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P13987

- CD59_HUMAN

UniProt

P13987 - CD59_HUMAN

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Protein

CD59 glycoprotein

Gene

CD59

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

Functioni

Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore. This inhibitor appears to be species-specific. Involved in signal transduction for T-cell activation complexed to a protein tyrosine kinase.
The soluble form from urine retains its specific complement binding activity, but exhibits greatly reduced ability to inhibit MAC assembly on cell membranes.

GO - Molecular functioni

  1. complement binding Source: RefGenome

GO - Biological processi

  1. blood coagulation Source: ProtInc
  2. cell activation Source: RefGenome
  3. cell surface receptor signaling pathway Source: ProtInc
  4. innate immune response Source: Reactome
  5. negative regulation of activation of membrane attack complex Source: Ensembl
  6. negative regulation of apoptotic process Source: Ensembl
  7. positive regulation of T cell proliferation Source: Ensembl
  8. regulation of complement activation Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_118707. Regulation of Complement cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
CD59 glycoprotein
Alternative name(s):
1F5 antigen
20 kDa homologous restriction factor
Short name:
HRF-20
Short name:
HRF20
MAC-inhibitory protein
Short name:
MAC-IP
MEM43 antigen
Membrane attack complex inhibition factor
Short name:
MACIF
Membrane inhibitor of reactive lysis
Short name:
MIRL
Protectin
CD_antigen: CD59
Gene namesi
Name:CD59
Synonyms:MIC11, MIN1, MIN2, MIN3, MSK21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:1689. CD59.

Subcellular locationi

Cell membrane; Lipid-anchorGPI-anchor. Secreted
Note: Soluble form found in a number of tissues.

GO - Cellular componenti

  1. anchored component of external side of plasma membrane Source: MGI
  2. cell surface Source: UniProtKB
  3. compact myelin Source: Ensembl
  4. extracellular region Source: RefGenome
  5. extracellular space Source: UniProt
  6. extracellular vesicular exosome Source: UniProtKB
  7. focal adhesion Source: UniProtKB
  8. membrane Source: ProtInc
  9. plasma membrane Source: Reactome
  10. sarcolemma Source: Ensembl
  11. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Hemolytic anemia, CD59-mediated, with or without polyneuropathy (HACD59) [MIM:612300]: An autosomal recessive disorder characterized by infantile onset of chronic hemolysis and a relapsing-remitting polyneuropathy, often exacerbated by infection, and manifested as hypotonia, limb muscle weakness, and hyporeflexia.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891C → Y in HACD59. 1 Publication
VAR_070124

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi29 – 291Y → R: No loss of function. 1 Publication
Mutagenesisi33 – 331N → R or Q: No loss of function. 1 Publication
Mutagenesisi37 – 371D → R: No loss of function. 1 Publication
Mutagenesisi48 – 481F → R: Some loss of function. Some lysis. 1 Publication
Mutagenesisi49 – 491D → R: Loss of function. Lysis. 1 Publication
Mutagenesisi58 – 581L → E: No loss of function. 1 Publication
Mutagenesisi63 – 631K → E: No loss of function. 1 Publication
Mutagenesisi65 – 651W → E: Complete loss of function. Lysis. 1 Publication
Mutagenesisi66 – 661K → D: No loss of function. 1 Publication
Mutagenesisi66 – 661K → Q: Loss of glycation mediated inactivation. 1 Publication
Mutagenesisi67 – 671F → K: No loss of function. 1 Publication
Mutagenesisi69 – 691H → Q: Loss of glycation mediated inactivation. 1 Publication
Mutagenesisi72 – 721F → E: Almost complete loss of function. Lysis. 1 Publication
Mutagenesisi78 – 781R → E: Loss of function. Lysis. 1 Publication
Mutagenesisi79 – 791L → D: No loss of function. 1 Publication
Mutagenesisi81 – 811E → R: Almost complete loss of function. Lysis. 1 Publication
Mutagenesisi82 – 821N → K: No loss of function. 1 Publication
Mutagenesisi87 – 871Y → R: No loss of function. 1 Publication

Keywords - Diseasei

Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

MIMi612300. phenotype.
Orphaneti169464. Primary CD59 deficiency.
PharmGKBiPA26228.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – 10277CD59 glycoproteinPRO_0000036108Add
BLAST
Propeptidei103 – 12826Removed in mature form1 PublicationPRO_0000036109Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 511 Publication
Disulfide bondi31 ↔ 381 Publication
Glycosylationi43 – 431N-linked (GlcNAc...)2 Publications
Disulfide bondi44 ↔ 641 Publication
Glycosylationi66 – 661N-linked (Glc) (glycation)
Glycosylationi69 – 691N-linked (Glc) (glycation)
Disulfide bondi70 ↔ 881 Publication
Glycosylationi76 – 761O-linked (GalNAc...)Curated
Glycosylationi77 – 771O-linked (GalNAc...)Curated
Disulfide bondi89 ↔ 941 Publication
Lipidationi102 – 1021GPI-anchor amidated asparagine2 Publications

