Record Information
Version2.0
Creation Date2009-03-06 11:58:02 -0700
Update Date2014-11-04 15:48:37 -0700
Accession NumberT3D0074
Identification
Common NameZinc
ClassSmall Molecule
DescriptionA metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with anemia, short stature, hypogonadism, impaired wound healing, and geophagia. It is known by the symbol Zn.
Compound Type
  • Drug
  • Food Toxin
  • Household Toxin
  • Industrial/Workplace Toxin
  • Inorganic Compound
  • Metabolite
  • Metal
  • Natural Compound
  • Pollutant
  • Trace Element
  • Zinc Compound
Chemical Structure
Thumb
Synonyms
Synonym
Zinc (II) cation
Zinc ion
Zinc ion (Zn2+)
Zinc(2+)
Zinc(2+) ion
Zinc(II)
Zn
Zn(2+)
Zn2+
Chemical FormulaZn
Average Molecular Mass65.408 g/mol
Monoisotopic Mass63.928 g/mol
CAS Registry Number7440-66-6
IUPAC Namezinc(2+) ion
Traditional Namezinc(2+) ion
SMILES[Zn++]
InChI IdentifierInChI=1S/Zn/q+2
InChI KeyInChIKey=PTFCDOFLOPIGGS-UHFFFAOYSA-N
Chemical Taxonomy
KingdomInorganic Compounds
Super ClassHomogeneous Metal Compounds
ClassHomogeneous Transition Metal Compounds
Sub ClassNot Available
Direct ParentHomogeneous Transition Metal Compounds
Alternative Parents
Substituents
  • Inorganic Cation
  • Acyclic Compound
  • Homogeneous Transition Metal
Molecular FrameworkAcyclic Compounds
External Descriptors
  • Monoatomic Dication (ChEBI)
  • Divalent Metal Cation (ChEBI)
  • A Cation (MetaCyc)
  • Zinc Cation (ChEBI)
Biological Properties
StatusDetected and Not Quantified
OriginEndogenous
Cellular Locations
  • Cytoplasm
  • Extracellular
Biofluid LocationsNot Available
Tissue LocationsNot Available
PathwaysNot Available
ApplicationsNot Available
Biological Roles
Chemical RolesNot Available
Physical Properties
StateSolid
AppearanceBluish-white metallic solid.
Experimental Properties
PropertyValue
Melting Point419.5°C
Boiling Point908°C
SolubilityNot Available
LogPNot Available
Predicted Properties
PropertyValueSource
logP0.16ChemAxon
pKa (Strongest Acidic)3.09ChemAxon
Physiological Charge2ChemAxon
Hydrogen Acceptor Count0ChemAxon
Hydrogen Donor Count0ChemAxon
Polar Surface Area0 Å2ChemAxon
Rotatable Bond Count0ChemAxon
Refractivity0 m3·mol-1ChemAxon
Polarizability1.78 Å3ChemAxon
Spectra
SpectraNot Available
Toxicity Profile
Route of ExposureOral (4) ; inhalation (4) ; dermal (113)
Mechanism of ToxicityExcessive zinc intake alters copper and iron absorption, most likely through competitive binding in intestinal mucosal cells. Stomach acid dissolves metallic zinc, producing zinc chloride, which is a corrosive product damaging the stomach lining. Metal fume fever is thought to be an immune response to inhaled zinc. (3, 4, 1)
MetabolismZinc enters the body through the lungs, skin, and gastrointestinal tract. Intestinal absorption of zinc is controlled by zinc carrier protein CRIP and metallothioneins. Zinc is widely distributed in tissues and tissues fluids, and concentrated in the liver, gastrointestinal tract, kidney, skin, lung, brain, heart, and pancreas. Zinc binds to carbonic anhydrase in erythrocytes, and to albumin, α2-macroglobulin, and amino acids in the the plasma. Albumin and amino acid bound zinc can diffuse across tissue membranes. Zinc is excreted in the urine and faeces. (4)
Toxicity ValuesLD50: 630 mg/kg (Oral, Rat) (2)
Lethal DoseNot Available
