ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P00450


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CERU_HUMAN
Primary accession number P00450
Secondary accession numbers Q14063 Q2PP18 Q9UKS4
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on August 13, 1987 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 113)
Name and origin of the protein
Protein name Ceruloplasmin [Precursor]
Synonyms EC 1.16.3.1
Ferroxidase
Gene name
Name: CP
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2873574 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1006/bbrc.1995.1437; PubMed=7702601 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/0014-5793(86)80739-6; PubMed=3755405 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1146/annurev.nutr.22.012502.114457; PubMed=12055353 [NCBI, ExPASy, EBI, Israel, Japan]
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, AND MASS SPECTROMETRY.
TISSUE=Bile;
DOI=10.1074/mcp.M400015-MCP200; PubMed=15084671 [NCBI, ExPASy, EBI, Israel, Japan]
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, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1002/pmic.200300556; PubMed=14760718 [NCBI, ExPASy, EBI, Israel, Japan]
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, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-784 AND TYR-787, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[19]
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).
[20]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), METAL-BINDING SITES, AND DISULFIDE BONDS.
DOI=10.1107/S090744490604947X; PubMed=17242517 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[21]
VARIANTS THR-63; LEU-477; GLU-544; ILE-551; HIS-793 AND ARG-841.
PubMed=15557511 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[22]
CHARACTERIZATION OF VARIANTS THR-63; GLU-544 AND HIS-793.
DOI=10.1096/fj.04-3486fje; PubMed=16150804 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M13699; AAA51976.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ314867; ABC40726.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D45045; BAA08085.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D00025; BAA00019.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04135; CAA27752.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04136; CAA27753.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04137; CAA27754.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X04138; CAA27755.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF132978; AAF02483.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M13536; AAA51975.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J05506; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
PIR A25443; KUHU.
RefSeq NP_000087.1; -.
UniGene Hs.558314
3D structure databases
PDB
1KCW; X-ray; 3.00 A; A=20-1065.[ExPASy / RCSB / EBI]
2J5W; X-ray; 2.80 A; A=1-1065.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1KCW; -.
2J5W; -.
ModBase P00450.
Protein-protein interaction databases
IntAct P00450; -.
PTM databases
GlycoSuiteDB P00450; -.
PhosphoSite P00450; -.
2D gel databases
SWISS-2DPAGE P00450; -.
DOSAC-COBS-2DPAGE P00450; -.
Siena-2DPAGE P00450; -.
Organism-specific databases
H-InvDB HIX0003762; -.
HGNC HGNC:2295; CP.
GenAtlas CP.
HPA CAB008591; -.
HPA001834; -.
MIM 117700; gene. [NCBI / EBI]
604290; phenotype. [NCBI / EBI]
Orphanet 48818; Aceruloplasminemia.
PharmGKB PA24362; -.
GeneCards P00450.
Gene expression databases
ArrayExpress P00450; -.
CleanEx HS_CP; -.
GermOnline ENSG00000047457; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (traceable author statement from ProtInc).
GO:0004322; Molecular function: ferroxidase activity (traceable author statement from ProtInc).
GO:0006879; Biological process: cellular iron ion homeostasis (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001117; Cu-oxidase.
IPR011706; Cu-oxidase_2.
IPR011707; Cu-oxidase_3.
IPR002355; Cu_oxidase_Cu_BS.
IPR008972; Cupredoxin.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.420; Cupredoxin; 6.
Pfam PF00394; Cu-oxidase; 1.
PF07731; Cu-oxidase_2; 1.
PF07732; Cu-oxidase_3; 3.
Pfam graphical view of domain structure.
PROSITE PS00079; MULTICOPPER_OXIDASE1; 3.
PS00080; MULTICOPPER_OXIDASE2; 1.
BLOCKS P00450.
Proteomic databases
PeptideAtlas P00450; -.
Genome annotation databases
Ensembl ENSG00000047457; Homo sapiens. [Contig view]
GeneID 1356; -.
KEGG hsa:1356; -.
Phylogenomic databases
HOGENOM P00450; -.
HOVERGEN P00450; -.
Other
DrugBank DB00055; Drotrecogin alfa.
LinkHub P00450; -.
SOURCE CP; Homo sapiens.
ProtoNet P00450.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Copper; Copper transport; Direct protein sequencing; Glycoprotein; Ion transport; Metal-binding; Oxidoreductase; Phosphoprotein; Polymorphism; Repeat; Secreted; Signal; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     19  19      
CHAIN   20   1065  1046     Ceruloplasmin. PRO_0000002912
DOMAIN   20    357  338     F5/8 type A 1. 
DOMAIN   20    200  181     Plastocyanin-like 1. 
DOMAIN   209    357  149     Plastocyanin-like 2. 
DOMAIN   370    718  349     F5/8 type A 2. 
DOMAIN   370    560  191     Plastocyanin-like 3. 
DOMAIN   570    718  149     Plastocyanin-like 4. 
DOMAIN   730   1061  332     F5/8 type A 3. 
DOMAIN   730    900  171     Plastocyanin-like 5. 
DOMAIN   908   1061  154     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   204    204        Phosphoserine. 
MOD_RES   784    784        Phosphotyrosine. 
MOD_RES   787    787        Phosphotyrosine. 
CARBOHYD   138    138        N-linked (GlcNAc...). 
CARBOHYD   358    358        N-linked (GlcNAc...). 
CARBOHYD   397    397        N-linked (GlcNAc...). 
CARBOHYD   588    588        N-linked (GlcNAc...). 
CARBOHYD   762    762        N-linked (GlcNAc...). 
CARBOHYD   926    926        N-linked (GlcNAc...). 
DISULFID   174    200        Probable. 
DISULFID   276    357        Probable. 
DISULFID   534    560        Probable. 
DISULFID   637    718        Probable. 
DISULFID   874    900        Probable. 
VARIANT   63     63  1     I -> T (retained in the ER due to impaired N-glycosylation; may present a vulnerability factor for iron induced oxidative stress in Parkinson disease). VAR_025655 
VARIANT   367    367  1     R -> C (in dbSNP:rs34624984 [NCBI]). VAR_032815 
VARIANT   477    477  1     P -> L (in dbSNP:rs35331711 [NCBI]). VAR_025656 
VARIANT   544    544  1     D -> E (reduced ferroxidase activity; may present a vulnerability factor for iron induced oxidative stress in Parkinson disease; dbSNP:rs701753 [NCBI]). VAR_025657 
VARIANT   551    551  1     T -> I. VAR_025658 
VARIANT   793    793  1     R -> H. VAR_025659 
VARIANT   841    841  1     T -> R. VAR_025660 
CONFLICT   1060   1060        E -> EGEYP (in Ref. 6; AAA51975). 
STRAND   23     29  7      
STRAND   32     34  3      
TURN   51     55  5      
STRAND   58     61  4      
STRAND   66     68  3      
STRAND   71     79  9      
STRAND   82     84  3      
HELIX   88     90  3      
STRAND   97    100  4      
STRAND   106    110  5      
STRAND   113    115  3      
STRAND   120    125  6      
HELIX   141    143  3      
STRAND   144    147  4      
STRAND   154    158  5      
STRAND   173    180  8      
HELIX   185    190  6      
STRAND   194    200  7      
STRAND   205    210  6      
STRAND   214    218  5      
STRAND   222    225  4      
TURN   226    228  3      
HELIX   232    239  8      
HELIX   243    245  3      
HELIX   251    255  5      
STRAND   258    264  7      
STRAND   274    276  3      
STRAND   279    286  8      
STRAND   295    299  5