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Protein

CD59 glycoprotein

Gene

CD59

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

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000085063-MONOMER.
ReactomeiR-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-5694530. Cargo concentration in the ER.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6807878. COPI-mediated anterograde transport.
R-HSA-977606. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:1689. CD59.

Subcellular locationi

GO - Cellular componenti

  • anchored component of external side of plasma membrane Source: MGI
  • cell surface Source: UniProtKB
  • compact myelin Source: Ensembl
  • endoplasmic reticulum-Golgi intermediate compartment membrane Source: Reactome
  • endoplasmic reticulum membrane Source: Reactome
  • ER to Golgi transport vesicle membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • Golgi membrane Source: Reactome
  • membrane Source: ProtInc
  • plasma membrane Source: Reactome
  • sarcolemma Source: Ensembl
  • 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)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:612300
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07012489C → Y in HACD59. 1 PublicationCorresponds to variant rs397514767dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi29Y → R: No loss of function. 1 Publication1
Mutagenesisi33N → R or Q: No loss of function. 1 Publication1
Mutagenesisi37D → R: No loss of function. 1 Publication1
Mutagenesisi48F → R: Some loss of function. Some lysis. 1 Publication1
Mutagenesisi49D → R: Loss of function. Lysis. 1 Publication1
Mutagenesisi58L → E: No loss of function. 1 Publication1
Mutagenesisi63K → E: No loss of function. 1 Publication1
Mutagenesisi65W → E: Complete loss of function. Lysis. 1 Publication1
Mutagenesisi66K → D: No loss of function. 1 Publication1
Mutagenesisi66K → Q: Loss of glycation mediated inactivation. 1 Publication1
Mutagenesisi67F → K: No loss of function. 1 Publication1
Mutagenesisi69H → Q: Loss of glycation mediated inactivation. 1 Publication1
Mutagenesisi72F → E: Almost complete loss of function. Lysis. 1 Publication1
Mutagenesisi78R → E: Loss of function. Lysis. 1 Publication1
Mutagenesisi79L → D: No loss of function. 1 Publication1
Mutagenesisi81E → R: Almost complete loss of function. Lysis. 1 Publication1
Mutagenesisi82N → K: No loss of function. 1 Publication1
Mutagenesisi87Y → R: No loss of function. 1 Publication1

Keywords - Diseasei

Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

DisGeNETi966.
MalaCardsiCD59.
MIMi612300. phenotype.
OpenTargetsiENSG00000085063.
Orphaneti169464. Primary CD59 deficiency.
PharmGKBiPA26228.

Polymorphism and mutation databases

BioMutaiCD59.
DMDMi116021.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Combined sources1 PublicationAdd BLAST25
ChainiPRO_000003610826 – 102CD59 glycoproteinAdd BLAST77
PropeptideiPRO_0000036109103 – 128Removed in mature form1 PublicationAdd BLAST26

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 511 Publication
Disulfide bondi31 ↔ 381 Publication
Glycosylationi43N-linked (GlcNAc...)2 Publications1
Disulfide bondi44 ↔ 641 Publication
Glycosylationi66N-linked (Glc) (glycation)1
Disulfide bondi70 ↔ 881 Publication
Glycosylationi76O-linked (GalNAc...)Curated1
Glycosylationi77O-linked (GalNAc...)Curated1
Disulfide bondi89 ↔ 941 Publication
Lipidationi102GPI-anchor amidated asparagine2 Publications1

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

EPDiP13987.
PaxDbiP13987.
PeptideAtlasiP13987.
PRIDEiP13987.

PTM databases

iPTMnetiP13987.
PhosphoSitePlusiP13987.
SwissPalmiP13987.
UniCarbKBiP13987.

Expressioni

Gene expression databases

BgeeiENSG00000085063.
CleanExiHS_CD59.
ExpressionAtlasiP13987. baseline and differential.
GenevisibleiP13987. HS.

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi107404. 33 interactors.
IntActiP13987. 25 interactors.
MINTiMINT-5000502.
STRINGi9606.ENSP00000340210.

