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Protein

Ceruloplasmin

Gene

CP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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).By similarity

Catalytic activityi

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

Cofactori

Cu cationNote: Binds 6 Cu cations per monomer.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi120Copper 1; type 21
Metal bindingi122Copper 2; type 31
Metal bindingi180Copper 2; type 31
Metal bindingi182Copper 3; type 31
Metal bindingi295Copper 4; type 11
Metal bindingi338Copper 4; type 11
Metal bindingi343Copper 4; type 11
Metal bindingi656Copper 5; type 11
Metal bindingi699Copper 5; type 11
Metal bindingi704Copper 5; type 11
Metal bindingi709Copper 5; type 11
Metal bindingi994Copper 6; type 11
Metal bindingi997Copper 1; type 21
Metal bindingi999Copper 3; type 31
Metal bindingi1039Copper 3; type 31
Metal bindingi1040Copper 6; type 11
Metal bindingi1041Copper 2; type 31
Metal bindingi1045Copper 6; type 11
Metal bindingi1050Copper 6; type 11

GO - Molecular functioni

  • chaperone binding Source: BHF-UCL
  • copper ion binding Source: InterPro
  • ferroxidase activity Source: Reactome

GO - Biological processi

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.
ZFISH:HS00590-MONOMER.
BRENDAi1.16.3.1. 2681.
ReactomeiR-HSA-425410. Metal ion SLC transporters.
R-HSA-917937. Iron uptake and transport.
SABIO-RKP00450.
SIGNORiP00450.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:2295. CP.

Subcellular locationi

  • Secreted

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

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Aceruloplasminemia (ACERULOP)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:604290

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

DisGeNETi1356.
MalaCardsiCP.
MIMi604290. phenotype.
Orphaneti48818. Aceruloplasminemia.
PharmGKBiPA26815.

Chemistry databases

DrugBankiDB00055. Drotrecogin alfa.

Polymorphism and mutation databases

BioMutaiCP.
DMDMi116117.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000000291220 – 1065CeruloplasminAdd BLAST1046

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi138N-linked (GlcNAc...) (complex)6 Publications1
Disulfide bondi174 ↔ 200Curated
Disulfide bondi276 ↔ 357Curated
Glycosylationi358N-linked (GlcNAc...) (complex)4 Publications1
Glycosylationi397N-linked (GlcNAc...) (complex)5 Publications1
Disulfide bondi534 ↔ 560Curated
Glycosylationi588N-linked (GlcNAc...)1 Publication1
Disulfide bondi637 ↔ 718Curated
Modified residuei722Phosphoserine; by FAM20C1 Publication1
Glycosylationi762N-linked (GlcNAc...) (complex)4 Publications1
Disulfide bondi874 ↔ 900Curated
Glycosylationi926N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP00450.
PaxDbiP00450.
PeptideAtlasiP00450.
PRIDEiP00450.

2D gel databases

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

PTM databases

iPTMnetiP00450.
PhosphoSitePlusiP00450.
UniCarbKBiP00450.

Miscellaneous databases

PMAP-CutDBP00450.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

BgeeiENSG00000047457.
CleanExiHS_CP.
ExpressionAtlasiP00450. baseline and differential.
GenevisibleiP00450. HS.

Organism-specific databases

HPAiCAB008591.
HPA001834.

Interactioni

GO - Molecular functioni

  • chaperone binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi107748. 9 interactors.
IntActiP00450. 5 interactors.
STRINGi9606.ENSP00000264613.

