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P10523

- ARRS_HUMAN

UniProt

P10523 - ARRS_HUMAN

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

Functioni

Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated-phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase.

GO - Molecular functioni

  1. protein phosphatase inhibitor activity Source: ProtInc

GO - Biological processi

  1. cell surface receptor signaling pathway Source: ProtInc
  2. negative regulation of catalytic activity Source: GOC
  3. phototransduction, visible light Source: Reactome
  4. regulation of rhodopsin mediated signaling pathway Source: Reactome
  5. rhodopsin mediated signaling pathway Source: Reactome
  6. visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
SignaLinkiP10523.

Names & Taxonomyi

Protein namesi
Recommended name:
S-arrestin
Alternative name(s):
48 kDa protein
Retinal S-antigen
Short name:
S-AG
Rod photoreceptor arrestin
Gene namesi
Name:SAG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:10521. SAG.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Night blindness, congenital stationary, Oguchi type 1 (CSNBO1) [MIM:258100]: A non-progressive retinal disorder characterized by impaired night vision, often associated with nystagmus and myopia. Congenital stationary night blindness Oguchi type is an autosomal recessive form associated with fundus discoloration and abnormally slow dark adaptation.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Retinitis pigmentosa 47 (RP47) [MIM:613758]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Keywords - Diseasei

Autoimmune uveitis, Congenital stationary night blindness, Retinitis pigmentosa

Organism-specific databases

MIMi258100. phenotype.
613758. phenotype.
Orphaneti215. Congenital stationary night blindness.
75382. Oguchi disease.
791. Retinitis pigmentosa.
PharmGKBiPA34929.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 405405S-arrestin
PRO_0000205186Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi132 ↔ 147 Inferred
Modified residuei234 – 2341Phosphothreonine By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP10523.
PRIDEiP10523.

PTM databases

PhosphoSiteiP10523.

Expressioni

Tissue specificityi

Retina and pineal gland.

Gene expression databases

ArrayExpressiP10523.
BgeeiP10523.
CleanExiHS_SAG.
GenevestigatoriP10523.

Interactioni

Subunit structurei

Monomer. Homodimer. Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi112202. 3 interactions.
IntActiP10523. 2 interactions.
STRINGi9606.ENSP00000386444.

Structurei

3D structure databases

ProteinModelPortaliP10523.
SMRiP10523. Positions 14-364.

Family & Domainsi

Sequence similaritiesi

Belongs to the arrestin family.

Phylogenomic databases

eggNOGiNOG330592.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP10523.
OMAiKEIYFHG.
PhylomeDBiP10523.
TreeFamiTF314260.

Family and domain databases

Gene3Di2.60.40.640. 1 hit.
2.60.40.840. 1 hit.
InterProiIPR000698. Arrestin.
IPR011021. Arrestin-like_N.
IPR014752. Arrestin_C.
IPR011022. Arrestin_C-like.
IPR017864. Arrestin_CS.
IPR014753. Arrestin_N.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR11792. PTHR11792. 1 hit.
PfamiPF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view]
PRINTSiPR00309. ARRESTIN.
SMARTiSM01017. Arrestin_C. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 2 hits.
PROSITEiPS00295. ARRESTINS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10523-1 [UniParc]FASTAAdd to Basket

