Record Information
Version1.0
Creation Date2016-09-30 22:43:51 UTC
Update Date2020-06-04 20:49:58 UTC
BMDB IDBMDB0001303
Secondary Accession Numbers
  • BMDB01303
Metabolite Identification
Common NameZinc
DescriptionZinc, also known as ZN2+ or zinc ion, belongs to the class of inorganic compounds known as homogeneous transition metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a transition metal atom. Zinc is possibly soluble (in water) and possibly neutral. Zinc exists in all living species, ranging from bacteria to humans. Zinc is a potentially toxic compound.
Structure
Thumb
Synonyms
ValueSource
Dietary zincChEBI
Zinc cationChEBI
ZINC ionChEBI
Zinc, ion (ZN2+)ChEBI
ZN(II)ChEBI
ZN(2+)ChEBI
ZN2+ChEBI
Mannosidase b, alphaMeSH
alpha Mannosidase bMeSH
alpha-D-Mannoside mannohydrolaseMeSH
Neutral alpha-mannosidaseMeSH
alpha D MannosidaseMeSH
alpha-D-MannosidaseMeSH
Lysosomal alpha-mannosidaseMeSH
Mannohydrolase, alpha-D-mannosideMeSH
alpha MannosidaseMeSH
alpha-MannosidaseMeSH
LAMANMeSH
Lysosomal alpha mannosidaseMeSH
Neutral alpha mannosidaseMeSH
alpha D Mannoside mannohydrolaseMeSH
alpha-Mannosidase, lysosomalMeSH
alpha-Mannosidase, neutralMeSH
Topostin bMeSH
Chemical FormulaZn
Average Molecular Weight65.409
Monoisotopic Molecular Weight63.929146578
IUPAC Namezinc(2+) ion
Traditional Namezinc(2+) ion
CAS Registry Number7440-66-6
SMILES
[Zn++]
InChI Identifier
InChI=1S/Zn/q+2
InChI KeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
Chemical Taxonomy
Description belongs to the class of inorganic compounds known as homogeneous transition metal compounds. These are inorganic compounds containing only metal atoms,with the largest atom being a transition metal atom.
KingdomInorganic compounds
Super ClassHomogeneous metal compounds
ClassHomogeneous transition metal compounds
Sub ClassNot Available
Direct ParentHomogeneous transition metal compounds
Alternative ParentsNot Available
Substituents
  • Homogeneous transition 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 PointNot AvailableNot Available
Boiling PointNot AvailableNot Available
Water SolubilityNot AvailableNot Available
LogPNot AvailableNot Available
Predicted Properties
PropertyValueSource
logP0.16ChemAxon
pKa (Strongest Acidic)3.09ChemAxon
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 FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Spectra
Spectra
Spectrum TypeDescriptionSplash Key
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-03di-9000000000-0cd08967c771fb645329View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-03di-9000000000-0cd08967c771fb645329View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-03di-9000000000-0cd08967c771fb645329View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-03di-9000000000-29976d3ebd17b2d11a4bView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-03di-9000000000-29976d3ebd17b2d11a4bView in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-03di-9000000000-29976d3ebd17b2d11a4bView in MoNA
Biological Properties
Cellular Locations
  • Cytoplasm
Biospecimen Locations
  • Blood
  • Brain
  • Erythrocyte
  • Liver
  • Milk
  • Ruminal Fluid
  • Testis
Pathways
Normal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified12 +/- 2 uMNot SpecifiedNot Specified
Normal
    • Aidin Foroutan, C...
details
BrainExpected but not QuantifiedNot QuantifiedNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
ErythrocyteExpected but not QuantifiedNot QuantifiedNot SpecifiedNot SpecifiedNormal
  • Not Applicable
details
LiverDetected and Quantified39 +/- 60 nmol/g of tissueNot SpecifiedNot Specified
Normal
    • Aidin Foroutan, C...
details
MilkDetected and Quantified81.0286 uMNot SpecifiedNot SpecifiedNormal
    • Park, Y. W; Juáre...
details
MilkDetected and Quantified70 +/- 16 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified55.0383 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified55.0383 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified64.211 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified61.154 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified58.096 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified68.798 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified61.154 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified64.211 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified68.798 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified62.683 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified44.306 +/- 1.911 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified64.211 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified20.578 +/- 1.468 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified64.211 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified49.733 +/- 3.134 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified63.294 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified18.713 +/- 1.162 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified63.294 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified20.945 +/- 1.177 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified58.096 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified15.518 +/- 2.920 uMNot SpecifiedNot Specified
Normal
    • Patricia Cava-Mon...