Structurei

Secondary structure

11065
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi21 – 36Combined sources16
Turni49 – 52Combined sources4
Helixi53 – 56Combined sources4
Beta strandi58 – 61Combined sources4
Beta strandi65 – 79Combined sources15
Beta strandi82 – 84Combined sources3
Helixi88 – 90Combined sources3
Beta strandi97 – 100Combined sources4
Beta strandi104 – 111Combined sources8
Beta strandi113 – 115Combined sources3
Beta strandi120 – 125Combined sources6
Helixi128 – 130Combined sources3
Helixi141 – 144Combined sources4
Helixi145 – 147Combined sources3
Beta strandi154 – 160Combined sources7
Beta strandi173 – 180Combined sources8
Helixi185 – 190Combined sources6
Beta strandi194 – 200Combined sources7
Beta strandi205 – 210Combined sources6
Beta strandi214 – 225Combined sources12
Helixi226 – 228Combined sources3
Helixi232 – 239Combined sources8
Helixi243 – 245Combined sources3
Helixi251 – 257Combined sources7
Beta strandi258 – 262Combined sources5
Beta strandi274 – 276Combined sources3
Beta strandi280 – 287Combined sources8
Beta strandi295 – 301Combined sources7
Beta strandi304 – 306Combined sources3
Beta strandi309 – 312Combined sources4
Beta strandi321 – 327Combined sources7
Beta strandi332 – 338Combined sources7
Helixi341 – 344Combined sources4
Turni345 – 347Combined sources3
Beta strandi349 – 355Combined sources7
Beta strandi367 – 385Combined sources19
Turni392 – 394Combined sources3
Beta strandi401 – 403Combined sources3
Helixi406 – 409Combined sources4
Beta strandi412 – 414Combined sources3
Beta strandi418 – 427Combined sources10
Beta strandi429 – 435Combined sources7
Helixi444 – 446Combined sources3
Beta strandi453 – 456Combined sources4
Beta strandi459 – 471Combined sources13
Beta strandi476 – 481Combined sources6
Helixi484 – 486Combined sources3
Beta strandi514 – 520Combined sources7
Turni523 – 525Combined sources3
Beta strandi529 – 531Combined sources3
Beta strandi533 – 540Combined sources8
Beta strandi542 – 544Combined sources3
Helixi545 – 551Combined sources7
Beta strandi554 – 560Combined sources7
Beta strandi575 – 580Combined sources6
Beta strandi582 – 586Combined sources5
Helixi587 – 589Combined sources3
Helixi593 – 600Combined sources8
Helixi604 – 606Combined sources3
Helixi612 – 617Combined sources6
Beta strandi619 – 623Combined sources5
Beta strandi635 – 637Combined sources3
Beta strandi642 – 647Combined sources6
Beta strandi656 – 660Combined sources5
Beta strandi665 – 667Combined sources3
Beta strandi670 – 677Combined sources8
Beta strandi682 – 687Combined sources6
Beta strandi693 – 699Combined sources7
Helixi702 – 706Combined sources5
Beta strandi710 – 716Combined sources7
Beta strandi729 – 745Combined sources17
Helixi750 – 759Combined sources10
Turni766 – 768Combined sources3
Turni771 – 773Combined sources3
Beta strandi777 – 789Combined sources13
Helixi800 – 805Combined sources6
Beta strandi812 – 815Combined sources4
Beta strandi818 – 826Combined sources9
Beta strandi828 – 830Combined sources3
Beta strandi835 – 838Combined sources4
Beta strandi842 – 844Combined sources3
Beta strandi854 – 860Combined sources7
Helixi863 – 865Combined sources3
Beta strandi869 – 871Combined sources3
Beta strandi873 – 880Combined sources8
Helixi885 – 890Combined sources6
Beta strandi894 – 900Combined sources7
Beta strandi913 – 924Combined sources12
Helixi925 – 927Combined sources3
Helixi931 – 938Combined sources8
Helixi942 – 944Combined sources3
Helixi950 – 955Combined sources6
Beta strandi957 – 961Combined sources5
Beta strandi973 – 975Combined sources3
Beta strandi979 – 986Combined sources8
Beta strandi994 – 998Combined sources5
Beta strandi1003 – 1006Combined sources4
Helixi1007 – 1009Combined sources3
Beta strandi1011 – 1018Combined sources8
Beta strandi1023 – 1028Combined sources6
Beta strandi1034 – 1040Combined sources7
Helixi1043 – 1047Combined sources5
Beta strandi1051 – 1057Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KCWX-ray3.00A20-1065[»]
2J5WX-ray2.80A1-1065[»]
4EJXX-ray4.69A1-1065[»]
4ENZX-ray2.60A1-1065[»]
ProteinModelPortaliP00450.
SMRiP00450.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00450.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 357F5/8 type A 1Add BLAST338
Domaini20 – 200Plastocyanin-like 1Add BLAST181
Domaini209 – 357Plastocyanin-like 2Add BLAST149
Domaini370 – 718F5/8 type A 2Add BLAST349
Domaini370 – 560Plastocyanin-like 3Add BLAST191
Domaini570 – 718Plastocyanin-like 4Add BLAST149
Domaini730 – 1061F5/8 type A 3Add BLAST332
Domaini730 – 900Plastocyanin-like 5Add BLAST171
Domaini908 – 1061Plastocyanin-like 6Add BLAST154

