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Ceruloplasmin (EC 1.16.3.1) (Ferroxidase)

 CERU_HUMAN              Reviewed;        1065 AA.
P00450; Q14063; Q2PP18; Q9UKS4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
13-FEB-2019, entry version 214.
RecName: Full=Ceruloplasmin;
EC=1.16.3.1;
AltName: Full=Ferroxidase;
Flags: Precursor;
Name=CP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2873574; DOI=10.1073/pnas.83.14.5086;
Koschinsky M.L., Funk W.D., van Oost B.A., McGillivray R.T.A.;
"Complete cDNA sequence of human preceruloplasmin.";
Proc. Natl. Acad. Sci. U.S.A. 83:5086-5090(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1006.
PubMed=7702601; DOI=10.1006/bbrc.1995.1437;
Daimon M., Yamatani K., Igarashi M., Fukase N., Kawanami T., Kato T.,
Tominaga M., Sasaki H.;
"Fine structure of the human ceruloplasmin gene.";
Biochem. Biophys. Res. Commun. 208:1028-1035(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-40; 549-599; 784-829 AND 919-952.
PubMed=3755405; DOI=10.1016/0014-5793(86)80739-6;
Mercer J.F.B., Grimes A.;
"Isolation of a human ceruloplasmin cDNA clone that includes the N-
terminal leader sequence.";
FEBS Lett. 203:185-190(1986).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
Bingle C.D.;
"Cloning and functional analysis of the human ceruloplasmin gene
minimal promoter.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 218-1065.
PubMed=3486416; DOI=10.1073/pnas.83.10.3257;
Yang F., Naylor S.L., Lum J.B., Cutshaw S., McCombs J.L.,
Naberhaus K.H., McGill J.R., Adrian G.S., Moore C.M., Barnett D.R.,
Bowman B.H.;
"Characterization, mapping, and expression of the human ceruloplasmin
gene.";
Proc. Natl. Acad. Sci. U.S.A. 83:3257-3261(1986).
[7]
PROTEIN SEQUENCE OF 20-1065.
PubMed=6582496; DOI=10.1073/pnas.81.2.390;
Takahashi N., Ortel T.L., Putnam F.W.;
"Single-chain structure of human ceruloplasmin: the complete amino
acid sequence of the whole molecule.";
Proc. Natl. Acad. Sci. U.S.A. 81:390-394(1984).
[8]
PROTEIN SEQUENCE OF 158-333; 518-724 AND 858-1065.
PubMed=6571985; DOI=10.1073/pnas.80.1.115;
Takahashi N., Bauman R.A., Ortel T.L., Dwulet F.E., Wang C.-C.,
Putnam F.W.;
"Internal triplication in the structure of human ceruloplasmin.";
Proc. Natl. Acad. Sci. U.S.A. 80:115-119(1983).
[9]
PROTEIN SEQUENCE OF 501-905.
PubMed=6940148; DOI=10.1073/pnas.78.2.790;
Dwulet F.E., Putnam F.W.;
"Complete amino acid sequence of a 50,000-dalton fragment of human
ceruloplasmin.";
Proc. Natl. Acad. Sci. U.S.A. 78:790-794(1981).
[10]
PROTEIN SEQUENCE OF 907-1065.
PubMed=6987229;
Kingston I.B., Kingston B.L., Putnam F.W.;
"Primary structure of a histidine-rich proteolytic fragment of human
ceruloplasmin. I. Amino acid sequence of the cyanogen bromide
peptides.";
J. Biol. Chem. 255:2878-2885(1980).
[11]
PROTEIN SEQUENCE OF 907-1065.
PubMed=6987230;
Kingston I.B., Kingston B.L., Putnam F.W.;
"Primary structure of a histidine-rich proteolytic fragment of human
ceruloplasmin. II. Amino acid sequence of the tryptic peptides.";
J. Biol. Chem. 255:2886-2896(1980).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1007-1061.
PubMed=2355023;
Yang F.M., Friedrichs W.E., Cupples R.L., Banifacio M.J.,
Sanford J.A., Horton W.A., Bowman B.H.;
"Human ceruloplasmin. Tissue-specific expression of transcripts
produced by alternative splicing.";
J. Biol. Chem. 265:10780-10785(1990).
[13]
REVIEW.