Post-translational modificationi

N- and O-glycosylated. The N-glycosylation mainly consists of a family of biantennary complex-type structures with and without lactosamine extensions and outer arm fucose residues. Also significant amounts of triantennary complexes (22%). Variable sialylation also present in the Asn-43 oligosaccharide. The predominant O-glycans are mono-sialylated forms of the disaccharide, Gal-beta-1,3GalNAc, and their sites of attachment are probably on Thr-76 and Thr-77. The GPI-anchor of soluble urinary CD59 has no inositol-associated phospholipid, but is composed of seven different GPI-anchor variants of one or more monosaccharide units. Major variants contain sialic acid, mannose and glucosamine. Sialic acid linked to an N-acetylhexosamine-galactose arm is present in two variants.2 Publications
Glycated. Glycation is found in diabetic subjects, but only at minimal levels in nondiabetic subjects. Glycated CD59 lacks MAC-inhibitory function and confers to vascular complications of diabetes.

Keywords - PTMi

Disulfide bond, Glycation, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiP13987.
PaxDbiP13987.
PeptideAtlasiP13987.
PRIDEiP13987.

PTM databases

PhosphoSiteiP13987.
UniCarbKBiP13987.

Expressioni

Gene expression databases

BgeeiP13987.
CleanExiHS_CD59.
ExpressionAtlasiP13987. baseline and differential.
GenevestigatoriP13987.

Organism-specific databases

HPAiCAB001448.
HPA026494.

Interactioni

Subunit structurei

Interacts with T-cell surface antigen CD2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CQ778I94EBI-297972,EBI-8716052From a different organism.
TMED10O355875EBI-297972,EBI-4405327From a different organism.
TMED2Q153634EBI-297972,EBI-998485

Protein-protein interaction databases

BioGridi107404. 17 interactions.
IntActiP13987. 11 interactions.
MINTiMINT-5000502.
STRINGi9606.ENSP00000340210.

Structurei

Secondary structure

1
128
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 293Combined sources
Beta strandi32 – 343Combined sources
Beta strandi41 – 433Combined sources
Beta strandi50 – 567Combined sources
Beta strandi59 – 657Combined sources
Helixi67 – 693Combined sources
Helixi72 – 798Combined sources
Beta strandi85 – 895Combined sources
Beta strandi91 – 933Combined sources
Helixi97 – 993Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CDQNMR-A26-102[»]
1CDRNMR-A26-102[»]
1CDSNMR-A26-102[»]
1ERGNMR-A26-95[»]
1ERHNMR-A26-95[»]
2J8BX-ray1.15A26-103[»]
2OFSX-ray2.12A26-99[»]
2UWRX-ray1.34A26-102[»]
2UX2X-ray1.80A/B/C26-102[»]
4BIKX-ray3.49B/D26-102[»]
ProteinModelPortaliP13987.
SMRiP13987. Positions 26-102.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13987.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 10883UPAR/Ly6Add
BLAST

Sequence similaritiesi

Contains 1 UPAR/Ly6 domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG83475.
HOGENOMiHOG000232180.
HOVERGENiHBG005284.
InParanoidiP13987.
KOiK04008.
OMAiKMNCILL.
PhylomeDBiP13987.
TreeFamiTF338524.

Family and domain databases

InterProiIPR018363. CD59_antigen_CS.
IPR027101. CD59_glyco.
IPR016054. LY6_UPA_recep-like.
IPR001526. LY6_UPAR.
[Graphical view]
PANTHERiPTHR10036:SF6. PTHR10036:SF6. 1 hit.
PfamiPF00021. UPAR_LY6. 1 hit.
[Graphical view]
SMARTiSM00134. LU. 1 hit.
[Graphical view]
PROSITEiPS00983. LY6_UPAR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P13987-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGIQGGSVLF GLLLVLAVFC HSGHSLQCYN CPNPTADCKT AVNCSSDFDA
60 70 80 90 100
CLITKAGLQV YNKCWKFEHC NFNDVTTRLR ENELTYYCCK KDLCNFNEQL
110 120
ENGGTSLSEK TVLLLVTPFL AAAWSLHP
Length:128
Mass (Da):14,177
Last modified:January 1, 1990 - v1
Checksum:i2F0D29CBE3C28505
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891C → Y in HACD59. 1 Publication
VAR_070124

