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P00450

- CERU_HUMAN

UniProt

P00450 - CERU_HUMAN

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Protein
Ceruloplasmin
Gene
CP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. Provides Cu2+ 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.

Catalytic activityi

4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.

Cofactori

Binds 6 copper ions per monomer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi120 – 1201Copper 1; type 2
Metal bindingi122 – 1221Copper 2; type 3
Metal bindingi180 – 1801Copper 2; type 3
Metal bindingi182 – 1821Copper 3; type 3
Metal bindingi295 – 2951Copper 4; type 1
Metal bindingi338 – 3381Copper 4; type 1
Metal bindingi343 – 3431Copper 4; type 1
Metal bindingi656 – 6561Copper 5; type 1
Metal bindingi699 – 6991Copper 5; type 1
Metal bindingi704 – 7041Copper 5; type 1
Metal bindingi709 – 7091Copper 5; type 1
Metal bindingi994 – 9941Copper 6; type 1
Metal bindingi997 – 9971Copper 1; type 2
Metal bindingi999 – 9991Copper 3; type 3
Metal bindingi1039 – 10391Copper 3; type 3
Metal bindingi1040 – 10401Copper 6; type 1
Metal bindingi1041 – 10411Copper 2; type 3
Metal bindingi1045 – 10451Copper 6; type 1
Metal bindingi1050 – 10501Copper 6; type 1

GO - Molecular functioni

  1. chaperone binding Source: BHF-UCL
  2. copper ion binding Source: Ensembl
  3. ferroxidase activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. cellular iron ion homeostasis Source: Reactome
  2. copper ion transport Source: UniProtKB-KW
  3. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Copper transport, Ion transport, Transport

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS00590-MONOMER.
ReactomeiREACT_20547. Metal ion SLC transporters.
REACT_25060. Iron uptake and transport.
SABIO-RKP00450.

Names & Taxonomyi

Protein namesi
Recommended name:
Ceruloplasmin (EC:1.16.3.1)
Alternative name(s):
Ferroxidase
Gene namesi
Name:CP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:2295. CP.

Subcellular locationi

Secreted
Note: Colocalizes with GCP1 in secretory intracellular compartments By similarity.

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: UniProtKB
  3. extracellular space Source: BHF-UCL
  4. extracellular vesicular exosome Source: UniProt
  5. lysosomal membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

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.
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.

Organism-specific databases

MIMi604290. phenotype.
Orphaneti48818. Aceruloplasminemia.
PharmGKBiPA26815.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 Publication
Add
BLAST
Chaini20 – 10651046Ceruloplasmin
PRO_0000002912Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi138 – 1381N-linked (GlcNAc...) (complex)6 Publications
Disulfide bondi174 ↔ 200 Inferred
Disulfide bondi276 ↔ 357 Inferred
Glycosylationi358 – 3581N-linked (GlcNAc...) (complex)4 Publications
Glycosylationi397 – 3971N-linked (GlcNAc...) (complex)5 Publications
Disulfide bondi534 ↔ 560 Inferred
Glycosylationi588 – 5881N-linked (GlcNAc...)1 Publication
Disulfide bondi637 ↔ 718 Inferred
Glycosylationi762 – 7621N-linked (GlcNAc...) (complex)4 Publications
Disulfide bondi874 ↔ 900 Inferred
Glycosylationi926 – 9261N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP00450.
PaxDbiP00450.
PeptideAtlasiP00450.
PRIDEiP00450.

2D gel databases

DOSAC-COBS-2DPAGEP00450.
SWISS-2DPAGEP00450.

PTM databases

PhosphoSiteiP00450.
UniCarbKBiP00450.

Miscellaneous databases

PMAP-CutDBP00450.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

ArrayExpressiP00450.
BgeeiP00450.
CleanExiHS_CP.
GenevestigatoriP00450.

Organism-specific databases

HPAiCAB008591.
HPA001834.