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

eggNOGiKOG1263. Eukaryota.
COG2132. LUCA.
HOGENOMiHOG000231499.
HOVERGENiHBG003674.
InParanoidiP00450.
KOiK13624.
OrthoDBiEOG091G00QL.
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.
IPR033138. Cu_oxidase_CS.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PANTHERiPTHR10127:SF664. PTHR10127:SF664. 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

        10         20         30         40         50
MKILILGIFL FLCSTPAWAK EKHYYIGIIE TTWDYASDHG EKKLISVDTE
60 70 80 90 100
HSNIYLQNGP DRIGRLYKKA LYLQYTDETF RTTIEKPVWL GFLGPIIKAE
110 120 130 140 150
TGDKVYVHLK NLASRPYTFH SHGITYYKEH EGAIYPDNTT DFQRADDKVY
160 170 180 190 200
PGEQYTYMLL ATEEQSPGEG DGNCVTRIYH SHIDAPKDIA SGLIGPLIIC
210 220 230 240 250
KKDSLDKEKE KHIDREFVVM FSVVDENFSW YLEDNIKTYC SEPEKVDKDN
260 270 280 290 300
EDFQESNRMY SVNGYTFGSL PGLSMCAEDR VKWYLFGMGN EVDVHAAFFH
310 320 330 340 350
GQALTNKNYR IDTINLFPAT LFDAYMVAQN PGEWMLSCQN LNHLKAGLQA
360 370 380 390 400
FFQVQECNKS SSKDNIRGKH VRHYYIAAEE IIWNYAPSGI DIFTKENLTA
410 420 430 440 450
PGSDSAVFFE QGTTRIGGSY KKLVYREYTD ASFTNRKERG PEEEHLGILG
460 470 480 490 500
PVIWAEVGDT IRVTFHNKGA YPLSIEPIGV RFNKNNEGTY YSPNYNPQSR
510 520 530 540 550
SVPPSASHVA PTETFTYEWT VPKEVGPTNA DPVCLAKMYY SAVDPTKDIF
560 570 580 590 600
TGLIGPMKIC KKGSLHANGR QKDVDKEFYL FPTVFDENES LLLEDNIRMF
610 620 630 640 650
TTAPDQVDKE DEDFQESNKM HSMNGFMYGN QPGLTMCKGD SVVWYLFSAG
660 670 680 690 700
NEADVHGIYF SGNTYLWRGE RRDTANLFPQ TSLTLHMWPD TEGTFNVECL
710 720 730 740 750
TTDHYTGGMK QKYTVNQCRR QSEDSTFYLG ERTYYIAAVE VEWDYSPQRE
760 770 780 790 800
WEKELHHLQE QNVSNAFLDK GEFYIGSKYK KVVYRQYTDS TFRVPVERKA
810 820 830 840 850
EEEHLGILGP QLHADVGDKV KIIFKNMATR PYSIHAHGVQ TESSTVTPTL
860 870 880 890 900
PGETLTYVWK IPERSGAGTE DSACIPWAYY STVDQVKDLY SGLIGPLIVC
910 920 930 940 950
RRPYLKVFNP RRKLEFALLF LVFDENESWY LDDNIKTYSD HPEKVNKDDE
960 970 980 990 1000
EFIESNKMHA INGRMFGNLQ GLTMHVGDEV NWYLMGMGNE IDLHTVHFHG
1010 1020 1030 1040 1050
HSFQYKHRGV YSSDVFDIFP GTYQTLEMFP RTPGIWLLHC HVTDHIHAGM
1060
ETTYTVLQNE DTKSG
Length:1,065
Mass (Da):122,205
Last modified:August 13, 1987 - v1
Checksum:i2F2F1294E2D30F58
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1060E → EGEYP in AAA51975 (PubMed:3486416).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02565563I → T Retained in the ER due to impaired N-glycosylation; may present a vulnerability factor for iron induced oxidative stress in Parkinson disease. 2 Publications1
Natural variantiVAR_032815367R → C.Corresponds to variant rs34624984dbSNPEnsembl.1
Natural variantiVAR_025656477P → L.1 PublicationCorresponds to variant rs35331711dbSNPEnsembl.1
Natural variantiVAR_025657544D → E Reduced ferroxidase activity; may present a vulnerability factor for iron induced oxidative stress in Parkinson disease. 2 PublicationsCorresponds to variant rs701753dbSNPEnsembl.1
Natural variantiVAR_025658551T → I.1 Publication1
Natural variantiVAR_025659793R → H.2 Publications1
Natural variantiVAR_025660841T → R.1 PublicationCorresponds to variant rs56033670dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.6. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Ceruloplasmin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KCWX-ray3.00A20-1065[»]
2J5WX-ray2.80A1-1065[»]
4EJXX-ray4.69A1-1065[»]
4ENZX-ray2.60A1-1065[»]
ProteinModelPortaliP00450.
SMRiP00450.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107748. 9 interactors.
IntActiP00450. 5 interactors.
STRINGi9606.ENSP00000264613.