Carcinogenicity (IARC Classification)Not Available
Uses/SourcesZinc has many commercial uses as coatings to prevent rust, in dry cell batteries, and can be mixed with other metals to produce alloys such as brass and bronze. Zinc compounds are widely used in industry to make paint, rubber, dyes, wood preservatives, and ointments. (4)
Minimum Risk LevelIntermediate Oral: 0.3 mg/kg/day (6) Chronic Oral: 0.3 mg/kg/day (6)
Health EffectsChronic exposure to zinc causes anemia, atazia, lethargy, and decreases the level of HDL (good) cholesterol in the body. It is also believed to cause pancreatic and reproductive damages. Unbalanced levels of copper and zinc binding to Cu,Zn-superoxide dismutase have been linked to amyotrophic lateral sclerosis (ALS). (4)
SymptomsIngestion of large doses of zinc causes stomach cramps, nausea, and vomiting. Acute inhalation of large amounts of zinc causes metal fume fever, which is characterized by chills, fever, headache, weakness, dryness of the nose and throat, chest pain, and coughing. Dermal contact with zinc results in skin irritation. (4)
TreatmentZinc poisoning is treated symptomatically, often by administering fluids such as water or milk, or with gastric lavage. (4)
Normal Concentrations
Not Available
Abnormal Concentrations
Not Available
DrugBank IDDB01593
HMDB IDHMDB15532
PubChem Compound ID23994
ChEMBL IDNot Available
ChemSpider ID22430
KEGG IDC00038
UniProt IDNot Available
OMIM ID103600 , 110900 , 113705 , 121300 , 125270 , 137164 , 138750 , 150330 , 163729 , 165240 , 180200 , 184757 , 188840 , 190080 , 191170 , 191290 , 194470 , 300414 , 300473 , 314998 , 600140 , 600310 , 600871 , 600993 , 601487 , 601757 , 601758 , 602432 , 602575 , 602630 , 603693 , 604386 , 604485 , 606829 , 607035 , 607102 , 607818 , 608072 , 608118
ChEBI ID30185
BioCyc IDZN%2b2
CTD IDD015032
Stitch IDZinc
PDB IDNot Available
ACToR ID6568
Wikipedia LinkZinc
References
Synthesis Reference

Robert Nicaise, “Production of zinc powder for electrochemical batteries.” U.S. Patent US4104188, issued 1877.

MSDSLink
General References
  1. Vonk WI, Klomp LW: Role of transition metals in the pathogenesis of amyotrophic lateral sclerosis. Biochem Soc Trans. 2008 Dec;36(Pt 6):1322-8. doi: 10.1042/BST0361322. [19021549 ]
  2. Ullmann's Encyclopedia of Industrial Chemistry (2003). 6th ed. Vol 1. Federal Republic of Germany: Wiley-VCH Verlag GmbH & Co.
  3. Wikipedia. Zinc. Last Updated 24 March 2009. [Link]
  4. ATSDR - Agency for Toxic Substances and Disease Registry (2005). Toxicological profile for zinc. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
  5. Wikipedia. Metallothionein. Last Updated 20 December 2008. [Link]
  6. ATSDR - Agency for Toxic Substances and Disease Registry (2001). Minimal Risk Levels (MRLs) for Hazardous Substances. U.S. Public Health Service in collaboration with U.S. Environmental Protection Agency (EPA). [Link]
Gene Regulation
Up-Regulated Genes
GeneGene SymbolGene IDInteractionChromosomeDetails
Down-Regulated Genes
GeneGene SymbolGene IDInteractionChromosomeDetails

Targets

General Function:
Involved in zinc ion transport
Specific Function:
Binds heavy metals. Contains three zinc and three copper atoms per polypeptide chain and only a negligible amount of cadmium. Inhibits survival and neurite formation of cortical neurons in vitro.
