Protein Phosphatase
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A protein phosphatase is a
phosphatase In biochemistry, a phosphatase is an enzyme that uses water to cleave a phosphoric acid Ester, monoester into a phosphate ion and an Alcohol (chemistry), alcohol. Because a phosphatase enzyme catalysis, catalyzes the hydrolysis of its Substrate ...
enzyme Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. A ...
that removes a phosphate group from the phosphorylated amino acid residue of its
substrate Substrate may refer to: Physical layers *Substrate (biology), the natural environment in which an organism lives, or the surface or medium on which an organism grows or is attached ** Substrate (locomotion), the surface over which an organism lo ...
protein. Protein phosphorylation is one of the most common forms of reversible protein posttranslational modification ( PTM), with up to 30% of all proteins being phosphorylated at any given time.
Protein kinases A protein kinase is a kinase which selectively modifies other proteins by covalently adding phosphates to them (phosphorylation) as opposed to kinases which modify lipids, carbohydrates, or other molecules. Phosphorylation usually results in a fun ...
(PKs) are the effectors of phosphorylation and catalyse the transfer of a γ-phosphate from ATP to specific amino acids on proteins. Several hundred PKs exist in mammals and are classified into distinct super-families. Proteins are phosphorylated predominantly on Ser, Thr and Tyr residues, which account for 79.3, 16.9 and 3.8% respectively of the phosphoproteome, at least in mammals. In contrast, protein phosphatases (PPs) are the primary effectors of dephosphorylation and can be grouped into three main classes based on sequence, structure and catalytic function. The largest class of PPs is the phosphoprotein phosphatase (PPP) family comprising PP1, PP2A, PP2B, PP4, PP5, PP6 and PP7, and the protein phosphatase Mg2+- or Mn2+-dependent (PPM) family, composed primarily of PP2C. The protein Tyr phosphatase (PTP) super-family forms the second group, and the aspartate-based protein phosphatases the third. The protein pseudophosphatases form part of the larger phosphatase family, and in most cases are thought to be catalytically inert, instead functioning as phosphate-binding proteins, integrators of signalling or subcellular traps. Examples of membrane-spanning protein phosphatases containing both active (phosphatase) and inactive (pseudophosphatase) domains linked in tandem are known, conceptually similar to the kinase and pseudokinase domain polypeptide structure of the JAK pseudokinases. A complete comparative analysis of human phosphatases and pseudophosphatases has been completed by Manning and colleagues, forming a companion piece to the ground-breaking analysis of the human kinome, which encodes the complete set of ~536 human
protein kinases A protein kinase is a kinase which selectively modifies other proteins by covalently adding phosphates to them (phosphorylation) as opposed to kinases which modify lipids, carbohydrates, or other molecules. Phosphorylation usually results in a fun ...
.


