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Protein Tyrosine Phosphatase 1B is the founding member of the protein tyrosine phosphatase (PTP) family, which was isolated and identified based on its enzymatic activity and amino acid sequence. PTPs catalyze the hydrolysis of the phosphate monoesters specifically on tyrosine residues. Members of the PTP family share a highly conserved catalytic motif, which is essential for the catalytic activity. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP has been shown to act as a negative regulator of INS signaling by dephosphorylating the phosphotryosine residues of INS receptor kinase. This PTP was also reported to dephosphorylate epidermal growth factor receptor kinase, as well as JAK2 and TYK2 kinases, which implicated the role of this PTP in cell growth control, and cell response to IFN stimulation.

Protein tyrosine phosphatase mitochondrial 1 (PTPMT1) is a broadly expressed PTP membrane protein with high expression levels in pancreatic beta cells. The PTPMT1 protein is completely restricted to the matrix face of the inner membrane of the mitochondrion. PTPMT1 is responsible for dephosphorylating mitochondrial proteins and thus has a major role in the production of ATP. PTPMT1 exhibits a specific preference for the lipid signaling molecule phosphatidylinositol 5-phosphate as substrate.

Transcription Factor 4 (TCF4) acts as a transcription factor and takes part in the initiation of neuronal differentiation. TCF4 recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a motif primary identified in immunoglobulin enhancers. TCF4 is mainly expressed in pre-B-cells, even though it is present in other tissues as well.

Protein Tyrosine Phosphatase Non Receptor Type-4, also known asPTPN4 belongs to the protein tyrosine phosphatase, PTP family. PTPs are identified as signaling molecules which regulate a variety of cellular processes as well as cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTPN4 is broadly expressed non-receptor protein tyrosine phosphatase. In addition, PTPN4 interacts with glutamate receptor delta 2 & epsilon, and affects glutamate receptors signaling and/or in regulation of their activities through tyrosine dephosphorylation.

Astyrosine-protein phosphatase non-receptor type 11 isoform 2 (PTPN11), is a member of the protein-tyrosine phosphatase family, non-receptor class 2 subfamily. PTPN11 takes part in signal transduction from the cell surface to the nucleus downstream of various cytosolic protein tyrosine kinases as well as receptors. PTPN11 deficient cells have poor mobility due to excessive phosphorylation of FAK as well as other proteins which interfere with the rotation of cell attachment points in the focal adhesion complex.

Transcription Factor 4 (TCF4) acts as a transcription factor and takes part in the initiation of neuronal differentiation. TCF4 recognizes an Ephrussi-box ('E-box') binding site ('CANNTG') - a motif primary identified in immunoglobulin enhancers. TCF4 is mainly expressed in pre-B-cells, even though it is present in other tissues as well.

PTPN7 performs specifically on tyrosine-phosphorylated MAPK1. PTPN7 takes part in the regulation of signal transduction and T and B-lymphocyte development.

GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

Protein Tyrosine Phosphatase Receptor Type N (PTPRN) is a catalytically inactive protein and a major target of autoimmune response in diabetes mellitus. The long C-terminal intracellular tail covers the majority of autoantibody epitopes. PTPRN is expressed in neural, neuroendocrine and pancreatic islet cells.

Thyroid-stimulating hormone (also known as TSH or thyrotropin) is a hormone synthesized and secreted by thyrotrope cells in the anterior pituitary gland which regulates the endocrine function of the thyroid gland.
TSH stimulates the thyroid gland to secrete the hormones thyroxine (T4) and triiodothyronine (T3). TSH production is controlled by a Thyrotropin Releasing Hormone, (TRH), which is manufactured in the hypothalamus and transported to the Anterior Pituitary gland, where it increases TSH production and release. Somatostatin is also produced by the hypothalamus, and has an opposite effect on the pituitary production of TSH, decreasing or inhibiting its release.
The level of Thyroid hormones (T3 and T4) in the blood have an additional effect on the pituitary release of TSH, When the levels of T3 and T4 are low, the production of TSH is increased, and conversely, when levels of T3 and T4 are high, then TSH production is decreased. This effect creates a regulatory negative feedback loop.
TSH is a glycoprotein and consists of two subunits, the alpha and the beta subunit.
The a (alpha) subunit is identical to that of human chorionic gonadotropin (HCG), luteinising hormone (LH), follicle-stimulating hormone (FSH).
The b (beta) subunit is unique to TSH, and therefore determines its function.

YWHAH belongs to the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. 14-3-3 ETA is found in plants and mammals, and there is 99% identity to the mouse, rat and bovine orthologs. YWHAH gene contains a 7 base pair repeat sequence in its 5' UTR, and changes in the number of this repeat has been associated with early-onset schizophrenia.
14-3-3 eta is specific to the site of joint inflammation.
14-3-3 proteins are colocalized with Lewy bodies in Parkinson disease, though there is no specific staining for the 14-3-3 eta subunit.
There are 3 different isoforms types of 14-3-3: Beta, Gamma and ETA that are DAL-1/Protein 4.1B-binding proteins.