Interactioni

Protein-protein interaction databases

BioGridi107748. 5 interactions.
IntActiP00450. 5 interactions.
STRINGi9606.ENSP00000264613.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 3616
Turni49 – 524
Helixi53 – 564
Beta strandi58 – 614
Beta strandi65 – 7915
Beta strandi82 – 843
Helixi88 – 903
Beta strandi97 – 1004
Beta strandi104 – 1118
Beta strandi113 – 1153
Beta strandi120 – 1256
Helixi128 – 1303
Helixi141 – 1444
Helixi145 – 1473
Beta strandi154 – 1607
Beta strandi173 – 1808
Helixi185 – 1906
Beta strandi194 – 2007
Beta strandi205 – 2106
Beta strandi214 – 22512
Helixi226 – 2283
Helixi232 – 2398
Helixi243 – 2453
Helixi251 – 2577
Beta strandi258 – 2625
Beta strandi274 – 2763
Beta strandi280 – 2878
Beta strandi295 – 3017
Beta strandi304 – 3063
Beta strandi309 – 3124
Beta strandi321 – 3277
Beta strandi332 – 3387
Helixi341 – 3444
Turni345 – 3473
Beta strandi349 – 3557
Beta strandi367 – 38519
Turni392 – 3943
Beta strandi401 – 4033
Helixi406 – 4094
Beta strandi412 – 4143
Beta strandi418 – 42710
Beta strandi429 – 4357
Helixi444 – 4463
Beta strandi453 – 4564
Beta strandi459 – 47113
Beta strandi476 – 4816
Helixi484 – 4863
Beta strandi514 – 5207
Turni523 – 5253
Beta strandi529 – 5313
Beta strandi533 – 5408
Beta strandi542 – 5443
Helixi545 – 5517
Beta strandi554 – 5607
Beta strandi575 – 5806
Beta strandi582 – 5865
Helixi587 – 5893
Helixi593 – 6008
Helixi604 – 6063
Helixi612 – 6176
Beta strandi619 – 6235
Beta strandi635 – 6373
Beta strandi642 – 6476
Beta strandi656 – 6605
Beta strandi665 – 6673
Beta strandi670 – 6778
Beta strandi682 – 6876
Beta strandi693 – 6997
Helixi702 – 7065
Beta strandi710 – 7167
Beta strandi729 – 74517
Helixi750 – 75910
Turni766 – 7683
Turni771 – 7733
Beta strandi777 – 78913
Helixi800 – 8056
Beta strandi812 – 8154
Beta strandi818 – 8269
Beta strandi828 – 8303
Beta strandi835 – 8384
Beta strandi842 – 8443
Beta strandi854 – 8607
Helixi863 – 8653
Beta strandi869 – 8713
Beta strandi873 – 8808
Helixi885 – 8906
Beta strandi894 – 9007
Beta strandi913 – 92412
Helixi925 – 9273
Helixi931 – 9388
Helixi942 – 9443
Helixi950 – 9556
Beta strandi957 – 9615
Beta strandi973 – 9753
Beta strandi979 – 9868
Beta strandi994 – 9985
Beta strandi1003 – 10064
Helixi1007 – 10093
Beta strandi1011 – 10188
Beta strandi1023 – 10286
Beta strandi1034 – 10407
Helixi1043 – 10475
Beta strandi1051 – 10577

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KCWX-ray3.00A20-1065[»]
2J5WX-ray2.80A1-1065[»]
4EJXX-ray4.69A1-1065[»]
4ENZX-ray2.60A1-1065[»]
ProteinModelPortaliP00450.

Miscellaneous databases

EvolutionaryTraceiP00450.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 357338F5/8 type A 1
Add
BLAST
Domaini20 – 200181Plastocyanin-like 1
Add
BLAST
Domaini209 – 357149Plastocyanin-like 2
Add
BLAST
Domaini370 – 718349F5/8 type A 2
Add
BLAST
Domaini370 – 560191Plastocyanin-like 3
Add
BLAST
Domaini570 – 718149Plastocyanin-like 4
Add
BLAST
Domaini730 – 1061332F5/8 type A 3
Add
BLAST
Domaini730 – 900171Plastocyanin-like 5
Add
BLAST
Domaini908 – 1061154Plastocyanin-like 6
Add
BLAST

Sequence similaritiesi

Contains 3 F5/8 type A domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG276067.
HOGENOMiHOG000231499.
HOVERGENiHBG003674.
InParanoidiP00450.
KOiK13624.
PhylomeDBiP00450.
TreeFamiTF329807.

