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P32297 (ACHA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neuronal acetylcholine receptor subunit alpha-3
Gene names
Name:CHRNA3
Synonyms:NACHRA3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.

Subunit structure

Neuronal AChR is composed of two different types of subunits: alpha and beta. Alpha-3 subunit can be combined to beta-2 or beta-4 to give rise to functional receptors. Interacts with RIC3; which is required for proper folding and assembly. Ref.12

Subcellular location

Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.

Polymorphism

Genetic variations in CHRNA3 have been associated with susceptibility to smoking-related behavioral traits and lung cancer, contributing to the smoking quantitative trait locus 3 (SQTL3) [MIM:612052].

Sequence similarities

Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-3/CHRNA3 sub-subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of transmembrane receptor protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

behavioral response to nicotine

Inferred from mutant phenotype PubMed 18227835. Source: UniProtKB

cation transport

Inferred from direct assay Ref.3. Source: GOC

ion transmembrane transport

Traceable author statement PubMed 20438829. Source: GOC

ion transport

Non-traceable author statement Ref.3. Source: UniProtKB

locomotory behavior

Inferred from sequence or structural similarity. Source: UniProtKB

nervous system development

Inferred from mutant phenotype Ref.6. Source: UniProtKB

regulation of acetylcholine secretion, neurotransmission

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of dendrite morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of excitatory postsynaptic membrane potential

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of membrane potential

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of smooth muscle contraction

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Inferred from direct assay Ref.3. Source: UniProtKB

synaptic transmission

Traceable author statement. Source: Reactome

synaptic transmission involved in micturition

Inferred from mutant phenotype Ref.6. Source: UniProtKB

synaptic transmission, cholinergic

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentacetylcholine-gated channel complex

Inferred from direct assay Ref.3. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Non-traceable author statement Ref.3. Source: UniProtKB

neuronal cell body

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic density

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetylcholine binding

Inferred by curator Ref.3. Source: UniProtKB

acetylcholine receptor activity

Inferred from direct assay Ref.3. Source: UniProtKB

acetylcholine-activated cation-selective channel activity

Inferred from direct assay Ref.3. Source: UniProtKB

ligand-gated ion channel activity

Traceable author statement PubMed 20438829. Source: DFLAT

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P32297-2)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: P32297-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MGSGPL → MALAV
Isoform 3 (identifier: P32297-3)

The sequence of this isoform differs from the canonical sequence as follows:
     464-505: IQDDWKYVAMVIDRIFLWVFTLVCILGTAGLFLQPLMAREDA → EQKAQEIQQLKRKEKSTETSDQEPGL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 505474Neuronal acetylcholine receptor subunit alpha-3
PRO_0000000346

Regions

Topological domain32 – 240209Extracellular Potential
Transmembrane241 – 26525Helical; Potential
Transmembrane273 – 29119Helical; Potential
Transmembrane307 – 32822Helical; Potential
Topological domain329 – 477149Cytoplasmic Potential
Transmembrane478 – 49720Helical; Potential

Amino acid modifications

Modified residue4131Phosphoserine By similarity
Modified residue4161Phosphoserine By similarity
Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation1721N-linked (GlcNAc...) Potential
Disulfide bond159 ↔ 173 By similarity
Disulfide bond223 ↔ 224Associated with receptor activation By similarity

Natural variations

Alternative sequence1 – 66MGSGPL → MALAV in isoform 1.
VSP_037750
Alternative sequence464 – 50542IQDDW…AREDA → EQKAQEIQQLKRKEKSTETS DQEPGL in isoform 3.
VSP_037751
Natural variant231Missing. Ref.3 Ref.4 Ref.5 Ref.9
VAR_013240
Natural variant371R → H.
Corresponds to variant rs8192475 [ dbSNP | Ensembl ].
VAR_059110

