P00450 (CERU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ceruloplasmin
EC=1.16.3.1

Alternative name(s):
Ferroxidase

Gene names

Name:

CP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1065 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Ceruloplasmin is a blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe2+ to Fe3+ without releasing radical oxygen species. It is involved in iron transport across the cell membrane.
Catalytic activity	4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.
Cofactor	Binds 6 copper ions per monomer.
Subcellular location	Secreted.
Tissue specificity	Expressed by the liver and secreted in plasma.
Involvement in disease	Defects in CP are the cause of aceruloplasminemia (ACERULOP) [MIM:604290]. It is 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=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.
Sequence similarities	Belongs to the multicopper oxidase family. Contains 3 F5/8 type A domains. Contains 6 plastocyanin-like domains.

Ontologies

Keywords
Biological process	Copper transport Ion transport Transport
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular iron ion homeostasis Traceable author statement. Source: Reactome copper ion transport Inferred from electronic annotation. Source: UniProtKB-KW transmembrane transport Traceable author statement. Source: Reactome
Cellular component	extracellular space Inferred from direct assay. Source: BHF-UCL
Molecular function	chaperone binding Inferred from physical interaction. Source: BHF-UCL ferroxidase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.7

Chain

20 – 1065

1046

Ceruloplasmin

PRO_0000002912

Regions

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

Sites

Metal binding

120

1

Copper 1; type 2

Metal binding

122

1

Copper 2; type 3

Metal binding

180

1

Copper 2; type 3

Metal binding

182

1

Copper 3; type 3

Metal binding

295

1

Copper 4; type 1

Metal binding

338

1

Copper 4; type 1

Metal binding

343

1

Copper 4; type 1

Metal binding

656

1

Copper 5; type 1

Metal binding

699

1

Copper 5; type 1

Metal binding

704

1

Copper 5; type 1

Metal binding

709

1

Copper 5; type 1

Metal binding

994

1

Copper 6; type 1

Metal binding

997

1

Copper 1; type 2

Metal binding

999

1

Copper 3; type 3

Metal binding

1039

1

Copper 3; type 3

Metal binding

1040

1

Copper 6; type 1

Metal binding

1041

1

Copper 2; type 3

Metal binding

1045

1

Copper 6; type 1

Metal binding

1050

1

Copper 6; type 1

Amino acid modifications

Modified residue

204

1

Phosphoserine Ref.18

Modified residue

784

1

Phosphotyrosine Ref.17

Modified residue

787

1

Phosphotyrosine Ref.17

Glycosylation

138

1

N-linked (GlcNAc...) (complex) Ref.14 Ref.15 Ref.16 Ref.19 Ref.20

Glycosylation

358

1

N-linked (GlcNAc...) (complex) Ref.16 Ref.19 Ref.20

Glycosylation

397

1

N-linked (GlcNAc...) (complex) Ref.15 Ref.16 Ref.19 Ref.20

Glycosylation

588

1

N-linked (GlcNAc...) Ref.16

Glycosylation

762

1

N-linked (GlcNAc...) Ref.15 Ref.16 Ref.19

Glycosylation

926

1

N-linked (GlcNAc...) Ref.16

Disulfide bond

174 ↔ 200

Probable

Disulfide bond

276 ↔ 357

Probable

Disulfide bond

534 ↔ 560

Probable

Disulfide bond

637 ↔ 718

Probable

Disulfide bond

874 ↔ 900

Probable

Natural variations

Natural variant

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. Ref.23 Ref.24

VAR_025655

Natural variant

367

1

R → C.
Corresponds to variant rs34624984 [ dbSNP | Ensembl ].

VAR_032815

Natural variant

477

1

P → L. Ref.23
Corresponds to variant rs35331711 [ dbSNP | Ensembl ].

VAR_025656

Natural variant

544

1

D → E Reduced ferroxidase activity; may present a vulnerability factor for iron induced oxidative stress in Parkinson disease. Ref.23 Ref.24
Corresponds to variant rs701753 [ dbSNP | Ensembl ].