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27909 mRNA. Translation: AAA60543.1.
M95708 mRNA. Translation: AAA60957.1.
X16447 mRNA. Translation: CAA34467.1.
X17198 mRNA. Translation: CAA35059.1.
M34671 mRNA. Translation: AAA51952.1.
M84345 Genomic DNA. No translation available.
M84349, M84346, M84348 Genomic DNA. Translation: AAA88793.1.
Z14113, Z14114, Z14115 Genomic DNA. Translation: CAA78486.1.
BT007104 mRNA. Translation: AAP35768.1.
BC001506 mRNA. Translation: AAH01506.1.
CCDSiCCDS7886.1.
PIRiA46252. RWHU59.
RefSeqiNP_000602.1. NM_000611.5.
NP_001120695.1. NM_001127223.1.
NP_001120697.1. NM_001127225.1.
NP_001120698.1. NM_001127226.1.
NP_001120699.1. NM_001127227.1.
NP_976074.1. NM_203329.2.
NP_976075.1. NM_203330.2.
NP_976076.1. NM_203331.2.
UniGeneiHs.278573.
Hs.709466.
Hs.710641.

Genome annotation databases

EnsembliENST00000351554; ENSP00000340210; ENSG00000085063.
ENST00000395850; ENSP00000379191; ENSG00000085063.
ENST00000415002; ENSP00000404822; ENSG00000085063.
ENST00000426650; ENSP00000402425; ENSG00000085063.
ENST00000437761; ENSP00000410182; ENSG00000085063.
ENST00000445143; ENSP00000403511; ENSG00000085063.
ENST00000525763; ENSP00000435179; ENSG00000085063.
ENST00000527577; ENSP00000432942; ENSG00000085063.
ENST00000528700; ENSP00000434617; ENSG00000085063.
GeneIDi966.
KEGGihsa:966.
UCSCiuc001mus.4. human.

Polymorphism databases

DMDMi116021.

Cross-referencesi

Web resourcesi

CD59base

CD59 mutation db

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27909 mRNA. Translation: AAA60543.1 .
M95708 mRNA. Translation: AAA60957.1 .
X16447 mRNA. Translation: CAA34467.1 .
X17198 mRNA. Translation: CAA35059.1 .
M34671 mRNA. Translation: AAA51952.1 .
M84345 Genomic DNA. No translation available.
M84349 , M84346 , M84348 Genomic DNA. Translation: AAA88793.1 .
Z14113 , Z14114 , Z14115 Genomic DNA. Translation: CAA78486.1 .
BT007104 mRNA. Translation: AAP35768.1 .
BC001506 mRNA. Translation: AAH01506.1 .
CCDSi CCDS7886.1.
PIRi A46252. RWHU59.
RefSeqi NP_000602.1. NM_000611.5.
NP_001120695.1. NM_001127223.1.
NP_001120697.1. NM_001127225.1.
NP_001120698.1. NM_001127226.1.
NP_001120699.1. NM_001127227.1.
NP_976074.1. NM_203329.2.
NP_976075.1. NM_203330.2.
NP_976076.1. NM_203331.2.
UniGenei Hs.278573.
Hs.709466.
Hs.710641.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CDQ NMR - A 26-102 [» ]
1CDR NMR - A 26-102 [» ]
1CDS NMR - A 26-102 [» ]
1ERG NMR - A 26-95 [» ]
1ERH NMR - A 26-95 [» ]
2J8B X-ray 1.15 A 26-103 [» ]
2OFS X-ray 2.12 A 26-99 [» ]
2UWR X-ray 1.34 A 26-102 [» ]
2UX2 X-ray 1.80 A/B/C 26-102 [» ]
4BIK X-ray 3.49 B/D 26-102 [» ]
ProteinModelPortali P13987.
SMRi P13987. Positions 26-102.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107404. 17 interactions.
IntActi P13987. 11 interactions.
MINTi MINT-5000502.
STRINGi 9606.ENSP00000340210.

PTM databases

PhosphoSitei P13987.
UniCarbKBi P13987.

Polymorphism databases

DMDMi 116021.

Proteomic databases

MaxQBi P13987.
PaxDbi P13987.
PeptideAtlasi P13987.
PRIDEi P13987.