Experimental info

Sequence conflict5 – 1410PLSLPLALSP → ALAAPGAVA in AAA59942. Ref.2
Sequence conflict12 – 154LSPP → CRA in AAC84176. Ref.1
Sequence conflict1021D → G in AAC84176. Ref.1
Sequence conflict134 – 1352DD → TT in AAC84176. Ref.1
Sequence conflict2371I → S in AAC84176. Ref.1
Sequence conflict4321L → V in AAC84176. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified July 28, 2009. Version 4.
Checksum: 478D7712D59ACB2D

FASTA50557,480
        10         20         30         40         50         60 
MGSGPLSLPL ALSPPRLLLL LLLSLLPVAR ASEAEHRLFE RLFEDYNEII RPVANVSDPV 

        70         80         90        100        110        120 
IIHFEVSMSQ LVKVDEVNQI METNLWLKQI WNDYKLKWNP SDYGGAEFMR VPAQKIWKPD 

       130        140        150        160        170        180 
IVLYNNAVGD FQVDDKTKAL LKYTGEVTWI PPAIFKSSCK IDVTYFPFDY QNCTMKFGSW 

       190        200        210        220        230        240 
SYDKAKIDLV LIGSSMNLKD YWESGEWAII KAPGYKHDIK YNCCEEIYPD ITYSLYIRRL 

       250        260        270        280        290        300 
PLFYTINLII PCLLISFLTV LVFYLPSDCG EKVTLCISVL LSLTVFLLVI TETIPSTSLV 

       310        320        330        340        350        360 
IPLIGEYLLF TMIFVTLSIV ITVFVLNVHY RTPTTHTMPS WVKTVFLNLL PRVMFMTRPT 

       370        380        390        400        410        420 
SNEGNAQKPR PLYGAELSNL NCFSRAESKG CKEGYPCQDG MCGYCHHRRI KISNFSANLT 

       430        440        450        460        470        480 
RSSSSESVDA VLSLSALSPE IKEAIQSVKY IAENMKAQNE AKEIQDDWKY VAMVIDRIFL 

       490        500 
WVFTLVCILG TAGLFLQPLM AREDA 

« Hide

Isoform 1 [UniParc].

Checksum: F4D2DA153F2B3476
Show »

FASTA50457,423
Isoform 3 [UniParc].

Checksum: F8C4F79BDC30A44E
Show »

