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Q9Y5X4 (NR2E3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Photoreceptor-specific nuclear receptor
Alternative name(s):
Nuclear receptor subfamily 2 group E member 3
Retina-specific nuclear receptor
Gene names
Name:NR2E3
Synonyms:PNR, RNR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Orphan nuclear receptor of retinal photoreceptor cells. Transcriptional factor that is an activator of rod development and repressor of cone development. Binds the promoter region of a number of rod- and cone-specific genes, including rhodopsin, M- and S-opsin and rod-specific phosphodiesterase beta subunit. Enhances rhodopsin expression. Represses M- and S-cone opsin expression. Ref.6 Ref.7

Subunit structure

Homodimer. Interacts with PIAS3; the interaction sumoylates NR2E3 and promotes repression of cone-specific gene transcription and activation of rod-specific genes By similarity. Component of a complex that includes NR2E3, PIAS3, NRL, CRX and/or NR1D1. Binds NR1D1. Binds direcly in the complex with CRX, PIAS3 and NR1D1 By similarity. Interacts (via the DNA-binding domain) with CRX (via its DNA binding domain); the interaction represses S- and M-cone opsin expression. Ref.6 Ref.7

Subcellular location

Nucleus Ref.6.

Tissue specificity

Eye specific; found solely in the outer nuclear layer of the adult neurosensory retina, where the nuclei of cone and rod photoreceptors reside. Ref.6

Post-translational modification

Di- and tri-sumoylated in developing retina. PIAS3-mediated sumoylation promotes repression of cone-specific gene expression and activation of rod-specific genes. Sumoylation on Lys-185 appears to be the main site By similarity.

Involvement in disease

Enhanced S cone syndrome (ESCS) [MIM:268100]: Autosomal recessive retinopathy in which patients have increased sensitivity to blue light; perception of blue light is mediated by what is normally the least populous cone photoreceptor subtype, the S (short wavelength, blue) cones. ESCS is also associated with visual loss, with night blindness occurring from early in life, varying degrees of L (long, red)- and M (middle, green)-cone vision, and retinal degeneration.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15

Retinitis pigmentosa 37 (RP37) [MIM:611131]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.15

Sequence similarities

Belongs to the nuclear hormone receptor family. NR2 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processSensory transduction
Transcription
Transcription regulation
Vision
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Retinitis pigmentosa
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionReceptor
Repressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processgene expression

Traceable author statement. Source: Reactome

intracellular receptor signaling pathway

Traceable author statement Ref.1. Source: GOC

phototransduction

Traceable author statement Ref.1. Source: ProtInc

signal transduction

Traceable author statement Ref.1. Source: ProtInc

transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

visual perception

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 17255935. Source: IntAct

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q9Y5X4-1)

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 Short (identifier: Q9Y5X4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     368-410: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 410410Photoreceptor-specific nuclear receptor
PRO_0000053599

Regions

DNA binding44 – 12077Nuclear receptor
Zinc finger47 – 6721NR C4-type
Zinc finger83 – 10826NR C4-type
Compositional bias371 – 3755Poly-Leu