Mechanism

Phosphorylation involves the transfer of phosphate groups from
ATP ATP may refer to: Companies and organizations * Association of Tennis Professionals, men's professional tennis governing body * American Technical Publishers, employee-owned publishing company * ', a Danish pension * Armenia Tree Project, non ...
to the enzyme, the energy for which comes from hydrolysing ATP into
ADP Adp or ADP may refer to: Aviation * Aéroports de Paris, airport authority for the Parisian region in France * Aeropuertos del Perú, airport operator for airports in northern Peru * SLAF Anuradhapura, an airport in Sri Lanka * Ampara Air ...
or
AMP #REDIRECT Amp #REDIRECT Amp {{Redirect category shell, {{R from other capitalisation{{R from ambiguous page ...
{{Redirect category shell, {{R from other capitalisation{{R from ambiguous page ...
. However, dephosphorylation releases phosphates into solution as free ions, because attaching them back to ATP would require energy input. Cysteine-dependent phosphatases (CDPs) catalyse the hydrolysis of a phosphoester bond via a phospho-cysteine intermediate. The free
cysteine Cysteine (symbol Cys or C; ) is a semiessential proteinogenic amino acid with the formula . The thiol side chain in cysteine often participates in enzymatic reactions as a nucleophile. When present as a deprotonated catalytic residue, sometime ...
nucleophile In chemistry, a nucleophile is a chemical species that forms bonds by donating an electron pair. All molecules and ions with a free pair of electrons or at least one pi bond can act as nucleophiles. Because nucleophiles donate electrons, they are ...
forms a bond with the
phosphorus Phosphorus is a chemical element with the symbol P and atomic number 15. Elemental phosphorus exists in two major forms, white phosphorus and red phosphorus, but because it is highly reactive, phosphorus is never found as a free element on Ear ...
atom of the phosphate moiety, and the P-O bond linking the phosphate group to the tyrosine is protonated, either by a suitably positioned acidic
amino acid Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although hundreds of amino acids exist in nature, by far the most important are the alpha-amino acids, which comprise proteins. Only 22 alpha am ...
residue (Asp in the diagram below) or a water molecule. The phospho-cysteine intermediate is then hydrolysed by another water molecule, thus regenerating the active site for another dephosphorylation reaction. Metallo-phosphatases (e.g. PP2C) co-ordinate 2 catalytically essential metal ions within their active site. There is currently some confusion of the identity of these metal ions, as successive attempts to identify them yield different answers. There is currently evidence that these metals could be
Magnesium Magnesium is a chemical element with the symbol Mg and atomic number 12. It is a shiny gray metal having a low density, low melting point and high chemical reactivity. Like the other alkaline earth metals (group 2 of the periodic ta ...
,
Manganese Manganese is a chemical element with the symbol Mn and atomic number 25. It is a hard, brittle, silvery metal, often found in minerals in combination with iron. Manganese is a transition metal with a multifaceted array of industrial alloy use ...
,
Iron Iron () is a chemical element with symbol Fe (from la, ferrum) and atomic number 26. It is a metal that belongs to the first transition series and group 8 of the periodic table. It is, by mass, the most common element on Earth, right in f ...
,
Zinc Zinc is a chemical element with the symbol Zn and atomic number 30. Zinc is a slightly brittle metal at room temperature and has a shiny-greyish appearance when oxidation is removed. It is the first element in group 12 (IIB) of the periodi ...
, or any combination thereof. It is thought that a hydroxyl ion bridging the two metal ions takes part in nucleophilic attack on the
phosphorus Phosphorus is a chemical element with the symbol P and atomic number 15. Elemental phosphorus exists in two major forms, white phosphorus and red phosphorus, but because it is highly reactive, phosphorus is never found as a free element on Ear ...
ion.


Sub-types

Phosphatases can be subdivided based upon their substrate specificity.


Serine/threonine PP (PPM/PPP) families

Protein Ser/Thr phosphatases were originally classified using biochemical assays as either, type 1 (PP1) or type 2 (PP2), and were further subdivided based on metal-ion requirement (PP2A, no metal ion; PP2B, Ca2+ stimulated; PP2C, Mg2+ dependent) (Moorhead et al., 2007). The protein Ser/Thr phosphatases PP1, PP2A and PP2B of the PPP family, together with PP2C of the PPM family, account for the majority of Ser/Thr PP activity in vivo (Barford et al., 1998). In the brain, they are present in different subcellular compartments in neuronal and glial cells, and contribute to different neuronal functions.


PPM

The PPM family, which includes PP2C and pyruvate dehydrogenase phosphatase, are enzymes with Mn2+/Mg2+ metal ions that are resistant to classic inhibitors and toxins of the PPP family. Unlike most PPPs, PP2C exists in only one subunit but, like PTPs, it displays a wide variety of structural domains that confer unique functions. In addition, PP2C does not seem to be evolutionarily related to the major family of Ser/Thr PPs and has no sequence homology to ancient PPP enzymes. The current assumption is that PPMs evolved separately from PPPs but converged during evolutionary development.


Class I: Cys-based PTPs

Class I PTPs constitute the largest family. They contain the well-known classical receptor (a) and non-receptor PTPs (b), which are strictly tyrosine-specific, and the DSPs (c) which target Ser/Thr as well as Tyr and are the most diverse in terms of substrate specificity.


