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P36544 (ACHA7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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-7
Gene names
Name:CHRNA7
Synonyms:NACHRA7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length502 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. The channel is blocked by alpha-bungarotoxin.

Subunit structure

Homopentamer. Interacts with RIC3; which is required for proper folding and assembly. Ref.14 Ref.15

Subcellular location

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

Sequence similarities

Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-7/CHRNA7 sub-subfamily. [View classification]

Mass spectrometry

Molecular mass is 54157.68 Da from positions 23 - 502. Determined by MALDI. Ref.13

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPK activity

Inferred from direct assay PubMed 10771023. Source: UniProtKB

calcium ion transport

Inferred from direct assay Ref.1. Source: UniProtKB

cellular calcium ion homeostasis

Inferred from mutant phenotype PubMed 16280133. Source: UniProtKB

cognition

Inferred from mutant phenotype PubMed 16754836. Source: UniProtKB

ion transport

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

memory

Non-traceable author statement PubMed 10681545. Source: UniProtKB

negative regulation of tumor necrosis factor production

Inferred from mutant phenotype PubMed 12508119. Source: UniProtKB

positive regulation of angiogenesis

Inferred from mutant phenotype PubMed 12189247PubMed 16280133. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 16280133PubMed 17498763. Source: UniProtKB

response to hypoxia

Inferred from direct assay PubMed 12189247. Source: UniProtKB

response to nicotine

Inferred from direct assay PubMed 12189247Ref.1. Source: UniProtKB

signal transduction

Inferred from direct assay Ref.3. Source: UniProtKB

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentacetylcholine-gated channel complex

Inferred from direct assay Ref.3. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

integral component of membrane

Non-traceable author statement Ref.1Ref.3. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 16280133. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetylcholine binding

Inferred from direct assay Ref.1. Source: UniProtKB

acetylcholine receptor activity

Inferred from direct assay Ref.3. Source: UniProtKB

acetylcholine-activated cation-selective channel activity

Inferred from direct assay Ref.1Ref.3. Source: UniProtKB

beta-amyloid binding

Inferred from physical interaction PubMed 10681545. Source: UniProtKB

chloride channel regulator activity

Inferred from direct assay Ref.1. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.1. Source: UniProtKB

toxic substance binding

Inferred from direct assay PubMed 12508119. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P36544-1)

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 2 (identifier: P36544-2)

The sequence of this isoform differs from the canonical sequence as follows:
     18-18: H → HGKATASPPSTPPWDPGHIPGASVRPAPGP
Note: No experimental confirmation available.
Isoform 3 (identifier: P36544-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-181: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Chain23 – 502480Neuronal acetylcholine receptor subunit alpha-7
PRO_0000000366

Regions

Topological domain23 – 230208Extracellular Potential
Transmembrane231 – 25525Helical; Potential
Transmembrane262 – 28019Helical; Potential
Transmembrane296 – 31722Helical; Potential
Topological domain318 – 469152Cytoplasmic Potential
Transmembrane470 – 49021Helical; Potential

Amino acid modifications

Glycosylation461N-linked (GlcNAc...) Potential
Glycosylation901N-linked (GlcNAc...) Potential
Glycosylation1331N-linked (GlcNAc...) Potential
Disulfide bond150 ↔ 164 By similarity
Disulfide bond212 ↔ 213Associated with receptor activation By similarity

Natural variations

Alternative sequence1 – 181181Missing in isoform 3.
VSP_044268
Alternative sequence181H → HGKATASPPSTPPWDPGHIP GASVRPAPGP in isoform 2.
VSP_043019

Experimental info

Sequence conflict111A → G in CAA49778. Ref.1
Sequence conflict581S → N in AAA83561. Ref.2
Sequence conflict581S → N in AAK68111. Ref.6
Sequence conflict1341S → P in AAA83561. Ref.2
Sequence conflict1341S → P in AAK68111. Ref.6
Sequence conflict3641C → S in CAA80672. Ref.11
Sequence conflict3751A → G in CAA49778. Ref.1
Sequence conflict409 – 4135RMACS → AWPAP in CAA80672. Ref.11