PubMed=12055353; DOI=10.1146/annurev.nutr.22.012502.114457;
Hellman N.E., Gitlin J.D.;
"Ceruloplasmin metabolism and function.";
Annu. Rev. Nutr. 22:439-458(2002).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138.
TISSUE=Bile;
PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,
Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
"A proteomic analysis of human bile.";
Mol. Cell. Proteomics 3:715-728(2004).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-397 AND ASN-762.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358; ASN-397;
ASN-588; ASN-762 AND ASN-926.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358; ASN-397 AND
ASN-762.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[18]
GLYCOSYLATION AT ASN-138; ASN-358; ASN-397 AND ASN-762.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358 AND ASN-397,
AND STRUCTURE OF CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
PHOSPHORYLATION AT SER-722.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[22]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), DISULFIDE BONDS, AND
METAL-BINDING SITES.
Zaitseva I., Zaitsev V., Card G., Moshkov K., Bax B., Ralph A.,
Lindley P.;
"The X-ray structure of human serum ceruloplasmin at 3.1 A: nature of
the copper centres.";
J. Biol. Inorg. Chem. 1:15-23(1996).
[23]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), METAL-BINDING SITES, AND
DISULFIDE BONDS.
PubMed=17242517; DOI=10.1107/S090744490604947X;
Bento I., Peixoto C., Zaitsev V.N., Lindley P.F.;
"Ceruloplasmin revisited: structural and functional roles of various
metal cation-binding sites.";
Acta Crystallogr. D 63:240-248(2007).
[24]
VARIANTS THR-63; LEU-477; GLU-544; ILE-551; HIS-793 AND ARG-841.
PubMed=15557511; DOI=10.1212/01.WNL.0000144276.29988.C3;
Hochstrasser H., Bauer P., Walter U., Behnke S., Spiegel J., Csoti I.,
Zeiler B., Bornemann A., Pahnke J., Becker G., Riess O., Berg D.;
"Ceruloplasmin gene variations and substantia nigra hyperechogenicity
in Parkinson disease.";
Neurology 63:1912-1917(2004).
[25]
CHARACTERIZATION OF VARIANTS THR-63; GLU-544 AND HIS-793.
PubMed=16150804; DOI=10.1096/fj.04-3486fje;
Hochstrasser H., Tomiuk J., Walter U., Behnke S., Spiegel J.,
Krueger R., Becker G., Riess O., Berg D.;
"Functional relevance of ceruloplasmin mutations in Parkinson's
disease.";
FASEB J. 19:1851-1853(2005).
-!- FUNCTION: Ceruloplasmin is a blue, copper-binding (6-7 atoms per
molecule) glycoprotein. It has ferroxidase activity oxidizing
Fe(2+) to Fe(3+) without releasing radical oxygen species. It is
involved in iron transport across the cell membrane. Provides
Cu(2+) ions for the ascorbate-mediated deaminase degradation of
the heparan sulfate chains of GPC1. May also play a role in fetal
lung development or pulmonary antioxidant defense (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
EC=1.16.3.1;
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Note=Binds 6 Cu cations per monomer.;
-!- SUBCELLULAR LOCATION: Secreted. Note=Colocalizes with GCP1 in
secretory intracellular compartments. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- DISEASE: Aceruloplasminemia (ACERULOP) [MIM:604290]: An autosomal
recessive disorder of iron metabolism characterized by iron
accumulation in the brain as well as visceral organs. Clinical
features consist of the triad of retinal degeneration, diabetes
mellitus and neurological disturbances. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- DISEASE: Note=Ceruloplasmin levels are decreased in Wilson
disease, in which copper cannot be incorporated into ceruloplasmin
in liver because of defects in the copper-transporting ATPase 2.
-!- SIMILARITY: Belongs to the multicopper oxidase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Ceruloplasmin entry;
URL="https://en.wikipedia.org/wiki/Ceruloplasmin";
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EMBL; M13699; AAA51976.1; -; mRNA.
EMBL; DQ314867; ABC40726.1; -; Genomic_DNA.
EMBL; D45045; BAA08085.1; -; Genomic_DNA.
EMBL; D00025; BAA00019.1; -; mRNA.
EMBL; X04135; CAA27752.1; -; mRNA.
EMBL; X04136; CAA27753.1; -; mRNA.
EMBL; X04137; CAA27754.1; -; mRNA.
EMBL; X04138; CAA27755.1; -; mRNA.