details
MilkDetected and Quantified68.798 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified61.154 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified62.683 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified73.384 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified73.384 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified62.683 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified62.683 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified61.154 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified62.683 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified45.865 - 61.154 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified56.567 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified56.567 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified71.856 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified64.0585 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified64.0585 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified54 +/- 8 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified65 +/- 5 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified69 +/- 6 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified65 +/- 3 uMNot SpecifiedNot Specified
Normal
details
MilkDetected and Quantified7.338 - 49.534 uMNot SpecifiedNot SpecifiedNormal
    • Semaghiul Birghil...
details
MilkDetected and Quantified45.865 +/- 3.0577 uMNot SpecifiedNot SpecifiedNormal details
MilkDetected and Quantified47.165 - 48.357 uMNot SpecifiedNot SpecifiedNormal
    • Z. Dobrzański, R....
details
Ruminal FluidDetected and Quantified2.39 +/- 0.51 uMNot SpecifiedNot Specified
Normal
    • Fozia Saleem, Sou...
details
Ruminal FluidDetected and Quantified10 +/- 3 uMNot SpecifiedNot Specified
Normal
    • Aidin Foroutan, C...
details
TestisDetected and Quantified4 +/- 1 nmol/g of tissueNot SpecifiedNot Specified
Normal
    • Aidin Foroutan, C...
details
Abnormal Concentrations
BiospecimenStatusValueAgeSexConditionReferenceDetails
BloodDetected but not QuantifiedNot QuantifiedNot SpecifiedNot Specified
Fatal bovine respiratory disease
details
HMDB IDHMDB0001303
DrugBank IDNot Available
Phenol Explorer Compound IDNot Available
FooDB IDFDB031256
KNApSAcK IDNot Available
Chemspider IDNot Available
KEGG Compound IDC00038
BioCyc IDNot Available
BiGG IDNot Available
Wikipedia LinkNot Available
METLIN IDNot Available
PubChem Compound32051
PDB IDNot Available
ChEBI ID29105
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. Campillo N, Vinas P, Lopez-Garcia I, Hernandez-Cordoba M: Direct determination of copper and zinc in cow milk, human milk and infant formula samples using electrothermal atomization atomic absorption spectrometry. Talanta. 1998 Aug;46(4):615-22. [PubMed:18967184 ]
  3. Gaucheron F: Milk and dairy products: a unique micronutrient combination. J Am Coll Nutr. 2011 Oct;30(5 Suppl 1):400S-9S. [PubMed:22081685 ]
  4. 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.
  5. Z. Dobrzański, R. Kołacz, H. Górecka, K. Chojnacka, A. Bartkowiak. (2005). Z. Dobrzański, R. Kołacz, H. Górecka, K. Chojnacka, A. Bartkowiak. 2005. The Content of Microelements and Trace Elements in Raw Milk from Cows in the Silesian Region. Pol. J. Environ. Stud. 14(5):685–689. Polish Journal of Environmental Studies.
  6. 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.
  7. 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.
  8. Patricia Cava-Montesinos, M. Luisa Cervera Agustín Pastor Miguel de la Guardia (2005). Patricia Cava-Montesinos, M. Luisa Cervera Agustín Pastor Miguel de la Guardia. 2005. Room temperature acid sonication ICP-MS multielemental analysis of milk.Analytica Chimica Acta Volume 531, Issue 1, Pages 111-123. Analytica Chimica Acta.
  9. USDA Food Composition Databases [Link]
  10. Fooddata+, The Technical University of Denmark (DTU) [Link]

Only showing the first 50 proteins. There are 389 proteins in total.

Enzymes

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:
Nucleotide transport and metabolism
Specific function:
Hydrolyzes extracellular nucleotides into membrane permeable nucleosides.
Gene Name:
NT5E
Uniprot ID:
Q05927
Molecular weight:
62966.0
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 metalloendopeptidase activity
Specific function:
Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (By similarity). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) (PubMed:10097139). Contributes to the normal cleavage of the cellular prion protein (By similarity). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (By similarity). Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (By similarity). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (By similarity). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Enhances the cleavage of CHL1 by BACE1 (By similarity). Cleaves NRCAM (By similarity). Cleaves TREM2, resulting in shedding of the TREM2 ectodomain (By similarity). Involved in the development and maturation of glomerular and coronary vasculature (By similarity). During development of the cochlear organ of Corti, promotes pillar cell separation by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions (By similarity). May regulate the EFNA5-EPHA3 signaling (By similarity).
