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P85a functions as the regulatory subunit of the class IA PI3-kinase isoforms a, b, and d.
It contains two SH2 domains that bind to tyrosine-phosphorylated growth factor receptors or substrate adaptor proteins.
It also contains a BH (breakpoint cluster region homology) domain that shows GAP activity towards the small GTPases Rab4, Rab5, Cdc42, Rac1 and to a lesser extend towards Rab6 and Rab11.
It was shown that PI3Ka catalytic subunit mediated phosphorylation of the p85a adapter reduces the lipid kinase activity of the heterodimer and this gives hints for PI3K-dependent signaling events not requiring production of 3’-phosphorylated phosphoinositides.
PI3Ka protein kinase activity has been implicated in IRS-1 serine phosphorylation in insulin-treated adipocytes and in STAT3 and IRS-1 phosphorylation upon activation of the type 1 IFN receptor by IFN-a.

Glypican-3 (GPC3) belongs to the glypican family, and is highly expressed in the lung, liver, and the kidney. In some tissues, GPC3 functionss as a tumor suppressor gene and an oncofetal protein. The Glypican-3 protein is currently considered as a tumor marker and potential target for immunotherapy. Glypican-3 binds to and inhibits the dipeptidyl peptidase activity of CD26, and it can also induce apoptosis in certain cell types. Deletion mutations in the GPC3 gene are linked with Simpson-Golabi-Behmel syndrome, aka Simpson dysmorphia syndrome.

VEGF-D belongs to the VEGF/PDGF family of proteins. VEGF-D promotes lymphangiogesis, endothelial cell growth, and regulates vascular permeability. In addition, VEGF-D has an important part in the creation of the venous and lymphatic vascular systems and in the growth and maintenance of differentiated lymphatic endothelium Mature VEGF-D forms a noncovalently linked homodimer, and binds to and activate both VEGFR-2 (flk1) and VEGFR-3 (flt4).

EFNB1 is a member of the Eph family. The cell-surface proteins Ephrins split into two groups, ephrin-A and ephrin-B, based on their structure and function and perform as ligands for Eph receptors. The transmembrane EFNB1 proteins have conserved cytoplasmic tyrosine residues that are phosphorylated upon interaction with an EphB receptor. In addition, EFNB1 transduces outside-in signals by C-terminal protein interfaces which influence integrin-mediated cell attachment and migration.

SORBS3 is an SH3 domain-containing adaptor protein. The existence of SH3 domains in the SORBS3 protein have a role in its capability to attach to other cytoplasmic molecules and contribute to cystoskeletal organization, cell adhesion and migration, signaling, and gene expression. Various transcript variants encoding different isoforms are known for this gene.

Cytochrome c oxidase subunit VB (COX5B) is the terminal enzyme of the mitochondrial respiratory chain. COX5B is a multi-subunit enzyme complex which couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane. There are two isoforms of COX5:COX5a and COX5b. Transcription of COX5A (the aerobic isoform) is up-regulated as the rate of cellular respiration increases, when oxygen levels within the cell are high. However, when oxygen levels are low, COX5B (the hypoxic isoform) transcription increases and functions to maximize the turnover rate of the COX apoenzyme.

SEPT2 is a GTPase which is mandatory for cytokinesis and related to exocytosis. Septin-2 protein is able to hetero-oligomerize with Septin6, 7 and in addition takes part in the organization of new growth in organisms. SEPT2 is associated with a Tau-based paired helical filament core and contributes to the creation of neurofibrillary tangle as integral constituents of paired helical filaments.

Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.

A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.

The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.

While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

Coagulation factor VII is a vitamin K-dependent factor which is essential for hemostasis. It circulates in the blood as a zymogen which is later converted to an active form by factor IXa, factor Xa, factor XIIa, or thrombin by minor proteolysis. Upon activation of factor VII, a heavy chain with a catalytic domain and a light chain with 2 EGF-like domains are generated, and the two chains are held together by a disulfide bond. The presence of factor III and calcium ions further activates the coagulation cascade by converting factor IX to factor IXa and/or factor X to factor Xa. Alternative splicing of factor VII results in 2 transcripts. Defects in coagulation factor VII can cause coagulopathy. Coagulation factor VII initiates the extrinsic pathway of blood coagulation. Minor proteolysis converts factor VII to factor VIIa by factors Xa, XIIa, IXa, or thrombin. Factor VIIa also converts factor IX to factor IXa in the presence of tissue factor and calcium.

Thyroxine binding globulin, also known as SERPINA7, is synthesized in the liver and carried in the blood.
SERPINA7 may be decreased or increased in a number of diseases. Its main value in diagnosis is to assess thyroid function by determining the amount of free T3/T4.
Thyroxine binding globulin, binds and transports thyroid hormones in the circulation. SERPINA7 carries the majority of the T3/T4 in the blood. SERPINA7 has only one binding site for T3/T4 and about 25% of Thyroxine binding globulin is usually saturated.

