DisGeNET - a database of gene-disease associations

RETINOSCHISIS 1, X-LINKED, JUVENILE, C3714753

Gene: RS1 ×

Source: UNIPROT ×

Results per page

Gene

Disease

Variant

Source

Association Type

Semantic type

Protein Class

Disease Class

Type

Original DB

Consequence

DSI _v

DPI _v

pLI

EI _vda

EL _gda

Score _vda

PMID

PMID Year

AF_EXOME

Num. PMIDs

Num. SNPs_gda

AF_GENOME

Variant

Gene

Risk Allele

Score _vda

Association Type

Original DB

Sentence supporting the association

PMID

PMID Year

dbSNP:

rs104894928

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs104894929

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs104894930

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs104894932

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs104894933

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs104894934

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs104894935

RS1

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs281865355

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs281865361

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs61752060

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs61752063

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs61752067

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs61752068

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs61752159

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs61753174

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs62645894

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Structural analysis of X-linked retinoschisis mutations reveals distinct classes which differentially effect retinoschisin function.

27798099

2016

dbSNP:

rs104894928

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Wild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamer.

19849666

2009

dbSNP:

rs104894929

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Wild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamer.

19849666

2009

dbSNP:

rs104894930

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Wild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamer.

19849666

2009

dbSNP:

rs104894932

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Wild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamer.

19849666

2009

dbSNP:

rs104894933

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Wild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamer.

19849666

2009

dbSNP:

rs104894934

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Wild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamer.

19849666

2009

dbSNP:

rs104894935

RS1

0.800

GeneticVariation

UNIPROT

Wild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamer.

19849666

2009

dbSNP:

rs281865355

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Wild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamer.

19849666

2009

dbSNP:

rs281865361

RS1 ; CDKL5

0.800

GeneticVariation

UNIPROT

Wild-type and missense mutants of retinoschisin co-assemble resulting in either intracellular retention or incorrect assembly of the functionally active octamer.

19849666

2009