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TAR DNA Binding Protein (TARDBP) was initially recognized as a transcriptional repressor which binds to chromosomally integrated TAR DNA and represses HIV-1 transcription. In addition, TARDBP has been detected in individuals diagnosed with chronic traumatic encephalopathy as well, which is a condition that often imitates ALS andhas been related with athletes who have experienced multiple concussions and other types of head injury.TARDBP has been shown to bind both DNA and RNA, it has multiple functions in transcriptional repression, pre-mRNAsplicing and translational regulation.

TIMP1 is a member of the TIMP family. TIMP1 is an inducible glycoprotein produced by various cell types. The TIMP1 glycoprotein is a natural inhibitor of the matrix metalloproteinases, which a group of peptidases involved in degradation of the extracellular matrix. TIMP1 binds in a reversible mode to MMPs, with regions in the N-terminal domain binding to the MMP substrate-binding site. On top of its inhibitory function against most of the known MMPs, TIMP1 is able to promote cell proliferation in a broad range of cell types, and may also have an anti-apoptotic role. Furthermore, TIMP1 has erthyroid-potentiating activity via translocation to the nucleus and also inhibits apoptosis in B-cells.
The TIMP1 gene is situated within intron 6 of the synapsin I gene and is transcribed in the opposite direction. TIMP1 activity is dependent on the existence of disulfide bonds.
TIMP1 transcription is extremely inducible in reaction to many cytokines and hormones.
Increased TIMP1 levels are connected with squamous cell laryngeal carcinoma. TIMP1 overexpression is linked to gastric cancer.

TP53I3 participates in the generation of reactive oxygen species (ROS). TP53I3 has low NADPH-dependent naphtoquinone reductase activity, with a preference for 1,2-naphtoquinone over 1,4-naphtoquinone. TP53I3 has low NADPH-dependent diamine reductase activity (in vitro). TP53I3 is localized to the cytoplasm and induced in primary, non-transformed and transformed cell cultures after exposure to genotoxic agents. TP53I3 microsatellite polymorphism is associated with differential susceptibility to cancer.

LanC Lantibiotic Synthetase Component C-Like 1 (LANCL1) belongs to the LanC family although formerly considered a part of the G-proteincoupled receptor superfamily. LANCL1 takes part in the biosynthesis of antimicrobial peptides. LANCL1 functions as a peptide-modifying enzyme component in eukaryotic cells. LANCL1 participates in EPS8 signaling and binds glutathione.

Obestatin is a hormone that is produced in the cells lining the stomach and small intestine of several mammals including humans; it drastically reduces appetite in mice and is expected to do the same in humans. Obestatin is a peptide hormone - a relatively small protein. It is encoded by the same gene that also encodes ghrelin, a peptide hormone that increases appetite. The protein produced by that gene breaks into two smaller peptides, ghrelin and obestatin. Ghrelin is an endogenous ligand for the growth hormone secretagogue receptor and is involved in regulating growth hormone release. Ghrelin is derived from a preprohormone called preproghrelin, which also generates a second peptide called obestatin. Ghrelin is an endogenous ligand for the orphan G protein-coupled receptor GPR39 and is involved in satiety and decreased food intake.

Phosphoribosyl Pyrophosphate Synthetase-Associated Protein 2 (PRPSAP2) is a protein which relates with the enzyme phosphoribosylpyrophosphate synthetase (PRS). PRS catalyzes the formation of phosphoribosylpyrophosphate which is a substrate for synthesis of purine, pyrimidine, histidine, tryptophan and NAD. PRS is a complex with 2 catalytic subunits and 2 associated subunits. PRPSAP2 encodes a non-catalytic associated subunit of PRS.

GroEL protein is the major heat shock protein of E.coli and belongs to the chaperonin (HSP60) family. GroEL protein prevents misfolding of proteins and promotes the refolding and proper assembly of unfolded polypeptiedes generated under stress condition.

