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O15537 (XLRS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinoschisin
Alternative name(s):
X-linked juvenile retinoschisis protein
Gene names
Name:RS1
Synonyms:XLRS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be active in cell adhesion processes during retinal development.

Subunit structure

Homooctamer of 4 homodimers; disulfide-linked. Ref.5

Subcellular location

Secreted Ref.4.

Tissue specificity

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). Ref.4

Developmental stage

Up-regulated during the differentiation of a retinoblastoma cell line. Ref.4

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Sequence similarities

Contains 1 F5/8 type C domain.

Ontologies

Keywords
   Biological processCell adhesion
Sensory transduction
Vision
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainSignal
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadaptation of rhodopsin mediated signaling

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Traceable author statement Ref.1. Source: ProtInc

multicellular organismal development

Traceable author statement Ref.1. Source: ProtInc

retina layer formation

Inferred from electronic annotation. Source: Ensembl

visual perception

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentextracellular space

Traceable author statement Ref.4. Source: ProtInc

extrinsic component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol-3,4-bisphosphate binding

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol-3,5-bisphosphate binding

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol-3-phosphate binding

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol-4,5-bisphosphate binding

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol-4-phosphate binding

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol-5-phosphate binding

Inferred from electronic annotation. Source: Ensembl

phosphatidylserine binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 224201Retinoschisin
PRO_0000022695

Regions

Domain63 – 219157F5/8 type C

Amino acid modifications

Disulfide bond40Interchain Ref.5
Disulfide bond59Interchain (with C-223) Ref.5
Disulfide bond63 ↔ 219 Ref.5
Disulfide bond110 ↔ 142 Ref.5
Disulfide bond223Interchain (with C-59) Ref.5

Natural variations

Natural variant121L → H in XLRS1.
VAR_008209
Natural variant131L → P in XLRS1. Ref.12
VAR_008210
Natural variant591C → S in XLRS1.
VAR_008211
Natural variant651Y → C in XLRS1.
VAR_008212
Natural variant701G → A in XLRS1. Ref.12
VAR_008213
Natural variant701G → S in XLRS1. Ref.12
VAR_008214
Natural variant721E → D in XLRS1.
VAR_008180
Natural variant721E → K in XLRS1. Ref.6 Ref.9 Ref.11 Ref.12 Ref.15
VAR_008181
Natural variant731S → P in XLRS1. Ref.14
VAR_065326
Natural variant741G → V in XLRS1. Ref.9 Ref.12
VAR_008182
Natural variant851Missing in XLRS1. Ref.12
VAR_023959
Natural variant891Y → C in XLRS1. Ref.11
VAR_008215
Natural variant961W → R in XLRS1. Ref.1 Ref.12
VAR_008183
Natural variant981A → E in XLRS1. Ref.8
VAR_008216
Natural variant1021R → Q in XLRS1. Ref.12 Ref.13 Ref.14
VAR_008217
Natural variant1021R → W in XLRS1. Ref.1
VAR_008184
Natural variant1031L → R in XLRS1.
VAR_008218
Natural variant1081F → C in XLRS1. Ref.8
VAR_008219
Natural variant1091G → E in XLRS1. Ref.11
VAR_008220
Natural variant1091G → R in XLRS1. Ref.9
VAR_008185
Natural variant1091G → W in XLRS1. Ref.8
VAR_008221
Natural variant1101C → Y in XLRS1.
VAR_008222
Natural variant1121W → C in XLRS1.
VAR_008223
Natural variant1131L → F in XLRS1.
VAR_008224
Natural variant1271L → P in XLRS1.
VAR_008225
Natural variant1351G → V in XLRS1.
VAR_008226
Natural variant1361I → T in XLRS1.
VAR_008227
Natural variant1381T → A in XLRS1.
VAR_008228
Natural variant1401G → E in XLRS1.
VAR_008229
Natural variant1401G → R in XLRS1. Ref.12 Ref.15
VAR_008230
Natural variant1411R → C in XLRS1. Ref.8 Ref.15
VAR_008231
Natural variant1411R → G in XLRS1.
VAR_008232
Natural variant1411R → H in XLRS1. Ref.15
VAR_008233
Natural variant1421C → W in XLRS1. Ref.12
VAR_008234
Natural variant1431D → V in XLRS1.
VAR_008235
Natural variant1451D → H in XLRS1. Ref.14
VAR_065327
Natural variant1461E → D in XLRS1.
VAR_008236
Natural variant1461E → K in XLRS1. Ref.8
VAR_008237
Natural variant1551Y → C in XLRS1.
VAR_008238
Natural variant1561R → G in XLRS1. Ref.14
VAR_065328
Natural variant1581D → N.
Corresponds to variant rs1800002 [ dbSNP | Ensembl ].
VAR_008239
Natural variant1631W → C in XLRS1. Ref.12
VAR_008240
Natural variant1781G → D in XLRS1.
VAR_008241
Natural variant1821R → C in XLRS1. Ref.11
VAR_008242
Natural variant1921P → L in XLRS1. Ref.15
VAR_065329
Natural variant1921P → R in XLRS1.
VAR_008243
Natural variant1921P → S in XLRS1. Ref.12 Ref.15
VAR_008244
Natural variant1931P → L in XLRS1. Ref.6
VAR_008245
Natural variant1931P → S in XLRS1. Ref.10
VAR_008246
Natural variant1971R → C in XLRS1. Ref.7
VAR_008247
Natural variant1971R → H in XLRS1.
VAR_008248
Natural variant1991I → T in XLRS1.
VAR_008249
Natural variant2001R → C in XLRS1. Ref.8 Ref.12 Ref.14
VAR_008251
Natural variant2001R → H in XLRS1. Ref.12
VAR_008252
Natural variant2031P → L in XLRS1. Ref.11
VAR_008253
Natural variant2071H → Q in XLRS1.
VAR_008254
Natural variant2091R → C in XLRS1. Ref.15
VAR_065330
Natural variant2091R → H in XLRS1. Ref.14
VAR_008255
Natural variant2131R → Q in XLRS1. Ref.14
VAR_065331
Natural variant2131R → W in XLRS1.
VAR_008256
Natural variant2151E → K in XLRS1. Ref.8
VAR_008257
Natural variant2151E → Q in XLRS1.
VAR_008258
Natural variant2161L → P in XLRS1.
VAR_008259
Natural variant2191C → G in XLRS1.
VAR_008260
Natural variant2191C → R in XLRS1.
VAR_008261
Natural variant2221K → N.
Corresponds to variant rs1800004 [ dbSNP | Ensembl ].
VAR_012078
Natural variant2231C → R in XLRS1. Ref.12 Ref.14
VAR_008262