Gene Name:
MT3
Uniprot ID:
P25713
Molecular Weight:
6926.855 Da
References
  1. Hasler DW, Jensen LT, Zerbe O, Winge DR, Vasak M: Effect of the two conserved prolines of human growth inhibitory factor (metallothionein-3) on its biological activity and structure fluctuation: comparison with a mutant protein. Biochemistry. 2000 Nov 28;39(47):14567-75. [11087412 ]
  2. Palumaa P, Eriste E, Njunkova O, Pokras L, Jornvall H, Sillard R: Brain-specific metallothionein-3 has higher metal-binding capacity than ubiquitous metallothioneins and binds metals noncooperatively. Biochemistry. 2002 May 14;41(19):6158-63. [11994011 ]
  3. Palumaa P, Njunkova O, Pokras L, Eriste E, Jornvall H, Sillard R: Evidence for non-isostructural replacement of Zn(2+) with Cd(2+) in the beta-domain of brain-specific metallothionein-3. FEBS Lett. 2002 Sep 11;527(1-3):76-80. [12220637 ]
  4. Roschitzki B, Vasak M: Redox labile site in a Zn4 cluster of Cu4,Zn4-metallothionein-3. Biochemistry. 2003 Aug 19;42(32):9822-8. [12911326 ]
  5. Eriste E, Kruusel K, Palumaa P, Jornvall H, Sillard R: Purification of recombinant human apometallothionein-3 and reconstitution with zinc. Protein Expr Purif. 2003 Sep;31(1):161-5. [12963354 ]
  6. Zheng WJ, Wu F, Zhuang HQ, Lu C, Yang F, Ma WL, Hua ZC: Expression of human metallothionein III and its metalloabsorption capability in Escherichia coli. Prep Biochem Biotechnol. 2004 Aug;34(3):265-78. [15461142 ]
  7. Palumaa P, Tammiste I, Kruusel K, Kangur L, Jornvall H, Sillard R: Metal binding of metallothionein-3 versus metallothionein-2: lower affinity and higher plasticity. Biochim Biophys Acta. 2005 Mar 14;1747(2):205-11. Epub 2004 Dec 19. [15698955 ]
  8. Toriumi S, Saito T, Hosokawa T, Takahashi Y, Numata T, Kurasaki M: Metal binding ability of metallothionein-3 expressed in Escherichia coli. Basic Clin Pharmacol Toxicol. 2005 Apr;96(4):295-301. [15755312 ]
  9. Kameo S, Nakai K, Kurokawa N, Kanehisa T, Naganuma A, Satoh H: Metal components analysis of metallothionein-III in the brain sections of metallothionein-I and metallothionein-II null mice exposed to mercury vapor with HPLC/ICP-MS. Anal Bioanal Chem. 2005 Apr;381(8):1514-9. Epub 2005 Mar 22. [15782327 ]
General Function:
Involved in binding
Specific Function:
The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis
Gene Name:
APP
Uniprot ID:
P05067
Molecular Weight:
86944.0 Da
References
  1. Syme CD, Viles JH: Solution 1H NMR investigation of Zn2+ and Cd2+ binding to amyloid-beta peptide (Abeta) of Alzheimer's disease. Biochim Biophys Acta. 2006 Feb;1764(2):246-56. Epub 2005 Oct 14. [16266835 ]
  2. Adlard PA, Bush AI: Metals and Alzheimer's disease. J Alzheimers Dis. 2006 Nov;10(2-3):145-63. [17119284 ]
General Function:
Amino acid transport and metabolism
Specific Function:
Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it act as a scavenger of NAA from body fluids
Gene Name:
ASPA
Uniprot ID:
P45381
Molecular Weight:
35736.0 Da
References