Class III: Cys-based PTPs

The third class of PTPs contains three cell cycle regulators, CDC25A, CDC25B and CDC25C, which dephosphorylate CDKs at their N-terminal, a reaction required to drive progression of the cell cycle. They are themselves regulated by phosphorylation and are degraded in response to DNA damage to prevent chromosomal abnormalities.


Class IV: Asp-based DSPs

The haloacid dehalogenase (HAD) superfamily is a further PP group that uses Asp as a nucleophile and was recently shown to have dual-specificity. These PPs can target both Ser and Tyr, but are thought to have greater specificity towards Tyr. A subfamily of HADs, the Eyes Absent Family (Eya), are also transcription factors and can therefore regulate their own phosphorylation and that of transcriptional cofactor/s, and contribute to the control of gene transcription. The combination of these two functions in Eya reveals a greater complexity of transcriptional gene control than previously thought . A further member of this class is the RNA polymerase II C-terminal domain phosphatase. While this family remains poorly understood, it is known to play important roles in development and nuclear morphology.


Alternative Structural Classification

Many phosphatases are promiscuous with respect to substrate type, or can evolve quickly to change substrate. An alternative structural classification notes that 20 distinct protein folds have phosphatase activity, and 10 of these contain protein phosphatases. * The CC1 fold is the most common, and includes tyrosine-specific (PTP), dual-specific (DSP) and even lipid-specific (PTEN) families. * The major serine/threonine-specific folds are PPM (PP2C) and PPPL (PPP). * The only known histidine phosphatases is in the PHP fold. * Other folds encode phosphatases that act on various combination of pSer, pThr, pTyr, and non-protein substrates (CC2, CC3,
HAD HAD CCD is the name of a technology Sony implemented on some of their Charge-coupled device, CCD image sensors. List of HAD CCD sensors See also *Sony BIONZ *Exmor, Sony Exmor *Nikon EXPEED References

Sony image sensors {{photograp ...
, HP, AP, RTR1).


