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P15382 (KCNE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Potassium voltage-gated channel subfamily E member 1
Alternative name(s):
Delayed rectifier potassium channel subunit IsK
IKs producing slow voltage-gated potassium channel subunit beta Mink
Minimal potassium channel
Gene names
Name:KCNE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length129 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNQ1/KVLQT1 is proposed to form the slowly activating delayed rectifier cardiac potassium (IKs) channel. The outward current reaches its steady state only after 50 seconds. Assembled with KCNH2/HERG may modulate the rapidly activating component of the delayed rectifying potassium current in heart (IKr).

Subunit structure

Associates with KCNQ1/KVLQT1 and KCNH2/HERG.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed in heart, lung, kidney, testis, ovaries, small intestine, peripheral blood leukocytes. Not detected in pancreas, spleen, prostate and colon. Restrictively localized in the apical membrane portion of epithelial cells. Ref.6

Post-translational modification

Phosphorylation inhibits the potassium current By similarity.

N-glycosylation at Asn-26 occurs post-translationally, and requires prior cotranslational glycosylation at Asn-5.

Involvement in disease

Jervell and Lange-Nielsen syndrome 2 (JLNS2) [MIM:612347]: An autosomal recessive disorder characterized by congenital deafness, prolongation of the QT interval, syncopal attacks due to ventricular arrhythmias, and a high risk of sudden death.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.13 Ref.14 Ref.17

Long QT syndrome 5 (LQT5) [MIM:613695]: A heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Sequence similarities

Belongs to the potassium channel KCNE family.

Sequence caution

The sequence AAH36452.1 differs from that shown. Reason: Erroneous termination at position 106. Translated as Cys.

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Transport
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseDeafness
Disease mutation
Long QT syndrome
   DomainTransmembrane
Transmembrane helix
   LigandPotassium
   Molecular functionIon channel
Potassium channel
Voltage-gated channel
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell action potential involved in contraction

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

cellular response to acidity

Inferred from electronic annotation. Source: Ensembl

cellular response to cAMP

Inferred from direct assay PubMed 11299204. Source: BHF-UCL

epithelial cell maturation

Inferred from electronic annotation. Source: Ensembl

heart contraction

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from electronic annotation. Source: Ensembl

membrane repolarization

Inferred from direct assay PubMed 8900283. Source: BHF-UCL

membrane repolarization during action potential

Inferred from direct assay PubMed 11299204PubMed 8900283. Source: BHF-UCL

membrane repolarization during cardiac muscle cell action potential

Inferred from direct assay PubMed 8900283. Source: BHF-UCL

negative regulation of protein targeting to membrane

Inferred from electronic annotation. Source: Ensembl

positive regulation of potassium ion transmembrane transport

Inferred from direct assay PubMed 8900283. Source: BHF-UCL

potassium ion export

Inferred from direct assay Ref.17PubMed 17289006PubMed 8900283. Source: BHF-UCL

potassium ion transmembrane transport

Inferred from direct assay PubMed 11299204PubMed 8900283Ref.15. Source: BHF-UCL

protein N-linked glycosylation

Inferred from direct assay Ref.10. Source: UniProtKB

protein O-linked glycosylation

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of delayed rectifier potassium channel activity

Inferred from direct assay Ref.17. Source: BHF-UCL

regulation of heart rate by cardiac conduction

Inferred from mutant phenotype Ref.17. Source: BHF-UCL

regulation of potassium ion transmembrane transport

Inferred from direct assay Ref.17. Source: BHF-UCL

regulation of ventricular cardiac muscle cell membrane repolarization

Inferred from mutant phenotype Ref.15. Source: BHF-UCL

sensory perception of sound

Traceable author statement PubMed 9020846. Source: ProtInc

ventricular cardiac muscle cell action potential

Inferred from mutant phenotype Ref.15. Source: BHF-UCL

   Cellular_componentZ disc

Inferred from sequence or structural similarity PubMed 11697903. Source: BHF-UCL

apical plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay Ref.17. Source: BHF-UCL

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

lysosome

Inferred from direct assay PubMed 16780588. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 16780588. Source: UniProtKB

voltage-gated potassium channel complex

Inferred from direct assay PubMed 17289006. Source: BHF-UCL

   Molecular_functiondelayed rectifier potassium channel activity

Inferred from electronic annotation. Source: Ensembl

potassium channel regulator activity

Inferred from direct assay Ref.17PubMed 12522251PubMed 8900283. Source: BHF-UCL

telethonin binding

Inferred from physical interaction PubMed 11697903. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KCNQ1P517874EBI-7043557,EBI-359667
rCG_32667A6HIS03EBI-7043557,EBI-8784724From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 129129Potassium voltage-gated channel subfamily E member 1
PRO_0000144278

