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Record Information
Version1.0
Creation Date2016-09-30 22:32:34 UTC
Update Date2020-05-11 22:28:07 UTC
BMDB IDBMDB0000547
Secondary Accession Numbers
  • BMDB00547
Metabolite Identification
Common NameMagnesium
DescriptionMagnesium, also known as magnesium ion or MG2+, belongs to the class of inorganic compounds known as homogeneous alkaline earth metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a alkaline earth metal atom. Magnesium exists as a solid, possibly soluble (in water), and possibly neutral molecule. Magnesium exists in all living species, ranging from bacteria to humans. Magnesium has been found to be associated with several diseases known as multiple sclerosis, alzheimer's disease, bartter syndrome, type 4a, neonatal, with sensorineural deafness, and bartter syndrome, type 3; also magnesium has been linked to the inborn metabolic disorders including primary hypomagnesemia.
Structure
Thumb
Synonyms
ValueSource
MAGNESIUM ionChEBI
Magnesium, doubly charged positive ionChEBI
Magnesium, ion (MG(2+))ChEBI
MG(2+)ChEBI
MG2+ChEBI
Magnesium(2+)Kegg
Magnesium ionsHMDB
Neuropeptide y (1-27)HMDB
Chemical FormulaMg
Average Molecular Weight24.305
Monoisotopic Molecular Weight23.985041898
IUPAC Namemagnesium(2+) ion
Traditional Namemagnesium(2+) ion
CAS Registry Number7439-95-4
SMILES
[Mg++]
InChI Identifier
InChI=1S/Mg/q+2
InChI KeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
Chemical Taxonomy
Description belongs to the class of inorganic compounds known as homogeneous alkaline earth metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a alkaline earth metal atom.
KingdomInorganic compounds
Super ClassHomogeneous metal compounds
ClassHomogeneous alkaline earth metal compounds
Sub ClassNot Available
Direct ParentHomogeneous alkaline earth metal compounds
Alternative ParentsNot Available
Substituents
  • Homogeneous alkaline earth metal
Molecular FrameworkNot Available
External Descriptors
Ontology
StatusDetected and Quantified
Origin
  • Exogenous
BiofunctionNot Available
ApplicationNot Available
Cellular locations
  • Cytoplasm
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point651 °CNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
logP-0.57ChemAxon
Physiological Charge2ChemAxon
Hydrogen Acceptor Count0ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area0 ŲChemAxon
Rotatable Bond Count0ChemAxon
Refractivity0 m³·mol⁻¹ChemAxon
Polarizability1.78 ųChemAxon
Number of Rings0ChemAxon
BioavailabilityYesChemAxon
Rule of FiveYesChemAxon
Ghose FilterNoChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleNoChemAxon
Spectra
SpectraNot Available
Biological Properties
Cellular Locations
  • Cytoplasm
Biospecimen Locations
  • Blood
  • Brain
  • Erythrocyte
  • Hair
  • Kidney
  • Leukocyte
  • Liver
  • Longissimus Thoracis Muscle
  • Milk
  • Platelet
  • Ruminal Fluid
  • Semimembranosus Muscle
  • Testis
Pathways
Normal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified1980 +/- 10 uMNot SpecifiedBothNormal details
BloodDetected and Quantified931+/-88 uMNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
BloodDetected and Quantified933.964 +/- 98.745 uMNot SpecifiedNot Specified
Normal
    • C. R. E. Cogginsa...
details
BrainExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
ErythrocyteExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
HairExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
KidneyExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
LeukocyteExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
LiverDetected and Quantified10+/-7 nmol/g of tissueNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
Longissimus Thoracis MuscleDetected and Quantified279+/-84 nmol/g of tissueNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
MilkDetected and Quantified4000 - 6000 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified4937.256 uMNot SpecifiedNot SpecifiedNormal
    • Park, Y. W; Juáre...
details
MilkDetected and Quantified4340.671 +/- 113.968 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified4570.664 +/- 95.0422 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified5272.989 +/- 105.740 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified5298.0868 +/- 102.0366 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified990.743 +/- 113.557 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified1074.265 +/- 65.419 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified1268.0518 +/- 54.310 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified1495.988 +/- 66.242 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified1588.562 +/- 63.773 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified3058.218 +/- 157.581 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified3266.406 +/- 90.928 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified3302.613 +/- 75.705 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified3709.525 +/- 93.396 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified3777.000617 +/- 97.0994 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified4048.961 +/- 197.490 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified4139 +/- 712 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5348.694 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5348.694 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4525.818 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4525.818 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified2057.19 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified6583.00761 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5760.132 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4525.818 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified6583.00761 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified6171.57 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4525.818 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4525.818 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4854.968 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4854.968 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5348.694 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified6583.00761 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5760.132 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified6171.57 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4525.818 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4525.818 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5019.543 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4978.4 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified5019.543 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4114.38 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4114.38 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4608.105 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified3815 +/- 255 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4566.962 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified3857 +/- 286 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4566.962 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4325 +/- 473 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4011 +/- 192 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4525.818 - 5348.694 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified4400 - 12100 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified4937.256 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified5727.628 - 37844.0650 uMNot SpecifiedNot SpecifiedNormal
    • Semaghiul Birghil...
details
PlateletExpected but not QuantifiedNot ApplicableNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
Ruminal FluidDetected and Quantified7465+/-3511 uMNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
Ruminal FluidDetected and Quantified102.0 +/- 6.0 uMNot SpecifiedNot Specified
Normal
    • Fozia Saleem, Sou...
details
Semimembranosus MuscleDetected and Quantified286+/-105 nmol/g of tissueNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
TestisDetected and Quantified70+/-23 nmol/g of tissueNot SpecifiedNot Specified
Normal
    • The Bovine Metabo...
details
Abnormal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
BloodDetected but not QuantifiedNot ApplicableNot SpecifiedNot Specified
Fatal bovine respiratory disease
details
HMDB IDHMDB0000547
DrugBank IDDB01378
Phenol Explorer Compound IDNot Available
FooDB IDFDB031004
KNApSAcK IDNot Available
Chemspider ID865
KEGG Compound IDC00305
BioCyc IDNot Available
BiGG IDNot Available
Wikipedia LinkMagnesium
METLIN IDNot Available
PubChem Compound888
PDB IDNot Available
ChEBI ID18420
References
Synthesis ReferenceNot Available
Material Safety Data Sheet (MSDS)Not Available
General References
  1. Zhang P, Allen JC: A novel dialysis procedure measuring free Zn2+ in bovine milk and plasma. J Nutr. 1995 Jul;125(7):1904-10. doi: 10.1093/jn/125.7.1904. [PubMed:7616307 ]
  2. Gaucheron F: The minerals of milk. Reprod Nutr Dev. 2005 Jul-Aug;45(4):473-83. doi: 10.1051/rnd:2005030. [PubMed:16045895 ]
  3. Tsioulpas A, Grandison AS, Lewis MJ: Changes in physical properties of bovine milk from the colostrum period to early lactation. J Dairy Sci. 2007 Nov;90(11):5012-7. doi: 10.3168/jds.2007-0192. [PubMed:17954740 ]
  4. Jensen HB, Poulsen NA, Andersen KK, Hammershoj M, Poulsen HD, Larsen LB: Distinct composition of bovine milk from Jersey and Holstein-Friesian cows with good, poor, or noncoagulation properties as reflected in protein genetic variants and isoforms. J Dairy Sci. 2012 Dec;95(12):6905-17. doi: 10.3168/jds.2012-5675. Epub 2012 Oct 3. [PubMed:23040012 ]
  5. Gaucheron F: Milk and dairy products: a unique micronutrient combination. J Am Coll Nutr. 2011 Oct;30(5 Suppl 1):400S-9S. [PubMed:22081685 ]
  6. Semaghiul Birghila, Simona Dobrinas, Gabriela Stanciu and Alina Soceanu (2008). Semaghiul Birghila, Simona Dobrinas, Gabriela Stanciu and Alina Soceanu. Determination of major and minor elements in milk through ICP-AES. Environmental Engineering and Management Journal. November/December 2008, Vol.7, No.6, 805-808. Environmental Engineering and Management Journal.