EMBL; AF132978; AAF02483.1; -; Genomic_DNA.
EMBL; M13536; AAA51975.1; -; mRNA.
EMBL; J05506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS3141.1; -.
PIR; A25443; KUHU.
RefSeq; NP_000087.1; NM_000096.3.
UniGene; Hs.558314; -.
PDB; 1KCW; X-ray; 3.00 A; A=20-1065.
PDB; 2J5W; X-ray; 2.80 A; A=1-1065.
PDB; 4EJX; X-ray; 4.69 A; A=1-1065.
PDB; 4ENZ; X-ray; 2.60 A; A=1-1065.
PDBsum; 1KCW; -.
PDBsum; 2J5W; -.
PDBsum; 4EJX; -.
PDBsum; 4ENZ; -.
ProteinModelPortal; P00450; -.
SMR; P00450; -.
BioGrid; 107748; 10.
CORUM; P00450; -.
IntAct; P00450; 6.
STRING; 9606.ENSP00000264613; -.
DrugBank; DB00055; Drotrecogin alfa.
TCDB; 8.A.105.1.2; the multi-copper-containing ferrooxidase (mcfo) family.
CarbonylDB; P00450; -.
GlyConnect; 85; -.
iPTMnet; P00450; -.
PhosphoSitePlus; P00450; -.
UniCarbKB; P00450; -.
BioMuta; CP; -.
DMDM; 116117; -.
DOSAC-COBS-2DPAGE; P00450; -.
SWISS-2DPAGE; P00450; -.
EPD; P00450; -.
jPOST; P00450; -.
MaxQB; P00450; -.
PaxDb; P00450; -.
PeptideAtlas; P00450; -.
PRIDE; P00450; -.
ProteomicsDB; 51251; -.
Ensembl; ENST00000264613; ENSP00000264613; ENSG00000047457.
GeneID; 1356; -.
KEGG; hsa:1356; -.
UCSC; uc003ewy.6; human.
CTD; 1356; -.
DisGeNET; 1356; -.
EuPathDB; HostDB:ENSG00000047457.13; -.
GeneCards; CP; -.
GeneReviews; CP; -.
HGNC; HGNC:2295; CP.
HPA; CAB008591; -.
HPA; HPA001834; -.
MalaCards; CP; -.
MIM; 117700; gene.
MIM; 604290; phenotype.
neXtProt; NX_P00450; -.
Orphanet; 48818; Aceruloplasminemia.
PharmGKB; PA26815; -.
eggNOG; KOG1263; Eukaryota.
eggNOG; COG2132; LUCA.
HOGENOM; HOG000231499; -.
HOVERGEN; HBG003674; -.
InParanoid; P00450; -.
KO; K13624; -.
OrthoDB; 454773at2759; -.
PhylomeDB; P00450; -.
TreeFam; TF329807; -.
BioCyc; MetaCyc:HS00590-MONOMER; -.
BRENDA; 1.16.3.1; 2681.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-425410; Metal ion SLC transporters.
Reactome; R-HSA-5619060; Defective CP causes aceruloplasminemia (ACERULOP).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-917937; Iron uptake and transport.
SABIO-RK; P00450; -.
SIGNOR; P00450; -.
ChiTaRS; CP; human.
EvolutionaryTrace; P00450; -.
GeneWiki; Ceruloplasmin; -.
GenomeRNAi; 1356; -.
PMAP-CutDB; P00450; -.
PRO; PR:P00450; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000047457; Expressed in 185 organ(s), highest expression level in liver.
ExpressionAtlas; P00450; baseline and differential.
Genevisible; P00450; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
GO; GO:0005507; F:copper ion binding; IEA:InterPro.
GO; GO:0004322; F:ferroxidase activity; IBA:GO_Central.
GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
GO; GO:0055072; P:iron ion homeostasis; IBA:GO_Central.
GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
Gene3D; 2.60.40.420; -; 6.
InterPro; IPR027150; CP.
InterPro; IPR001117; Cu-oxidase.
InterPro; IPR011706; Cu-oxidase_2.
InterPro; IPR011707; Cu-oxidase_3.
InterPro; IPR033138; Cu_oxidase_CS.
InterPro; IPR002355; Cu_oxidase_Cu_BS.
InterPro; IPR008972; Cupredoxin.
PANTHER; PTHR44048:SF5; PTHR44048:SF5; 1.