  1. Herga S, Berrin JG, Perrier J, Puigserver A, Giardina T: Identification of the zinc binding ligands and the catalytic residue in human aspartoacylase, an enzyme involved in Canavan disease. FEBS Lett. 2006 Oct 30;580(25):5899-904. Epub 2006 Oct 2. [17027983 ]
  2. Bitto E, Bingman CA, Wesenberg GE, McCoy JG, Phillips GN Jr: Structure of aspartoacylase, the brain enzyme impaired in Canavan disease. Proc Natl Acad Sci U S A. 2007 Jan 9;104(2):456-61. Epub 2006 Dec 28. [17194761 ]
General Function:
Involved in negative regulation of growth
Specific Function:
Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
Gene Name:
MT1A
Uniprot ID:
P04731
Molecular Weight:
6120.19 Da
References
  1. Aravindakumar CT, Ceulemans J, De Ley M: Nitric oxide induces Zn2+ release from metallothionein by destroying zinc-sulphur clusters without concomitant formation of S-nitrosothiol. Biochem J. 1999 Nov 15;344 Pt 1:253-8. [10548558 ]
  2. Sutherland DE, Willans MJ, Stillman MJ: Supermetalation of the beta domain of human metallothionein 1a. Biochemistry. 2010 May 4;49(17):3593-601. doi: 10.1021/bi1003537. [20329713 ]
General Function:
Involved in negative regulation of growth
Specific Function:
Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
Gene Name:
MT2A
Uniprot ID:
P02795
Molecular Weight:
6042.05 Da
References
  1. Palumaa P, Tammiste I, Kruusel K, Kangur L, Jornvall H, Sillard R: Metal binding of metallothionein-3 versus metallothionein-2: lower affinity and higher plasticity. Biochim Biophys Acta. 2005 Mar 14;1747(2):205-11. Epub 2004 Dec 19. [15698955 ]
  2. Yang F, Zhou M, He Z, Liu X, Sun L, Sun Y, Chen Z: High-yield expression in Escherichia coli of soluble human MT2A with native functions. Protein Expr Purif. 2007 May;53(1):186-94. Epub 2006 Dec 15. [17224279 ]
General Function:
Involved in copper, zinc superoxide dismutase activity
Specific Function:
Destroys radicals which are normally produced within the cells and which are toxic to biological systems
Gene Name:
SOD1
Uniprot ID:
P00441
Molecular Weight:
15936.0 Da
References
  1. Vonk WI, Klomp LW: Role of transition metals in the pathogenesis of amyotrophic lateral sclerosis. Biochem Soc Trans. 2008 Dec;36(Pt 6):1322-8. doi: 10.1042/BST0361322. [19021549 ]
  2. Huang YH, Shih CM, Huang CJ, Lin CM, Chou CM, Tsai ML, Liu TP, Chiu JF, Chen CT: Effects of cadmium on structure and enzymatic activity of Cu,Zn-SOD and oxidative status in neural cells. J Cell Biochem. 2006 Jun 1;98(3):577-89. [16440303 ]
General Function:
Involved in viral process
Specific Function:
Induces CD27-mediated apoptosis. Inhibits BCL2L1 isoform Bcl-x(L) anti-apoptotic activity. Inhibits activation of NF-kappa-B and promotes T-cell receptor-mediated apoptosis.
Gene Name:
SIVA1
Uniprot ID:
O15304
Molecular Weight:
18694.45 Da
References
  1. Nestler M, Martin U, Hortschansky P, Saluz HP, Henke A, Munder T: The zinc containing pro-apoptotic protein siva interacts with the peroxisomal membrane protein pmp22. Mol Cell Biochem. 2006 Jul;287(1-2):147-55. Epub 2006 May 9. [16683188 ]
General Function:
Involved in sensory perception of pain
Specific Function:
This is a receptor for bradykinin. Could be a factor in chronic pain and inflammation.