  7. Park, Y. W; Juárez, Manuela ; Ramos, M.; Haenlein, G. F. W. (2007). Park, Y. W; Juárez, Manuela ; Ramos, M.; Haenlein, G. F. W.. Physico-chemical characteristics of goat and sheep milk. Small Ruminant Res.(2007) 68:88-113 doi: 10.1016/j.smallrumres.2006.09.013. Small Ruminant Research.
  8. A. Foroutan et al. (2019). A. Foroutan et al. The Chemical Composition of Commercial Cow's Milk (in preparation). Journal of Agricultural and Food Chemistry.
  9. USDA Food Composition Databases [Link]
  10. Fooddata+, The Technical University of Denmark (DTU) [Link]

Only showing the first 50 proteins. There are 155 proteins in total.

Enzymes

General function:
Amino acid transport and metabolism
Specific function:
Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine (By similarity).
Gene Name:
SRR
Uniprot ID:
A0JNI4
Molecular weight:
36181.0
General function:
Involved in ATP binding
Specific function:
Kinase that can phosphorylate various inositol polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. Phosphorylates Ins(3,4,5,6)P4 at position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor of plasma membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5 is not. Also acts as an inositol polyphosphate phosphatase that dephosphorylate Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 to Ins(1,3,4)P3, and Ins(1,3,4,5,6)P5 to Ins(3,4,5,6)P4. May also act as an isomerase that interconverts the inositol tetrakisphosphate isomers Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 in the presence of ADP and magnesium. Probably acts as the rate-limiting enzyme of the InsP6 pathway. Modifies TNF-alpha-induced apoptosis by interfering with the activation of TNFRSF1A-associated death domain (By similarity). Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate (InsP6) pathway. Plays an important role in MLKL-mediated necroptosis. Produces highly phosphorylated inositol phosphates such as inositolhexakisphosphate (InsP6) which bind to MLKL mediating the release of an N-terminal auto-inhibitory region leading to its activation. Essential for activated phospho-MLKL to oligomerize and localize to the cell membrane during necroptosis (By similarity).
Gene Name:
ITPK1
Uniprot ID:
P0C0T1
Molecular weight:
45842.0
General function:
Coenzyme transport and metabolism
Specific function:
Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NaAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Involved in the synthesis of ATP in the nucleus, together with PARP1, PARG and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+) (By similarity). Protects against axonal degeneration following mechanical or toxic insults (By similarity).
Gene Name:
NMNAT1
Uniprot ID:
Q0VD50
Molecular weight:
32200.0
General function:
Coenzyme transport and metabolism
Specific function:
Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor (By similarity). Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency. Cannot use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NaAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+) (By similarity). Axon survival factor required for the maintenance of healthy axons: acts by delaying Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons (By similarity).
Gene Name:
NMNAT2
Uniprot ID:
Q0VC59
Molecular weight:
34468.0
General function:
Involved in calcium ion binding
Specific function:
Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix (ECM) degradation and remodeling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. Essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans. Acts as procoagulant by enhancing the generation of activated factor X/F10 in the presence of tissue factor/TF and activated factor VII/F7. Independent of its enzymatic activity, increases cell adhesion to the extracellular matrix (ECM). Enhances AKT1/PKB phosphorylation, possibly via interaction with a lipid raft-resident receptor. Plays a role in the regulation of osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis (By similarity).
Gene Name:
HPSE
Uniprot ID:
Q9MYY0
Molecular weight:
61077.0
General function:
Posttranslational modification, protein turnover, chaperones
Specific function:
ADP-ribose glycohydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on serine, free poly(ADP-ribose) and O-acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds. Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos. Also hydrolyzes free poly(ADP-ribose) in mitochondria. Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins. Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl-ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers.
Gene Name:
ADPRS
Uniprot ID:
Q3SYV9
Molecular weight:
39221.0
General function:
Involved in ADP-ribose diphosphatase activity
Specific function:
Hydrolyzes ADP-ribose, IDP-ribose, CDP-glycerol, CDP-choline and CDP-ethanolamine, but not other non-reducing ADP-sugars or CDP-glucose. May be involved in immune cell signaling as suggested by the second-messenger role of ADP-ribose, which activates TRPM2 as a mediator of oxidative/nitrosative stress (By similarity).