Gene Name:
ADAM10
Uniprot ID:
Q10741
Molecular weight:
84188.0
General function:
Involved in histone-lysine N-methyltransferase activity
Specific function:
Not Available
Gene Name:
EHMT1
Uniprot ID:
A5PK11
Molecular weight:
138734.0
General function:
Replication, recombination and repair
Specific function:
Not Available
Gene Name:
Dnmt1
Uniprot ID:
B1P383
Molecular weight:
153086.0
General function:
Amino acid transport and metabolism
Specific function:
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
Gene Name:
LAP3
Uniprot ID:
P00727
Molecular weight:
56289.0
General function:
Amino acid transport and metabolism
Specific function:
Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage.
Gene Name:
CPE
Uniprot ID:
P04836
Molecular weight:
53309.0
General function:
Amino acid transport and metabolism
Specific function:
Not Available
Gene Name:
CPB1
Uniprot ID:
P00732
Molecular weight:
47348.0
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 (By similarity).
Gene Name:
ASPA
Uniprot ID:
P46446
Molecular weight:
35738.0
General function:
Amino acid transport and metabolism
Specific function:
Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II.
Gene Name:
ENPEP
Uniprot ID:
Q32LQ0
Molecular weight:
109801.0
General function:
Involved in cytidine deaminase activity
Specific function:
Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation (SHM), gene conversion, and class-switch recombination (CSR) in B-lymphocytes by deaminating C to U during transcription of Ig-variable (V) and Ig-switch (S) region DNA. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation.
Gene Name:
AICDA
Uniprot ID:
Q2PT36
Molecular weight:
24052.0
General function:
Inorganic ion transport and metabolism
Specific function:
Not Available
Gene Name:
SOD1
Uniprot ID:
A4URH1
Molecular weight:
10512.0
General function:
Inorganic ion transport and metabolism
Specific function:
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Gene Name:
ECSOD
Uniprot ID:
A3KLR9
Molecular weight:
26177.0
General function:
Amino acid transport and metabolism
Specific function:
Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
Gene Name:
DDAH1
Uniprot ID:
P56965
Molecular weight:
31289.0
General function:
Amino acid transport and metabolism
Specific function:
Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Catalyzes the production of N-lactoyl-amino acids from lactate and amino acids by reverse proteolysis.
Gene Name:
CNDP2
Uniprot ID:
Q3ZC84
Molecular weight:
52655.0
General function:
Involved in copper ion binding
Specific function:
Bifunctional enzyme that catalyzes the post-translational modification of inactive peptidylglycine precursors to the corresponding bioactive alpha-amidated peptides, a terminal modification in biosynthesis of many neural and endocrine peptides (PubMed:2059626). Alpha-amidation involves two sequential reactions, both of which are catalyzed by separate catalytic domains of the enzyme. The first step, catalyzed by peptidyl alpha-hydroxylating monoxygenase (PHM) domain, is the copper-, ascorbate-, and O2- dependent stereospecific hydroxylation (with S stereochemistry) at the alpha-carbon (C-alpha) of the C-terminal glycine of the peptidylglycine substrate (PubMed:2059626). The second step, catalyzed by the peptidylglycine amidoglycolate lyase (PAL) domain, is the zinc-dependent cleavage of the N-C-alpha bond, producing the alpha-amidated peptide and glyoxylate (PubMed:2059626). Similarly, catalyzes the two-step conversion of an N-fatty acylglycine to a primary fatty acid amide and glyoxylate (By similarity).
Gene Name:
PAM
Uniprot ID:
P10731
Molecular weight:
108177.0
General function:
Amino acid transport and metabolism
Specific function:
Polyol dehydrogenase that catalyzes the reversible NAD(+)-dependent oxidation of various sugar alcohols. Is mostly active with xylitol, D-sorbitol (D-glucitol) and L-iditol as substrates, leading to the C2-oxidized products D-xylulose, D-fructose and L-sorbose, respectively (PubMed:9143345). Is a key enzyme in the polyol pathway that interconverts glucose and fructose via sorbitol, which constitutes an important alternate route for glucose metabolism. May play a role in sperm motility by using sorbitol as an alternative energy source for sperm motility (By similarity). Cannot use NADP(+) as the electron acceptor. Has no activity on ethanol, methanol, glycerol, galactitol and fructose 6-phosphate (PubMed:9143345).