VAR_025657

Natural variant

551

1

T → I. Ref.23

VAR_025658

Natural variant

793

1

R → H. Ref.23 Ref.24

VAR_025659

Natural variant

841

1

T → R. Ref.23
Corresponds to variant rs56033670 [ dbSNP | Ensembl ].

VAR_025660

Experimental info

Sequence conflict

1060

1

E → EGEYP in AAA51975. Ref.6

Secondary structure

1

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1065

Helix Strand Turn

Details...

Beta strand

21 – 35

15

Beta strand

49 – 51

3

Helix

53 – 56

4

Beta strand

65 – 79

15

Helix

88 – 90

3

Beta strand

97 – 100

4

Beta strand

104 – 115

12

Beta strand

120 – 125

6

Helix

128 – 130

3

Helix

141 – 143

3

Helix

145 – 147

3

Beta strand

154 – 160

7

Beta strand

173 – 180

8

Helix

185 – 191

7

Beta strand

194 – 200

7

Beta strand

205 – 210

6

Beta strand

215 – 225

11

Helix

226 – 228

3

Helix

232 – 239

8

Helix

243 – 245

3

Helix

251 – 256

6

Beta strand

258 – 262

5

Beta strand

274 – 276

3

Beta strand

280 – 287

8

Beta strand

295 – 299

5

Beta strand

304 – 306

3

Beta strand

309 – 316

8

Beta strand

321 – 327

7

Beta strand

332 – 338

7

Helix

341 – 345

5

Beta strand

349 – 355

7

Beta strand

369 – 385

17

Turn

392 – 394

3

Helix

406 – 409

4

Beta strand

418 – 430

13

Helix

441 – 446

6

Beta strand

453 – 456

4

Beta strand

459 – 467

9

Beta strand

469 – 471

3

Beta strand

476 – 481

6

Helix

484 – 486

3

Beta strand

514 – 520

7

Helix

523 – 525

3

Beta strand

529 – 531

3

Beta strand

533 – 540

8

Beta strand

542 – 544

3

Helix

545 – 551

7

Beta strand

554 – 560

7

Beta strand

575 – 580

6

Beta strand

582 – 586

5

Helix

587 – 589

3

Helix

593 – 600

8

Helix

604 – 606

3

Helix

612 – 617

6

Beta strand

619 – 623

5

Beta strand

635 – 637

3

Beta strand

642 – 647

6

Beta strand

656 – 660

5

Beta strand

665 – 667

3

Beta strand

670 – 677

8

Beta strand

682 – 687

6

Beta strand

693 – 699

7

Helix

702 – 706

5

Beta strand

710 – 716

7

Beta strand

729 – 745

17

Helix

750 – 759

10

Turn

766 – 768

3

Turn

771 – 773

3

Beta strand

777 – 789

13

Helix

800 – 805

6

Beta strand

812 – 815

4

Beta strand

818 – 826

9

Beta strand

828 – 830

3

Beta strand

835 – 838

4

Beta strand

854 – 860

7

Helix

863 – 865

3

Beta strand

873 – 880

8

Helix

885 – 890

6

Beta strand

894 – 900

7

Beta strand

913 – 924

12

Helix

925 – 927

3

Helix

931 – 938

8

Helix

942 – 944

3

Helix

950 – 955

6

Beta strand

957 – 961

5

Beta strand

973 – 975

3

Beta strand

979 – 986

8

Beta strand

994 – 1000

7

Beta strand

1003 – 1005

3

Turn

1006 – 1009

4

Beta strand

1011 – 1018

8

Beta strand

1023 – 1028

6

Beta strand

1034 – 1040

7

Helix

1043 – 1047

5

Beta strand

1051 – 1057

7

Sequences

	Sequence		Length	Mass (Da)
	P00450 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: 2F2F1294E2D30F58	FASTA	1,065	122,205