PTTG1 (Securin) is mainly involved in the regulation of sister chromatid separation during cell division. Securin is a regulatory protein, which has a central role in chromosome stability, in the p53/TP53 pathway, and DNA repair. Additional two roles have been identified for PTTG1; the first one is to facilitate the transport of separase (cysteine protease) to the nucleus and the second role is to hinder the catalytic activity of separase. PTTG1 is ubiquitinated by the APC (Anaphase Promoting Complex), and subsequently degraded by the Proteasome, releasing separase. During the mitosis, PTTG1 blocks Separase/ESPL1 function, thus preventing the proteolysis of the cohesin complex and the ensuing segregation of the chromosomes. However, PTTG1 function is not restricted to a blocking activity only, since it is required to activate ESPL1. PTTG1 is ubiquitinated at the beginning of anaphase, leading to its destruction and to the liberation of ESPL1.
PTTG1 contains two PXXP motifs, which are necessary for its transforming and tumorigenic activities, in addition to its stimulation of basic fibroblast growth factor expression. It also contains a D box (destruction box) which is essential for its degradation by the APC. The acidic C-terminal region of the Securin can function as a transactivation domain. Even though, PTTG1 is primarily a cytosolic protein, it partially localizes in the nucleus.
PTTG1 is highly expressed in various tumors; it also has transforming activity in vitro and tumorigenic activity in vivo. Furthermore, PTTG1 negatively regulates the transcriptional activity and related apoptosis activity of TP53.

Troponin-T is one of three subunits that form the troponin complex of the thin filaments of striated muscle, it regulates muscle contraction in response to alterations in intracellular calcium ion concentration. TnTc is expressed only in the heart and has proved to be a specific biomarker for heart disease.
Mutations in TNNT2 are associated with familial hypertrophic cardiomyopathy as well as with dilated cardiomyopathy.
Alternative splicing results in many tissue-specific isoforms.

CTLA-4 is a member of the immunoglobulin superfamily and encodes a protein which transmits an inhibitory signal to T cells. The protein contains a V domain, a transmembrane domain, and a cytoplasmic tail. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. The membrane-bound isoform functions as a homodimer interconnected by a disulfide bond, while the soluble isoform functions as a monomer. Mutations in this gene have been associated with insulin-dependent diabetes mellitus, Graves disease, Hashimoto thyroiditis, celiac disease, systemic lupus erythematosus, thyroid-associated orbitopathy, and other autoimmune diseases.

MSH6 deficiency result in hereditary non-polyposis colorectal cancer (Lynch syndrome). HNPCC is an autosomal, dominantly inherited disease linked with rise in cancer susceptibility. MSH6 is is known by its familial predisposition to premature onset colorectal carcinoma (crc).
MSH6 is involved in repairing DNA. MSH6 protein repairs mistakes that occure during DNA replication in preparation for cell division. The MSH6 protein bonds with MSH2 protein and form an active protein complex which recognizes specific parts on the DNA where mistakes have been made during DNA replication. MLH1-PMS2 protein complex, afterwards takes over with the repair. MSH6 gene is part of the set of the mismatch repair (MMR) genes.

Angiopoietin-related protein 7 (ANGPTL7), belongs to the angiopoietin-like family of molecules. ANGPTL7 is expressed in the corneal stroma, trabecular meshwork, and sclera. ANGPTL7 production is up-regulated in trabecular meshwork cells by glucocorticoids and TGF-Beta and in cartilage by TNF-alpha.

The enzyme Arylsulfatase A, also known as cerebroside-sulfatase, is responsible to break down sulfatides. The main molecule that Arylsulfatase A breaks down is cerebroside 3-sulfate into cerebroside and sulfate. The enzyme is encoded by the ARSA gene in humans. Phosphate can form a covalent bond with the Arylsulfatase A’s active site 3-oxoalanine, thus, inhibits the protein.

U2 small nuclear ribonucleoprotein A (SNRPA1), a 255 amino acid protein, is a component of the U2 snRNP which forms a complex with U2 snRNP B (U2B). U2 snRNP A and U2 snRNP B form together a complex which binds to the U2 snRNA hairpin IV. The configuration of the U2 snRNP A/U2 snRNP B dimer and the delicate variations of a few key residues regulate the snRNP-RNA-binding specificity.

