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Myosin light polypeptide 6 (MYL6) is a hexameric ATPase cellular motor protein. MYL6 is composed of 2 heavy chains, 2 nonphosphorylatable alkali light chains, and 2o phosphorylatable regulatory light chains. MYL6 is a myosin alkali light chain which is expressed in smooth muscle and non-muscle tissues. MYL6 partakes in generating the force for cellular movements, thus having an imperative role in overall cellular function.

ANXA4 is part of the annexin family of calcium-dependent phospholipid binding proteins. ANXA4 has 45%-59% identity with other proteins of its family and shares a related size and exon-intron organization. ANXA4 interacts with ATP, and has in vitro anticoagulant activity and also inhibits phospholipase A2 activity. ANXA4 is exclusively expressed in epithelial cells. ANXA4 is a Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis.

Haptoglogin participates in intestinal permeability, permitting intercellular tight junction disassembly, and controlling the equilibrium among tolerance and immunity to non-self antigens. Haptoglobin has antibacterial activity and takes part in modulating many aspects of the acute phase response. Haptoglobin is processed to yield both alpha and beta chains, which later unite as a tetramer to produce haptoglobin. Haptoglobin binds free hemoglobin (Hb) secreted from erythrocytes In blood plasma with high affinity and thus inhibits its oxidative activity. Further, the haptoglobin-hemoglobin complex is being removed by the reticuloendothelial system.

Adenylosuccinate lyase (ADSL) is an enzyme which converts adenylosuccinate to AMP and fumarate as part of the purine nucleotide cycle. ADSL is involved in both de novo synthesis of purines and formation of adenosine monophosphate from inosine monophosphate. ADSL catalyzes 2 reactions in AMP biosynthesis: the removal of a fumarate from succinylaminoimidazole carboxamide (SAICA) ribotide to yield aminoimidazole carboxamide ribotide (AICA) and removal of fumarate from adenylosuccinate to yield AMP. Defects in the ADSL are the cause of adenylosuccinase deficiency (ADSL deficiency). ADSL deficiency is an autosomal recessive disorder distinguished by the accumulation in the body fluids of succinylaminoimidazole-carboxamide riboside (SAICA-riboside) and succinyladenosine (S-Ado). Adenylosuccinase deficiency results in succinylpurinemic autism, psychomotor retardation, and in some cases, growth retardation associated with muscle wasting and epilepsy.

AKT Serine/Threonine Kinase 3 (Akt3) is a member of the Akt subfamily of serine/threonine protein kinases. Akt3is 1/3 closely related serine/threonine-protein kinases (Akt1, Akt2 and Akt3) called the Akt kinase and which regulate various processes including proliferation, metabolism, cell survival, growth and angiogenesis. The mentioned above is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Akt3 takes part in brain development and is critical for the viability of malignant glioma cells.

Gamma-SNAP (NAPG) is a cytoplasmic protein which binds to a membrane receptor complex composed of VAMP, SNAP25 and syntaxin. NAPG mediates the membrane binding of NSF, which is crucial for membrane fusion reactions. NSF and SNAPs seem to be general components of the intracellular membrane fusion system, and their action at specific sites of fusion needs be controlled by SNAP receptors specific to the membranes being fused. NAPG mediates platelet exocytosis and controls the membrane fusion events of this process.

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.

SMARCA4 belongs to the SWI/SNF family of proteins and is similar to the brahma protein of Drosophila. Proteins in this family have helicase and ATPase activities and are considered to regulate transcription ofcertain genes by altering the chromatin structure around those genes. SMARCA4 is part of the large ATP-dependent chromatin remodeling complex SNF/SWI, which is essential for transcriptional activation of genesnormally repressed by chromatin. In addition, SMARCA4 is able to bind BRCA1, as well as regulating the expression ofthe tumorigenic protein CD44. Moreover, mutations in SMARCA4 cause rhabdoid tumor predisposition syndrome type 2.

SNTN is a member of to the S-100 family. SNTN is localized solely to the bridging structure between the cell membrane and peripheral singlet microtubules that specifically exists in the narrowed distal portion of cilia. Exogenously expressed sentan displayed affinity for the membrane protrusions, and a protein-lipid binding assay discovered that sentan bounds to phosphatidylserine which indicate that sentan is the leading molecular component of the ciliary tip to link the cell membrane and peripheral singlet microtubules, making the distal portion of the cilia narrow and stiff to permit better airway approval or ovum transport.

Sperm Associated Antigen 7 (SPAG7) is comprised of 1 R3H domain. SPAG7 is detected in fetal brain and localized in the nucleus.