FASTA48955,637

References

« Hide 'large scale' references
[1]"Molecular cloning of human neuronal nicotinic receptor alpha 3-subunit."
Fornasari D., Chini B., Tarroni P., Clementi F.
Neurosci. Lett. 111:351-356(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Expression of mRNAs in human thymus coding for the alpha 3 subunit of a neuronal acetylcholine receptor."
Mihovilovic M., Roses A.D.
Exp. Neurol. 111:175-180(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Thymus.
[3]"Comparative structure of human neuronal alpha 2-alpha 7 and beta 2-beta 4 nicotinic acetylcholine receptor subunits and functional expression of the alpha 2, alpha 3, alpha 4, alpha 7, beta 2, and beta 4 subunits."
Elliott K.J., Ellis S.B., Berckhan K.J., Urrutia A., Chavez-Noriega L.E., Johnson E.C., Velicelebi G., Harpold M.M.
J. Mol. Neurosci. 7:217-228(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-23 DEL.
[4]"Cloning and sequence of full-length cDNAs encoding the human neuronal nicotinic acetylcholine receptor (nAChR) subunits beta3 and beta4 and expression of seven nAChR subunits in the human neuroblastoma cell line SH-SY5Y and/or IMR-32."
Groot Kormelink P.J., Luyten W.H.M.L.
FEBS Lett. 400:309-314(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-23 DEL.
[5]"The structures of the human neuronal nicotinic acetylcholine receptor beta2- and alpha3-subunit genes (CHRNB2 and CHRNA3)."
Rempel N., Heyers S., Engels H., Sleegers E., Steinlein O.K.
Hum. Genet. 103:645-653(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), VARIANT LEU-23 DEL.
[6]"Characterization of the human beta4 nAChR gene and polymorphisms in CHRNA3 and CHRNB4."
Lev-Lehman E., Bercovich D., Xu W., Stockton D.W., Beaudet A.L.
J. Hum. Genet. 46:362-366(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"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] (ISOFORMS 2 AND 3).
[8]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 2 AND 3), VARIANT LEU-23 DEL.
Tissue: Brain and Lung.
[10]"Cloning cholinergic receptors in human keratinocytes."
Arredondo J., Grando S.A.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-495 (ISOFORMS 1/2).
Tissue: Keratinocyte.
[11]Anand R., Lindstrom J.
Submitted (JUN-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-505 (ISOFORMS 1/2).
Tissue: Brain.
[12]"RIC-3 enhances functional expression of multiple nicotinic acetylcholine receptor subtypes in mammalian cells."
Lansdell S.J., Gee V.J., Harkness P.C., Doward A.I., Baker E.R., Gibb A.J., Millar N.S.
Mol. Pharmacol. 68:1431-1438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RIC3.
[13]"Genomics: when the smoke clears."
Chanock S.J., Hunter D.J.
Nature 452:537-538(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SQTL3 AND LUNG CANCER.
[14]"A susceptibility locus for lung cancer maps to nicotinic acetylcholine receptor subunit genes on 15q25."
Hung R.J., McKay J.D., Gaborieau V., Boffetta P., Hashibe M., Zaridze D., Mukeria A., Szeszenia-Dabrowska N., Lissowska J., Rudnai P., Fabianova E., Mates D., Bencko V., Foretova L., Janout V., Chen C., Goodman G., Field J.K. expand/collapse author list , Liloglou T., Xinarianos G., Cassidy A., McLaughlin J., Liu G., Narod S., Krokan H.E., Skorpen F., Elvestad M.B., Hveem K., Vatten L., Linseisen J., Clavel-Chapelon F., Vineis P., Bueno-de-Mesquita H.B., Lund E., Martinez C., Bingham S., Rasmuson T., Hainaut P., Riboli E., Ahrens W., Benhamou S., Lagiou P., Trichopoulos D., Holcatova I., Merletti F., Kjaerheim K., Agudo A., Macfarlane G., Talamini R., Simonato L., Lowry R., Conway D.I., Znaor A., Healy C., Zelenika D., Boland A., Delepine M., Foglio M., Lechner D., Matsuda F., Blanche H., Gut I., Heath S., Lathrop M., Brennan P.
Nature 452:633-637(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SQTL3 AND LUNG CANCER.
[15]"A variant associated with nicotine dependence, lung cancer and peripheral arterial disease."
Thorgeirsson T.E., Geller F., Sulem P., Rafnar T., Wiste A., Magnusson K.P., Manolescu A., Thorleifsson G., Stefansson H., Ingason A., Stacey S.N., Bergthorsson J.T., Thorlacius S., Gudmundsson J., Jonsson T., Jakobsdottir M., Saemundsdottir J., Olafsdottir O. expand/collapse author list , Gudmundsson L.J., Bjornsdottir G., Kristjansson K., Skuladottir H., Isaksson H.J., Gudbjartsson T., Jones G.T., Mueller T., Gottsaeter A., Flex A., Aben K.K.H., de Vegt F., Mulders P.F.A., Isla D., Vidal M.J., Asin L., Saez B., Murillo L., Blondal T., Kolbeinsson H., Stefansson J.G., Hansdottir I., Runarsdottir V., Pola R., Lindblad B., van Rij A.M., Dieplinger B., Haltmayer M., Mayordomo J.I., Kiemeney L.A., Matthiasson S.E., Oskarsson H., Tyrfingsson T., Gudbjartsson D.F., Gulcher J.R., Jonsson S., Thorsteinsdottir U., Kong A., Stefansson K.
Nature 452:638-642(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SQTL3 AND LUNG CANCER.
[16]"Genome-wide association scan of tag SNPs identifies a susceptibility locus for lung cancer at 15q25.1."
Amos C.I., Wu X., Broderick P., Gorlov I.P., Gu J., Eisen T., Dong Q., Zhang Q., Gu X., Vijayakrishnan J., Sullivan K., Matakidou A., Wang Y., Mills G., Doheny K., Tsai Y.-Y., Chen W.V., Shete S., Spitz M.R., Houlston R.S.
Nat. Genet. 40:616-622(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SQTL3 AND LUNG CANCER.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86383 mRNA. Translation: AAC84176.1.
M37981 mRNA. Translation: AAA59942.1.
U62432 mRNA. Translation: AAB40110.1.
Y08418 mRNA. Translation: CAA69695.1.
AJ007783 expand/collapse EMBL AC list , AJ007784, AJ007785, AJ007786, AJ007787 Genomic DNA. Translation: CAA07682.1.
BT006646 mRNA. Translation: AAP35292.1.
BT006897 mRNA. Translation: AAP35543.1.
AC027228 Genomic DNA. No translation available.
AC067863 Genomic DNA. No translation available.
BC000513 mRNA. Translation: AAH00513.1.
BC001642 mRNA. Translation: AAH01642.1.
BC002996 mRNA. Translation: AAH02996.1.
BC006114 mRNA. Translation: AAH06114.1.
BC098443 mRNA. Translation: AAH98443.1.
AF385584 mRNA. Translation: AAK68110.1.
X53559 mRNA. Translation: CAA37625.1.
CCDSCCDS10305.1. [P32297-2]
CCDS53964.1. [P32297-3]
PIRA37040.
A53956.
RefSeqNP_000734.2. NM_000743.4. [P32297-2]
NP_001160166.1. NM_001166694.1. [P32297-3]
UniGeneHs.89605.