Pfam; PF00394; Cu-oxidase; 1.
Pfam; PF07731; Cu-oxidase_2; 1.
Pfam; PF07732; Cu-oxidase_3; 2.
SUPFAM; SSF49503; SSF49503; 6.
PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Copper; Copper transport;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Ion transport; Metal-binding; Oxidoreductase; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Secreted; Signal; Transport.
SIGNAL 1 19 {ECO:0000269|PubMed:6582496}.
CHAIN 20 1065 Ceruloplasmin.
/FTId=PRO_0000002912.
DOMAIN 20 357 F5/8 type A 1.
DOMAIN 20 200 Plastocyanin-like 1.
DOMAIN 209 357 Plastocyanin-like 2.
DOMAIN 370 718 F5/8 type A 2.
DOMAIN 370 560 Plastocyanin-like 3.
DOMAIN 570 718 Plastocyanin-like 4.
DOMAIN 730 1061 F5/8 type A 3.
DOMAIN 730 900 Plastocyanin-like 5.
DOMAIN 908 1061 Plastocyanin-like 6.
METAL 120 120 Copper 1; type 2.
METAL 122 122 Copper 2; type 3.
METAL 180 180 Copper 2; type 3.
METAL 182 182 Copper 3; type 3.
METAL 295 295 Copper 4; type 1.
METAL 338 338 Copper 4; type 1.
METAL 343 343 Copper 4; type 1.
METAL 656 656 Copper 5; type 1.
METAL 699 699 Copper 5; type 1.
METAL 704 704 Copper 5; type 1.
METAL 709 709 Copper 5; type 1.
METAL 994 994 Copper 6; type 1.
METAL 997 997 Copper 1; type 2.
METAL 999 999 Copper 3; type 3.
METAL 1039 1039 Copper 3; type 3.
METAL 1040 1040 Copper 6; type 1.
METAL 1041 1041 Copper 2; type 3.
METAL 1045 1045 Copper 6; type 1.
METAL 1050 1050 Copper 6; type 1.
MOD_RES 722 722 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
CARBOHYD 138 138 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:15084671,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169}.
CARBOHYD 358 358 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169}.
CARBOHYD 397 397 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19838169}.
CARBOHYD 588 588 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 762 762 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 926 926 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 174 200 {ECO:0000305}.
DISULFID 276 357 {ECO:0000305}.
DISULFID 534 560 {ECO:0000305}.
DISULFID 637 718 {ECO:0000305}.
DISULFID 874 900 {ECO:0000305}.
VARIANT 63 63 I -> T (retained in the ER due to
impaired N-glycosylation; may present a
vulnerability factor for iron induced
oxidative stress in Parkinson disease).
{ECO:0000269|PubMed:15557511,
ECO:0000269|PubMed:16150804}.
/FTId=VAR_025655.
VARIANT 367 367 R -> C (in dbSNP:rs34624984).
/FTId=VAR_032815.
VARIANT 477 477 P -> L (in dbSNP:rs35331711).
{ECO:0000269|PubMed:15557511}.
/FTId=VAR_025656.
VARIANT 544 544 D -> E (reduced ferroxidase activity; may
present a vulnerability factor for iron
induced oxidative stress in Parkinson
disease; dbSNP:rs701753).
{ECO:0000269|PubMed:15557511,
ECO:0000269|PubMed:16150804}.
/FTId=VAR_025657.
VARIANT 551 551 T -> I. {ECO:0000269|PubMed:15557511}.
/FTId=VAR_025658.
VARIANT 793 793 R -> H. {ECO:0000269|PubMed:15557511,
ECO:0000269|PubMed:16150804}.
/FTId=VAR_025659.
VARIANT 841 841 T -> R (in dbSNP:rs56033670).
{ECO:0000269|PubMed:15557511}.
/FTId=VAR_025660.
CONFLICT 1060 1060 E -> EGEYP (in Ref. 6; AAA51975).
{ECO:0000305}.
STRAND 21 36 {ECO:0000244|PDB:4ENZ}.
TURN 49 52 {ECO:0000244|PDB:4ENZ}.
HELIX 53 56 {ECO:0000244|PDB:4ENZ}.
STRAND 58 61 {ECO:0000244|PDB:1KCW}.
STRAND 65 79 {ECO:0000244|PDB:4ENZ}.