Amino acid modifications

Modified residue3331Phosphothreonine By similarity
Cross-link185Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link330Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link337Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence368 – 41043Missing in isoform Short.
VSP_003679
Natural variant441S → L Associated with autosomal recessive retinitis pigmentosa. Ref.14
VAR_062768
Natural variant561G → R in RP37. Ref.13 Ref.15
VAR_037026
Natural variant67 – 693Missing in ESCS.
VAR_009265
Natural variant761R → Q in ESCS. Ref.9
VAR_009266
Natural variant761R → W in ESCS. Ref.9
VAR_009267
Natural variant881G → V in ESCS. Ref.11
VAR_020839
Natural variant971R → H in ESCS. Ref.9 Ref.10 Ref.11
VAR_010025
Natural variant1041R → Q Associated with ESCS. Ref.12
VAR_062769
Natural variant1041R → W in ESCS. Ref.9 Ref.11
VAR_010026
Natural variant1211E → K in ESCS. Ref.9
VAR_010027
Natural variant1401E → G. Ref.9 Ref.14
Corresponds to variant rs1805020 [ dbSNP | Ensembl ].
VAR_010028
Natural variant1631M → T. Ref.9 Ref.14
Corresponds to variant rs1805021 [ dbSNP | Ensembl ].
VAR_010029
Natural variant2321V → I. Ref.9
Corresponds to variant rs1805023 [ dbSNP | Ensembl ].
VAR_010030
Natural variant2341W → S in ESCS. Ref.9 Ref.11
VAR_010031
Natural variant2561A → E in ESCS. Ref.10 Ref.11
VAR_020840
Natural variant2631L → P in ESCS; impairs protein folding. Ref.7 Ref.11
VAR_020841
Natural variant2871G → S Associated with autosomal recessive retinitis pigmentosa. Ref.14
VAR_062770
Natural variant3021V → I. Ref.9
Corresponds to variant rs1805025 [ dbSNP | Ensembl ].
VAR_010032
Natural variant3091R → G in ESCS; impairs protein folding and stability. Ref.7 Ref.9 Ref.11
VAR_010033
Natural variant3111R → Q in ESCS; impairs protein folding and stability and hinders the ability to form stable dimers. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15
Corresponds to variant rs28937873 [ dbSNP | Ensembl ].
VAR_010034
Natural variant3241K → R Associated with autosomal recessive retinitis pigmentosa. Ref.14
VAR_062771
Natural variant3341R → G Associated with ESCS; impairs protein folding and stability. Ref.7 Ref.12
VAR_062772
Natural variant3361L → P in ESCS; impairs protein folding and stability. Ref.7 Ref.11
VAR_020842
Natural variant3531L → V in ESCS; impairs protein folding and stability. Ref.7 Ref.11
VAR_020843
Natural variant3851R → P in ESCS. Ref.9
VAR_010035
Natural variant4071M → K in ESCS; impairs protein folding and stability. Ref.7 Ref.9 Ref.11
VAR_010036

Experimental info

Mutagenesis3721L → R: Reduces transcription repressor activity. Ref.7
Mutagenesis3751L → R: Reduces transcription repressor activity. Ref.7

Sequences

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

Last modified November 1, 1999. Version 1.
Checksum: D49525830ED0A000

FASTA41044,692
        10         20         30         40         50         60 
METRPTALMS STVAAAAPAA GAASRKESPG RWGLGEDPTG VSPSLQCRVC GDSSSGKHYG 

        70         80         90        100        110        120 
IYACNGCSGF FKRSVRRRLI YRCQVGAGMC PVDKAHRNQC QACRLKKCLQ AGMNQDAVQN 

       130        140        150        160        170        180 
ERQPRSTAQV HLDSMESNTE SRPESLVAPP APAGRSPRGP TPMSAARALG HHFMASLITA 

       190        200        210        220        230        240 
ETCAKLEPED ADENIDVTSN DPEFPSSPYS SSSPCGLDSI HETSARLLFM AVKWAKNLPV 

       250        260        270        280        290        300 
FSSLPFRDQV ILLEEAWSEL FLLGAIQWSL PLDSCPLLAP PEASAAGGAQ GRLTLASMET 

       310        320        330        340        350        360 
RVLQETISRF RALAVDPTEF ACMKALVLFK PETRGLKDPE HVEALQDQSQ VMLSQHSKAH 

       370        380        390        400        410 
HPSQPVRFGK LLLLLPSLRF ITAERIELLF FRKTIGNTPM EKLLCDMFKN 

« Hide

Isoform Short [UniParc].

Checksum: F67A09D430754B3D
Show »