SOS1, also known as Gingival Fibromatosis, is a Ras & Rac guanine nucleotide exchange factor. SOS1 is comprised of a number of significant domains. The REM and CDC25 domains provide the catalytic activity of SOS1 towards Ras and the histone fold DH/PH (Dbl homology & Pleckstrin homology) domains function, in tandem, to stimulate GTP/GDP exchange for Rac. Moreover, binding of GTP activates Ras proteins, and subsequent hydrolysis of the bound GTP to GDP and phosphate inactivates signaling by these proteins. GTP binding can be catalyzed by guanine nucleotide exchange factors for RAS, and GTP hydrolysis can be enhanced by GTPase-activating proteins.

Brain Abundant Membrane Attached Signal Protein 1 (BASP1) is a membrane bound protein with numerous transient phosphorylation positions and PEST motifs. Preservation of proteins with PEST sequences amongst diverse species supports their functional significance. PEST sequences take place in proteins with high turnover rates. Immunological attributes of this protein are species specific. BASP1 undergoes N-terminal myristoylation.

HSPBAP1 holds a jumonji C (JMJC) domain. HSPBAP1 protein has a part in regulating stress response in the living cell. HSPBAP1 is known to interact with CRYAB and HSPB1.

MMP-3 enzyme is also known as Stromelysin-1or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. It dissolves the intervertebral nucleus pulposus and annulus fibrosus of Herniated Lumbar Intervertebral Disk . MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL1-beta.

Cytokeratin 8 belongs to the type B (basic) subfamily of high molecular weight keratins and exists in combination with keratin 18. Cytokeratin 8 is primarily found in the non-squamous epithelia and is present in majority of adenocarcinomas and ductal carcinomas. It is absent in squamous cell carcinomas. Hepatocellular carcinomas are defined by the use of antibodies that recognize only cytokeratin polypeptides 8 and 18.

HTLV-1 is the etiological agent for Adult T-Cell Leukemia which encodes a 40kDa cell-transforming oncoprotein called Tax. HTLV-1 Tax protein sensitizes cells to apoptotic cell death induced by DNA damaging agents. Constitutive Activation of TAK1 by HTLV-1 Tax-dependent Overexpression of TAB2 Induces Activation of JNK-ATF2 but Not IKK-NF-kB.

40S ribosomal protein S3 is a member of the S3P family of ribosomal proteins. RPS3 facilitates the formation of the mRNA binding site 3' of the codon in the decoding site. Moreover, RPS3 takes part in DNA damage recognition due to its affinity for abasic sites and 7, 8-dihydro-8-oxoguanine residues and its collaboration with human base excision repair proteins OGG1 and Ref-1. Expression of RPS3 is higher in colon adenocarcinomas and adenomatous polyps compared to adjacent normal colonic mucosa.

40S ribosomal protein S5 (RPS5) is a ribosomal protein, which is a member of the ribosomal protein S7P family.Ribosomes, which are the organelles that catalyze protein synthesis, composed of a small subunit and a large subunit that comprise of over 80 distinct ribosomal proteins. RPS5 is a 204 amino acid component of the 40S complex. RPS5 proteins exist as multiple processed pseudogenes which are scattered throughout the genome. RPS5 is expressed at varying amounts in colorectal cancer cells, proposing a possible role in carconigenesis.

SAM Domain SH3 Domain and Nuclear Localization Signal 1 (SAMSN1) is a member of a known adaptors and scaffold proteins containing SH3 and SAM (sterile alpha motif) domains. SAMSN1 is a negative regulator of B-cell activation and is down-regulates cell proliferation. SAMSN1 is up-regulated by IL-4 in activated B cells and expressed mainly in dendritic cells. SAMSN1 owns a function which is similar to other adaptor proteins that link signaling molecules in signal transduction cascades.