STRAND 82 84 {ECO:0000244|PDB:1KCW}.
HELIX 88 90 {ECO:0000244|PDB:4ENZ}.
STRAND 97 100 {ECO:0000244|PDB:4ENZ}.
STRAND 104 111 {ECO:0000244|PDB:4ENZ}.
STRAND 113 115 {ECO:0000244|PDB:4ENZ}.
STRAND 120 125 {ECO:0000244|PDB:4ENZ}.
HELIX 128 130 {ECO:0000244|PDB:4ENZ}.
HELIX 141 144 {ECO:0000244|PDB:4ENZ}.
HELIX 145 147 {ECO:0000244|PDB:4ENZ}.
STRAND 154 160 {ECO:0000244|PDB:4ENZ}.
STRAND 173 180 {ECO:0000244|PDB:4ENZ}.
HELIX 185 190 {ECO:0000244|PDB:4ENZ}.
STRAND 194 200 {ECO:0000244|PDB:4ENZ}.
STRAND 205 210 {ECO:0000244|PDB:2J5W}.
STRAND 214 225 {ECO:0000244|PDB:4ENZ}.
HELIX 226 228 {ECO:0000244|PDB:4ENZ}.
HELIX 232 239 {ECO:0000244|PDB:4ENZ}.
HELIX 243 245 {ECO:0000244|PDB:4ENZ}.
HELIX 251 257 {ECO:0000244|PDB:4ENZ}.
STRAND 258 262 {ECO:0000244|PDB:4ENZ}.
STRAND 274 276 {ECO:0000244|PDB:4ENZ}.
STRAND 280 287 {ECO:0000244|PDB:4ENZ}.
STRAND 295 301 {ECO:0000244|PDB:4ENZ}.
STRAND 304 306 {ECO:0000244|PDB:4ENZ}.
STRAND 309 312 {ECO:0000244|PDB:4ENZ}.
STRAND 321 327 {ECO:0000244|PDB:4ENZ}.
STRAND 332 338 {ECO:0000244|PDB:4ENZ}.
HELIX 341 344 {ECO:0000244|PDB:4ENZ}.
TURN 345 347 {ECO:0000244|PDB:4ENZ}.
STRAND 349 355 {ECO:0000244|PDB:4ENZ}.
STRAND 367 385 {ECO:0000244|PDB:4ENZ}.
TURN 392 394 {ECO:0000244|PDB:4ENZ}.
STRAND 401 403 {ECO:0000244|PDB:1KCW}.
HELIX 406 409 {ECO:0000244|PDB:4ENZ}.
STRAND 412 414 {ECO:0000244|PDB:1KCW}.
STRAND 418 427 {ECO:0000244|PDB:4ENZ}.
STRAND 429 435 {ECO:0000244|PDB:4ENZ}.
HELIX 444 446 {ECO:0000244|PDB:4ENZ}.
STRAND 453 456 {ECO:0000244|PDB:4ENZ}.
STRAND 459 471 {ECO:0000244|PDB:4ENZ}.
STRAND 476 481 {ECO:0000244|PDB:4ENZ}.
HELIX 484 486 {ECO:0000244|PDB:4ENZ}.
STRAND 514 520 {ECO:0000244|PDB:4ENZ}.
TURN 523 525 {ECO:0000244|PDB:4ENZ}.
STRAND 529 531 {ECO:0000244|PDB:2J5W}.
STRAND 533 540 {ECO:0000244|PDB:4ENZ}.
STRAND 542 544 {ECO:0000244|PDB:2J5W}.
HELIX 545 551 {ECO:0000244|PDB:4ENZ}.
STRAND 554 560 {ECO:0000244|PDB:4ENZ}.
STRAND 575 580 {ECO:0000244|PDB:4ENZ}.
STRAND 582 586 {ECO:0000244|PDB:4ENZ}.
HELIX 587 589 {ECO:0000244|PDB:4ENZ}.
HELIX 593 600 {ECO:0000244|PDB:4ENZ}.
HELIX 604 606 {ECO:0000244|PDB:4ENZ}.
HELIX 612 617 {ECO:0000244|PDB:4ENZ}.
STRAND 619 623 {ECO:0000244|PDB:4ENZ}.
STRAND 635 637 {ECO:0000244|PDB:4ENZ}.
STRAND 642 647 {ECO:0000244|PDB:4ENZ}.