FASTA36739,638

References

« Hide 'large scale' references
[1]"Identification of a photoreceptor cell-specific nuclear receptor."
Kobayashi M., Takezawa S., Hara K., Yu R.T., Umesono Y., Agata K., Taniwaki M., Yasuda K., Umesono K.
Proc. Natl. Acad. Sci. U.S.A. 96:4814-4819(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: Retinoblastoma.
[2]"Retina-specific nuclear receptor: a potential regulator of cellular retinaldehyde-binding protein expressed in retinal pigment epithelium and Muller glial cells."
Chen F., Figueroa D.J., Marmorstein A.D., Zhang Q., Petrukhin K., Caskey C.T., Austin C.P.
Proc. Natl. Acad. Sci. U.S.A. 96:15149-15154(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Tissue: Retina.
[3]"Assignment of the photoreceptor-specific nuclear receptor (PNR) gene to 15q22.32-q24.1 in the Bardet-Biedl Syndrome (BBS4) region."
Rendtorf N., Vissing H., Shilahtaroglu A., Tommerup N.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
[4]"Comprehensive DNA-binding analysis of human hormone nuclear receptors by fluorescence correlation spectroscopy based on cell-free system."
Kobayashi T., Kodani Y., Sawasaki T., Endo Y.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The photoreceptor-specific nuclear receptor Nr2e3 interacts with Crx and exerts opposing effects on the transcription of rod versus cone genes."
Peng G.H., Ahmad O., Ahmad F., Liu J., Chen S.
Hum. Mol. Genet. 14:747-764(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRX, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION.
[7]"The crystal structure of the orphan nuclear receptor NR2E3/PNR ligand binding domain reveals a dimeric auto-repressed conformation."
Tan M.H., Zhou X.E., Soon F.F., Li X., Li J., Yong E.L., Melcher K., Xu H.E.
PLoS ONE 8:E74359-E74359(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 217-410, SUBUNIT, MUTAGENESIS OF LEU-372 AND LEU-375, FUNCTION, CHARACTERIZATION OF VARIANT ASSOCIATED WITH ESCS GLY-334, CHARACTERIZATION OF VARIANTS ESCS PRO-263; GLY-309; GLN-311; PRO-336; VAL-353 AND LYS-407.
[8]"The photoreceptor cell-specific nuclear receptor gene (PNR) accounts for retinitis pigmentosa in the Crypto-Jews from Portugal (Marranos), survivors from the Spanish Inquisition."
Gerber S., Rozet J.-M., Takezawa S., dos Santos L.C., Lopes L., Gribouval O., Penet C., Perrault I., Ducroq D., Souied E., Jeanpierre M., Romana S., Frezal J., Ferraz F., Yu-Umesono R., Munnich A., Kaplan J.
Hum. Genet. 107:276-284(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ESCS GLN-311, CHARACTERIZATION OF VARIANT ESCS GLN-311.
[9]"Mutation of a nuclear receptor gene, NR2E3, causes enhanced S cone syndrome, a disorder of retinal cell fate."
Haider N.B., Jacobson S.G., Cideciyan A.V., Swiderski R., Streb L.M., Searby C., Beck G., Hockey R., Hanna D.B., Gorman S., Duhl D., Carmi R., Bennett J., Weleber R.G., Fishman G.A., Wright A.F., Stone E.M., Sheffield V.C.
Nat. Genet. 24:127-131(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ESCS 67-CYS--GLY-69 DEL; GLN-76; TRP-76; HIS-97; TRP-104; LYS-121; SER-234; GLY-309; GLN-311; PRO-385 AND LYS-407, VARIANTS GLY-140; THR-163; ILE-232 AND ILE-302.
[10]"Shared mutations in NR2E3 in enhanced S-cone syndrome, Goldmann-Favre syndrome, and many cases of clumped pigmentary retinal degeneration."
Sharon D., Sandberg M.A., Caruso R.C., Berson E.L., Dryja T.P.
Arch. Ophthalmol. 121:1316-1323(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ESCS 67-CYS--GLY-69 DEL; HIS-97; GLU-256 AND GLN-311.
[11]"Mutation analysis of NR2E3 and NRL genes in enhanced S cone syndrome."
Wright A.F., Reddick A.C., Schwartz S.B., Ferguson J.S., Aleman T.S., Kellner U., Jurklies B., Schuster A., Zrenner E., Wissinger B., Lennon A., Shu X., Cideciyan A.V., Stone E.M., Jacobson S.G., Swaroop A.
Hum. Mutat. 24:439-439(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ESCS 67-CYS--GLY-69 DEL; VAL-88; HIS-97; TRP-104; SER-234; GLU-256; PRO-263; GLY-309; GLN-311; PRO-336; VAL-353 AND LYS-407.
[12]"Novel NR2E3 mutations (R104Q, R334G) associated with a mild form of enhanced S-cone syndrome demonstrate compound heterozygosity."
Hayashi T., Gekka T., Goto-Omoto S., Takeuchi T., Kubo A., Kitahara K.
Ophthalmology 112:2115-2115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLN-104 AND GLY-334, ASSOCIATION OF VARIANTS GLN-104 AND GLY-334 WITH ESCS.
[13]"Recurrent mutation in the first zinc finger of the orphan nuclear receptor NR2E3 causes autosomal dominant retinitis pigmentosa."
Coppieters F., Leroy B.P., Beysen D., Hellemans J., De Bosscher K., Haegeman G., Robberecht K., Wuyts W., Coucke P.J., De Baere E.
Am. J. Hum. Genet. 81:147-157(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP37 ARG-56.
[14]"Analysis of the involvement of the NR2E3 gene in autosomal recessive retinal dystrophies."
Bernal S., Solans T., Gamundi M.J., Hernan I., de Jorge L., Carballo M., Navarro R., Tizzano E., Ayuso C., Baiget M.
Clin. Genet. 73:360-366(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ESCS GLN-311, VARIANTS LEU-44; GLY-140; THR-163; SER-287 AND ARG-324.
[15]"Mutations in NR2E3 can cause dominant or recessive retinal degenerations in the same family."
Escher P., Gouras P., Roduit R., Tiab L., Bolay S., Delarive T., Chen S., Tsai C.C., Hayashi M., Zernant J., Merriam J.E., Mermod N., Allikmets R., Munier F.L., Schorderet D.F.
Hum. Mutat. 30:342-351(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RP37 ARG-56, VARIANT ESCS GLN-311.
+Additional computationally mapped references.