Sequences

Sequence LengthMass (Da)Tools
O15537 [UniParc].

Last modified August 1, 1998. Version 2.
Checksum: A3893895E6A7E292

FASTA22425,592
        10         20         30         40         50         60 
MSRKIEGFLL LLLFGYEATL GLSSTEDEGE DPWYQKACKC DCQGGPNALW SAGATSLDCI 

        70         80         90        100        110        120 
PECPYHKPLG FESGEVTPDQ ITCSNPEQYV GWYSSWTANK ARLNSQGFGC AWLSKFQDSS 

       130        140        150        160        170        180 
QWLQIDLKEI KVISGILTQG RCDIDEWMTK YSVQYRTDER LNWIYYKDQT GNNRVFYGNS 

       190        200        210        220 
DRTSTVQNLL RPPIISRFIR LIPLGWHVRI AIRMELLECV SKCA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Japanese juvenile retinoschisis is caused by mutations of the XLRS1 gene."
Hotta Y., Fujiki K., Hayakawa M., Ohta T., Fujimaki T., Tamaki K., Yokoyama T., Kanai A., Hirakata A., Hida T., Nishina S., Azuma N.
Hum. Genet. 103:142-144(1998) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Mutations of the RS1 gene

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF018963 expand/collapse EMBL AC list , 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.
RefSeqNP_000321.1. NM_000330.3.
UniGeneHs.715725.

3D structure databases

ProteinModelPortalO15537.
SMRO15537. Positions 32-220.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000369320.

PTM databases

PhosphoSiteO15537.

Proteomic databases

PaxDbO15537.
PRIDEO15537.

Protocols and materials databases

DNASU6247.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379984; ENSP00000369320; ENSG00000102104.
GeneID6247.
KEGGhsa:6247.
UCSCuc004cyo.3. human.

Organism-specific databases

CTD6247.
GeneCardsGC0XM018567.
HGNCHGNC:10457. RS1.
MIM300839. gene.
312700. phenotype.
neXtProtNX_O15537.
Orphanet792. X-linked retinoschisis.
PharmGKBPA34871.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG130479.
HOGENOMHOG000006700.
HOVERGENHBG061301.
InParanoidO15537.
OMAAWLSKYQ.
OrthoDBEOG7SBNPV.
PhylomeDBO15537.

Gene expression databases

ArrayExpressO15537.
BgeeO15537.
CleanExHS_RS1.
GenevestigatorO15537.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
InterProIPR000421. Coagulation_fac_5/8-C_type_dom.
IPR008979. Galactose-bd-like.
[Graphical view]
PfamPF00754. F5_F8_type_C. 1 hit.
[Graphical view]
SMARTSM00231. FA58C. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
PROSITEPS01285. FA58C_1. 1 hit.
PS50022. FA58C_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRetinoschisin.
GenomeRNAi6247.
NextBio24257.
PROO15537.
SOURCESearch...

Entry information

Entry nameXLRS1_HUMAN
AccessionPrimary (citable) accession number: O15537
Secondary accession number(s): Q0QD39
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: March 19, 2014
This is version 126 of the entry and version 2 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

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 X

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