Protocols and materials databases

DNASUi 966.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000351554 ; ENSP00000340210 ; ENSG00000085063 .
ENST00000395850 ; ENSP00000379191 ; ENSG00000085063 .
ENST00000415002 ; ENSP00000404822 ; ENSG00000085063 .
ENST00000426650 ; ENSP00000402425 ; ENSG00000085063 .
ENST00000437761 ; ENSP00000410182 ; ENSG00000085063 .
ENST00000445143 ; ENSP00000403511 ; ENSG00000085063 .
ENST00000525763 ; ENSP00000435179 ; ENSG00000085063 .
ENST00000527577 ; ENSP00000432942 ; ENSG00000085063 .
ENST00000528700 ; ENSP00000434617 ; ENSG00000085063 .
GeneIDi 966.
KEGGi hsa:966.
UCSCi uc001mus.4. human.

Organism-specific databases

CTDi 966.
GeneCardsi GC11M033721.
H-InvDB HIX0171358.
HGNCi HGNC:1689. CD59.
HPAi CAB001448.
HPA026494.
MIMi 107271. gene.
612300. phenotype.
neXtProti NX_P13987.
Orphaneti 169464. Primary CD59 deficiency.
PharmGKBi PA26228.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG83475.
HOGENOMi HOG000232180.
HOVERGENi HBG005284.
InParanoidi P13987.
KOi K04008.
OMAi KMNCILL.
PhylomeDBi P13987.
TreeFami TF338524.

Enzyme and pathway databases

Reactomei REACT_118707. Regulation of Complement cascade.

Miscellaneous databases

ChiTaRSi CD59. human.
EvolutionaryTracei P13987.
GeneWikii CD59.
GenomeRNAii 966.
NextBioi 4034.
PROi P13987.
SOURCEi Search...

Gene expression databases

Bgeei P13987.
CleanExi HS_CD59.
ExpressionAtlasi P13987. baseline and differential.
Genevestigatori P13987.