YWHAH belongs to the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. 14-3-3 ETA is found in plants and mammals, and there is 99% identity to the mouse, rat and bovine orthologs. YWHAH gene contains a 7 base pair repeat sequence in its 5' UTR, and changes in the number of this repeat has been associated with early-onset schizophrenia.
14-3-3 eta is specific to the site of joint inflammation.
14-3-3 proteins are colocalized with Lewy bodies in Parkinson disease, though there is no specific staining for the 14-3-3 eta subunit.
There are 3 different isoforms types of 14-3-3: Beta, Gamma and ETA that are DAL-1/Protein 4.1B-binding proteins.

Apolipoprotein H (APOH) attaches to numerous kinds of negatively charged substances for instance heparin, phospholipids, and dextran sulfate. APOH prevents activation of the intrinsic blood coagulation cascade by attaching to phospholipids on the surface of damaged cells. APOH expressed by the liver and secreted in the plasma.

Protein Tyrosine Phosphatase Type IVA Member 3 (PTP4A3) is a member of a small class of prenylated protein tyrosine phosphatases (PTPs) which remove phosphate modifications from tyrosine residues on proteins. PTP4A3 enhances cell proliferation, cell motility and invasive activity. PTP4A3 functions as a protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. PTP4A3 is mostly expressed in cardiomyocytes and skeletal muscle; it is also found in the pancreas.
PTP4A3 is always overexpressed in colon cancer metastasis. PTP4A3 is notably overexpressed in liver metastasis of colorectal cancer. High levels of PTP4A3 expression are linked to tumorigenesis and metastasis; therefore it is overexpressed in metastatic colorectal, ovarian, liver and skin cancers. PTP4A3 may be involved in the progression of cardiac hypertrophy by inhibiting intracellular calcium mobilization in response to angiotensin II. PTP4A3 is inhibited by sodium orthovanadate and peroxovanadium compounds.

Prothymosin alpha (PTMA) is a part of the pro/parathymosin family. PTMA mediates immune function by conferring resistance to some opportunistic infections.

PTEN, a tumor suppressor, has been implicated in a large number of human tumors and is conserved from humans to worms. PTEN has a tensin like domain and a catalytic domain similar to that of the dual specificity protein tyrosine phosphatases. Characterization of PTEN protein showed that it is a phosphatase that acts on proteins and on 3-phosphorylated phosphoinositides, and can therefore modulate signal transduction pathways that involve lipid second messengers. In contrast to most of the protein tyrosine phosphatases, PTEN preferentially dephosphorylates phosphoinositide substrates. PTEN negatively regulates intracellular levels of phosphatidylinositol-3,4,5-trisphosphate in cells and acts as a tumor suppressor by negative regulation of AKT/PKB signaling pathway. Recent results indicate that at least part of its role is to regulate the activity of the serine/threonine kinase AKT/PKB, and thus influence cell survival signaling.

Insulin decreases blood glucose concentration. it increases cell permeability to monosaccharides, amino acids and fatty acids. it accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.

Human Oxytocin stimulates uterine smooth muscle contractions indirectly and stimulates the mammary glands to increase lactation without increasing the production of milk.

Protein Tyrosine Phosphatase Non Receptor Type-11 or PTPN11 has 2 Src homology 2 domains and part of the tyrosine phosphatase group of proteins. PTPN11 is responsible for the catalyzation of tyrosine residues dephosphorylation in proteins and takes part in the stimulation and activation of Erk/MAP kinase transduction via signals from tyrosine kinase. Noonan syndrome and acute myeloid leukemia can be caused from mutations in PTPN11.

TSHB is a hormone synthesized and secreted by thyrotrope cells in the anterior pituitary gland which regulates the endocrine function of the T gland. Stimulates the gland to secrete the hormones (T4) and triiodothyronine (T3). Production is controlled by a Thyrotropin Releasing Hormone, (TRH), which is manufactured in the hypothalamus and transported to the Anterior Pituitary gland, where it increases production and release. Somatostatin is also produced by the hypothalamus, and has an opposite effect on the pituitary production, decreasing or inhibiting its release. The level of T hormones (T3 and T4) in the blood have an additional effect on the pituitary release of TSH, When the levels of T3 and T4 are low, the production is increased, and conversely, when levels of T3 and T4 are high, then production is decreased. This effect creates a regulatory negative feedback loop.

Prostaglandin Reductase 2 (PTGR2) is a member of the medium-chain dehydrogenase/reductase superfamily. PTGR2 is an enzyme involved in the metabolism of prostaglandins. PTGR2 catalyzes an NADPH-dependent reduction of the conjugated alpha, beta-unsaturated double bond of 15-keto-PGE(2), which is a fundamental step in terminal inactivation of prostaglandins and suppression of PPARgamma-mediated adipocyte differentiation. PTGR2 may also be involved in controlling activation of the peroxisome proliferator-activated receptor.

PTP4A2 is part of a small class of the protein tyrosine phosphatase (PTP) family. PTP4A2 is localized to the early endosome that take part in a variety of cellular activities. PTP4A2 protein interacts with the beta-subunit of Rab geranylgeranyltransferase II (beta GGT II), therefore has a role as a regulator of GGT II activity. Overexpression of PTP4A2 in mammalian cells conferred a transformed phenotype, which suggested its role in tumorigenesis.