Gene Name:
BDKRB1
Uniprot ID:
P46663
Molecular Weight:
40494.29 Da
References
  1. Ignjatovic T, Tan F, Brovkovych V, Skidgel RA, Erdos EG: Novel mode of action of angiotensin I converting enzyme inhibitors: direct activation of bradykinin B1 receptor. J Biol Chem. 2002 May 10;277(19):16847-52. Epub 2002 Mar 5. [11880373 ]
General Function:
Involved in beta2-adrenergic receptor activity
Specific Function:
Beta-adrenergic receptors mediate the catecholamine- induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine
Gene Name:
ADRB2
Uniprot ID:
P07550
Molecular Weight:
46557.0 Da
References
  1. Elling CE, Frimurer TM, Gerlach LO, Jorgensen R, Holst B, Schwartz TW: Metal ion site engineering indicates a global toggle switch model for seven-transmembrane receptor activation. J Biol Chem. 2006 Jun 23;281(25):17337-46. Epub 2006 Mar 27. [16567806 ]
General Function:
Involved in DNA binding
Specific Function:
Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression
Gene Name:
TP53
Uniprot ID:
P04637
Molecular Weight:
43654.0 Da
References
  1. Wang Y, Rosengarth A, Luecke H: Structure of the human p53 core domain in the absence of DNA. Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):276-81. Epub 2007 Feb 21. [17327663 ]
General Function:
Involved in superoxide metabolic process
Specific Function:
Delivers copper to copper zinc superoxide dismutase (SOD1).
Gene Name:
CCS
Uniprot ID:
O14618
Molecular Weight:
29040.445 Da
References
  1. Stasser JP, Eisses JF, Barry AN, Kaplan JH, Blackburn NJ: Cysteine-to-serine mutants of the human copper chaperone for superoxide dismutase reveal a copper cluster at a domain III dimer interface. Biochemistry. 2005 Mar 8;44(9):3143-52. [15736924 ]
General Function:
Involved in response to UV
Specific Function:
Involved in DNA excision repair. Initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region. Required for UV-induced CHEK1 phosphorylation and the recruitment of CEP164 to cyclobutane pyrimidine dimmers (CPD), sites of DNA damage after UV irradiation.
Gene Name:
XPA
Uniprot ID:
P23025
Molecular Weight:
31367.71 Da
References
  1. Blessing H, Kraus S, Heindl P, Bal W, Hartwig A: Interaction of selenium compounds with zinc finger proteins involved in DNA repair. Eur J Biochem. 2004 Aug;271(15):3190-9. [15265038 ]
General Function:
Involved in protein localization to microtubule
Specific Function:
Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination.
Gene Name:
MID1
Uniprot ID:
O15344
Molecular Weight:
75249.94 Da
References
  1. Massiah MA, Simmons BN, Short KM, Cox TC: Solution structure of the RBCC/TRIM B-box1 domain of human MID1: B-box with a RING. J Mol Biol. 2006 Apr 28;358(2):532-45. Epub 2006 Feb 20. [16529770 ]
General Function:
Involved in transcription factor activity
Specific Function:
Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues
Gene Name:
ESR1
Uniprot ID:
P03372
Molecular Weight:
66217.0 Da
References
  1. Payne JC, Rous BW, Tenderholt AL, Godwin HA: Spectroscopic determination of the binding affinity of zinc to the DNA-binding domains of nuclear hormone receptors. Biochemistry. 2003 Dec 9;42(48):14214-24. [14640689 ]
General Function:
Involved in establishment of epithelial cell polarity
Specific Function:
Keratin-binding protein required for epithelial cell polarization. Involved in apical junction complex (AJC) assembly via its interaction with PARD3. Required for ciliogenesis.