	10 20 30 40 50 60 MKILILGIFL FLCSTPAWAK EKHYYIGIIE TTWDYASDHG EKKLISVDTE HSNIYLQNGP 70 80 90 100 110 120 DRIGRLYKKA LYLQYTDETF RTTIEKPVWL GFLGPIIKAE TGDKVYVHLK NLASRPYTFH 130 140 150 160 170 180 SHGITYYKEH EGAIYPDNTT DFQRADDKVY PGEQYTYMLL ATEEQSPGEG DGNCVTRIYH 190 200 210 220 230 240 SHIDAPKDIA SGLIGPLIIC KKDSLDKEKE KHIDREFVVM FSVVDENFSW YLEDNIKTYC 250 260 270 280 290 300 SEPEKVDKDN EDFQESNRMY SVNGYTFGSL PGLSMCAEDR VKWYLFGMGN EVDVHAAFFH 310 320 330 340 350 360 GQALTNKNYR IDTINLFPAT LFDAYMVAQN PGEWMLSCQN LNHLKAGLQA FFQVQECNKS 370 380 390 400 410 420 SSKDNIRGKH VRHYYIAAEE IIWNYAPSGI DIFTKENLTA PGSDSAVFFE QGTTRIGGSY 430 440 450 460 470 480 KKLVYREYTD ASFTNRKERG PEEEHLGILG PVIWAEVGDT IRVTFHNKGA YPLSIEPIGV 490 500 510 520 530 540 RFNKNNEGTY YSPNYNPQSR SVPPSASHVA PTETFTYEWT VPKEVGPTNA DPVCLAKMYY 550 560 570 580 590 600 SAVDPTKDIF TGLIGPMKIC KKGSLHANGR QKDVDKEFYL FPTVFDENES LLLEDNIRMF 610 620 630 640 650 660 TTAPDQVDKE DEDFQESNKM HSMNGFMYGN QPGLTMCKGD SVVWYLFSAG NEADVHGIYF 670 680 690 700 710 720 SGNTYLWRGE RRDTANLFPQ TSLTLHMWPD TEGTFNVECL TTDHYTGGMK QKYTVNQCRR 730 740 750 760 770 780 QSEDSTFYLG ERTYYIAAVE VEWDYSPQRE WEKELHHLQE QNVSNAFLDK GEFYIGSKYK 790 800 810 820 830 840 KVVYRQYTDS TFRVPVERKA EEEHLGILGP QLHADVGDKV KIIFKNMATR PYSIHAHGVQ 850 860 870 880 890 900 TESSTVTPTL PGETLTYVWK IPERSGAGTE DSACIPWAYY STVDQVKDLY SGLIGPLIVC 910 920 930 940 950 960 RRPYLKVFNP RRKLEFALLF LVFDENESWY LDDNIKTYSD HPEKVNKDDE EFIESNKMHA 970 980 990 1000 1010 1020 INGRMFGNLQ GLTMHVGDEV NWYLMGMGNE IDLHTVHFHG HSFQYKHRGV YSSDVFDIFP 1030 1040 1050 1060 GTYQTLEMFP RTPGIWLLHC HVTDHIHAGM ETTYTVLQNE DTKSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete cDNA sequence of human preceruloplasmin." Koschinsky M.L., Funk W.D., van Oost B.A., McGillivray R.T.A. Proc. Natl. Acad. Sci. U.S.A. 83:5086-5090(1986) [PubMed: 2873574] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Fine structure of the human ceruloplasmin gene." Daimon M., Yamatani K., Igarashi M., Fukase N., Kawanami T., Kato T., Tominaga M., Sasaki H. Biochem. Biophys. Res. Commun. 208:1028-1035(1995) [PubMed: 7702601] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1006.
[4]	"Isolation of a human ceruloplasmin cDNA clone that includes the N-terminal leader sequence." Mercer J.F.B., Grimes A. FEBS Lett. 203:185-190(1986) [PubMed: 3755405] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-40; 549-599; 784-829 AND 919-952.
[5]	"Cloning and functional analysis of the human ceruloplasmin gene minimal promoter." Bingle C.D. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[6]	"Characterization, mapping, and expression of the human ceruloplasmin gene." 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. Proc. Natl. Acad. Sci. U.S.A. 83:3257-3261(1986) [PubMed: 3486416] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 218-1065.
[7]	"Single-chain structure of human ceruloplasmin: the complete amino acid sequence of the whole molecule." Takahashi N., Ortel T.L., Putnam F.W. Proc. Natl. Acad. Sci. U.S.A. 81:390-394(1984) [PubMed: 6582496] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-1065.
[8]	"Internal triplication in the structure of human ceruloplasmin." Takahashi N., Bauman R.A., Ortel T.L., Dwulet F.E., Wang C.-C., Putnam F.W. Proc. Natl. Acad. Sci. U.S.A. 80:115-119(1983) [PubMed: 6571985] [Abstract] Cited for: PROTEIN SEQUENCE OF 158-333; 518-724 AND 858-1065.
[9]	"Complete amino acid sequence of a 50,000-dalton fragment of human ceruloplasmin." Dwulet F.E., Putnam F.W. Proc. Natl. Acad. Sci. U.S.A. 78:790-794(1981) [PubMed: 6940148] [Abstract] Cited for: PROTEIN SEQUENCE OF 501-905.
[10]	"Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. I. Amino acid sequence of the cyanogen bromide peptides." Kingston I.B., Kingston B.L., Putnam F.W. J. Biol. Chem. 255:2878-2885(1980) [PubMed: 6987229] [Abstract] Cited for: PROTEIN SEQUENCE OF 907-1065.