Secondary structure

............. 502
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1997. Version 5.
Checksum: D94B3A482EAA0E42

FASTA50256,449
        10         20         30         40         50         60 
MRCSPGGVWL ALAASLLHVS LQGEFQRKLY KELVKNYNPL ERPVANDSQP LTVYFSLSLL 

        70         80         90        100        110        120 
QIMDVDEKNQ VLTTNIWLQM SWTDHYLQWN VSEYPGVKTV RFPDGQIWKP DILLYNSADE 

       130        140        150        160        170        180 
RFDATFHTNV LVNSSGHCQY LPPGIFKSSC YIDVRWFPFD VQHCKLKFGS WSYGGWSLDL 

       190        200        210        220        230        240 
QMQEADISGY IPNGEWDLVG IPGKRSERFY ECCKEPYPDV TFTVTMRRRT LYYGLNLLIP 

       250        260        270        280        290        300 
CVLISALALL VFLLPADSGE KISLGITVLL SLTVFMLLVA EIMPATSDSV PLIAQYFAST 

       310        320        330        340        350        360 
MIIVGLSVVV TVIVLQYHHH DPDGGKMPKW TRVILLNWCA WFLRMKRPGE DKVRPACQHK 

       370        380        390        400        410        420 
QRRCSLASVE MSAVAPPPAS NGNLLYIGFR GLDGVHCVPT PDSGVVCGRM ACSPTHDEHL 

       430        440        450        460        470        480 
LHGGQPPEGD PDLAKILEEV RYIANRFRCQ DESEAVCSEW KFAACVVDRL CLMAFSVFTI 

       490        500 
ICTIGILMSA PNFVEAVSKD FA 

« Hide

Isoform 2 [UniParc].

Checksum: 824BAFD78601D1FD
Show »

FASTA53159,235
Isoform 3 [UniParc].

Checksum: 2998C11DD1F15A89
Show »

FASTA32135,482

References

« Hide 'large scale' references
[1]"Human alpha 7 acetylcholine receptor: cloning of the alpha 7 subunit from the SH-SY5Y cell line and determination of pharmacological properties of native receptors and functional alpha 7 homomers expressed in Xenopus oocytes."
Peng X., Katz M., Gerzanich V., Anand R., Lindstrom J.
Mol. Pharmacol. 45:546-554(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Nucleotide sequence and transcript size of the alpha-7 neuronal nicotinic acetylcholine receptor in human postmortem brain."
Logel J., Drebing C., Barnhart M., Antle C., Leonard S.
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Hippocampus.
[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 1).
[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).
[5]Groot Kormelink P.J., Luyten W.H.M.L.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[6]"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] (ISOFORM 1).
Tissue: Keratinocyte.
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Amygdala and Stomach.
[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] (ISOFORM 3).
Tissue: Brain.
[10]"Cloning and sequence of the human alpha-7 nicotinic acetylcholine receptor."
Doucette-Stamm L., Monteggia L.M., Donnelly-Roberts D., Wang M.T., Lee J., Tian J., Giordano T.
Drug Dev. Res. 30:252-256(1993)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-502 (ISOFORM 1).
Tissue: Brain.
[11]"Molecular cloning and chromosomal localization of the human alpha 7-nicotinic receptor subunit gene (CHRNA7)."
Chini B., Raimondi E., Elgoyhen A.B., Moralli D., Balzaretti M., Heinemann S.F.
Genomics 19:379-381(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-502 (ISOFORM 1).
Tissue: Retina.
[12]"A 3-Mb map of a large segmental duplication overlapping the alpha7-nicotinic acetylcholine receptor gene (CHRNA7) at human 15q13-q14."
Riley B., Williamson M., Collier D., Wilkie H., Makoff A.
Genomics 79:197-209(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-129.
[13]"Cluster analysis of an extensive human breast cancer cell line protein expression map database."
Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Tissue: Mammary cancer.
[14]"Ric-3 promotes functional expression of the nicotinic acetylcholine receptor alpha7 subunit in mammalian cells."
Williams M.E., Burton B., Urrutia A., Shcherbatko A., Chavez-Noriega L.E., Cohen C.J., Aiyar J.
J. Biol. Chem. 280:1257-1263(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RIC3.
[15]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70297 mRNA. Translation: CAA49778.1.
U40583 mRNA. Translation: AAA83561.1.
U62436 mRNA. Translation: AAB40114.1.
Y08420 mRNA. Translation: CAA69697.1.
AF385585 mRNA. Translation: AAK68111.1.
AK292069 mRNA. Translation: BAF84758.1.
AK294229 mRNA. Translation: BAG57531.1.
AC004460 Genomic DNA. No translation available.
AC009562 Genomic DNA. No translation available.
AC012236 Genomic DNA. No translation available.
AC021316 Genomic DNA. No translation available.
AC026150 Genomic DNA. No translation available.
AC026951 Genomic DNA. No translation available.
AC058803 Genomic DNA. No translation available.
AC068448 Genomic DNA. No translation available.
AC079969 Genomic DNA. No translation available.
AC087481 Genomic DNA. No translation available.
AC090829 Genomic DNA. No translation available.
AC091057 Genomic DNA. No translation available.
AC104266 Genomic DNA. No translation available.
AC104759 Genomic DNA. No translation available.
BC037571 mRNA. Translation: AAH37571.1.
BC101345 mRNA. Translation: AAI01346.1.
L25827 mRNA. No translation available.
Z23141 mRNA. Translation: CAA80672.1.
AF332758 Genomic DNA. Translation: AAK19515.1.
PIRG02259.
ACHUA7. I37185.
RefSeqNP_000737.1. NM_000746.5.
NP_001177384.1. NM_001190455.2.
NP_683709.1. NM_148911.1.
XP_005254807.1. XM_005254750.1.
UniGeneHs.510853.
Hs.511772.
Hs.713151.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2MAWNMR-A228-326[»]
A467-495[»]
ProteinModelPortalP36544.
SMRP36544. Positions 23-495.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107561. 3 interactions.
IntActP36544. 2 interactions.
STRING9606.ENSP00000303727.