Regions

Transmembrane44 – 6623Helical; Potential
Topological domain67 – 12963Cytoplasmic Potential

Amino acid modifications

Modified residue1021Phosphoserine; by PKC By similarity
Glycosylation51N-linked (GlcNAc...) Ref.9 Ref.10
Glycosylation71O-linked (GalNAc...) Ref.10
Glycosylation261N-linked (GlcNAc...) Ref.9

Natural variations

Natural variant71T → I in JLNS2; impairs glycosylation at N-5. Ref.9 Ref.14
Corresponds to variant rs28933384 [ dbSNP | Ensembl ].
VAR_008897
Natural variant321R → H in LQT5; uncertain pathological significance. Ref.5 Ref.18
Corresponds to variant rs17857111 [ dbSNP | Ensembl ].
VAR_009906
Natural variant381S → G. Ref.2 Ref.5 Ref.21
Corresponds to variant rs1805127 [ dbSNP | Ensembl ].
VAR_001558
Natural variant471V → F in JLNS2. Ref.17
VAR_008898
Natural variant511L → H in JLNS2. Ref.17
VAR_008899
Natural variant521G → A.
Corresponds to variant rs17173509 [ dbSNP | Ensembl ].
VAR_048024
Natural variant58 – 592TL → PP in JLNS2.
VAR_001559
Natural variant741S → L in LQT5. Ref.15
VAR_008900
Natural variant761D → N in LQT5 and JLNS2; suppresses KCNQ1 currents markedly. Ref.14 Ref.15 Ref.16 Ref.17
VAR_008901
Natural variant851D → N Predisposes to acquired LQT5 susceptibility; shows a significant difference in current density and midpoint potential compared to the wild-type channel. Ref.12 Ref.20 Ref.21
Corresponds to variant rs1805128 [ dbSNP | Ensembl ].
VAR_008902
Natural variant871W → R in LQT5. Ref.17
VAR_008903
Natural variant981R → W in LQT5. Ref.18
VAR_009907
Natural variant1091V → I in LQT5; mild phenotype; significantly reduced the wild-type I(KS) current amplitude. Ref.19
VAR_012802
Natural variant1271P → T in LQT5. Ref.18
VAR_009908

Experimental info

Mutagenesis51N → Q: No measurable effect on assembly with KCNQ1 or cell surface expression of the KCNE1/KCNQ1 channel complex, and loss of glycosylation at N-5; when associated with T-28. Ref.10
Mutagenesis61T → F: No measurable effect on assembly with KCNQ1 or cell surface expression of the KCNE1/KCNQ1 channel complex. Loss of glycosylation at T-7. Ref.10
Mutagenesis71T → A: 50% reduction of cell surface expression of the KCNE1/KCNQ1 channel complex, and loss of glycosylation at N-5 and T-7; when associated with T-28. Ref.10
Mutagenesis281S → T: No measurable effect on assembly with KCNQ1 or cell surface expression of the KCNE1/KCNQ1 channel complex, and loss of glycosylation at N-5; when associated with Q-5. 50% reduction of cell surface expression of the KCNE1/KCNQ1 channel complex, and loss of glycosylation at N-5 and T-7; when associated with A-7. Ref.10
Mutagenesis691K → H: Lowers current 2-fold and leads to faster deactivation of KCNQ1/KCNE1 channel. Ref.8

Secondary structure

................. 129
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15382 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 5442D70929D4E87E

FASTA12914,675
        10         20         30         40         50         60 
MILSNTTAVT PFLTKLWQET VQQGGNMSGL ARRSPRSSDG KLEALYVLMV LGFFGFFTLG 

        70         80         90        100        110        120 
IMLSYIRSKK LEHSNDPFNV YIESDAWQEK DKAYVQARVL ESYRSCYVVE NHLAIEQPNT 