3D structure databases

ProteinModelPortalP32297.
SMRP32297. Positions 32-345, 431-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107558. 1 interaction.
STRING9606.ENSP00000315602.

Chemistry

BindingDBP32297.
ChEMBLCHEMBL2111384.
GuidetoPHARMACOLOGY464.

PTM databases

PhosphoSiteP32297.

Polymorphism databases

DMDM254763435.

Proteomic databases

PaxDbP32297.
PRIDEP32297.

Protocols and materials databases

DNASU1136.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326828; ENSP00000315602; ENSG00000080644. [P32297-2]
ENST00000348639; ENSP00000267951; ENSG00000080644. [P32297-3]
ENST00000559658; ENSP00000452896; ENSG00000080644. [P32297-2]
GeneID1136.
KEGGhsa:1136.
UCSCuc002beb.3. human. [P32297-3]
uc002bec.3. human. [P32297-2]

Organism-specific databases

CTD1136.
GeneCardsGC15M078885.
H-InvDBHIX0017542.
HGNCHGNC:1957. CHRNA3.
HPAHPA029430.
MIM118503. gene.
612052. phenotype.
neXtProtNX_P32297.
PharmGKBPA113.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290206.
HOVERGENHBG003756.
InParanoidP32297.
KOK04805.
OMARTESKGC.
OrthoDBEOG72JWGV.
PhylomeDBP32297.
TreeFamTF315605.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.

Gene expression databases

ArrayExpressP32297.
BgeeP32297.
CleanExHS_CHRNA3.
GenevestigatorP32297.

Family and domain databases

Gene3D1.20.120.370. 2 hits.
2.70.170.10. 1 hit.
InterProIPR027361. Acetylcholine_rcpt_TM.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
IPR002394. Nicotinic_acetylcholine_rcpt.
[Graphical view]
PANTHERPTHR18945. PTHR18945. 1 hit.
PfamPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSPR00254. NICOTINICR.
PR00252. NRIONCHANNEL.
SUPFAMSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsTIGR00860. LIC. 1 hit.
PROSITEPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCHRNA3. human.
GeneWikiCHRNA3.
GenomeRNAi1136.
NextBio4726.
PROP32297.
SOURCESearch...

Entry information

Entry nameACHA3_HUMAN
AccessionPrimary (citable) accession number: P32297
Secondary accession number(s): Q15823 expand/collapse secondary AC list , Q4KMN8, Q86U77, Q96RH3, Q99553, Q9BQ93, Q9BRR4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: July 28, 2009
Last modified: July 9, 2014
This is version 154 of the entry and version 4 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

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 15

Human chromosome 15: entries, gene names and cross-references to MIM