STRAND 656 660 {ECO:0000244|PDB:4ENZ}.
STRAND 665 667 {ECO:0000244|PDB:4ENZ}.
STRAND 670 677 {ECO:0000244|PDB:4ENZ}.
STRAND 682 687 {ECO:0000244|PDB:4ENZ}.
STRAND 693 699 {ECO:0000244|PDB:4ENZ}.
HELIX 702 706 {ECO:0000244|PDB:4ENZ}.
STRAND 710 716 {ECO:0000244|PDB:4ENZ}.
STRAND 729 745 {ECO:0000244|PDB:4ENZ}.
HELIX 750 759 {ECO:0000244|PDB:4ENZ}.
TURN 766 768 {ECO:0000244|PDB:4ENZ}.
TURN 771 773 {ECO:0000244|PDB:4ENZ}.
STRAND 777 789 {ECO:0000244|PDB:4ENZ}.
HELIX 800 805 {ECO:0000244|PDB:4ENZ}.
STRAND 812 815 {ECO:0000244|PDB:4ENZ}.
STRAND 818 826 {ECO:0000244|PDB:4ENZ}.
STRAND 828 830 {ECO:0000244|PDB:4ENZ}.
STRAND 835 838 {ECO:0000244|PDB:4ENZ}.
STRAND 842 844 {ECO:0000244|PDB:1KCW}.
STRAND 854 860 {ECO:0000244|PDB:4ENZ}.
HELIX 863 865 {ECO:0000244|PDB:4ENZ}.
STRAND 869 871 {ECO:0000244|PDB:1KCW}.
STRAND 873 880 {ECO:0000244|PDB:4ENZ}.
HELIX 885 890 {ECO:0000244|PDB:4ENZ}.
STRAND 894 900 {ECO:0000244|PDB:4ENZ}.
STRAND 913 924 {ECO:0000244|PDB:4ENZ}.
HELIX 925 927 {ECO:0000244|PDB:4ENZ}.
HELIX 931 938 {ECO:0000244|PDB:4ENZ}.
HELIX 942 944 {ECO:0000244|PDB:4ENZ}.
HELIX 950 955 {ECO:0000244|PDB:4ENZ}.
STRAND 957 961 {ECO:0000244|PDB:4ENZ}.
STRAND 973 975 {ECO:0000244|PDB:4ENZ}.
STRAND 979 986 {ECO:0000244|PDB:4ENZ}.
STRAND 994 998 {ECO:0000244|PDB:4ENZ}.
STRAND 1003 1006 {ECO:0000244|PDB:4ENZ}.
HELIX 1007 1009 {ECO:0000244|PDB:4ENZ}.
STRAND 1011 1018 {ECO:0000244|PDB:4ENZ}.
STRAND 1023 1028 {ECO:0000244|PDB:4ENZ}.
STRAND 1034 1040 {ECO:0000244|PDB:4ENZ}.
HELIX 1043 1047 {ECO:0000244|PDB:4ENZ}.
STRAND 1051 1057 {ECO:0000244|PDB:4ENZ}.
