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O15537

- XLRS1_HUMAN

UniProt

O15537 - XLRS1_HUMAN

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Protein

Retinoschisin

Gene

RS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

May be active in cell adhesion processes during retinal development.

GO - Molecular functioni

  1. phosphatidylinositol-3,4,5-trisphosphate binding Source: Ensembl
  2. phosphatidylinositol-3,4-bisphosphate binding Source: Ensembl
  3. phosphatidylinositol-3,5-bisphosphate binding Source: Ensembl
  4. phosphatidylinositol-3-phosphate binding Source: Ensembl
  5. phosphatidylinositol-4,5-bisphosphate binding Source: Ensembl
  6. phosphatidylinositol-4-phosphate binding Source: Ensembl
  7. phosphatidylinositol-5-phosphate binding Source: Ensembl
  8. phosphatidylserine binding Source: Ensembl

GO - Biological processi

  1. adaptation of rhodopsin mediated signaling Source: Ensembl
  2. cell adhesion Source: ProtInc
  3. multicellular organismal development Source: ProtInc
  4. retina layer formation Source: Ensembl
  5. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Sensory transduction, Vision

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoschisin
Alternative name(s):
X-linked juvenile retinoschisis protein
Gene namesi
Name:RS1
Synonyms:XLRS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:10457. RS1.