Web resources

Mutations of the NR2E3 gene

Retina International's Scientific Newsletter

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF121129 mRNA. Translation: AAD28301.1.
AF148128 mRNA. Translation: AAF22227.1.
AJ276674 Genomic DNA. Translation: CAB82769.1.
AB307710 mRNA. Translation: BAH02301.1.
CH471082 Genomic DNA. Translation: EAW77876.1.
RefSeqNP_055064.1. NM_014249.3. [Q9Y5X4-1]
NP_057430.1. NM_016346.3. [Q9Y5X4-2]
UniGeneHs.187354.
Hs.636007.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4LOGX-ray2.70A/B217-410[»]
ProteinModelPortalQ9Y5X4.
SMRQ9Y5X4. Positions 47-410.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115320. 24 interactions.
IntActQ9Y5X4. 12 interactions.
MINTMINT-4302911.
STRING9606.ENSP00000317199.

Chemistry

BindingDBQ9Y5X4.
ChEMBLCHEMBL4374.

PTM databases

PhosphoSiteQ9Y5X4.

Polymorphism databases

DMDM8928275.

Proteomic databases

MaxQBQ9Y5X4.
PaxDbQ9Y5X4.
PRIDEQ9Y5X4.

Protocols and materials databases

DNASU10002.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID10002.
KEGGhsa:10002.
UCSCuc002ath.1. human. [Q9Y5X4-1]

Organism-specific databases

CTD10002.
GeneCardsGC15P072084.
GeneReviewsNR2E3.
HGNCHGNC:7974. NR2E3.
MIM268100. phenotype.
604485. gene.
611131. phenotype.
neXtProtNX_Q9Y5X4.
Orphanet53540. Goldmann-Favre syndrome.
791. Retinitis pigmentosa.
PharmGKBPA31757.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG277339.
HOGENOMHOG000260820.
HOVERGENHBG005606.
InParanoidQ9Y5X4.
KOK08546.
PhylomeDBQ9Y5X4.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkQ9Y5X4.

Gene expression databases

CleanExHS_NR2E3.
GenevestigatorQ9Y5X4.

Family and domain databases

Gene3D1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR000003. Retinoid-X_rcpt/HNF4.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00545. RETINOIDXR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 2 hits.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPhotoreceptor_cell-specific_nuclear_receptor.
GenomeRNAi10002.
NextBio37775.
PROQ9Y5X4.
SOURCESearch...

Entry information

Entry nameNR2E3_HUMAN
AccessionPrimary (citable) accession number: Q9Y5X4
Secondary accession number(s): B6ZGU0, Q9UHM4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 143 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 15

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