Survivin is part of the of the inhibitor of apoptosis (IAP) family, which encodes negative regulatory proteins that prevent apoptotic cell death. Members of the IAP family include multiple baculovirus IAP repeat (BIR) domains, but Survivin has only a single BIR domain.
Survivin is an inhibitor of caspase activation therefore leading to negative regulation of apoptosis. BIRC5 is expressed in Merkel cell carcinoma.
BIRC5 polymorphism causes survivin expression, thus contributing to the genetic susceptibility to lung cancer. BIRC5 expression in large cell lung cancer is substantially higher than in normal tissue cells. Survivin mRNA is up-regulated in tumors. Apoptotic response of infected intestinal epithelial cells is suppressed by C. parvum via upregulation of BIRC5, favoring parasite infection. Up-regulation of of Survivin is associated with breast carcinomas.
BIRC5 increases the activity of an oncolytic adenovirus in the presence of low-dose radiotherapy. ER- breast cancer cells become dependent on Notch-survivin signaling for their maintenance, in vivo. Survivin mRNA positive cases are related with bladder tumour recurrence elevated expression of survivin might play an important role of development in nasal polyps.

Otubain 1 (OTUB1) belongs to the ovarian tumor (OUT) superfamily of predicted cysteine proteases and inhibits cytokine gene transcription in the immune system through its interaction with a ubiquitin protease and E3 ubiquitin ligase. OTUB1 is a highly specific ubiquitin iso-peptidase, it cleaves ubiquitin from branched poly-ubiquitin chains but not from ubiquitinated substrates. OTUB1 is believed to work in specific ubiquitin-dependent pathways, possibly by providing an editing function of polyubiquitin chain growth. OTUB1 is a hydrolase that removes conjugated ubiquitin from proteins in vitro and may therefore have a significant regulatory role in the level of protein turnover by preventing degradation. Additionally, OTUB1 is a regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered impassive to antigen re-challenge and no longer respond to their cognate antigen. OTUB1 acts via its interaction with RNF128/GRAIL, which is an essential inductor of CD4 T-cell anergy.

ER Lipid Raft Associated 2 (ERLIN2) is a domain-containing protein which is a member of the band 7/mec-2 family. ERLIN2 is a ubiquitously expressed 339 amino acid protein.ERLIN2 which is localized to the lipid raft-like domains in the membrane of the endoplasmic reticulum (ER), plays a key role in the ER-associated degradation (ERAD) pathway that eliminates metabolically regulated and abnormal proteins from the ER.

Chemokine (C-C motif) ligand 6 (CCL6) is a small cytokine belonging to the CC chemokine family that has only been identified in rodents.
In mice, CCL6 is expressed in cells from neutrophil and macrophage lineages, and can be greatly induced under conditions suitable for myeloid cell differentiation. It is highly expressed in bone marrow cultures that have been stimulated with the cytokine GM-CSF. Some low levels of gene expression also occur in certain cell lines of myeloid origin (e.g. the immature myeloid cell lines DA3 and 32D cl3, and the macrophage cell line P388D) that can also be greatly induced in culture with GM-CSF. However, in activated T cell lines, expression of CCL6 is greatly reduced. CCL6 can also be induced in the mouse lung by the cytokine interleukin 13. Mouse CCL6 is located on chromosome 11. The cell surface receptor for CCL6 is believed to be the chemokine receptor CCR1.

CCDC104 also known as coiled-coil domain-containing protein 104 is a 342 amino acid protein that exists as two alternatively spliced isoforms. CCDC104 undergoes post-translational phosphorylation following DNA damage, most likely by either ATR or ATM. Among the diseases associated with CCDC104 are pancreatic cancer, and pancreatitis.

Cytokeratin 17 also known as KRT17 is a type I cytokeratin. KRT17 is found in nail beds, hair follicles, sebaceous glands, and other epidermal appendages. Mutations in KRT17 lead to Jackson-Lawler type pachyonychia congenita and steatocystoma multiplex. KRT17 takes part in the formation and maintenance of a variety of skin appendages, particularly in determining shape and orientation of hair. KRT17 also modulates the function of TNF-alpha in the precise context of hair cycling. Moreover, KRT17 regulates protein synthesis and epithelial cell growth all through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway.

TRAPPC3 is a part of the TRAPP complex that takes part in connection of transport vesicles to the cis-Golgi membrane. Additionally, TRAPPC3 is involved in vesicular transport from endoplasmic reticulum to Golgi.

