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P13987 (CD59_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CD59
Synonyms:MIC11, MIN1, MIN2, MIN3, MSK21
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length128 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Interacts with T-cell surface antigen CD2. Ref.13

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor. Secreted. Note: Soluble form found in a number of tissues. Ref.12 Ref.16 Ref.20

Post-translational modification

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. Ref.11 Ref.16

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.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.25 Ref.26

Sequence similarities

Contains 1 UPAR/Ly6 domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   DiseaseDisease mutation
Hereditary hemolytic anemia
   DomainSignal
   PTMDisulfide bond
Glycation
Glycoprotein
GPI-anchor
Lipoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement Ref.6. Source: ProtInc

cell activation

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell surface receptor signaling pathway

Traceable author statement PubMed 7691713. Source: ProtInc

innate immune response

Traceable author statement. Source: Reactome

negative regulation of activation of membrane attack complex

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of complement activation

Traceable author statement. Source: Reactome

   Cellular_componentanchored component of external side of plasma membrane

Inferred from direct assay PubMed 9724629. Source: MGI

cell surface

Inferred from direct assay PubMed 15907827. Source: UniProtKB

compact myelin

Inferred from electronic annotation. Source: Ensembl

extracellular region

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular space

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337. Source: UniProt

membrane

Traceable author statement Ref.6. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

sarcolemma

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncomplement binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CQ778I94EBI-297972,EBI-8716052From a different organism.
TMED10O355875EBI-297972,EBI-4405327From a different organism.
TMED2Q153634EBI-297972,EBI-998485

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.16
Chain26 – 10277CD59 glycoprotein
PRO_0000036108
Propeptide103 – 12826Removed in mature form
PRO_0000036109

Regions

Domain26 – 10883UPAR/Ly6

Amino acid modifications

Lipidation1021GPI-anchor amidated asparagine Ref.12 Ref.16 Ref.18 Ref.19 Ref.20
Glycosylation431N-linked (GlcNAc...) Ref.11 Ref.21
Glycosylation661N-linked (Glc) (glycation) Ref.17
Glycosylation691N-linked (Glc) (glycation) Ref.17
Glycosylation761O-linked (GalNAc...) Probable
Glycosylation771O-linked (GalNAc...) Probable
Disulfide bond28 ↔ 51 Ref.12
Disulfide bond31 ↔ 38 Ref.12
Disulfide bond44 ↔ 64 Ref.12
Disulfide bond70 ↔ 88 Ref.12
Disulfide bond89 ↔ 94 Ref.12

Natural variations

Natural variant891C → Y in HACD59. Ref.26
VAR_070124

Experimental info

Mutagenesis291Y → R: No loss of function.
Mutagenesis331N → R or Q: No loss of function.
Mutagenesis371D → R: No loss of function.
Mutagenesis481F → R: Some loss of function. Some lysis.
Mutagenesis491D → R: Loss of function. Lysis.
Mutagenesis581L → E: No loss of function.
Mutagenesis631K → E: No loss of function.
Mutagenesis651W → E: Complete loss of function. Lysis.
Mutagenesis661K → D: No loss of function. Ref.17
Mutagenesis661K → Q: Loss of glycation mediated inactivation. Ref.17
Mutagenesis671F → K: No loss of function.
Mutagenesis691H → Q: Loss of glycation mediated inactivation. Ref.17
Mutagenesis721F → E: Almost complete loss of function. Lysis.
Mutagenesis781R → E: Loss of function. Lysis.
Mutagenesis791L → D: No loss of function.
Mutagenesis811E → R: Almost complete loss of function. Lysis.
Mutagenesis821N → K: No loss of function.
Mutagenesis871Y → R: No loss of function.

Secondary structure

..................... 128
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13987 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 2F0D29CBE3C28505

FASTA12814,177
        10         20         30         40         50         60 
MGIQGGSVLF GLLLVLAVFC HSGHSLQCYN CPNPTADCKT AVNCSSDFDA CLITKAGLQV 

        70         80         90        100        110        120 
YNKCWKFEHC NFNDVTTRLR ENELTYYCCK KDLCNFNEQL ENGGTSLSEK TVLLLVTPFL 


AAAWSLHP 

« Hide

References

« Hide 'large scale' references
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRRWHU59. A46252.
RefSeqNP_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.
UniGeneHs.278573.
Hs.709466.
Hs.710641.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP13987.
SMRP13987. Positions 26-102.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107404. 15 interactions.
IntActP13987. 11 interactions.
MINTMINT-5000502.
STRING9606.ENSP00000340210.

PTM databases

PhosphoSiteP13987.
UniCarbKBP13987.

Polymorphism databases

DMDM116021.

Proteomic databases

PaxDbP13987.
PeptideAtlasP13987.
PRIDEP13987.

Protocols and materials databases

DNASU966.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351554; 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.
GeneID966.
KEGGhsa:966.
UCSCuc001mus.4. human.

Organism-specific databases

CTD966.
GeneCardsGC11M033721.
H-InvDBHIX0171358.
HGNCHGNC:1689. CD59.
HPACAB001448.
HPA026494.
MIM107271. gene.
612300. phenotype.
neXtProtNX_P13987.
Orphanet169464. Primary CD59 deficiency.
PharmGKBPA26228.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG83475.
HOGENOMHOG000232180.
HOVERGENHBG005284.
InParanoidP13987.
KOK04008.
OMAGHSLTCY.
PhylomeDBP13987.
TreeFamTF338524.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP13987.
BgeeP13987.
CleanExHS_CD59.
GenevestigatorP13987.

Family and domain databases

InterProIPR018363. CD59_antigen_CS.
IPR027101. CD59_glyco.
IPR016054. LY6_UPA_recep-like.
IPR001526. LY6_UPAR.
[Graphical view]
PANTHERPTHR10036:SF0. PTHR10036:SF0. 1 hit.
PfamPF00021. UPAR_LY6. 1 hit.
[Graphical view]
SMARTSM00134. LU. 1 hit.
[Graphical view]
PROSITEPS00983. LY6_UPAR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCD59. human.
EvolutionaryTraceP13987.
GeneWikiCD59.
GenomeRNAi966.
NextBio4034.
PROP13987.
SOURCESearch...

Entry information

Entry nameCD59_HUMAN
AccessionPrimary (citable) accession number: P13987
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries