethora of ligand-activated receptor tyrosine kinases (RTKs), for example, MERTK, EGFR, HER2 and PDGFR to initiate intracellular signaling cascades. It binds to both poly- and mono-ubiquitin and regulates ligand-induced degradation of EGFR. ACK1 transduces extracellular signals to cytosolic and nuclear effectors such as the protein kinase AKT/PKB and androgen receptor (AR), to promote cell survival and growth. ACK1 participates in tumorigenesis, cell survival, and migration. Gene amplification and overexpression of ACK1 were found in many cancer types such as those of the lung and prostate. Recently, four somatic missense mutations of ACK1, which occur in the N-terminal region, the C-lobe of the kinase domain, and the SH3 domain, were identified in cancer tissue samples.

NCKIPSD is localized exclusively in the cell nucleus. It plays a role in signal transduction and may function in the maintenance of sarcomeres and the assembly of myofibrils into sarcomeres. NCKIPSD also plays an important role in stress fiber formation. NCKIPSD gene is involved in therapy-related leukemia by a chromosomal translocation t(3;11)(p21;q23) that involves this gene and the myeloid/lymphoid leukemia gene. Alternative splicing occurs in this locus and two transcript variants encoding distinct isoforms have been identified. NCKIPSD is an SH3 domain protein. Fas ligand is a cytotoxic effector molecule of T and NK cells which is characterized by an intracellular N-terminal polyproline region that serves as a docking site for SH3 and WW domain proteins. Several previously described Fas ligand-interacting SH3 domain proteins turned out to be crucial for the regulation of storage, expression, and function of the death factor. Recent observations, however, indicate that Fas ligand is also subject to posttranslational modifications including shedding and intramembrane proteolysis.

FOP( fibroblast growth factor receptor 1 oncogene partner) is a largely hydrophilic protein postulated to be a leucine-rich protein family member. FOP contains 1 LisH domain. A t(6;8)(q27;p11) chromosomal translocation, fusing FOP gene and the fibroblast growth factor receptor 1 (FGFR1) gene, has been found in cases of myeloproliferative disorder. The resulting chimeric protein contains the N-terminal leucine-rich region of this encoded protein fused to the catalytic domain of FGFR1. FOP gene is thought to play an important role in normal proliferation and differentiation of the erythroid lineage. Alternatively spliced transcript variants that encode different proteins have been identified.

CKB(Creatine kinase B type) contains 1 phosphagen kinase C-terminal domain and 1 phosphagen kinase N-terminal domain. It belongs to the ATP:guanido phosphotransferase family. CKB consists of a homodimer of two identical brain-type CK-B subunits. CKB is a cytoplasmic enzyme involved in cellular energy homeostasis, with certain fractions of the enzyme being bound to cell membranes, ATPases, and a variety of ATP-requiring enzymes in the cell. There, CKB forms tightly coupled microcompartments for in situ regeneration of ATP that has been used up. CKB reversibly catalyzes the transfer of energy-rich phosphate between ATP and creatine or between phospho-creatine (PCr) and ADP. Its functional entity is a homodimer in brain, smooth muscle as well as in other tissues and cells such as neuronal cells, retina, kidney, bone etc.

Cell surface glycoprotein CD200 Receptor 1 (CD200R1) is the receptor for the CD200 (OX-2) membrane glycoprotein. CD200R1 contains one C2- type Ig-like domain and one V-type Ig-like domain within its extracellular domain and a PTB-signaling motif in cytoplasmic domain. CD200R1 and CD200 associate via their respective N-terminal Ig-like domains. CD200R1 is restricted primarily to mast cells, basophils, macrophages, and dendritic cells. It propagates inhibitory signals despite its lacking a cytoplasmic ITIM (immunoreceptor tyrosinebased inhibitory motif). The receptor-substrate interaction may function as a myeloid downregulatory signal.