Gene Name:
FBF1
Uniprot ID:
Q8TES7
Molecular Weight:
125445.19 Da
References
  1. Enyedy EA, Horvath L, Gajda-Schrantz K, Galbacs G, Kiss T: An in vitro study of interactions between insulin-mimetic zinc(II) complexes and selected plasma components. J Inorg Biochem. 2006 Dec;100(12):1936-45. Epub 2006 Aug 30. [17034863 ]
General Function:
Chromatin structure and dynamics
Specific Function:
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes
Gene Name:
HDAC1
Uniprot ID:
Q13547
Molecular Weight:
55104.0 Da
References
  1. Bhuiyan MP, Kato T, Okauchi T, Nishino N, Maeda S, Nishino TG, Yoshida M: Chlamydocin analogs bearing carbonyl group as possible ligand toward zinc atom in histone deacetylases. Bioorg Med Chem. 2006 May 15;14(10):3438-46. Epub 2006 Jan 24. [16439135 ]
General Function:
Not Available
Specific Function:
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D
Gene Name:
HDAC4
Uniprot ID:
P56524
Molecular Weight:
119071.0 Da
References
  1. Bhuiyan MP, Kato T, Okauchi T, Nishino N, Maeda S, Nishino TG, Yoshida M: Chlamydocin analogs bearing carbonyl group as possible ligand toward zinc atom in histone deacetylases. Bioorg Med Chem. 2006 May 15;14(10):3438-46. Epub 2006 Jan 24. [16439135 ]
General Function:
Chromatin structure and dynamics
Specific Function:
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes
Gene Name:
HDAC8
Uniprot ID:
Q9BY41
Molecular Weight:
41758.0 Da
References
  1. Gantt SL, Gattis SG, Fierke CA: Catalytic activity and inhibition of human histone deacetylase 8 is dependent on the identity of the active site metal ion. Biochemistry. 2006 May 16;45(19):6170-8. [16681389 ]
General Function:
Not Available
Specific Function:
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
Gene Name:
INS
Uniprot ID:
P01308
Molecular Weight:
11981.0 Da
References
  1. Huus K, Havelund S, Olsen HB, van de Weert M, Frokjaer S: Chemical and thermal stability of insulin: effects of zinc and ligand binding to the insulin zinc-hexamer. Pharm Res. 2006 Nov;23(11):2611-20. Epub 2006 Sep 13. [16969698 ]
General Function:
Involved in interleukin-3 receptor binding
Specific Function:
This CSF induces granulocytes, macrophages, mast cells, stem cells, erythroid cells, eosinophils and megakaryocytes
Gene Name:
IL3
Uniprot ID:
P08700
Molecular Weight:
17233.0 Da
References
  1. Smit V, van Veelen PA, Tjaden UR, van der Greef J, Haaijman JJ: Human interleukin-3 contains a discontinuous zinc binding domain. Biochem Biophys Res Commun. 1992 Sep 16;187(2):859-66. [1530641 ]
General Function:
Involved in proteolysis and tissue remodeling
Specific Function:
May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond
Gene Name:
Not Available
Uniprot ID:
P14780
Molecular Weight:
78428.0 Da
References
  1. Martens E, Leyssen A, Van Aelst I, Fiten P, Piccard H, Hu J, Descamps FJ, Van den Steen PE, Proost P, Van Damme J, Liuzzi GM, Riccio P, Polverini E, Opdenakker G: A monoclonal antibody inhibits gelatinase B/MMP-9 by selective binding to part of the catalytic domain and not to the fibronectin or zinc binding domains. Biochim Biophys Acta. 2007 Feb;1770(2):178-86. Epub 2006 Oct 26. [17137715 ]
General Function:
Replication, recombination and repair
Specific Function:
Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. This is a suicide reaction:the enzyme is irreversibly inactivated
Gene Name:
MGMT
Uniprot ID:
P16455
Molecular Weight:
21646.0 Da
References
  1. Guengerich FP, Fang Q, Liu L, Hachey DL, Pegg AE: O6-alkylguanine-DNA alkyltransferase: low pKa and high reactivity of cysteine 145. Biochemistry. 2003 Sep 23;42(37):10965-70. [12974631 ]
General Function:
Involved in peptidoglycan catabolic process
Specific Function:
May play a scavenger role by digesting biologically active peptidoglycan (PGN) into biologically inactive fragments. Has no direct bacteriolytic activity.