Physiological relevance

Phosphatases act in opposition to kinases/
phosphorylases In biochemistry, phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate+hydrogen) to an acceptor. :A-B + P A + P-B They include allosteric enzymes that catalyze the production of gluco ...
, which add phosphate groups to proteins. The addition of a phosphate group may activate or de-activate an enzyme (e.g., kinase signalling pathways) or enable a protein-protein interaction to occur (e.g., SH2 domains ); therefore phosphatases are integral to many
signal transduction Signal transduction is the process by which a chemical or physical signal is transmitted through a cell as a series of molecular events, most commonly protein phosphorylation catalyzed by protein kinases, which ultimately results in a cellula ...
pathways. Phosphate addition and removal do not necessarily correspond to enzyme activation or inhibition, and that several enzymes have separate phosphorylation sites for activating or inhibiting functional regulation. CDK, for example, can be either activated or deactivated depending on the specific amino acid residue being phosphorylated.
Phosphate In chemistry, a phosphate is an anion, salt, functional group or ester derived from a phosphoric acid. It most commonly means orthophosphate, a derivative of orthophosphoric acid . The phosphate or orthophosphate ion is derived from phospho ...
s are important in
signal transduction Signal transduction is the process by which a chemical or physical signal is transmitted through a cell as a series of molecular events, most commonly protein phosphorylation catalyzed by protein kinases, which ultimately results in a cellula ...
because they regulate the proteins to which they are attached. To reverse the regulatory effect, the phosphate is removed. This occurs on its own by
hydrolysis Hydrolysis (; ) is any chemical reaction in which a molecule of water breaks one or more chemical bonds. The term is used broadly for substitution reaction, substitution, elimination reaction, elimination, and solvation reactions in which water ...
, or is mediated by protein phosphatases. Protein phosphorylation plays a crucial role in biological functions and controls nearly every cellular process, including metabolism, gene transcription and translation, cell-cycle progression, cytoskeletal rearrangement, protein-protein interactions, protein stability, cell movement, and
apoptosis Apoptosis (from grc, ἀπόπτωσις, apóptōsis, 'falling off') is a form of programmed cell death that occurs in multicellular organisms. Biochemical events lead to characteristic cell changes (morphology) and death. These changes incl ...
. These processes depend on the highly regulated and opposing actions of PKs and PPs, through changes in the phosphorylation of key proteins. Histone phosphorylation, along with methylation, ubiquitination, sumoylation and acetylation, also regulates access to DNA through chromatin reorganisation. One of the major switches for neuronal activity is the activation of PKs and PPs by elevated intracellular calcium. The degree of activation of the various isoforms of PKs and PPs is controlled by their individual sensitivities to calcium. Furthermore, a wide range of specific inhibitors and targeting partners such as scaffolding, anchoring, and adaptor proteins also contribute to the control of PKs and PPs and recruit them into signalling complexes in neuronal cells. Such signalling complexes typically act to bring PKs and PPs in close proximity with target substrates and signalling molecules as well as enhance their selectivity by restricting accessibility to these substrate proteins. Phosphorylation events, therefore, are controlled not only by the balanced activity of PKs and PPs but also by their restricted localisation. Regulatory subunits and domains serve to restrict specific proteins to particular subcellular compartments and to modulate protein specificity. These regulators are essential for maintaining the coordinated action of signalling cascades, which in neuronal cells include short-term (synaptic) and long-term (nuclear) signalling. These functions are, in part, controlled by allosteric modification by secondary messengers and reversible protein phosphorylation. It is thought that around 30% of known PPs are present in all tissues, with the rest showing some level of tissue restriction. While protein phosphorylation is a cell-wide regulatory mechanism, recent quantitative proteomics studies have shown that phosphorylation preferentially targets nuclear proteins. Many PPs that regulate nuclear events, are often enriched or exclusively present in the nucleus. In neuronal cells, PPs are present in multiple cellular compartments and play a critical role at both pre- and post-synapses, in the cytoplasm and in the nucleus where they regulate gene expression. Phosphoprotein phosphatase is activated by the hormone
insulin Insulin (, from Latin ''insula'', 'island') is a peptide hormone produced by beta cells of the pancreatic islets encoded in humans by the ''INS'' gene. It is considered to be the main anabolic hormone of the body. It regulates the metabolism o ...
, which indicates that there is a high concentration of
glucose Glucose is a simple sugar with the molecular formula . Glucose is overall the most abundant monosaccharide, a subcategory of carbohydrates. Glucose is mainly made by plants and most algae during photosynthesis from water and carbon dioxide, using ...
in the
blood Blood is a body fluid in the circulatory system of humans and other vertebrates that delivers necessary substances such as nutrients and oxygen to the cells, and transports metabolic waste products away from those same cells. Blood in the c ...
. The enzyme then acts to dephosphorylate other enzymes, such as
phosphorylase kinase Phosphorylase kinase (PhK) is a serine/threonine-specific protein kinase which activates glycogen phosphorylase to release glucose-1-phosphate from glycogen. PhK phosphorylates glycogen phosphorylase at two serine residues, triggering a conformatio ...
, glycogen phosphorylase, and
glycogen synthase Glycogen synthase (UDP-glucose-glycogen glucosyltransferase) is a key enzyme in glycogenesis, the conversion of glucose into glycogen. It is a glycosyltransferase () that catalyses the reaction of UDP-glucose and (1,4--D-glucosyl)n to yield UD ...
. This leads to phosphorylase kinase and glycogen phosphorylase's becoming inactive, while glycogen synthase is activated. As a result,
glycogen Glycogen is a multibranched polysaccharide of glucose that serves as a form of energy storage in animals, fungi, and bacteria. The polysaccharide structure represents the main storage form of glucose in the body. Glycogen functions as one o ...
synthesis is increased and
glycogenolysis Glycogenolysis is the breakdown of glycogen (n) to glucose-1-phosphate and glycogen (n-1). Glycogen branches are catabolized by the sequential removal of glucose monomers via phosphorolysis, by the enzyme glycogen phosphorylase. Mechanism The ...
is decreased, and the net effect is for energy to enter and be stored inside the cell.