Gene Name:
SORD
Uniprot ID:
Q58D31
Molecular weight:
38099.0
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Gene Name:
METAP1
Uniprot ID:
A6QLA4
Molecular weight:
43183.0
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Gene Name:
METAP2
Uniprot ID:
Q3ZC89
Molecular weight:
52812.0
General function:
Involved in metalloendopeptidase activity
Specific function:
Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Cleaves aggrecan at the '392-Glu-|-Ala-393' site.
Gene Name:
ADAMTS4
Uniprot ID:
Q9TT93
Molecular weight:
90280.0
General function:
Involved in 3'-5' exonuclease activity
Specific function:
Nuclease involved in single-strand and double-strand DNA break repair. Recruited to sites of DNA damage through interaction with poly(ADP-ribose), a polymeric post-translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions. Displays apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro. Also able to introduce nicks at hydroxyuracil and other types of pyrimidine base damage. Together with PARP3, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ).
Gene Name:
APLF
Uniprot ID:
A0JNH9
Molecular weight:
54326.0
General function:
Replication, recombination and repair
Specific function:
Functions as a weak 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. Displays also double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes (By similarity).
Gene Name:
APEX2
Uniprot ID:
Q5E9N9
Molecular weight:
56938.0
General function:
Amino acid transport and metabolism
Specific function:
Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation.
Gene Name:
CPN1
Uniprot ID:
Q2KJ83
Molecular weight:
52669.0
General function:
Energy production and conversion
Specific function:
Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione. Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate. Class-III ADH is remarkably ineffective in oxidizing ethanol.
Gene Name:
ADH5
Uniprot ID:
Q3ZC42
Molecular weight:
39677.0
General function:
Involved in carboxypeptidase activity
Specific function:
Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety (By similarity).
Gene Name:
ACE
Uniprot ID:
P12820
Molecular weight:
10681.0
General function:
Inorganic ion transport and metabolism
Specific function:
Reversible hydration of carbon dioxide.
Gene Name:
CA1
Uniprot ID:
Q1LZA1
Molecular weight:
28822.0
General function:
Involved in ATP binding
Specific function:
Not Available
Gene Name:
PRKCZ
Uniprot ID:
A0JNH7
Molecular weight:
67733.0
General function:
Amino acid transport and metabolism
Specific function:
Not Available
Gene Name:
AP-B
Uniprot ID:
A2T1U6
Molecular weight:
71976.0
General function:
Involved in metalloendopeptidase activity
Specific function:
Cleaves aggrecan, a cartilage proteoglycan, at the '392-Glu-|-Ala-393' site, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. May play a role in proteolytic processing mostly during the peri-implantation period.
Gene Name:
ADAMTS5
Uniprot ID:
Q9TT92
Molecular weight:
22576.0
General function:
Involved in ATP binding
Specific function:
Not Available
Gene Name:
PRKCA
Uniprot ID:
B0JYP1
Molecular weight:
76793.0
General function:
Involved in carboxypeptidase activity
Specific function:
Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator (By similarity). Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. By cleavage of angiotensin II, may be an important regulator of heart function (By similarity). By cleavage of angiotensin II, may also have a protective role in acute lung injury (By similarity). Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 in intestine, regulating trafficking, expression on the cell surface, and its catalytic activity (By similarity).
Gene Name:
ACE2
Uniprot ID:
Q58DD0
Molecular weight:
93067.0
General function:
Involved in metallopeptidase activity
Specific function:
Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination.
Gene Name:
BRCC3
Uniprot ID:
A5PJP6
Molecular weight:
36152.0
General function:
Involved in DNA binding
Specific function:
E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The E3 ubiquitin-protein ligase activity is required for its tumor suppressor function. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for normal cell cycle progression from G2 to mitosis. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8. Acts as a transcriptional activator.
Gene Name:
BRCA1
Uniprot ID:
Q864U1
Molecular weight:
206279.0
General function:
Amino acid transport and metabolism
Specific function:
Not Available
Gene Name:
CPA1
Uniprot ID:
A6H6Y4
Molecular weight:
47010.0
General function:
Involved in metalloendopeptidase activity
Specific function:
Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. Could have a direct role in sperm-zona binding or migration of sperm from the uterus into the oviduct. Interactions with egg membrane could be mediated via binding between its disintegrin-like domain to one or more integrins receptors on the egg. This is a non catalytic metalloprotease-like protein (By similarity).
Gene Name:
ADAM2
Uniprot ID:
O77780
Molecular weight:
83150.0
General function:
Inorganic ion transport and metabolism
Specific function:
Reversible hydration of carbon dioxide. Its role in saliva is unknown.