Gene Name:
ADPRM
Uniprot ID:
A7YY53
Molecular weight:
39235.0
General function:
Posttranslational modification, protein turnover, chaperones
Specific function:
Specifically acts as a arginine mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to arginine residues on proteins.
Gene Name:
ADPRH
Uniprot ID:
Q32KR8
Molecular weight:
39152.0
General function:
Inorganic ion transport and metabolism
Specific function:
This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.
Gene Name:
ATP1A1
Uniprot ID:
Q08DA1
Molecular weight:
112643.0
General function:
Involved in activin receptor activity
Specific function:
On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A. Mediates induction of adipogenesis by GDF6.
Gene Name:
ACVR2A
Uniprot ID:
Q28043
Molecular weight:
57952.0
General function:
Involved in 5'-nucleotidase activity
Specific function:
May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides.
Gene Name:
NT5C2
Uniprot ID:
O46411
Molecular weight:
64841.0
General function:
Carbohydrate transport and metabolism
Specific function:
Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations and probably participates in glycogen synthesis from carbohydrate precursors, such as lactate.
Gene Name:
FBP2
Uniprot ID:
Q2KJJ9
Molecular weight:
36767.0
General function:
Involved in activin receptor activity
Specific function:
Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor (By similarity).
Gene Name:
ACVR2B
Uniprot ID:
Q95126
Molecular weight:
57569.0
General function:
Inorganic ion transport and metabolism
Specific function:
This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Gene Name:
ATP2C1
Uniprot ID:
P57709
Molecular weight:
104780.0
General function:
Inorganic ion transport and metabolism
Specific function:
Not Available
Gene Name:
ATP9B
Uniprot ID:
A1A4J6
Molecular weight:
127457.0
General function:
Inorganic ion transport and metabolism
Specific function:
This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport of various nutrients (By similarity).
Gene Name:
ATP1A2
Uniprot ID:
A2VDL6
Molecular weight:
112179.0
General function:
Involved in ATP binding
Specific function:
In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well.
Gene Name:
ENTPD1
Uniprot ID:
O18956
Molecular weight:
58114.0
General function:
Coenzyme transport and metabolism
Specific function:
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Gene Name:
MAT2A
Uniprot ID:
A7E3T7
Molecular weight:
43691.0
General function:
Energy production and conversion
Specific function:
Catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA, the latter serving as common substrate for de novo cholesterol and fatty acid synthesis.
Gene Name:
ACLY
Uniprot ID:
Q32PF2
Molecular weight:
119789.0
General function:
Carbohydrate transport and metabolism
Specific function:
Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain.
Gene Name:
FBP1
Uniprot ID:
Q3SZB7
Molecular weight:
36728.0
General function:
Involved in ATP binding
Specific function:
Non-receptor tyrosine-protein and serine/threonine-protein kinase that is implicated in cell spreading and migration, cell survival, cell growth and proliferation. Transduces extracellular signals to cytosolic and nuclear effectors. Phosphorylates AKT1, AR, MCF2, WASL and WWOX. Implicated in trafficking and clathrin-mediated endocytosis through binding to epidermal growth factor receptor (EGFR) and clathrin. Binds to both poly- and mono-ubiquitin and regulates ligand-induced degradation of EGFR, thereby contributing to the accumulation of EGFR at the limiting membrane of early endosomes. Downstream effector of CDC42 which mediates CDC42-dependent cell migration via phosphorylation of BCAR1. May be involved both in adult synaptic function and plasticity and in brain development. Activates AKT1 by phosphorylating it on 'Tyr-176'. Phosphorylates AR on 'Tyr-267' and 'Tyr-363' thereby promoting its recruitment to androgen-responsive enhancers (AREs). Phosphorylates WWOX on 'Tyr-287'. Phosphorylates MCF2, thereby enhancing its activity as a guanine nucleotide exchange factor (GEF) toward Rho family proteins. Contributes to the control of AXL receptor levels. Confers metastatic properties on cancer cells and promotes tumor growth by negatively regulating tumor suppressor such as WWOX and positively regulating pro-survival factors such as AKT1 and AR (By similarity).