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular space Source: ProtInc
  2. extrinsic component of plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Retinoschisis juvenile X-linked 1 (XLRS1) [MIM:312700]: A vitreo-retinal dystrophy characterized by macular pathology and by splitting of the superficial layer of the retina. Macular changes are present in almost all cases. In the fundi, radially oriented intraretinal foveomacular cysts are seen in a spoke-wheel configuration, with the absence of foveal reflex in most cases. In addition, approximately half of cases have bilateral peripheral retinoschisis in the inferotemporal part of the retina. Aside from the typical fundus appearance, strabismus, nystagmus, axial hyperopia, defective color vision and foveal ectopy can be present. The most important complications are vitreous hemorrhage, retinal detachment, and neovascular glaucoma.11 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121L → H in XLRS1.
VAR_008209
Natural varianti13 – 131L → P in XLRS1. 1 Publication
VAR_008210
Natural varianti59 – 591C → S in XLRS1.
VAR_008211
Natural varianti65 – 651Y → C in XLRS1.
VAR_008212
Natural varianti70 – 701G → A in XLRS1. 1 Publication
VAR_008213
Natural varianti70 – 701G → S in XLRS1. 1 Publication
VAR_008214
Natural varianti72 – 721E → D in XLRS1.
VAR_008180
Natural varianti72 – 721E → K in XLRS1. 5 Publications
VAR_008181
Natural varianti73 – 731S → P in XLRS1. 1 Publication
VAR_065326
Natural varianti74 – 741G → V in XLRS1. 2 Publications
VAR_008182
Natural varianti85 – 851Missing in XLRS1. 1 Publication
VAR_023959
Natural varianti89 – 891Y → C in XLRS1. 1 Publication
VAR_008215
Natural varianti96 – 961W → R in XLRS1. 2 Publications
VAR_008183
Natural varianti98 – 981A → E in XLRS1. 1 Publication
VAR_008216
Natural varianti102 – 1021R → Q in XLRS1. 3 Publications
VAR_008217
Natural varianti102 – 1021R → W in XLRS1. 1 Publication
VAR_008184
Natural varianti103 – 1031L → R in XLRS1.
VAR_008218
Natural varianti108 – 1081F → C in XLRS1. 1 Publication
VAR_008219
Natural varianti109 – 1091G → E in XLRS1. 1 Publication
VAR_008220
Natural varianti109 – 1091G → R in XLRS1. 1 Publication
VAR_008185
Natural varianti109 – 1091G → W in XLRS1. 1 Publication
VAR_008221
Natural varianti110 – 1101C → Y in XLRS1.
VAR_008222
Natural varianti112 – 1121W → C in XLRS1.
VAR_008223
Natural varianti113 – 1131L → F in XLRS1.
VAR_008224
Natural varianti127 – 1271L → P in XLRS1.
VAR_008225
Natural varianti135 – 1351G → V in XLRS1.
VAR_008226
Natural varianti136 – 1361I → T in XLRS1.
VAR_008227
Natural varianti138 – 1381T → A in XLRS1.
VAR_008228
Natural varianti140 – 1401G → E in XLRS1.
VAR_008229
Natural varianti140 – 1401G → R in XLRS1. 2 Publications
VAR_008230
Natural varianti141 – 1411R → C in XLRS1. 2 Publications
VAR_008231
Natural varianti141 – 1411R → G in XLRS1.
VAR_008232
Natural varianti141 – 1411R → H in XLRS1. 1 Publication
VAR_008233
Natural varianti142 – 1421C → W in XLRS1. 1 Publication
VAR_008234
Natural varianti143 – 1431D → V in XLRS1.
VAR_008235
Natural varianti145 – 1451D → H in XLRS1. 1 Publication
VAR_065327
Natural varianti146 – 1461E → D in XLRS1.
VAR_008236
Natural varianti146 – 1461E → K in XLRS1. 1 Publication
VAR_008237
Natural varianti155 – 1551Y → C in XLRS1.
VAR_008238
Natural varianti156 – 1561R → G in XLRS1. 1 Publication
VAR_065328
Natural varianti163 – 1631W → C in XLRS1. 1 Publication
VAR_008240
Natural varianti178 – 1781G → D in XLRS1.
VAR_008241
Natural varianti182 – 1821R → C in XLRS1. 1 Publication
VAR_008242
Natural varianti192 – 1921P → L in XLRS1. 1 Publication
VAR_065329
Natural varianti192 – 1921P → R in XLRS1.
VAR_008243
Natural varianti192 – 1921P → S in XLRS1. 2 Publications
VAR_008244
Natural varianti193 – 1931P → L in XLRS1. 1 Publication
VAR_008245
Natural varianti193 – 1931P → S in XLRS1. 1 Publication
VAR_008246
Natural varianti197 – 1971R → C in XLRS1. 1 Publication
VAR_008247
Natural varianti197 – 1971R → H in XLRS1.
VAR_008248
Natural varianti199 – 1991I → T in XLRS1.
VAR_008249
Natural varianti200 – 2001R → C in XLRS1. 3 Publications
VAR_008251
Natural varianti200 – 2001R → H in XLRS1. 1 Publication
VAR_008252
Natural varianti203 – 2031P → L in XLRS1. 1 Publication
VAR_008253
Natural varianti207 – 2071H → Q in XLRS1.
VAR_008254
Natural varianti209 – 2091R → C in XLRS1. 1 Publication
VAR_065330
Natural varianti209 – 2091R → H in XLRS1. 1 Publication
VAR_008255
Natural varianti213 – 2131R → Q in XLRS1. 1 Publication
VAR_065331
Natural varianti213 – 2131R → W in XLRS1.
VAR_008256
Natural varianti215 – 2151E → K in XLRS1. 1 Publication
VAR_008257
Natural varianti215 – 2151E → Q in XLRS1.
VAR_008258
Natural varianti216 – 2161L → P in XLRS1.
VAR_008259
Natural varianti219 – 2191C → G in XLRS1.
VAR_008260
Natural varianti219 – 2191C → R in XLRS1.
VAR_008261
Natural varianti223 – 2231C → R in XLRS1. 2 Publications
VAR_008262

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi312700. phenotype.
Orphaneti792. X-linked retinoschisis.
PharmGKBiPA34871.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 224201RetinoschisinPRO_0000022695Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 – 40Interchain1 PublicationPROSITE-ProRule annotation
Disulfide bondi59 – 59Interchain (with C-223)1 PublicationPROSITE-ProRule annotation
Disulfide bondi63 ↔ 2191 PublicationPROSITE-ProRule annotation
Disulfide bondi110 ↔ 1421 PublicationPROSITE-ProRule annotation
Disulfide bondi223 – 223Interchain (with C-59)1 PublicationPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiO15537.
PRIDEiO15537.

