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O15537

- XLRS1_HUMAN

UniProt

O15537 - XLRS1_HUMAN

Protein

Retinoschisin

Gene

RS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (01 Aug 1998)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiO15537.
    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.
    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

    MSRKIEGFLL LLLFGYEATL GLSSTEDEGE DPWYQKACKC DCQGGPNALW    50
    SAGATSLDCI PECPYHKPLG FESGEVTPDQ ITCSNPEQYV GWYSSWTANK 100
    ARLNSQGFGC AWLSKFQDSS QWLQIDLKEI KVISGILTQG RCDIDEWMTK 150
    YSVQYRTDER LNWIYYKDQT GNNRVFYGNS DRTSTVQNLL RPPIISRFIR 200
    LIPLGWHVRI AIRMELLECV SKCA 224
    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.
    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

    ArrayExpressi O15537.
    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

    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 1, 2014
    This is version 129 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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