TREM1 is a transmembrane receptor protein that is involved in monocytic activation and in the inflammatory response. TREM1 is expressed on the surface of neutrophils, mature monocytes and macrophages. TREM1 stimulates neutrophil and monocyte-mediated inflammatory responses. TREM1 also triggers the release of pro-inflammatory chemokines and cytokines, as well as increased surface expression of cell activation markers. Furthermore, TREM1 is an amplifier of inflammatory responses that are triggered by bacterial and fungal infections and is a fundamental mediator of septic shock. The expression of the soluble form of TREM1 increases during sepsis and can consequently be used as a biological marker for septic shock. TREM1 is strongly expressed in acute inflammatory lesions caused by bacteria and fungi. Increased TREM1 expression on monocytes is related to both infectious and noninfectious inflammatory processes.
TREM1 is vastly expressed in adult liver, lung and spleen than in corresponding fetal tissue. TREM1 is also expressed in the lymph node, placenta, spinal cord and heart tissues. TREM1 expression is more elevated in peripheral blood leukocytes than in the bone marrow and in normal cells than malignant cells. TREM1 is expressed at low levels in the early development of the hematopoietic system and in the promonocytic stage and at high levels in mature monocytes.

LGALS2 is a soluble beta-galactoside binding lectin that controls cell-to-cell adhesion and cell-to-extracellular matrix interactions and takes part in tumor progression, pre-mRNA splicing and apoptosis. LGALS2 induces apoptosis in activated T cells and binds to the cytokine lymphotoxin-alpha (LTA) with threat of myocardial infarction.

Gankyrin (proteasome 26S subunit) is a multicatalytic proteinase oncoprotein commonly overexpressed in most hepatocellular carcinomas. Proteasomes are found throughout eukaryotic cells at a high concentrations and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. Gankyrin interacts with S6 ATPase of the 19S regulatory particle of the 26S proteasome. Gankyrin is involved in theregulation of the phosphorylation of the retinoblastoma protein by CDK4, and to enhance the ubiquitinylation of p53 by MDM2. Gankyrin consists of 7 ankyrin repeats and is structurally similar to I kappa Bs. Gankyrin acts as a regulatory subunit of the 26s proteasome which is involved in the atp-dependent degradation of ubiquitinated proteins. Gankyrin is involved in progression of esophageal squamous cell carcinoma. gankyrin plays an oncogenic role especially in early stages of human epatocarcinogenesis. Gankyrin binds to NF-kappaB and suppresses its activity at the transcription level by modulating acetylation through SIRT1. Structural comparison between Gankyrin & p16(INK4A) identified numerous residues of gankyrin that are potentially important for CDK4 binding.

Synaptobrevin 2 which is an 18 kDa integral membrane protein localized to the cytoplasmic surface of synaptic vesicle, consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal. Synaptobrevin 2 is predominantly expressed in Langerhans islets and glomerular cells. The N-terminal domain of the protein (residues 1-89) forms a specific SNARE complex with the target membrane-associated t- or Q-SNAREs syntaxin 1 and SNAP-25.

VAMP5 is part of the vesicle-associated membrane protein (VAMP)/synaptobrevin family and the SNARE superfamily. VAMP5 is involved is vesicle trafficking events that are associated with myogenesis.

MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4.
CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph node CCL22 is expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+).
Furthermore, CCL22 is expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. In addition, MDC has a role in hindering progression of lung cancer. Moreover, significantly higher CCL22 expression is linked to gastric cancer.

Pancreatitis-associated protein (PAP) is a secretory protein not normally expressed in healthy pancreas but highly induced during acute pancreatitis. While PAP has been shown to be anti-bacterial and antiapoptotic in vitro, its definitive biological function in vivo is not clear. Using antisepse oligonucleotides, inhibition of PAP expression significantly worsened pancreatitis in a rat model. During pancreatitis, PAP released by the pancreas could mediate lung inflammation through induction of hepatic TNF- alpha expression and subsequent increase in circulating TNF-alpha.
PAP is activated in primary liver cancers. In normal liver, the protein is undetectable in normal mature hepatocytes and found only in some ductular cells, representing potential hepatic progenitor cells. PAP can be considered hepatic cytokine that combines mitogenic and anti-apoptotic functions regarding hepatocytes, and consequently acts as a growth factor in vivo to enhance liver regeneration. In pancreatic cancor, PAP was overexpressed in 79% (30 of 38) of pancreatic ductal adenocarcinoma, 19% (7 of 36) of chronic pancreatitis, and 29% (2 of 7) of mucinous cystadenoma. PAP was found in malignant ductular structures in pancreatic carcinomas as well as in benign proliferating ductules and acinar cells in chronic pancreatitis. Elevation of PAP in patients with pancreatic cancer is not merely explainable by concomitant pancreatitis, but seems to be due to increased PAP production by the cancer cells and is also correlated to tumour load as expressed by the UICC stages.
Epithelial expression of PAP was induced under intestinal mucosal inflammation initiated by exposure to commensal bacteria or DSS as well as inflamed IBD colon. Increased serum level of PAP diagnosed ileal location in active Crohn disease with a sensitivity of 60%, a specificity of 94%, a positive predictive value of 84% and a negative predictive value of 81%. Elevated serum PAP (> 50 ng/mL) is significantly associated with disease activity and ileal location of Crohn disease.