O15537 (XLRS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Retinoschisin

Alternative name(s):
X-linked juvenile retinoschisis protein

Gene names

Name:	RS1
Synonyms:	XLRS1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	224 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.4
Subcellular location	Secreted Ref.3.
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.3
Developmental stage	Up-regulated during the differentiation of a retinoblastoma cell line. Ref.3
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.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Sequence similarities	Contains 1 F5/8 type C domain.

Ontologies

Keywords
Biological process	Cell adhesion Sensory transduction Vision
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Signal
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adaptation of rhodopsin mediated signaling Inferred from electronic annotation. Source: Compara 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: Compara visual perception Traceable author statement Ref.1. Source: ProtInc
Cellular_component	extracellular space Traceable author statement Ref.3. Source: ProtInc extrinsic to plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	phosphatidylinositol-3,4,5-trisphosphate binding Inferred from electronic annotation. Source: Compara phosphatidylinositol-3,4-bisphosphate binding Inferred from electronic annotation. Source: Compara phosphatidylinositol-3,5-bisphosphate binding Inferred from electronic annotation. Source: Compara phosphatidylinositol-3-phosphate binding Inferred from electronic annotation. Source: Compara phosphatidylinositol-4,5-bisphosphate binding Inferred from electronic annotation. Source: Compara phosphatidylinositol-4-phosphate binding Inferred from electronic annotation. Source: Compara phosphatidylinositol-5-phosphate binding Inferred from electronic annotation. Source: Compara phosphatidylserine binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 224	201	Retinoschisin		PRO_0000022695
Regions
	Domain	63 – 219	157	F5/8 type C
Amino acid modifications
	Disulfide bond	40		Interchain Ref.4
	Disulfide bond	59		Interchain (with C-223) Ref.4
	Disulfide bond	63 ↔ 219		Ref.4
	Disulfide bond	110 ↔ 142		Ref.4
	Disulfide bond	223		Interchain (with C-59) Ref.4
Natural variations
	Natural variant	12	1	L → H in XLRS1.		VAR_008209
	Natural variant	13	1	L → P in XLRS1. Ref.11		VAR_008210
	Natural variant	59	1	C → S in XLRS1.		VAR_008211
	Natural variant	65	1	Y → C in XLRS1.		VAR_008212
	Natural variant	70	1	G → A in XLRS1. Ref.11		VAR_008213
	Natural variant	70	1	G → S in XLRS1. Ref.11		VAR_008214
	Natural variant	72	1	E → D in XLRS1.		VAR_008180
	Natural variant	72	1	E → K in XLRS1. Ref.5 Ref.8 Ref.10 Ref.11 Ref.14		VAR_008181
	Natural variant	73	1	S → P in XLRS1. Ref.13		VAR_065326
	Natural variant	74	1	G → V in XLRS1. Ref.8 Ref.11		VAR_008182
	Natural variant	85	1	Missing in XLRS1. Ref.11		VAR_023959
	Natural variant	89	1	Y → C in XLRS1. Ref.10		VAR_008215
	Natural variant	96	1	W → R in XLRS1. Ref.1 Ref.11		VAR_008183
	Natural variant	98	1	A → E in XLRS1. Ref.7		VAR_008216
	Natural variant	102	1	R → Q in XLRS1. Ref.11 Ref.12 Ref.13		VAR_008217
	Natural variant	102	1	R → W in XLRS1. Ref.1		VAR_008184
	Natural variant	103	1	L → R in XLRS1.		VAR_008218
	Natural variant	108	1	F → C in XLRS1. Ref.7		VAR_008219
	Natural variant	109	1	G → E in XLRS1. Ref.10		VAR_008220
	Natural variant	109	1	G → R in XLRS1. Ref.8		VAR_008185
	Natural variant	109	1	G → W in XLRS1. Ref.7		VAR_008221
	Natural variant	110	1	C → Y in XLRS1.		VAR_008222
	Natural variant	112	1	W → C in XLRS1.		VAR_008223
	Natural variant	113	1	L → F in XLRS1.		VAR_008224
	Natural variant	127	1	L → P in XLRS1.		VAR_008225
	Natural variant	135	1	G → V in XLRS1.		VAR_008226
	Natural variant	136	1	I → T in XLRS1.		VAR_008227
	Natural variant	138	1	T → A in XLRS1.		VAR_008228
	Natural variant	140	1	G → E in XLRS1.		VAR_008229
	Natural variant	140	1	G → R in XLRS1. Ref.11 Ref.14		VAR_008230
	Natural variant	141	1	R → C in XLRS1. Ref.7 Ref.14		VAR_008231
	Natural variant	141	1	R → G in XLRS1.		VAR_008232
	Natural variant	141	1	R → H in XLRS1. Ref.14		VAR_008233
	Natural variant	142	1	C → W in XLRS1. Ref.11		VAR_008234
	Natural variant	143	1	D → V in XLRS1.		VAR_008235
	Natural variant	145	1	D → H in XLRS1. Ref.13		VAR_065327
	Natural variant	146	1	E → D in XLRS1.		VAR_008236
	Natural variant	146	1	E → K in XLRS1. Ref.7		VAR_008237
	Natural variant	155	1	Y → C in XLRS1.		VAR_008238
	Natural variant	156	1	R → G in XLRS1. Ref.13		VAR_065328
	Natural variant	158	1	D → N. Corresponds to variant rs1800002 [ dbSNP | Ensembl ].		VAR_008239
	Natural variant	163	1	W → C in XLRS1. Ref.11		VAR_008240
	Natural variant	178	1	G → D in XLRS1.		VAR_008241
	Natural variant	182	1	R → C in XLRS1. Ref.10		VAR_008242
	Natural variant	192	1	P → L in XLRS1. Ref.14		VAR_065329
	Natural variant	192	1	P → R in XLRS1.		VAR_008243
	Natural variant	192	1	P → S in XLRS1. Ref.11 Ref.14		VAR_008244
	Natural variant	193	1	P → L in XLRS1. Ref.5		VAR_008245
	Natural variant	193	1	P → S in XLRS1. Ref.9		VAR_008246
	Natural variant	197	1	R → C in XLRS1. Ref.6		VAR_008247
	Natural variant	197	1	R → H in XLRS1.		VAR_008248
	Natural variant	199	1	I → T in XLRS1.		VAR_008249
	Natural variant	200	1	R → C in XLRS1. Ref.7 Ref.11 Ref.13		VAR_008251
	Natural variant	200	1	R → H in XLRS1. Ref.11		VAR_008252
	Natural variant	203	1	P → L in XLRS1. Ref.10		VAR_008253
	Natural variant	207	1	H → Q in XLRS1.		VAR_008254
	Natural variant	209	1	R → C in XLRS1. Ref.14		VAR_065330
	Natural variant	209	1	R → H in XLRS1. Ref.13		VAR_008255
	Natural variant	213	1	R → Q in XLRS1. Ref.13		VAR_065331
	Natural variant	213	1	R → W in XLRS1.		VAR_008256
	Natural variant	215	1	E → K in XLRS1. Ref.7		VAR_008257
	Natural variant	215	1	E → Q in XLRS1.		VAR_008258
	Natural variant	216	1	L → P in XLRS1.		VAR_008259
	Natural variant	219	1	C → G in XLRS1.		VAR_008260
	Natural variant	219	1	C → R in XLRS1.		VAR_008261
	Natural variant	222	1	K → N. Corresponds to variant rs1800004 [ dbSNP | Ensembl ].		VAR_012078
	Natural variant	223	1	C → R in XLRS1. Ref.11 Ref.13		VAR_008262