Family and domain databases

Gene3Di2.60.40.420. 6 hits.
InterProiIPR027150. CP.
IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PANTHERiPTHR10127:SF294. PTHR10127:SF294. 1 hit.
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 2 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 6 hits.
PROSITEiPS00079. MULTICOPPER_OXIDASE1. 3 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00450-1 [UniParc]FASTAAdd to Basket

« Hide

MKILILGIFL FLCSTPAWAK EKHYYIGIIE TTWDYASDHG EKKLISVDTE     50
HSNIYLQNGP DRIGRLYKKA LYLQYTDETF RTTIEKPVWL GFLGPIIKAE 100
TGDKVYVHLK NLASRPYTFH SHGITYYKEH EGAIYPDNTT DFQRADDKVY 150
PGEQYTYMLL ATEEQSPGEG DGNCVTRIYH SHIDAPKDIA SGLIGPLIIC 200
KKDSLDKEKE KHIDREFVVM FSVVDENFSW YLEDNIKTYC SEPEKVDKDN 250
EDFQESNRMY SVNGYTFGSL PGLSMCAEDR VKWYLFGMGN EVDVHAAFFH 300
GQALTNKNYR IDTINLFPAT LFDAYMVAQN PGEWMLSCQN LNHLKAGLQA 350
FFQVQECNKS SSKDNIRGKH VRHYYIAAEE IIWNYAPSGI DIFTKENLTA 400
PGSDSAVFFE QGTTRIGGSY KKLVYREYTD ASFTNRKERG PEEEHLGILG 450
PVIWAEVGDT IRVTFHNKGA YPLSIEPIGV RFNKNNEGTY YSPNYNPQSR 500
SVPPSASHVA PTETFTYEWT VPKEVGPTNA DPVCLAKMYY SAVDPTKDIF 550
TGLIGPMKIC KKGSLHANGR QKDVDKEFYL FPTVFDENES LLLEDNIRMF 600
TTAPDQVDKE DEDFQESNKM HSMNGFMYGN QPGLTMCKGD SVVWYLFSAG 650
NEADVHGIYF SGNTYLWRGE RRDTANLFPQ TSLTLHMWPD TEGTFNVECL 700
TTDHYTGGMK QKYTVNQCRR QSEDSTFYLG ERTYYIAAVE VEWDYSPQRE 750
WEKELHHLQE QNVSNAFLDK GEFYIGSKYK KVVYRQYTDS TFRVPVERKA 800
EEEHLGILGP QLHADVGDKV KIIFKNMATR PYSIHAHGVQ TESSTVTPTL 850
PGETLTYVWK IPERSGAGTE DSACIPWAYY STVDQVKDLY SGLIGPLIVC 900
RRPYLKVFNP RRKLEFALLF LVFDENESWY LDDNIKTYSD HPEKVNKDDE 950
EFIESNKMHA INGRMFGNLQ GLTMHVGDEV NWYLMGMGNE IDLHTVHFHG 1000
HSFQYKHRGV YSSDVFDIFP GTYQTLEMFP RTPGIWLLHC HVTDHIHAGM 1050
ETTYTVLQNE DTKSG 1065
Length:1,065
Mass (Da):122,205
Last modified:August 13, 1987 - v1
Checksum:i2F2F1294E2D30F58
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti63 – 631I → T Retained in the ER due to impaired N-glycosylation; may present a vulnerability factor for iron induced oxidative stress in Parkinson disease. 2 Publications
VAR_025655
Natural varianti367 – 3671R → C.
Corresponds to variant rs34624984 [ dbSNP | Ensembl ].
VAR_032815
Natural varianti477 – 4771P → L.1 Publication
Corresponds to variant rs35331711 [ dbSNP | Ensembl ].
VAR_025656
Natural varianti544 – 5441D → E Reduced ferroxidase activity; may present a vulnerability factor for iron induced oxidative stress in Parkinson disease. 2 Publications
Corresponds to variant rs701753 [ dbSNP | Ensembl ].
VAR_025657
Natural varianti551 – 5511T → I.1 Publication
VAR_025658
Natural varianti793 – 7931R → H.2 Publications
VAR_025659
Natural varianti841 – 8411T → R.1 Publication
Corresponds to variant rs56033670 [ dbSNP | Ensembl ].
VAR_025660

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1060 – 10601E → EGEYP in AAA51975. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3141.1.
PIRiA25443. KUHU.
RefSeqiNP_000087.1. NM_000096.3.
UniGeneiHs.558314.

