Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P00450

- CERU_HUMAN

UniProt

P00450 - CERU_HUMAN

Protein

Ceruloplasmin

Gene

CP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.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

    GO - Biological processi

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

    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

    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 PublicationAdd
    BLAST
    Chaini20 – 10651046CeruloplasminPRO_0000002912Add
    BLAST

    Amino acid modifications

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

    1
    1065
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00450.

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Belongs to the multicopper oxidase family.Curated
    Contains 3 F5/8 type A domains.Curated
    Contains 6 plastocyanin-like domains.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1060 – 10601E → EGEYP in AAA51975. (PubMed:3486416)Curated

    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. 1 Publication
    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. 1 Publication
    Corresponds to variant rs701753 [ dbSNP | Ensembl ].
    VAR_025657
    Natural varianti551 – 5511T → I.1 Publication
    VAR_025658
    Natural varianti793 – 7931R → H.1 Publication
    VAR_025659
    Natural varianti841 – 8411T → R.1 Publication
    Corresponds to variant rs56033670 [ dbSNP | Ensembl ].
    VAR_025660

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 172 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