[11]	"Primary structure of a histidine-rich proteolytic fragment of human ceruloplasmin. II. Amino acid sequence of the tryptic peptides." Kingston I.B., Kingston B.L., Putnam F.W. J. Biol. Chem. 255:2886-2896(1980) [PubMed: 6987230] [Abstract] Cited for: PROTEIN SEQUENCE OF 907-1065.
[12]	"Human ceruloplasmin. Tissue-specific expression of transcripts produced by alternative splicing." Yang F.M., Friedrichs W.E., Cupples R.L., Banifacio M.J., Sanford J.A., Horton W.A., Bowman B.H. J. Biol. Chem. 265:10780-10785(1990) [PubMed: 2355023] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1007-1061.
[13]	"Ceruloplasmin metabolism and function." Hellman N.E., Gitlin J.D. Annu. Rev. Nutr. 22:439-458(2002) [PubMed: 12055353] [Abstract] Cited for: REVIEW.
[14]	"A proteomic analysis of human bile." Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A. Mol. Cell. Proteomics 3:715-728(2004) [PubMed: 15084671] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138, MASS SPECTROMETRY. Tissue: Bile.
[15]	"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry." Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R. Proteomics 4:454-465(2004) [PubMed: 14760718] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-397 AND ASN-762, MASS SPECTROMETRY. Tissue: Plasma.
[16]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358; ASN-397; ASN-588; ASN-762 AND ASN-926, MASS SPECTROMETRY. Tissue: Plasma.
[17]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." 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. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-784 AND TYR-787, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[18]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358; ASN-397 AND ASN-762, MASS SPECTROMETRY. Tissue: Liver.
[20]	"Enrichment of glycopeptides for glycan structure and attachment site identification." Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G. Nat. Methods 6:809-811(2009) [PubMed: 19838169] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358 AND ASN-397, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY. Tissue: Cerebrospinal fluid.
[21]	"The X-ray structure of human serum ceruloplasmin at 3.1 A: nature of the copper centres." Zaitseva I., Zaitsev V., Card G., Moshkov K., Bax B., Ralph A., Lindley P. J. Biol. Inorg. Chem. 1:15-23(1996) Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), DISULFIDE BONDS, METAL-BINDING SITES.
[22]	"Ceruloplasmin revisited: structural and functional roles of various metal cation-binding sites." Bento I., Peixoto C., Zaitsev V.N., Lindley P.F. Acta Crystallogr. D 63:240-248(2007) [PubMed: 17242517] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), METAL-BINDING SITES, DISULFIDE BONDS.
[23]	"Ceruloplasmin gene variations and substantia nigra hyperechogenicity in Parkinson disease." Hochstrasser H., Bauer P., Walter U., Behnke S., Spiegel J., Csoti I., Zeiler B., Bornemann A., Pahnke J., Becker G., Riess O., Berg D. Neurology 63:1912-1917(2004) [PubMed: 15557511] [Abstract] Cited for: VARIANTS THR-63; LEU-477; GLU-544; ILE-551; HIS-793 AND ARG-841.
[24]	"Functional relevance of ceruloplasmin mutations in Parkinson's disease." Hochstrasser H., Tomiuk J., Walter U., Behnke S., Spiegel J., Krueger R., Becker G., Riess O., Berg D. FASEB J. 19:1851-1853(2005) [PubMed: 16150804] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS THR-63; GLU-544 AND HIS-793.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