Chemistry

BindingDBP36544.
ChEMBLCHEMBL2492.
DrugBankDB00184. Nicotine.
DB01273. Varenicline.
GuidetoPHARMACOLOGY468.

Protein family/group databases

TCDB1.A.9.1.7. the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.

PTM databases

PhosphoSiteP36544.

Polymorphism databases

DMDM2506127.

Proteomic databases

PaxDbP36544.
PRIDEP36544.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306901; ENSP00000303727; ENSG00000175344. [P36544-1]
ENST00000454250; ENSP00000407546; ENSG00000175344. [P36544-2]
ENST00000455693; ENSP00000405989; ENSG00000175344. [P36544-3]
GeneID1139.
89832.
KEGGhsa:1139.
hsa:89832.
UCSCuc001zft.4. human. [P36544-1]
uc021sic.2. human. [P36544-2]

Organism-specific databases

CTD1139.
89832.
GeneCardsGC15P032322.
HGNCHGNC:1960. CHRNA7.
HPACAB033624.
HPA029422.
MIM118511. gene.
neXtProtNX_P36544.
Orphanet199318. 15q13.3 microdeletion syndrome.
PharmGKBPA114.
PA26483.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG235631.
HOGENOMHOG000006756.
HOVERGENHBG003756.
InParanoidP36544.
KOK04809.
OMAESEAICS.
OrthoDBEOG72JWGV.
PhylomeDBP36544.
TreeFamTF315605.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.
SignaLinkP36544.

Gene expression databases

ArrayExpressP36544.
BgeeP36544.
CleanExHS_CHRNA7.
GenevestigatorP36544.

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

GeneWikiCHRFAM7A.
CHRNA7.
NextBio4738.
PROP36544.
SOURCESearch...

Entry information

Entry nameACHA7_HUMAN
AccessionPrimary (citable) accession number: P36544
Secondary accession number(s): A8K7Q4 expand/collapse secondary AC list , B4DFS0, Q15826, Q8IUZ4, Q96RH2, Q99555, Q9BXH0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 149 of the entry and version 5 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 chromosome 15

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