Genome annotation databases

EnsembliENST00000264613; ENSP00000264613; ENSG00000047457.
GeneIDi1356.
KEGGihsa:1356.
UCSCiuc003ewy.4. human.

Polymorphism databases

DMDMi116117.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Ceruloplasmin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS3141.1.
PIRi A25443. KUHU.
RefSeqi NP_000087.1. NM_000096.3.
UniGenei Hs.558314.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KCW X-ray 3.00 A 20-1065 [» ]
2J5W X-ray 2.80 A 1-1065 [» ]
4EJX X-ray 4.69 A 1-1065 [» ]
4ENZ X-ray 2.60 A 1-1065 [» ]
ProteinModelPortali P00450.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107748. 5 interactions.
IntActi P00450. 5 interactions.
STRINGi 9606.ENSP00000264613.

Chemistry

DrugBanki DB00055. Drotrecogin alfa.

PTM databases

PhosphoSitei P00450.
UniCarbKBi P00450.

Polymorphism databases

DMDMi 116117.

2D gel databases

DOSAC-COBS-2DPAGE P00450.
SWISS-2DPAGE P00450.

Proteomic databases

MaxQBi P00450.
PaxDbi P00450.
PeptideAtlasi P00450.
PRIDEi P00450.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264613 ; ENSP00000264613 ; ENSG00000047457 .
GeneIDi 1356.
KEGGi hsa:1356.
UCSCi uc003ewy.4. human.

Organism-specific databases

CTDi 1356.
GeneCardsi GC03M148880.
GeneReviewsi CP.
HGNCi HGNC:2295. CP.
HPAi CAB008591.
HPA001834.
MIMi 117700. gene.
604290. phenotype.
neXtProti NX_P00450.
Orphaneti 48818. Aceruloplasminemia.
PharmGKBi PA26815.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG276067.
HOGENOMi HOG000231499.
HOVERGENi HBG003674.
InParanoidi P00450.
KOi K13624.
PhylomeDBi P00450.
TreeFami TF329807.

Enzyme and pathway databases

BioCyci MetaCyc:HS00590-MONOMER.
Reactomei REACT_20547. Metal ion SLC transporters.
REACT_25060. Iron uptake and transport.
SABIO-RK P00450.

Miscellaneous databases

EvolutionaryTracei P00450.
GeneWikii Ceruloplasmin.
GenomeRNAii 1356.
NextBioi 5493.
PMAP-CutDB P00450.
PROi P00450.
SOURCEi Search...

Gene expression databases

ArrayExpressi P00450.
Bgeei P00450.
CleanExi HS_CP.
Genevestigatori P00450.

Family and domain databases

Gene3Di 2.60.40.420. 6 hits.
InterProi IPR027150. CP.
IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view ]
PANTHERi PTHR10127:SF294. PTHR10127:SF294. 1 hit.
Pfami PF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 2 hits.
[Graphical view ]
SUPFAMi SSF49503. SSF49503. 6 hits.
PROSITEi PS00079. MULTICOPPER_OXIDASE1. 3 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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] [Europe PMC] [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. 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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-1065.
  8. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1007-1061.
  13. Cited for: REVIEW.
  14. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138.
    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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-397 AND ASN-762.
    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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358; ASN-397; ASN-588; ASN-762 AND ASN-926.
    Tissue: Plasma.
  17. "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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358; ASN-397 AND ASN-762.
    Tissue: Liver.
  18. Cited for: GLYCOSYLATION AT ASN-138; ASN-358; ASN-397 AND ASN-762.
  19. "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] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-138; ASN-358 AND ASN-397, STRUCTURE OF CARBOHYDRATES.
    Tissue: Cerebrospinal fluid.
  20. "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.
  21. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), METAL-BINDING SITES, DISULFIDE BONDS.
  22. "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] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-63; LEU-477; GLU-544; ILE-551; HIS-793 AND ARG-841.
  23. "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] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS THR-63; GLU-544 AND HIS-793.

Entry informationi

Entry nameiCERU_HUMAN
AccessioniPrimary (citable) accession number: P00450
Secondary accession number(s): Q14063, Q2PP18, Q9UKS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: September 3, 2014
This is version 171 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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