Sequences

	Sequence		Length	Mass (Da)
	O15537 [UniParc]. Last modified August 1, 1998. Version 2. Checksum: A3893895E6A7E292	FASTA	224	25,592
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[4]	"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.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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 , 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.
IPI	IPI00007331.
RefSeq	NP_000321.1. NM_000330.3.
UniGene	Hs.715725.
3D structure databases
ProteinModelPortal	O15537.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000369320.
PTM databases
PhosphoSite	O15537.
Proteomic databases
PaxDb	O15537.
PRIDE	O15537.
Protocols and materials databases
DNASU	6247.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000379984; ENSP00000369320; ENSG00000102104.
GeneID	6247.
KEGG	hsa:6247.
UCSC	uc004cyo.3. human.
Organism-specific databases
CTD	6247.
GeneCards	GC0XM018567.
HGNC	HGNC:10457. RS1.
MIM	300839. gene. 312700. phenotype.
neXtProt	NX_O15537.
Orphanet	792. X-linked retinoschisis.
PharmGKB	PA34871.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG130479.
HOGENOM	HOG000006700.
HOVERGEN	HBG061301.
InParanoid	O15537.
OMA	AWLSKYQ.
OrthoDB	EOG40P47P.
PhylomeDB	O15537.
Gene expression databases
ArrayExpress	O15537.
Bgee	O15537.
CleanEx	HS_RS1.
Genevestigator	O15537.
GermOnline	ENSG00000102104. Homo sapiens.
Family and domain databases
InterPro	IPR000421. Coagulation_fac_5/8-C_type_dom. IPR008979. Galactose-bd-like. IPR027161. Retinoschisin. [Graphical view]
PANTHER	PTHR10127:SF27. PTHR10127:SF27. 1 hit.
Pfam	PF00754. F5_F8_type_C. 1 hit. [Graphical view]
SMART	SM00231. FA58C. 1 hit. [Graphical view]
SUPFAM	SSF49785. Gal_bind_like. 1 hit.
PROSITE	PS01285. FA58C_1. 1 hit. PS01286. FA58C_2. False negative. PS50022. FA58C_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	6247.
NextBio	24257.
SOURCE	Search...

Entry information

Entry name

XLRS1_HUMAN

Accession

Primary (citable) accession number: O15537

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	May 1, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.