Family and domain databases

InterProi IPR018363. CD59_antigen_CS.
IPR027101. CD59_glyco.
IPR016054. LY6_UPA_recep-like.
IPR001526. LY6_UPAR.
[Graphical view ]
PANTHERi PTHR10036:SF6. PTHR10036:SF6. 1 hit.
Pfami PF00021. UPAR_LY6. 1 hit.
[Graphical view ]
SMARTi SM00134. LU. 1 hit.
[Graphical view ]
PROSITEi PS00983. LY6_UPAR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "CD59, an LY-6-like protein expressed in human lymphoid cells, regulates the action of the complement membrane attack complex on homologous cells."
    Davies A., Simmons D.L., Hale G., Harrison R.A., Tighe H., Lachmann P.J., Waldmann H.
    J. Exp. Med. 170:637-654(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: T-cell.
  2. "The CD59 antigen is a structural homologue of murine Ly-6 antigens but lacks interferon inducibility."
    Philbrick W.M., Palfree R.G.E., Roger G.E., Maher S.E., Bridgett M.M., Sirlin S., Bothwell A.L.M.
    Eur. J. Immunol. 20:87-92(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "20 KDa homologous restriction factor of complement resembles T cell activating protein."
    Okada H., Nagami Y., Takahashi K., Okada N., Hideshima T., Takizawa H., Kondo J.
    Biochem. Biophys. Res. Commun. 162:1553-1559(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Molecular cloning and characterization of MACIF, an inhibitor of membrane channel formation of complement."
    Sugita Y., Tobe T., Oda E., Tomita M., Yasukawa K., Yamaji N., Takemoto T., Furuichi K., Takayama M., Yano S.
    J. Biochem. 106:555-557(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Isolation and expression of the full-length cDNA encoding CD59 antigen of human lymphocytes."
    Sawada R., Ohashi K., Anaguchi H., Okazaki H., Hattori M., Minato N., Naruto M.
    DNA Cell Biol. 9:213-220(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. "Structure of the CD59-encoding gene: further evidence of a relationship to murine lymphocyte antigen Ly-6 protein."
    Petranka J.G., Fleenor D.E., Sykes K., Kaufman R.E., Rosse W.F.
    Proc. Natl. Acad. Sci. U.S.A. 89:7876-7879(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "Gene structure of human CD59 and demonstration that discrete mRNAs are generated by alternative polyadenylation."
    Tone M., Walsh L.A., Waldmann H.
    J. Mol. Biol. 227:971-976(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Blood.
  8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  10. "Complementary DNA sequence and deduced peptide sequence for CD59/MEM-43 antigen, the human homologue of murine lymphocyte antigen Ly-6C."
    Sawada R., Ohashi K., Okano K., Hattori M., Minato N., Naruto M.
    Nucleic Acids Res. 17:6728-6728(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-128.
  11. "Structural composition and functional characterization of soluble CD59: heterogeneity of the oligosaccharide and glycophosphoinositol (GPI) anchor revealed by laser-desorption mass spectrometric analysis."
    Meri S., Lehto T., Sutton C.W., Tyynelaa J., Baumann M.
    Biochem. J. 316:923-935(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT ASN-43, STRUCTURE OF CARBOHYDRATES.
  12. "Determination of carboxyl-terminal residue and disulfide bonds of MACIF (CD59), a glycosyl-phosphatidylinositol-anchored membrane protein."
    Sugita Y., Nakano Y., Oda E., Noda K., Tobe T., Miura N.H., Tomita M.
    J. Biochem. 114:473-477(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR AT ASN-102, DISULFIDE BONDS.
  13. "The human complement regulatory protein CD59 binds to the alpha-chain of C8 and to the ''b'' domain of C9."
    Ninomiya H., Sims P.J.
    J. Biol. Chem. 267:13675-13680(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C8 AND C9.
  14. "Mapping the regions of the complement inhibitor CD59 responsible for its species selective activity."
    Yu J., Dong S., Rushmere N.K., Morgan B.P., Abagyan R., Tomlinson S.
    Biochemistry 36:9423-9428(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF COMPLEMENT INHIBITORY DOMAIN.
  15. "Mutational analysis of the active site and antibody epitopes of the complement-inhibitory glycoprotein, CD59."
    Bodian D.L., Davis S.J., Morgan B.P., Rushmere N.K.
    J. Exp. Med. 185:507-516(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  16. "The glycosylation of the complement regulatory protein, human erythrocyte CD59."
    Rudd P.M., Morgan B.P., Wormald M.R., Harvey D.J., van den Berg C.W., Davis S.J., Ferguson M.A., Dwek R.A.
    J. Biol. Chem. 272:7229-7244(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF CARBOHYDRATES, STRUCTURE OF THE GPI-ANCHOR, PROTEIN SEQUENCE OF N-TERMINUS.
  17. "Molecular basis for a link between complement and the vascular complications of diabetes."
    Acosta J., Hettinga J., Flueckiger R., Krumrei N., Goldfine A., Angarita L., Halperin J.
    Proc. Natl. Acad. Sci. U.S.A. 97:5450-5455(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITION BY GLYCATION, GLYCATION AT LYS-66 AND HIS-69, MUTAGENESIS OF LYS-66 AND HIS-69.
  18. "Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins."
    Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C., Jensen O.N.
    Mol. Cell. Proteomics 2:1261-1270(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."
    Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N.
    J. Proteome Res. 5:935-943(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Computational approach for identification and characterization of GPI-anchored peptides in proteomics experiments."
    Omaetxebarria M.J., Elortza F., Rodriguez-Suarez E., Aloria K., Arizmendi J.M., Jensen O.N., Matthiesen R.
    Proteomics 7:1951-1960(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR AT ASN-102, IDENTIFICATION BY MASS SPECTROMETRY.
  21. "Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
    Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
    Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-43.
    Tissue: Milk.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Three-dimensional solution structure of the extracellular region of the complement regulatory protein CD59, a new cell-surface protein domain related to snake venom neurotoxins."
    Kieffer B., Driscoll P.C., Campbell I.D., Willis A.C., van der Merwe P.A., Davis S.J.
    Biochemistry 33:4471-4482(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 26-95.
  24. "Structure of a soluble, glycosylated form of the human complement regulatory protein CD59."
    Fletcher C.M., Harrison R.A., Lachmann P.J., Neuhaus D.
    Structure 2:185-199(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 26-102.
    Tissue: Urine.
  25. "Paroxysmal nocturnal hemoglobinuria due to hereditary nucleotide deletion in the HRF20 (CD59) gene."
    Motoyama N., Okada N., Yamashina M., Okada H.
    Eur. J. Immunol. 22:2669-2673(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN HACD59.
  26. "CD59 deficiency is associated with chronic hemolysis and childhood relapsing immune-mediated polyneuropathy."
    Nevo Y., Ben-Zeev B., Tabib A., Straussberg R., Anikster Y., Shorer Z., Fattal-Valevski A., Ta-Shma A., Aharoni S., Rabie M., Zenvirt S., Goldshmidt H., Fellig Y., Shaag A., Mevorach D., Elpeleg O.
    Blood 121:129-135(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HACD59 TYR-89.

Entry informationi

Entry nameiCD59_HUMAN
AccessioniPrimary (citable) accession number: P13987
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 26, 2014
This is version 170 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 cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

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