PTM databases

PhosphoSiteiO15537.

Expressioni

Tissue specificityi

Restricted to the retina (at protein level). At the mRNA level, detected only within the photoreceptor cell layer, most prominently within the inner segments of the photoreceptors. Undetectable in the inner plexiform layers and the inner nuclear layer. At the protein level, found in the inner segment of the photoreceptors, the inner nuclear layer, the inner plexiform layer and the ganglion cell layer. At the macula, expressed in both the outer and inner nuclear layers and in the inner plexiform layer (at protein level).1 Publication

Developmental stagei

Up-regulated during the differentiation of a retinoblastoma cell line.1 Publication

Gene expression databases

BgeeiO15537.
CleanExiHS_RS1.
GenevestigatoriO15537.

Interactioni

Subunit structurei

Homooctamer of 4 homodimers; disulfide-linked.1 Publication

Protein-protein interaction databases

STRINGi9606.ENSP00000369320.

Structurei

3D structure databases

ProteinModelPortaliO15537.
SMRiO15537. Positions 68-219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 219157F5/8 type CPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 F5/8 type C domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG130479.
GeneTreeiENSGT00760000119073.
HOGENOMiHOG000006700.
HOVERGENiHBG061301.
InParanoidiO15537.
OMAiAWLSKYQ.
OrthoDBiEOG7SBNPV.
PhylomeDBiO15537.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000421. Coagulation_fac_5/8-C_type_dom.
IPR008979. Galactose-bd-like.
[Graphical view]
PfamiPF00754. F5_F8_type_C. 1 hit.
[Graphical view]
SMARTiSM00231. FA58C. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
PROSITEiPS01285. FA58C_1. 1 hit.
PS50022. FA58C_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O15537-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRKIEGFLL LLLFGYEATL GLSSTEDEGE DPWYQKACKC DCQGGPNALW
60 70 80 90 100
SAGATSLDCI PECPYHKPLG FESGEVTPDQ ITCSNPEQYV GWYSSWTANK
110 120 130 140 150
ARLNSQGFGC AWLSKFQDSS QWLQIDLKEI KVISGILTQG RCDIDEWMTK
160 170 180 190 200
YSVQYRTDER LNWIYYKDQT GNNRVFYGNS DRTSTVQNLL RPPIISRFIR
210 220
LIPLGWHVRI AIRMELLECV SKCA
Length:224
Mass (Da):25,592
Last modified:August 1, 1998 - v2
Checksum:iA3893895E6A7E292
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121L → H in XLRS1.
VAR_008209
Natural varianti13 – 131L → P in XLRS1. 1 Publication
VAR_008210
Natural varianti59 – 591C → S in XLRS1.
VAR_008211
Natural varianti65 – 651Y → C in XLRS1.
VAR_008212
Natural varianti70 – 701G → A in XLRS1. 1 Publication
VAR_008213
Natural varianti70 – 701G → S in XLRS1. 1 Publication
VAR_008214
Natural varianti72 – 721E → D in XLRS1.
VAR_008180
Natural varianti72 – 721E → K in XLRS1. 5 Publications
VAR_008181
Natural varianti73 – 731S → P in XLRS1. 1 Publication
VAR_065326
Natural varianti74 – 741G → V in XLRS1. 2 Publications
VAR_008182
Natural varianti85 – 851Missing in XLRS1. 1 Publication
VAR_023959
Natural varianti89 – 891Y → C in XLRS1. 1 Publication
VAR_008215
Natural varianti96 – 961W → R in XLRS1. 2 Publications
VAR_008183
Natural varianti98 – 981A → E in XLRS1. 1 Publication
VAR_008216
Natural varianti102 – 1021R → Q in XLRS1. 3 Publications
VAR_008217
Natural varianti102 – 1021R → W in XLRS1. 1 Publication
VAR_008184
Natural varianti103 – 1031L → R in XLRS1.
VAR_008218
Natural varianti108 – 1081F → C in XLRS1. 1 Publication
VAR_008219
Natural varianti109 – 1091G → E in XLRS1. 1 Publication