Chemistry databases

DrugBankiDB00055. Drotrecogin alfa.

PTM databases

iPTMnetiP00450.
PhosphoSitePlusiP00450.
UniCarbKBiP00450.

Polymorphism and mutation databases

BioMutaiCP.
DMDMi116117.

2D gel databases

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

Proteomic databases

MaxQBiP00450.
PaxDbiP00450.
PeptideAtlasiP00450.
PRIDEiP00450.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264613; ENSP00000264613; ENSG00000047457.
GeneIDi1356.
KEGGihsa:1356.
UCSCiuc003ewy.6. human.

Organism-specific databases

CTDi1356.
DisGeNETi1356.
GeneCardsiCP.
GeneReviewsiCP.
HGNCiHGNC:2295. CP.
HPAiCAB008591.
HPA001834.
MalaCardsiCP.
MIMi117700. gene.
604290. phenotype.
neXtProtiNX_P00450.
Orphaneti48818. Aceruloplasminemia.
PharmGKBiPA26815.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1263. Eukaryota.
COG2132. LUCA.
HOGENOMiHOG000231499.
HOVERGENiHBG003674.
InParanoidiP00450.
KOiK13624.
OrthoDBiEOG091G00QL.
PhylomeDBiP00450.
TreeFamiTF329807.

Enzyme and pathway databases

BioCyciMetaCyc:HS00590-MONOMER.
ZFISH:HS00590-MONOMER.
BRENDAi1.16.3.1. 2681.
ReactomeiR-HSA-425410. Metal ion SLC transporters.
R-HSA-917937. Iron uptake and transport.
SABIO-RKP00450.
SIGNORiP00450.

Miscellaneous databases

ChiTaRSiCP. human.
EvolutionaryTraceiP00450.
GeneWikiiCeruloplasmin.
GenomeRNAii1356.
PMAP-CutDBP00450.
PROiP00450.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000047457.
CleanExiHS_CP.
ExpressionAtlasiP00450. baseline and differential.
GenevisibleiP00450. HS.

Family and domain databases

Gene3Di2.60.40.420. 6 hits.
InterProiIPR027150. CP.
IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PANTHERiPTHR10127:SF664. PTHR10127:SF664. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 196 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.