Prothrombin produced in the liver is a vitamin K-dependent plasma protein. Before prothrombin is secreted into the plasma it goes through post translational modification by vitamin K-dependent carboxylase. The vitamin K-dependent carboxylase convertsprothrombin to 10 glutamic acid residues to gamma carboxyglutamic acid. Prothrombin comprises of 2 kringle regions which are found among residues a.a. 40 & 270 of the mature plasma protein and substitute the growth factor domains located in numerous plasma serine proteases.

Hepatitis E virus (HEV), the major etiologic agent of enterically transmitted non-A, non-B hepatitis worldwide, is a spherical, non-enveloped, single stranded RNA virus that is approximately 32 to 34 nm in diameter. HEV belongs to a genus of HEV-like viruses (unassigned genus). HEV has a single-stranded polyadenylated RNA genome of approximately 8 kb. Based on its physicochemical properties it is presumed to be a calici-like virus.

A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.

The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.

While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

Recombinant Human Holo Transferrin is an iron-delivery signaling protein which functions in the delivery of Fe³⁺ iron to cells using transferrin receptor-1 (TfR1/CD71).
Holo-transferrin binds TfR1, undergoes receptor-mediated endocytosis and the iron is released intracellularly. Transferrin Human Recombinant is crucial for brain and the nervous system, neuronal mitochondrial metabolism, neurotransmitter synthesis, oligodendrocyte myelination and synaptic activity. Recombinant holo-transferrin can be used in cell therapy, stem-cell expansion, CHO production, or drug-delivery platforms.

Based on sequence similarity to VEGF-A, a gene encoding a VEGF homologue has recently been discovered in the genome of Orf virus (OV) (Lyttle et al., 1994). Different isolates of Orf virus show significant amino acid sequence similarity to VEGF-A and described as a viral virulence factor that appears to be derived from captured host genes. All eight cysteine residues of the central cysteine knot motif characteristic of members of the VEGF family are conserved among other residues in the VEGF-E proteins (Dehio et al., 1999; Wise et al., 1999). Alignment of all mammalian VEGF sequences indicated that VEGF-E is distinct from the previously described VEGFs but most closely related to VEGF-A. Like VEGF-A, VEGF-E was found to bind with high affinity to VEGF receptor-2 (KDR) resulting in receptor autophosphorylation, whilst in contrast to VEGF-A, VEGF-E can not bind to VEGF receptor-1 (Flt-1). Furthermore VEGF-E can also not bind to VEGF receptor-3 (FLT-4). Therefore VEGF-E is a potent angiog

Eledoisin is an undecapeptide formed in the venom gland of several species of octopuses and is used as a vasodilator and a contraction agent of extravascular smooth muscle.

Influenza-B virus is a genus in the virusfamily Orthomyxoviridae. The only species in this genus is called "Influenza B virus". Influenza B virus only infects humansand seals. This limited host range is apparently in contrast with those caused by the similar Influenza virus Aas both mutate by both genetic drift and reassortment. Influenza-B virus evolves slower than A viruses and faster than C viruses. Influenza-B virus mutates at a rate 2-3 times lower than type A. However, influenza B mutates enough that lasting immunity is not possible. The Influenza B virus capsidis enveloped while its virionconsists of a matrix protein + envelope + nucleoprotein complex + nucleocapsid, and a polymerasecomplex. Influenza B is sometimes spherical and sometimes filamentous. Its 500 or so surface projections are made of hemagglutinin and neuraminidase.
The Influenza B virus is 14648 nucleotideslong and consists of eight segments of linear negative-sense, single-stranded RNA. The multipartite genome is encapsidated, each segment in a separate nucleocapsid, and the nucleocapsids are surrounded by one envelope.

Actin Filament Associated Protein 1 (AFAP1) is a Src binding partner. AFAP1 is a possible modulator of actin filament integrity in response to cellular signals, and is also playing a role as an adaptor protein by connecting Src family members to actin filaments. AFAP1 takes partin the development and progression of prostate adenocarcinoma by regulating cell-matrix adhesions and migration in the cancer cells.

ASCC1 is a subunit of the triggering signal cointegrator 1 (ASC-1) complex which is a transcriptional coactivator. ASC-1 complex takes a vital part in gene transactivation using various transcription factors such as activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and serum response factor (SRF). ASCC1 has an N-terminal KH-type RNA-binding motif, essential for AP-1 transactivation by the ASC-1 complex. Alterations in ASCC1 result in Barrett esophagus and esophageal adenocarcinoma.

Nogginwhich is encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may play and important role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. Noggin was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. There are several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1). All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

Neurogranin (NRGN) is a calmodulin-binding protein which is expressed solely in the brain, mainly in dendritic spines. NRGN is also taking part in the protein kinase C signaling pathway by being a "third messenger" substrate of protein kinase C-mediated molecular cascades during synaptic development and remodeling. NRGN binds to calmodulin in the absence of calcium. NRGN protein’s phosphorylation by protein kinase C lowers its binding ability.

EIF2S1 participates in the premature steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA which binds to a 40S ribosomal subunit, followed by mRNA binding to create a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 should exchange with GTP by way of a reaction catalyzed by eIF-2B.