HLPETKPSP 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and sequence analysis of human genomic DNA encoding a novel membrane protein which exhibits a slowly activating potassium channel activity."
Murai T., Kakizuka A., Takumi T., Ohkubo H., Nakanishi S.
Biochem. Biophys. Res. Commun. 161:176-181(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Polymorphism of the gene encoding a human minimal potassium ion channel (minK)."
Lai L.P., Deng C.L., Moss A.J., Kass R.S., Liang C.S.
Gene 151:339-340(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-38.
Tissue: Leukocyte.
[3]"Delayed rectifier potassium channel subunit from human cornea epithelium."
Rae J.L.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cornea.
[4]NHLBI resequencing and genotyping service (RS&G)
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"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], VARIANTS HIS-32 AND GLY-38.
Tissue: Testis.
[6]"Properties of KvLQT1 K+ channel mutations in Romano-Ward and Jervell and Lange-Nielsen inherited cardiac arrhythmias."
Chouabe C., Neyroud N., Guicheney P., Lazdunski M., Romey G., Barhanin J.
EMBO J. 16:5472-5479(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"A minK-HERG complex regulates the cardiac potassium current I(Kr)."
McDonald T.V., Yu Z., Ming Z., Palma E., Meyers M.B., Wang K.-W., Goldstein S.A.N., Fishman G.I.
Nature 388:289-292(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNH2.
[8]"Disease-associated mutations in KCNE potassium channel subunits (MiRPs) reveal promiscuous disruption of multiple currents and conservation of mechanism."
Abbott G.W., Goldstein S.A.N.
FASEB J. 16:390-400(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-69.
[9]"Post-translational N-glycosylation of type I transmembrane KCNE1 peptides: implications for membrane protein biogenesis and disease."
Bas T., Gao G.Y., Lvov A., Chandrasekhar K.D., Gilmore R., Kobertz W.R.
J. Biol. Chem. 286:28150-28159(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-5 AND ASN-26, CHARACTERIZATION OF VARIANT JLNS2 ILE-7.
[10]"O-glycosylation of the cardiac I(Ks) complex."
Chandrasekhar K.D., Lvov A., Terrenoire C., Gao G.Y., Kass R.S., Kobertz W.R.
J. Physiol. (Lond.) 589:3721-3730(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-5 AND THR-7, MUTAGENESIS OF ASN-5; THR-6; THR-7 AND SER-28.
[11]"Structure of KCNE1 and implications for how it modulates the KCNQ1 potassium channel."
Kang C., Tian C., Soennichsen F.D., Smith J.A., Meiler J., George A.L. Jr., Vanoye C.G., Kim H.J., Sanders C.R.
Biochemistry 47:7999-8006(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[12]"Exclusion of KCNE1 (IsK) as a candidate gene for Jervell and Lange-Nielsen syndrome."
Tesson F., Donger C., Denjoy I., Berthet M., Bennaceur M., Petit C., Coumel P., Schwartz K., Guicheney P.
J. Mol. Cell. Cardiol. 28:2051-2055(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASN-85.
[13]"IsK and KvLQT1: mutation in either of the two subunits of the slow component of the delayed rectifier potassium channel can cause Jervell and Lange-Nielsen syndrome."
Tyson J., Tranebjaerg L., Bellman S., Wren C., Taylor J.F.N., Bathen J., Aslaksen B., Soerland S.J., Lund O., Malcolm S., Pembrey M., Bhattacharya S., Bitner-Glindzicz M.
Hum. Mol. Genet. 6:2179-2185(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT JLNS2 58-PRO-PRO-59.
[14]"KCNE1 mutations cause Jervell and Lange-Nielsen syndrome."
Schulze-Bahr E., Wang Q., Wedekind H., Haverkamp W., Chen Q., Sun Y., Rubie C., Hordt M., Towbin J.A., Borggrefe M., Assmann G., Qu X., Somberg J.C., Breithardt G., Oberti C., Funke H.
Nat. Genet. 17:267-268(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS JLNS2 ILE-7 AND ASN-76.
[15]"Mutations in the hminK gene cause long QT syndrome and suppress IKs function."
Splawski I., Tristani-Firouzi M., Lehmann M.H., Sanguinetti M.C., Keating M.T.
Nat. Genet. 17:338-340(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LQT5 LEU-74 AND ASN-76.
[16]"Mutation of the gene for IsK associated with both Jervell and Lange-Nielsen and Romano-Ward forms of Long-QT syndrome."
Duggal P., Vesely M.R., Wattanasirichaigoon D., Villafane J., Kaushik V., Beggs A.H.
Circulation 97:142-146(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT5 ASN-76.
[17]"Cellular dysfunction of LQT5-minK mutants: abnormalities of IKs, IKr and trafficking in long QT syndrome."
Bianchi L., Shen Z., Dennis A.T., Priori S.G., Napolitano C., Ronchetti E., Bryskin R., Schwartz P.J., Brown A.M.
Hum. Mol. Genet. 8:1499-1507(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS JLNS2 PHE-47; HIS-51 AND ASN-76, VARIANT LQT5 ARG-87.
[18]"Spectrum of mutations in long-QT syndrome genes. KVLQT1, HERG, SCN5A, KCNE1, and KCNE2."
Splawski I., Shen J., Timothy K.W., Lehmann M.H., Priori S.G., Robinson J.L., Moss A.J., Schwartz P.J., Towbin J.A., Vincent G.M., Keating M.T.
Circulation 102:1178-1185(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LQT5 HIS-32; TRP-98 AND THR-127.
[19]"A novel long-QT 5 gene mutation in the C-terminus (V109I) is associated with a mild phenotype."
Schulze-Bahr E., Schwarz M., Hauenschild S., Wedekind H., Funke H., Haverkamp W., Breithardt W., Pongs O., Isbrandt D., Breithardt G.
J. Mol. Med. 79:504-509(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT5 ILE-109.
[20]"Compound mutations: a common cause of severe long-QT syndrome."
Westenskow P., Splawski I., Timothy K.W., Keating M.T., Sanguinetti M.C.
Circulation 109:1834-1841(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASN-85.
[21]"The contribution of genes involved in potassium-recycling in the inner ear to noise-induced hearing loss."
Van Laer L., Carlsson P.-I., Ottschytsch N., Bondeson M.-L., Konings A., Vandevelde A., Dieltjens N., Fransen E., Snyders D., Borg E., Raes A., Van Camp G.
Hum. Mutat. 27:786-795(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLY-38 AND ASN-85, CHARACTERIZATION OF VARIANT ASN-85.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26685 Genomic DNA. Translation: AAA36129.1.
L33815 Genomic DNA. Translation: AAA63905.1.
L28168 mRNA. Translation: AAA58418.1.
AF135188 mRNA. Translation: AAD25096.1.
DQ784803 Genomic DNA. Translation: ABQ01238.1.
BC036452 mRNA. Translation: AAH36452.1. Sequence problems.
PIRA32447.
RefSeqNP_000210.2. NM_000219.4.
NP_001121140.1. NM_001127668.2.
NP_001121141.1. NM_001127669.2.
NP_001121142.1. NM_001127670.2.
NP_001257331.1. NM_001270402.1.
NP_001257332.1. NM_001270403.1.
NP_001257333.1. NM_001270404.1.
NP_001257334.1. NM_001270405.1.
UniGeneHs.121495.
Hs.745384.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K21NMR-A1-129[»]
ProteinModelPortalP15382.
SMRP15382. Positions 1-129.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109955. 2 interactions.
IntActP15382. 3 interactions.
MINTMINT-7297782.
STRING9606.ENSP00000337255.