VAR_008220
Natural varianti109 – 1091G → R in XLRS1. 1 Publication
VAR_008185
Natural varianti109 – 1091G → W in XLRS1. 1 Publication
VAR_008221
Natural varianti110 – 1101C → Y in XLRS1.
VAR_008222
Natural varianti112 – 1121W → C in XLRS1.
VAR_008223
Natural varianti113 – 1131L → F in XLRS1.
VAR_008224
Natural varianti127 – 1271L → P in XLRS1.
VAR_008225
Natural varianti135 – 1351G → V in XLRS1.
VAR_008226
Natural varianti136 – 1361I → T in XLRS1.
VAR_008227
Natural varianti138 – 1381T → A in XLRS1.
VAR_008228
Natural varianti140 – 1401G → E in XLRS1.
VAR_008229
Natural varianti140 – 1401G → R in XLRS1. 2 Publications
VAR_008230
Natural varianti141 – 1411R → C in XLRS1. 2 Publications
VAR_008231
Natural varianti141 – 1411R → G in XLRS1.
VAR_008232
Natural varianti141 – 1411R → H in XLRS1. 1 Publication
VAR_008233
Natural varianti142 – 1421C → W in XLRS1. 1 Publication
VAR_008234
Natural varianti143 – 1431D → V in XLRS1.
VAR_008235
Natural varianti145 – 1451D → H in XLRS1. 1 Publication
VAR_065327
Natural varianti146 – 1461E → D in XLRS1.
VAR_008236
Natural varianti146 – 1461E → K in XLRS1. 1 Publication
VAR_008237
Natural varianti155 – 1551Y → C in XLRS1.
VAR_008238
Natural varianti156 – 1561R → G in XLRS1. 1 Publication
VAR_065328
Natural varianti158 – 1581D → N.
Corresponds to variant rs1800002 [ dbSNP | Ensembl ].
VAR_008239
Natural varianti163 – 1631W → C in XLRS1. 1 Publication
VAR_008240
Natural varianti178 – 1781G → D in XLRS1.
VAR_008241
Natural varianti182 – 1821R → C in XLRS1. 1 Publication
VAR_008242
Natural varianti192 – 1921P → L in XLRS1. 1 Publication
VAR_065329
Natural varianti192 – 1921P → R in XLRS1.
VAR_008243
Natural varianti192 – 1921P → S in XLRS1. 2 Publications
VAR_008244
Natural varianti193 – 1931P → L in XLRS1. 1 Publication
VAR_008245
Natural varianti193 – 1931P → S in XLRS1. 1 Publication
VAR_008246
Natural varianti197 – 1971R → C in XLRS1. 1 Publication
VAR_008247
Natural varianti197 – 1971R → H in XLRS1.
VAR_008248
Natural varianti199 – 1991I → T in XLRS1.
VAR_008249
Natural varianti200 – 2001R → C in XLRS1. 3 Publications
VAR_008251
Natural varianti200 – 2001R → H in XLRS1. 1 Publication
VAR_008252
Natural varianti203 – 2031P → L in XLRS1. 1 Publication
VAR_008253
Natural varianti207 – 2071H → Q in XLRS1.
VAR_008254
Natural varianti209 – 2091R → C in XLRS1. 1 Publication
VAR_065330
Natural varianti209 – 2091R → H in XLRS1. 1 Publication
VAR_008255
Natural varianti213 – 2131R → Q in XLRS1. 1 Publication
VAR_065331
Natural varianti213 – 2131R → W in XLRS1.
VAR_008256
Natural varianti215 – 2151E → K in XLRS1. 1 Publication
VAR_008257
Natural varianti215 – 2151E → Q in XLRS1.
VAR_008258
Natural varianti216 – 2161L → P in XLRS1.
VAR_008259
Natural varianti219 – 2191C → G in XLRS1.
VAR_008260
Natural varianti219 – 2191C → R in XLRS1.
VAR_008261
Natural varianti222 – 2221K → N.
Corresponds to variant rs1800004 [ dbSNP | Ensembl ].
VAR_012078
Natural varianti223 – 2231C → R in XLRS1. 2 Publications
VAR_008262

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF018963
, AF018958, AF018959, AF018960, AF018961, AF018962 Genomic DNA. Translation: AAC18405.1.
AF014459 mRNA. Translation: AAC17928.1.
Z92542, Z94056 Genomic DNA. Translation: CAI42483.1.
Z94056, Z92542 Genomic DNA. Translation: CAI42776.1.
DQ426892 mRNA. Translation: ABD90543.1.
CCDSiCCDS14187.1.
RefSeqiNP_000321.1. NM_000330.3.
UniGeneiHs.715725.