Gene Name:
TNK2
Uniprot ID:
Q17R13
Molecular weight:
114868.0
General function:
Inorganic ion transport and metabolism
Specific function:
Not Available
Gene Name:
ATP10D
Uniprot ID:
A7Z029
Molecular weight:
159526.0
General function:
Involved in magnesium ion binding
Specific function:
Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5. Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis. Plays an important role in hypaxial muscle development together with SIX1 and DACH2; in this it is functionally redundant with EYA1.
Gene Name:
EYA2
Uniprot ID:
Q58DB6
Molecular weight:
58807.0
General function:
Carbohydrate transport and metabolism
Specific function:
Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6 (By similarity).
Gene Name:
BPNT1
Uniprot ID:
Q3ZCK3
Molecular weight:
33328.0
General function:
Inorganic ion transport and metabolism
Specific function:
May play a role in the transport of aminophospholipids from the outer to the inner leaflet of various membranes and the maintenance of asymmetric distribution of phospholipids, mainly in secretory vesicles.
Gene Name:
ATP8A1
Uniprot ID:
Q29449
Molecular weight:
130026.0
General function:
Inorganic ion transport and metabolism
Specific function:
Not Available
Gene Name:
LOC100125266
Uniprot ID:
A6QQR9
Molecular weight:
57050.0
General function:
Involved in activin receptor activity, type I
Specific function:
On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for TGF-beta. May also bind activin.
Gene Name:
ACVR1
Uniprot ID:
Q28041
Molecular weight:
57190.0
General function:
Inorganic ion transport and metabolism
Specific function:
Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen (PubMed:22387132). Contributes to calcium sequestration involved in muscular excitation/contraction.
Gene Name:
ATP2A1
Uniprot ID:
Q0VCY0
Molecular weight:
109290.0
General function:
Energy production and conversion
Specific function:
Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
Gene Name:
ENOPH1
Uniprot ID:
Q0VD27
Molecular weight:
28930.0
General function:
Carbohydrate transport and metabolism
Specific function:
Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine (PubMed:15580268). Pyridoxal phosphate (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), with order of substrate preference PLP > PNP > PMP (By similarity).
Gene Name:
PDXP
Uniprot ID:
Q3ZBF9
Molecular weight:
31749.0
General function:
Involved in magnesium ion binding
Specific function:
Phosphatase that has high activity toward pyridoxal 5'-phosphate (PLP). Also active at much lower level toward pyrophosphate, phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine, fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate (By similarity).
Gene Name:
PHOSPHO2
Uniprot ID:
Q2KI06
Molecular weight:
27751.0
General function:
Lipid transport and metabolism
Specific function:
Critical branch point enzyme of isoprenoid biosynthesis that is thought to regulate the flux of isoprene intermediates through the sterol pathway.
Gene Name:
FDFT1
Uniprot ID:
Q32KR6
Molecular weight:
48304.0
General function:
Coenzyme transport and metabolism
Specific function:
Although its dehydrogenase activity is NAD-specific, it can also utilize NADP at a reduced efficiency.
Gene Name:
MTHFD2
Uniprot ID:
Q0P5C2
Molecular weight:
37767.0
General function:
Carbohydrate transport and metabolism
Specific function:
Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde, and the splitting of ribonucleoside diphosphate-X compounds among which FAD is the best substrate. Represses IFIH1-mediated cellular antiviral response.
Gene Name:
TKFC
Uniprot ID:
Q58DK4
Molecular weight:
59124.0
General function:
Lipid transport and metabolism
Specific function:
Catalyzes phosphatidylcholine biosynthesis from CDP-choline. It thereby plays a central role in the formation and maintenance of vesicular membranes (By similarity).
Gene Name:
CHPT1
Uniprot ID:
Q1LZE6
Molecular weight:
45249.0
General function:
Involved in ethanolaminephosphotransferase activity
Specific function:
Catalyzes phosphatidylethanolamine biosynthesis from CDP-ethanolamine. It thereby plays a central role in the formation and maintenance of vesicular membranes. Involved in the foramtion of phosphatidylethanolamine via 'Kennedy' pathway (By similarity).