Chemistry

BindingDBP15382.
ChEMBLCHEMBL4872.
DrugBankDB00808. Indapamide.

PTM databases

PhosphoSiteP15382.

Polymorphism databases

DMDM116416.

Proteomic databases

PaxDbP15382.
PRIDEP15382.

Protocols and materials databases

DNASU3753.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337385; ENSP00000337255; ENSG00000180509.
ENST00000399284; ENSP00000382225; ENSG00000180509.
ENST00000399286; ENSP00000382226; ENSG00000180509.
ENST00000399289; ENSP00000382228; ENSG00000180509.
ENST00000416357; ENSP00000416258; ENSG00000180509.
ENST00000432085; ENSP00000412498; ENSG00000180509.
GeneID3753.
KEGGhsa:3753.
UCSCuc002ytz.4. human.

Organism-specific databases

CTD3753.
GeneCardsGC21M035818.
HGNCHGNC:6240. KCNE1.
HPAHPA013752.
MIM176261. gene.
612347. phenotype.
613695. phenotype.
neXtProtNX_P15382.
Orphanet334. Familial atrial fibrillation.
90647. Jervell and Lange-Nielsen syndrome.
101016. Romano-Ward syndrome.
PharmGKBPA211.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41824.
HOGENOMHOG000113207.
HOVERGENHBG052226.
InParanoidP15382.
KOK04894.
OMAALYILMV.
OrthoDBEOG7WMCMH.
PhylomeDBP15382.
TreeFamTF335976.

Gene expression databases

ArrayExpressP15382.
BgeeP15382.
CleanExHS_KCNE1.
GenevestigatorP15382.

Family and domain databases

InterProIPR000369. K_chnl_volt-dep_bsu_KCNE.
IPR005424. K_chnl_volt-dep_bsu_KCNE1.
[Graphical view]
PANTHERPTHR17028. PTHR17028. 1 hit.
PfamPF02060. ISK_Channel. 1 hit.
[Graphical view]
PRINTSPR01604. KCNE1CHANNEL.
PR00168. KCNECHANNEL.
ProtoNetSearch...

Other

EvolutionaryTraceP15382.
GeneWikiKCNE1.
GenomeRNAi3753.
NextBio14697.
PROP15382.
SOURCESearch...

Entry information

Entry nameKCNE1_HUMAN
AccessionPrimary (citable) accession number: P15382
Secondary accession number(s): A5H1P2, Q8N709, Q91Z94
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 152 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 21

Human chromosome 21: entries, gene names and cross-references to MIM