Genome annotation databases

EnsembliENST00000379984; ENSP00000369320; ENSG00000102104.
GeneIDi6247.
KEGGihsa:6247.
UCSCiuc004cyo.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the RS1 gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF018963
, AF018958 , AF018959 , AF018960 , AF018961 , AF018962 Genomic DNA. Translation: AAC18405.1 .
AF014459 mRNA. Translation: AAC17928.1 .
Z92542 , Z94056 Genomic DNA. Translation: CAI42483.1 .
Z94056 , Z92542 Genomic DNA. Translation: CAI42776.1 .
DQ426892 mRNA. Translation: ABD90543.1 .
CCDSi CCDS14187.1.
RefSeqi NP_000321.1. NM_000330.3.
UniGenei Hs.715725.

3D structure databases

ProteinModelPortali O15537.
SMRi O15537. Positions 68-219.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000369320.

PTM databases

PhosphoSitei O15537.

Proteomic databases

PaxDbi O15537.
PRIDEi O15537.

Protocols and materials databases

DNASUi 6247.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379984 ; ENSP00000369320 ; ENSG00000102104 .
GeneIDi 6247.
KEGGi hsa:6247.
UCSCi uc004cyo.3. human.

Organism-specific databases

CTDi 6247.
GeneCardsi GC0XM018567.
GeneReviewsi RS1.
HGNCi HGNC:10457. RS1.
MIMi 300839. gene.
312700. phenotype.
neXtProti NX_O15537.
Orphaneti 792. X-linked retinoschisis.
PharmGKBi PA34871.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG130479.
GeneTreei ENSGT00760000119073.
HOGENOMi HOG000006700.
HOVERGENi HBG061301.
InParanoidi O15537.
OMAi AWLSKYQ.
OrthoDBi EOG7SBNPV.
PhylomeDBi O15537.

Miscellaneous databases

GeneWikii Retinoschisin.
GenomeRNAii 6247.
NextBioi 24257.
PROi O15537.
SOURCEi Search...