Structurei

Secondary structure

1128
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 29Combined sources3
Beta strandi32 – 34Combined sources3
Beta strandi41 – 43Combined sources3
Beta strandi50 – 56Combined sources7
Beta strandi59 – 65Combined sources7
Helixi67 – 69Combined sources3
Helixi72 – 79Combined sources8
Beta strandi85 – 89Combined sources5
Beta strandi91 – 93Combined sources3
Helixi97 – 99Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5IMTX-ray2.70D26-102[»]
5IMYX-ray2.40C/D26-102[»]
ProteinModelPortaliP13987.
SMRiP13987.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13987.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 108UPAR/Ly6Add BLAST83

Sequence similaritiesi

Contains 1 UPAR/Ly6 domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J39P. Eukaryota.
ENOG410ZEQP. LUCA.
GeneTreeiENSGT00390000016309.
HOGENOMiHOG000232180.
HOVERGENiHBG005284.
InParanoidiP13987.
KOiK04008.
OMAiNKAAFSI.
PhylomeDBiP13987.
TreeFamiTF338524.

Family and domain databases

InterProiIPR018363. CD59_antigen_CS.
IPR027101. CD59_glyco.
IPR016054. LY6_UPA_recep-like.
[Graphical view]
PANTHERiPTHR10036:SF9. PTHR10036:SF9. 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_07012489C → Y in HACD59. 1 PublicationCorresponds to variant rs397514767dbSNPEnsembl.1

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.

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.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5IMTX-ray2.70D26-102[»]
5IMYX-ray2.40C/D26-102[»]
ProteinModelPortaliP13987.
SMRiP13987.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107404. 33 interactors.
IntActiP13987. 25 interactors.
MINTiMINT-5000502.
STRINGi9606.ENSP00000340210.

PTM databases

iPTMnetiP13987.
PhosphoSitePlusiP13987.
SwissPalmiP13987.
UniCarbKBiP13987.

Polymorphism and mutation databases

BioMutaiCD59.
DMDMi116021.

Proteomic databases

EPDiP13987.
PaxDbiP13987.
PeptideAtlasiP13987.
PRIDEiP13987.

Protocols and materials databases

DNASUi966.
Structural Biology KnowledgebaseSearch...

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.

Organism-specific databases

CTDi966.
DisGeNETi966.
GeneCardsiCD59.
H-InvDBHIX0171358.
HGNCiHGNC:1689. CD59.
HPAiCAB001448.
HPA026494.
MalaCardsiCD59.
MIMi107271. gene.
612300. phenotype.
neXtProtiNX_P13987.
OpenTargetsiENSG00000085063.
Orphaneti169464. Primary CD59 deficiency.
PharmGKBiPA26228.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J39P. Eukaryota.
ENOG410ZEQP. LUCA.
GeneTreeiENSGT00390000016309.
HOGENOMiHOG000232180.
HOVERGENiHBG005284.
InParanoidiP13987.
KOiK04008.
OMAiNKAAFSI.
PhylomeDBiP13987.
TreeFamiTF338524.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000085063-MONOMER.
ReactomeiR-HSA-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-HSA-5694530. Cargo concentration in the ER.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6807878. COPI-mediated anterograde transport.
R-HSA-977606. Regulation of Complement cascade.

Miscellaneous databases

ChiTaRSiCD59. human.
EvolutionaryTraceiP13987.
GeneWikiiCD59.
GenomeRNAii966.
PROiP13987.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000085063.
CleanExiHS_CD59.
ExpressionAtlasiP13987. baseline and differential.
GenevisibleiP13987. HS.

Family and domain databases

InterProiIPR018363. CD59_antigen_CS.
IPR027101. CD59_glyco.
IPR016054. LY6_UPA_recep-like.
[Graphical view]
PANTHERiPTHR10036:SF9. PTHR10036:SF9. 1 hit.
PfamiPF00021. UPAR_LY6. 1 hit.
[Graphical view]
SMARTiSM00134. LU. 1 hit.
[Graphical view]
PROSITEiPS00983. LY6_UPAR. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 30, 2016
This is version 191 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

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.