SEQUENCE 1065 AA; 122205 MW; 2F2F1294E2D30F58 CRC64;
MKILILGIFL FLCSTPAWAK EKHYYIGIIE TTWDYASDHG EKKLISVDTE HSNIYLQNGP
DRIGRLYKKA LYLQYTDETF RTTIEKPVWL GFLGPIIKAE TGDKVYVHLK NLASRPYTFH
SHGITYYKEH EGAIYPDNTT DFQRADDKVY PGEQYTYMLL ATEEQSPGEG DGNCVTRIYH
SHIDAPKDIA SGLIGPLIIC KKDSLDKEKE KHIDREFVVM FSVVDENFSW YLEDNIKTYC
SEPEKVDKDN EDFQESNRMY SVNGYTFGSL PGLSMCAEDR VKWYLFGMGN EVDVHAAFFH
GQALTNKNYR IDTINLFPAT LFDAYMVAQN PGEWMLSCQN LNHLKAGLQA FFQVQECNKS
SSKDNIRGKH VRHYYIAAEE IIWNYAPSGI DIFTKENLTA PGSDSAVFFE QGTTRIGGSY
KKLVYREYTD ASFTNRKERG PEEEHLGILG PVIWAEVGDT IRVTFHNKGA YPLSIEPIGV
RFNKNNEGTY YSPNYNPQSR SVPPSASHVA PTETFTYEWT VPKEVGPTNA DPVCLAKMYY
SAVDPTKDIF TGLIGPMKIC KKGSLHANGR QKDVDKEFYL FPTVFDENES LLLEDNIRMF
TTAPDQVDKE DEDFQESNKM HSMNGFMYGN QPGLTMCKGD SVVWYLFSAG NEADVHGIYF
SGNTYLWRGE RRDTANLFPQ TSLTLHMWPD TEGTFNVECL TTDHYTGGMK QKYTVNQCRR
QSEDSTFYLG ERTYYIAAVE VEWDYSPQRE WEKELHHLQE QNVSNAFLDK GEFYIGSKYK
KVVYRQYTDS TFRVPVERKA EEEHLGILGP QLHADVGDKV KIIFKNMATR PYSIHAHGVQ
TESSTVTPTL PGETLTYVWK IPERSGAGTE DSACIPWAYY STVDQVKDLY SGLIGPLIVC
RRPYLKVFNP RRKLEFALLF LVFDENESWY LDDNIKTYSD HPEKVNKDDE EFIESNKMHA
INGRMFGNLQ GLTMHVGDEV NWYLMGMGNE IDLHTVHFHG HSFQYKHRGV YSSDVFDIFP
GTYQTLEMFP RTPGIWLLHC HVTDHIHAGM ETTYTVLQNE DTKSG


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Related Genes :
[CP] Ceruloplasmin (EC 1.16.3.1) (Ferroxidase)
[Cp] Ceruloplasmin (EC 1.16.3.1) (Ferroxidase)
[Cp] Ceruloplasmin (EC 1.16.3.1) (Ferroxidase)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CRD98_26150 D3I61_11545 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTL84_23375 DTM25_06080 EC95NR1_00961 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 SAMEA3753106_00003 SAMEA3753391_00513 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[al-2 B22I21.230 NCU00585] Bifunctional lycopene cyclase/phytoene synthase (Protein albino-2) [Includes: Lycopene beta-cyclase (EC 5.5.1.19) (Carotene cyclase) (Lycopene cyclase); Phytoene synthase (EC 2.5.1.32)]
[al-3 B8P8.010 NCU01427] Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Albino-3 protein) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[dim-5 29E8.110 NCU04402] Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.43) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[CP] Ceruloplasmin (EC 1.16.3.1) (Ferroxidase)
[Or22a AN11 DOR22A.1 dor53 Or22A.1 CG12193] Odorant receptor 22a
[pyrG A6592_02570 A8M42_16405 A9R57_06965 AC067_22330 AC789_1c31020 ACN002_2797 ACN77_07080 ACN81_20385 ACU57_24415 ACU90_23015 AJ318_22735 AKG99_03555 AM270_00945 AM446_06950 AM464_05605 AM465_10605 AML07_12460 AML35_05300 APT94_17890 APU18_18535 APZ14_09290 ARC77_10140 AU473_08010 AUQ13_17535 AUS26_15660 AW059_10675 AW106_00665 AWP75_20610 AZZ83_003241 B1K96_20050 B7C53_10055 B9M99_21725 B9N33_09475 B9T59_19685 BB545_13920 BE963_03670 BEN53_16995 BET08_07180 BH694_13410 BHF46_05050 BHS81_16640 BHS87_15735 BIQ87_15835 BIU72_09520 BIZ41_16885 BJJ90_05265 BK248_12970 BK292_23205 BK334_11935 BK373_15870 BK375_10085 BK383_11680 BK400_05820 BMT49_17330 BMT53_21250 BMT91_11105 BN17_26661 BTQ04_11510 BTQ06_23845 BUE81_06975 BVL39_12970 BW690_04975 BWP17_05185 BXT93_24405 BZL31_00820 BZL69_02125 C1I57_04860 C2M16_17770 C2U48_20025 