Gene expression databases

Bgeei O15537.
CleanExi HS_RS1.
Genevestigatori O15537.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
InterProi IPR000421. Coagulation_fac_5/8-C_type_dom.
IPR008979. Galactose-bd-like.
[Graphical view ]
Pfami PF00754. F5_F8_type_C. 1 hit.
[Graphical view ]
SMARTi SM00231. FA58C. 1 hit.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 1 hit.
PROSITEi PS01285. FA58C_1. 1 hit.
PS50022. FA58C_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Positional cloning of the gene associated with X-linked juvenile retinoschisis."
    Sauer C.G., Gehrig A., Warneke-Wittstock R., Marquardt A., Ewing C.C., Gibson A., Lorenz B., Jurklies B., Weber B.H.
    Nat. Genet. 17:164-170(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS XLRS1 ARG-96 AND TRP-102.
    Tissue: Retina.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Mapping of transcription start sites of human retina expressed genes."
    Roni V., Carpio R., Wissinger B.
    BMC Genomics 8:42-42(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-35.
    Tissue: Retina.
  4. "Retinoschisin, the X-linked retinoschisis protein, is a secreted photoreceptor protein, and is expressed and released by Weri-Rb1 cells."
    Grayson C., Reid S.N., Ellis J.A., Rutherford A., Sowden J.C., Yates J.R., Farber D.B., Trump D.
    Hum. Mol. Genet. 9:1873-1879(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
  5. "RS1, a discoidin domain-containing retinal cell adhesion protein associated with X-linked retinoschisis, exists as a novel disulfide-linked octamer."
    Wu W.W., Wong J.P., Kast J., Molday R.S.
    J. Biol. Chem. 280:10721-10730(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, DISULFIDE BONDS.
  6. Cited for: VARIANTS XLRS1 LYS-72 AND LEU-193.
  7. "Recurrent missense (R197C) and nonsense (Y89X) mutations in the XLRS1 gene in families with X-linked retinoschisis."
    Shastry B.S., Hejtmancik F.J., Trese M.T.
    Biochem. Biophys. Res. Commun. 256:317-319(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT XLRS1 CYS-197.
  8. "Assessment of RS1 in X-linked juvenile retinoschisis and sporadic senile retinoschisis."
    Gehrig A., White K., Lorenz B., Andrassi M., Clemens S., Weber B.H.
    Clin. Genet. 55:461-465(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS XLRS1 GLU-98; CYS-108; TRP-109; CYS-141; LYS-146; CYS-200 AND LYS-215.
  9. "Three widespread founder mutations contribute to high incidence of X-linked juvenile retinoschisis in Finland."
    Huopaniemi L., Rantala A., Forsius H., Somer M., de la Chapelle A., Alitalo T.
    Eur. J. Hum. Genet. 7:368-376(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS XLRS1 LYS-72; VAL-74 AND ARG-109.
  10. "X-linked retinoschisis with a novel substitutive amino acid (P193S) in XLRS1."
    Duval P.-A., Marlhens F., Griffoin J.-M., Millet P., Arnaud B., Hamel C.P.
    Hum. Mutat. 13:259-259(1999)
    Cited for: VARIANT XLRS1 SER-193.
  11. "Identification of four novel mutations of the XLRS1 gene in Japanese patients with X-linked juvenile retinoschisis."
    Mashima Y., Shinoda K., Ishida S., Ozawa Y., Kudoh J., Iwata T., Oguchi Y., Shimizu N.
    Hum. Mutat. 13:338-338(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS XLRS1 LYS-72; CYS-89; GLU-109; CYS-182 AND LEU-203.
  12. "Novel mutations in XLRS1 causing retinoschisis, including first evidence of putative leader sequence change."
    Hiriyanna K.T., Bingham E.L., Yashar B.M., Ayyagari R., Fishman G., Small K.W., Weinberg D.V., Weleber R.G., Lewis R.A., Andreasson S., Richards J.E., Sieving P.A.
    Hum. Mutat. 14:423-427(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS XLRS1 PRO-13; SER-70; ALA-70; LYS-72; VAL-74; ASN-85 DEL; ARG-96; GLN-102; ARG-140; TRP-142; CYS-163; SER-192; CYS-200; HIS-200 AND ARG-223.
  13. "X-linked retinoschisis in a female with a heterozygous RS1 missense mutation."
    Saldana M., Thompson J., Monk E., Trump D., Long V., Sheridan E.
    Am. J. Med. Genet. A 143:608-609(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT XLRS1 GLN-102.
  14. "Clinical features of X linked juvenile retinoschisis in Chinese families associated with novel mutations in the RS1 gene."
    Li X., Ma X., Tao Y.
    Mol. Vis. 13:804-812(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS XLRS1 PRO-73; GLN-102; HIS-145; GLY-156; CYS-200; HIS-209; GLN-213 AND ARG-223.
  15. "Clinical and genetic findings in Hungarian patients with X-linked juvenile retinoschisis."
    Lesch B., Szabo V., Kanya M., Somfai G.M., Vamos R., Varsanyi B., Pamer Z., Knezy K., Salacz G., Janaky M., Ferencz M., Hargitai J., Papp A., Farkas A.
    Mol. Vis. 14:2321-2332(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS XLRS1 LYS-72; ARG-140; CYS-141; HIS-141; SER-192; LEU-192 AND CYS-209.

Entry informationi

Entry nameiXLRS1_HUMAN
AccessioniPrimary (citable) accession number: O15537
Secondary accession number(s): Q0QD39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: October 29, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

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