Ceruloplasmin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M13699 mRNA. Translation: AAA51976.1.
DQ314867 Genomic DNA. Translation: ABC40726.1.
D45045 Genomic DNA. Translation: BAA08085.1.
D00025 mRNA. Translation: BAA00019.1.
X04135 mRNA. Translation: CAA27752.1.
X04136 mRNA. Translation: CAA27753.1.
X04137 mRNA. Translation: CAA27754.1.
X04138 mRNA. Translation: CAA27755.1.
AF132978 Genomic DNA. Translation: AAF02483.1.
M13536 mRNA. Translation: AAA51975.1.
J05506 Genomic DNA. No translation available.

IPI

IPI00017601.

PIR

KUHU. A25443.

RefSeq

NP_000087.1. NM_000096.3.

UniGene

Hs.558314.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KCW	X-ray	3.00	A	20-1065	[»]
2J5W	X-ray	2.80	A	1-1065	[»]

ProteinModelPortal

P00450.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00450. 5 interactions.

STRING

P00450.

PTM databases

GlycoSuiteDB

P00450.

PhosphoSite

P00450.

Polymorphism databases

DMDM

116117.

2D gel databases

SWISS-2DPAGE

P00450.

DOSAC-COBS-2DPAGE

P00450.

Siena-2DPAGE

P00450.

Proteomic databases

PeptideAtlas

P00450.

PRIDE

P00450.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264613; ENSP00000264613; ENSG00000047457.

GeneID

1356.

KEGG

hsa:1356.

UCSC

uc003ewy.2. human.

Organism-specific databases

CTD

1356.

GeneCards

GC03M148880.

H-InvDB

HIX0003762.

HGNC

HGNC:2295. CP.

HPA

CAB008591.
HPA001834.

MIM

117700. gene.
604290. phenotype.

neXtProt

NX_P00450.

Orphanet

48818. Aceruloplasminemia.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19766.

HOGENOM

HBG357170.

HOVERGEN

HBG003674.

InParanoid

P00450.

Enzyme and pathway databases

BioCyc

MetaCyc:HS00590-MONOMER.

Pathway_Interaction_DB

hif1_tfpathway. HIF-1-alpha transcription factor network.

Reactome

REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpress

P00450.

Bgee

P00450.

CleanEx

HS_CP.

Genevestigator

P00450.

GermOnline

ENSG00000047457. Homo sapiens.

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]

Gene3D

G3DSA:2.60.40.420. Cupredoxin. 6 hits.

KO

K13624.

Pfam

PF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 2 hits.
[Graphical view]

SUPFAM

SSF49503. Cupredoxin. 6 hits.

PROSITE

PS00079. MULTICOPPER_OXIDASE1. 3 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00055. Drotrecogin alfa.

NextBio

5493.

PMAP-CutDB

P00450.

SOURCE

Search...

Entry information

Entry name

CERU_HUMAN

Accession

Primary (citable) accession number: P00450
Secondary accession number(s): Q14063, Q2PP18, Q9UKS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 13, 1987
Last modified:	January 25, 2012
This is version 147 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.