Gene Name:
PGLYRP2
Uniprot ID:
Q96PD5
Molecular Weight:
62216.365 Da
References
  1. Wang ZM, Li X, Cocklin RR, Wang M, Wang M, Fukase K, Inamura S, Kusumoto S, Gupta D, Dziarski R: Human peptidoglycan recognition protein-L is an N-acetylmuramoyl-L-alanine amidase. J Biol Chem. 2003 Dec 5;278(49):49044-52. Epub 2003 Sep 23. [14506276 ]
General Function:
Involved in DNA binding
Specific Function:
Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks
Gene Name:
PARP1
Uniprot ID:
P09874
Molecular Weight:
113085.0 Da
References
  1. Mendes F, Groessl M, Nazarov AA, Tsybin YO, Sava G, Santos I, Dyson PJ, Casini A: Metal-based inhibition of poly(ADP-ribose) polymerase--the guardian angel of DNA. J Med Chem. 2011 Apr 14;54(7):2196-206. doi: 10.1021/jm2000135. Epub 2011 Mar 3. [21370912 ]
General Function:
Involved in vascular endothelial growth factor receptor-2 signaling pathway
Specific Function:
Calcium-binding protein required for T-cell receptor-, Fas-, and glucocorticoid-induced cell death. May mediate Ca(2+)-regulated signals along the death pathway (By similarity). Calcium-dependent adapter necessary for the association between PDCD6IP and TSG101. Interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity. May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphoprylation of the Akt signaling pathway. Seems to play a role in the regulation of the distribution and function of MCOLN1 in the endosomal pathway. Isoform 2 has a lower Ca(2+) affinity than isoform 1. Isoform 1 and, to a lesser extend, isoform 2, can stabilize SHISA5.
Gene Name:
PDCD6
Uniprot ID:
O75340
Molecular Weight:
21868.32 Da
References
  1. Suzuki H, Kawasaki M, Kakiuchi T, Shibata H, Wakatsuki S, Maki M: Crystallization and X-ray diffraction analysis of N-terminally truncated human ALG-2. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Nov 1;64(Pt 11):974-7. doi: 10.1107/S1744309108030297. Epub 2008 Oct 31. [18997320 ]
General Function:
Involved in calcium ion binding
Specific Function:
May act as a modulator against excess calcium accumulation in normal human mammary epithelial cells. May also play a role in suppressing tumor cell growth
Gene Name:
S100A2
Uniprot ID:
P29034
Molecular Weight:
11116.7 Da
References
  1. Koch M, Bhattacharya S, Kehl T, Gimona M, Vasak M, Chazin W, Heizmann CW, Kroneck PM, Fritz G: Implications on zinc binding to S100A2. Biochim Biophys Acta. 2007 Mar;1773(3):457-70. Epub 2006 Dec 19. [17239974 ]
General Function:
Involved in insemination
Specific Function:
Predominant protein in semen. It participates in the formation of a gel matrix entrapping the accessory gland secretions and ejaculated spermatozoa. Fragments of semenogelin and/or fragments of the related proteins may contribute to the activation of progressive sperm movements as the gel-forming proteins are fragmented by KLK3/PSA.Alpha-inhibin-92 and alpha-inhibin-31, derived from the proteolytic degradation of semenogelin, inhibit the secretion of pituitary follicle-stimulating hormone.
Gene Name:
SEMG1
Uniprot ID:
P04279
Molecular Weight:
52130.885 Da
References
  1. Jonsson M, Lundwall A, Linse S, Frohm B, Malm J: Truncated semenogelin I binds zinc and is cleaved by prostate-specific antigen. J Androl. 2006 Jul-Aug;27(4):542-7. Epub 2006 Apr 1. [16582407 ]
General Function:
Involved in ferric iron binding
Specific Function:
Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation
Gene Name:
TF
Uniprot ID:
P02787
Molecular Weight:
77050.0 Da
References
  1. Enyedy EA, Horvath L, Gajda-Schrantz K, Galbacs G, Kiss T: An in vitro study of interactions between insulin-mimetic zinc(II) complexes and selected plasma components. J Inorg Biochem. 2006 Dec;100(12):1936-45. Epub 2006 Aug 30. [17034863 ]