Learning and memory

In the adult brain, PPs are essential for synaptic functions and are involved in the negative regulation of higher-order brain functions such as learning and memory. Dysregulation of their activity has been linked to several disorders including cognitive ageing and neurodegeneration, as well as cancer, diabetes and obesity.


Examples

Human genes that encode proteins with phosphoprotein phosphatase activity include:


Protein serine/threonine phosphatase

* PPP1CA, PPP1CB, PPP1CC,
PPP2CA Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform is an enzyme that (in humans) is encoded by the ''PPP2CA'' gene. Function This gene encodes the phosphatase 2A catalytic subunit. Protein phosphatase 2A is one of the fou ...
,
PPP2CB Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform is an enzyme that in humans is encoded by the ''PPP2CB'' gene. Function This gene encodes the phosphatase 2A catalytic subunit. Protein phosphatase 2A is one of the four ma ...
,
PPP3CA Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform (PP2BA) is a protein that in humans is encoded by the ''PPP3CA'' gene In biology, the word gene (from , ; "... Wilhelm Johannsen coined the word gene to describe the M ...
,
PPP3CB Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform (PP2BB) is an enzyme that in humans is encoded by the ''PPP3CB'' gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Men ...
,
PPP3CC Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform (PP2BC) is an enzyme that in humans is encoded by the ''PPP3CC'' gene. Calmodulin-dependent protein phosphatase, calcineurin, is involved in a wide range of biologic activiti ...
,
PPP4C Serine/threonine-protein phosphatase 4 catalytic subunit is an enzyme that in humans is encoded by the ''PPP4C'' gene. Interactions PPP4C has been shown to interact with: * CCDC6, * CCT2, * CCT3, * CCT4, * CCT5, * CCT6A, * CCT7, * IG ...
* PPP5C,
PPP6C Serine/threonine-protein phosphatase 6 catalytic subunit is an enzyme that in humans is encoded by the ''PPP6C'' gene. Interactions PPP6C has been shown to interact with IGBP1 Immunoglobulin-binding protein 1 is a protein that in humans is ...


Protein tyrosine phosphatase

* CDC14s:
CDC14A Dual specificity protein phosphatase CDC14A is an enzyme that in humans is encoded by the ''CDC14A'' gene. The protein encoded by this gene is a member of the dual specificity protein tyrosine phosphatase family. This protein is highly similar to ...
, CDC14B, CDC14C,
CDKN3 Cyclin-dependent kinase inhibitor 3 is an enzyme that in humans is encoded by the ''CDKN3'' gene. The protein encoded by this gene belongs to the dual specificity protein phosphatase family. It was identified as a cyclin-dependent kinase inhibito ...
* Phosphatase and tensin homologs: PTEN * slingshot:
SSH1 ''For the SSH-1 protocol, see Secure Shell#Version 1'' Protein phosphatase Slingshot homolog 1 is an enzyme that in humans is encoded by the ''SSH1'' gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to de ...
,
SSH2 Protein phosphatase Slingshot homolog 2 is an enzyme that in humans is encoded by the ''SSH2'' gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''g ...
,
SSH3 Protein phosphatase Slingshot homolog 3 is an enzyme that in humans is encoded by the ''SSH3'' gene. Function The ADF (actin-depolymerizing factor)/cofilin family (see MIM 601442) is composed of stimulus-responsive mediators of actin dynamics ...