Gene Name:
CA6
Uniprot ID:
P18915
Molecular weight:
37007.0
General function:
Involved in zinc ion binding
Specific function:
Not Available
Gene Name:
TIMM13
Uniprot ID:
A1A4M0
Molecular weight:
10470.0
General function:
Involved in calcium ion binding
Specific function:
Not Available
Gene Name:
MMP2
Uniprot ID:
A6QPN5
Molecular weight:
73834.0
General function:
Amino acid transport and metabolism
Specific function:
Not Available
Gene Name:
pCPB
Uniprot ID:
B1PZ69
Molecular weight:
47348.0
General function:
Involved in cysteine-type peptidase activity
Specific function:
Deubiquitinating enzyme involved in beta-2 adrenergic receptor (ADRB2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity).
Gene Name:
USP20
Uniprot ID:
A7Z056
Molecular weight:
101815.0
General function:
Involved in metalloendopeptidase activity
Specific function:
Cleaves the propeptides of type I and II collagen prior to fibril assembly (PubMed:7622483). Does not act on type III collagen (PubMed:7622483). Cleaves lysyl oxidase LOX at a site downstream of its propeptide cleavage site to produce a short LOX form with reduced collagen-binding activity (By similarity).
Gene Name:
ADAMTS2
Uniprot ID:
P79331
Molecular weight:
133888.0
General function:
Posttranslational modification, protein turnover, chaperones
Specific function:
ATP-dependent protease which is essential for axonal and neuron development. In neurons, mediates degradation of SMDT1/EMRE before its assembly with the uniporter complex, limiting the availability of SMDT1/EMRE for MCU assembly and promoting efficient assembly of gatekeeper subunits with MCU. Required for the maturation of paraplegin (SPG7) after its cleavage by mitochondrial-processing peptidase (MPP), converting it into a proteolytically active mature form. Required for the maturation of PINK1 into its 52kDa mature form after its cleavage by mitochondrial-processing peptidase (MPP) (By similarity).
Gene Name:
AFG3L2
Uniprot ID:
Q2KJI7
Molecular weight:
89388.0
General function:
Replication, recombination and repair
Specific function:
Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.
Gene Name:
TOP3A
Uniprot ID:
A0JN73
Molecular weight:
111512.0
General function:
Involved in ubiquitin thiolesterase activity
Specific function:
Not Available
Gene Name:
USP5
Uniprot ID:
A1L548
Molecular weight:
80066.0
General function:
Involved in cytochrome-c oxidase activity
Specific function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Gene Name:
COX5B
Uniprot ID:
P00428
Molecular weight:
13834.0
General function:
Translation, ribosomal structure and biogenesis
Specific function:
Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Has endonuclease activity, and functions as mRNA 3'-end-processing endonuclease. Also involved in the histone 3'-end pre-mRNA processing. U7 snRNP-dependent protein that induces both the 3'-endoribonucleolytic cleavage of histone pre-mRNAs and acts as a 5' to 3' exonuclease for degrading the subsequent downstream cleavage product (DCP) of mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3' sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the upstream fragment containing the stem loop (SL) and 5' phosphate on the downstream cleavage product (DCP) starting with CU nucleotides. The U7-dependent 5' to 3' exonuclease activity is processive and degrades the DCP RNA substrate even after complete removal of the U7-binding site. Binds to the downstream cleavage product (DCP) of histone pre-mRNAs and the cleaved DCP RNA substrate in a U7 snRNP dependent manner. Required for the selective processing of microRNAs (miRNAs) during embryonic stem cell differentiation via its interaction with ISY1 (By similarity). Required for the biogenesis of all miRNAs from the pri-miR-17-92 primary transcript except miR-92a (By similarity). Only required for the biogenesis of miR-290 and miR-96 from the pri-miR-290-295 and pri-miR-96-183 primary transcripts, respectively (By similarity).
Gene Name:
CPSF3
Uniprot ID:
P79101
Molecular weight:
77488.0
General function:
Amino acid transport and metabolism
Specific function:
Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin.
Gene Name:
CPB2
Uniprot ID:
Q2KIG3
Molecular weight:
48822.0
General function:
Involved in hydrolase activity, acting on carbon-nitrog
Specific function:
Probable C to U editing enzyme whose physiological substrate is not yet known. Does not display detectable apoB mRNA editing. Has a low intrinsic cytidine deaminase activity. May play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation.
Gene Name:
APOBEC2
Uniprot ID:
Q3SYR3
Molecular weight:
25962.0
General function:
Amino acid transport and metabolism
Specific function:
Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline (By similarity).
Gene Name:
BHMT
Uniprot ID:
Q5I597
Molecular weight:
44878.0

Only showing the first 50 proteins. There are 389 proteins in total.