C3K24_08940 C4J69_11655 C4K41_05275 C4M78_00835 C5715_23540 C5N07_06155 C5P01_05005 C5P43_15935 C5P44_09340 C6669_14670 C6986_17750 C6B13_03370 C7235_05745 C7B02_19400 C7B06_11630 C7B07_14530 C7B08_01430 C9E25_03325 CA593_12975 CCZ14_04445 CCZ17_10850 CDL37_13440 CG691_07365 CG692_07005 CG705_05530 CG706_07860 CIJ94_12220 COD30_01795 COD46_07095 CR538_05495 CR539_18815 CRE06_03485 CRM83_26360 CSB64_15850 CT143_09630 CT146_00680 CV83915_03339 CVH05_06295 CWM24_00790 CWS33_03125 CXB56_08765 D0X26_06660 D1900_12730 D2183_19100 D2F89_14380 D3I61_16000 DD762_13665 DIV22_29760 DIV25_29790 DL545_05995 DL800_20505 DNQ41_18960 DNR41_08670 DQE83_04685 DS732_20695 DS966_06010 DTL43_09355 DTL84_00105 DTL90_02675 DTM10_03745 DTM25_22630 DTM27_13675 DTM45_13530 EC1094V2_904 EC3234A_48c00890 EC95NR1_02021 ECONIH1_15890 ECs3640 EL75_0914 EL79_0915 EL80_0918 ERS085365_02427 ERS085366_03042 ERS085374_03279 ERS085386_03410 ERS085416_02898 ERS139211_02072 ERS150873_02003 ERS150876_01467 FORC28_1110 GJ11_18025 HMPREF3040_01161 HW43_18180 JD73_16335 MJ49_17095 MS6198_30910 MS8345_02965 NCTC10082_03473 NCTC10090_04050 NCTC10418_01701 NCTC10764_00296 NCTC10766_00690 NCTC10767_02309 NCTC11022_02860 NCTC11112_00121 NCTC11181_03277 NCTC12950_01251 NCTC13125_04353 NCTC13127_01436 NCTC13462_04807 NCTC13846_01212 NCTC7152_00995 NCTC7927_01209 NCTC8500_01090 NCTC8960_03783 NCTC9007_03892 NCTC9010_01168 NCTC9036_01135 NCTC9037_01243 NCTC9045_01221 NCTC9050_04166 NCTC9058_00847 NCTC9062_02131 NCTC9075_01630 NCTC9077_01409 NCTC9081_05851 NCTC9117_01609 NCTC9119_01271 NCTC9434_01004 NCTC9706_03296 NCTC9775_04845 NCTC9777_02704 NCTC9969_01292 PU06_02080 RG28_07675 RK56_023165 SAMEA3472033_01264 SAMEA3472044_02272 SAMEA3472047_00339 SAMEA3472056_05455 SAMEA3472067_02540 SAMEA3472070_01673 SAMEA3472080_03155 SAMEA3472090_00131 SAMEA3472108_00527 SAMEA3472110_03462 SAMEA3472112_03722 SAMEA3472114_02432 SAMEA3472147_03296 SAMEA3484427_03298 SAMEA3484429_03415 SAMEA3484433_01660 SAMEA3484434_01581 SAMEA3485101_02257 SAMEA3485113_02257 SAMEA3752372_03639 SAMEA3752557_03040 SAMEA3752559_02995 SAMEA3752620_01282 SAMEA3753064_02287 SAMEA3753097_02219 SAMEA3753106_03183 SAMEA3753164_01192 SAMEA3753290_02847 SAMEA3753300_01107 SAMEA3753391_02580 SAMEA3753397_04005 SK85_03024 SY51_15605 UC41_20365 UN91_03645 WM48_14990 WQ89_10170 WR15_06090 YDC107_1339] CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
[AHK4 CRE1 RAW1 WOL At2g01830 T23K3.2] Histidine kinase 4 (EC 2.7.13.3) (Arabidopsis histidine kinase 4) (AtHK4) (Cytokinin receptor CYTOKININ RESPONSE 1) (AtCRE1) (Cytokinin receptor CRE1) (Phosphoprotein phosphatase AHK4) (EC 3.1.3.16) (Protein AUTHENTIC HIS-KINASE 4) (Protein ROOT AS IN WOL 1) (Protein WOODEN LEG)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[ppnP OR16_09104] Pyrimidine/purine nucleoside phosphorylase (EC 2.4.2.1) (EC 2.4.2.2) (Adenosine phosphorylase) (Cytidine phosphorylase) (Guanosine phosphorylase) (EC 2.4.2.15) (Inosine phosphorylase) (Thymidine phosphorylase) (EC 2.4.2.4) (Uridine phosphorylase) (EC 2.4.2.3) (Xanthosine phosphorylase)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

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