Dual-specificity phosphatase

*
DUSP1 Dual specificity protein phosphatase 1 is an enzyme that in humans is encoded by the ''DUSP1'' gene. Function The expression of DUSP1 gene is induced in human skin fibroblasts by oxidative/heat stress and growth factors. It specifies a protei ...
, DUSP2, DUSP3,
DUSP4 Dual specificity protein phosphatase 4 is an enzyme that in humans is encoded by the ''DUSP4'' gene. Function The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate th ...
,
DUSP5 Dual specificity protein phosphatase 5 is an enzyme that in humans is encoded by the ''DUSP5'' gene. Function The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate th ...
, DUSP6, DUSP7, DUSP8, DUSP9 * DUSP10, DUSP11,
DUSP12 Dual specificity protein phosphatase 12 is an enzyme that in humans is encoded by the ''DUSP12'' gene. The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target ...
,
DUSP13 Dual specificity phosphatase 13 is an enzyme that in humans is encoded by the ''DUSP13'' gene. Function Members of the protein tyrosine phosphatase superfamily cooperate with protein kinase A protein kinase is a kinase which selectively mo ...
, DUSP14,
DUSP15 Dual specificity protein phosphatase 15 is an enzyme that in humans is encoded by the ''DUSP15'' gene. The protein encoded by this gene belongs to the non-receptor class of the protein-tyrosine phosphatase family. The encoded protein has both pro ...
, DUSP16, DUSP18, DUSP19 *
DUSP21 Dual-specificity phosphatase (DUSP; DSP) is a form of phosphatase that can act upon tyrosine or serine/threonine residues. There are several families of dual-specificity phosphatase enzymes in mammals. All share a similar catalytic mechanism, by w ...
, DUSP22,
DUSP23 Dual specificity protein phosphatase 23, also known as low molecular mass dual specificity phosphatase 3 (LDP-3), is an enzyme ( and ) that in humans is encoded by the ''DUSP23'' gene In biology, the word gene (from , ; "...Wilhelm Johannsen ...
,
DUSP26 Dual-specificity phosphatase (DUSP; DSP) is a form of phosphatase that can act upon tyrosine or serine/threonine residues. There are several families of dual-specificity phosphatase enzymes in mammals. All share a similar catalytic mechanism, by w ...
,
DUSP27 Dual specificity phosphatase 27, atypical is a protein that in humans is encoded by the DUSP27 gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''g ...
,
DUSP28 Dual-specificity phosphatase (DUSP; DSP) is a form of phosphatase that can act upon tyrosine or serine/threonine residues. There are several families of dual-specificity phosphatase enzymes in mammals. All share a similar catalytic mechanism, by w ...


Ungrouped

* CTDP1 * CTDSP1, CTDSP2, CTDSPL * DULLARD *
EPM2A Laforin, encoded by the ''EPM2A'' gene, is a phosphatase, with a carbohydrate-binding module, carbohydrate-binding domain, which is mutated in patients with Lafora disease. It contains a dual specificity phosphatase domain (DSP) and a carbohydrat ...
* ILKAP *
MDSP {{refimprove, date=January 2012 MDSP is a multiprocessor DSP family from Cradle Technologies. Currently used mostly in streaming video processing in broadcast (internet and terrestrial) and video surveillance security markets. It is a loosely co ...
* PGAM5 * PHLPP1,
PHLPP2 The PHLPP isoforms (PH domain and Leucine rich repeat Protein Phosphatases) are a pair of protein phosphatases, PHLPP1 and PHLPP2, that are important regulators of Akt serine-threonine kinases (Akt1, Akt2, Akt3) and conventional/novel prote ...
* PPEF1, PPEF2 * PPM1A,
PPM1B Protein phosphatase 1B is an enzyme that in humans is encoded by the ''PPM1B'' gene. Function The protein encoded by this gene is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulato ...
, PPM1D, PPM1E,
PPM1F Protein phosphatase 1F is an enzyme that in humans is encoded by the ''PPM1F'' gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''b ...
, PPM1G, PPM1H, PPM1J,
PPM1K Protein phosphatase 1K, mitochondrial is an enzyme that in humans is encoded by the ''PPM1K'' gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''gene ...
, PPM1L, PPM1M, PPM1N * PPTC7 *
PTPMT1 Protein tyrosine phosphatase, mitochondrial 1 is a protein in humans that is primarily coded by the gene PTPMT1 gene In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredit ...
* SSU72 * UBLCP1


References

{{Portal bar, Biology, border=no Enzymes Post-translational modification Signal transduction