Gene Name:
SELENOI
Uniprot ID:
Q17QM4
Molecular weight:
45214.0
General function:
Coenzyme transport and metabolism
Specific function:
Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Gene Name:
MAT1A
Uniprot ID:
Q2KJC6
Molecular weight:
43761.0
General function:
Involved in catechol O-methyltransferase activity
Specific function:
Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol (By similarity).
Gene Name:
COMT
Uniprot ID:
A7MBI7
Molecular weight:
30485.0
General function:
Secondary metabolites biosynthesis, transport and catabolism
Specific function:
Not Available
Gene Name:
FAH
Uniprot ID:
A5PKH3
Molecular weight:
46156.0
General function:
Involved in 3',5'-cyclic-GMP phosphodiesterase activity
Specific function:
Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP (PubMed:8530505). Specifically regulates nitric-oxide-generated cGMP (By similarity).
Gene Name:
PDE5A
Uniprot ID:
Q28156
Molecular weight:
98627.0
General function:
Nucleotide transport and metabolism
Specific function:
Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway (By similarity).
Gene Name:
HPRT1
Uniprot ID:
Q3SZ18
Molecular weight:
24498.0
General function:
Involved in galactosylceramide sulfotransferase activity
Specific function:
Transfers a sulfate to position 3 of non-reducing beta-galactosyl residues in N-glycans and core2-branched O-glycans. Has high activity towards Gal-beta-1,4-GlcNAc, Gal-beta-1,4(Fuc-alpha-1,3)GlcNAc and lower activity towards Gal-beta-1,3(Fuc-alpha-1,4)GlcNAc (By similarity).
Gene Name:
GAL3ST3
Uniprot ID:
Q0VCH4
Molecular weight:
48699.0
General function:
Signal transduction mechanisms
Specific function:
Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:2472670, PubMed:2022671. PubMed:19029295). Mediates responses to increased cellular Ca(2+)/calmodulin levels (PubMed:2022671, PubMed:19029295). May be involved in regulatory processes in the central nervous system. May play a role in memory and learning. Plays a role in the regulation of the circadian rhythm of daytime contrast sensitivity probably by modulating the rhythmic synthesis of cyclic AMP in the retina (By similarity).
Gene Name:
ADCY1
Uniprot ID:
P19754
Molecular weight:
123979.0
General function:
Involved in magnesium ion binding
Specific function:
3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization (By similarity). Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails (By similarity) (PubMed:10698948, PubMed:9736620). Also able to recognize poly(A) tails of microRNAs such as MIR21 and H/ACA box snoRNAs (small nucleolar RNAs) leading to microRNAs degradation or snoRNA increased stability (By similarity).
Gene Name:
PARN
Uniprot ID:
P69341
Molecular weight:
73182.0
General function:
Involved in hydrolase activity
Specific function:
RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.
Gene Name:
NUDT16
Uniprot ID:
A1A4Q9
Molecular weight:
21399.0
General function:
Replication, recombination and repair
Specific function:
Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate.
Gene Name:
NUDT11
Uniprot ID:
Q58CW0
Molecular weight:
18519.0
General function:
Carbohydrate transport and metabolism
Specific function:
This enzyme participates in both the breakdown and synthesis of glucose.
Gene Name:
PGM1
Uniprot ID:
Q08DP0
Molecular weight:
61589.0
General function:
Replication, recombination and repair
Specific function:
Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA (By similarity).
Gene Name:
APEX1
Uniprot ID:
P23196
Molecular weight:
35570.0
General function:
Energy production and conversion
Specific function:
Plays a role in intermediary metabolism and energy production. It may tightly associate or interact with the pyruvate dehydrogenase complex.
Gene Name:
IDH2
Uniprot ID:
Q04467
Molecular weight:
50739.0
General function:
Carbohydrate transport and metabolism
Specific function:
Not Available
Gene Name:
PKM
Uniprot ID:
B3IVN4
Molecular weight:
16527.0

Only showing the first 50 proteins. There are 155 proteins in total.