« Hide

MAASGKTSKS EPNHVIFKKI SRDKSVTIYL GNRDYIDHVS QVQPVDGVVL    50
VDPDLVKGKK VYVTLTCAFR YGQEDIDVIG LTFRRDLYFS RVQVYPPVGA 100
ASTPTKLQES LLKKLGSNTY PFLLTFPDYL PCSVMLQPAP QDSGKSCGVD 150
FEVKAFATDS TDAEEDKIPK KSSVRLLIRK VQHAPLEMGP QPRAEAAWQF 200
FMSDKPLHLA VSLNKEIYFH GEPIPVTVTV TNNTEKTVKK IKAFVEQVAN 250
VVLYSSDYYV KPVAMEEAQE KVPPNSTLTK TLTLLPLLAN NRERRGIALD 300
GKIKHEDTNL ASSTIIKEGI DRTVLGILVS YQIKVKLTVS GFLGELTSSE 350
VATEVPFRLM HPQPEDPAKE SYQDANLVFE EFARHNLKDA GEAEEGKRDK 400
NDVDE 405
Length:405
Mass (Da):45,120
Last modified:June 27, 2006 - v3
Checksum:iCBBF65845A5F891E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 761I → V.2 Publications
Corresponds to variant rs7565275 [ dbSNP | Ensembl ].
VAR_008263
Natural varianti84 – 841R → C.1 Publication
Corresponds to variant rs115857633 [ dbSNP | Ensembl ].
VAR_008264
Natural varianti125 – 1251T → M.1 Publication
Corresponds to variant rs137886124 [ dbSNP | Ensembl ].
VAR_008265
Natural varianti364 – 3641P → L.1 Publication
Corresponds to variant rs112613526 [ dbSNP | Ensembl ].
VAR_008266
Natural varianti378 – 3781V → I.1 Publication
Corresponds to variant rs200602069 [ dbSNP | Ensembl ].
VAR_008267
Natural varianti384 – 3841R → C.1 Publication
VAR_008268
Natural varianti403 – 4031V → A.2 Publications
Corresponds to variant rs1046976 [ dbSNP | Ensembl ].
VAR_048333
Natural varianti403 – 4031V → I.
Corresponds to variant rs1046974 [ dbSNP | Ensembl ].
VAR_033524

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti176 – 1761L → Y in CAA30984. 1 Publication
Sequence conflicti180 – 1801K → S in CAA30984. 1 Publication
Sequence conflicti197 – 1971A → T in CAA30984. 1 Publication
Sequence conflicti215 – 2151K → R in CAA30984. 1 Publication
Sequence conflicti244 – 2441F → C in CAA30984. 1 Publication
Sequence conflicti372 – 3721Y → I in CAA30984. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12453 mRNA. Translation: CAA30984.1.
U70976
, U70962, U70963, U70964, U70965, U70966, U70967, U70968, U70969, U70970, U70971, U70972, U70973, U70974, U70975 Genomic DNA. Translation: AAC50992.1.
AC013726 Genomic DNA. Translation: AAY14861.1.
DQ980620 mRNA. Translation: ABJ97141.1.
CCDSiCCDS46545.1.
PIRiA30357.
RefSeqiNP_000532.2. NM_000541.4.
XP_005246156.1. XM_005246099.1.
UniGeneiHs.32721.

Genome annotation databases

EnsembliENST00000409110; ENSP00000386444; ENSG00000130561.
GeneIDi6295.
KEGGihsa:6295.
UCSCiuc002vuh.2. human.

Polymorphism databases

DMDMi109940055.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the SAG gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12453 mRNA. Translation: CAA30984.1 .
U70976
, U70962 , U70963 , U70964 , U70965 , U70966 , U70967 , U70968 , U70969 , U70970 , U70971 , U70972 , U70973 , U70974 , U70975 Genomic DNA. Translation: AAC50992.1 .
AC013726 Genomic DNA. Translation: AAY14861.1 .
DQ980620 mRNA. Translation: ABJ97141.1 .
CCDSi CCDS46545.1.
PIRi A30357.
RefSeqi NP_000532.2. NM_000541.4.
XP_005246156.1. XM_005246099.1.
UniGenei Hs.32721.

3D structure databases

ProteinModelPortali P10523.
SMRi P10523. Positions 14-364.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112202. 3 interactions.
IntActi P10523. 2 interactions.
STRINGi 9606.ENSP00000386444.

PTM databases

PhosphoSitei P10523.

Polymorphism databases

DMDMi 109940055.

Proteomic databases

PaxDbi P10523.
PRIDEi P10523.

Protocols and materials databases

DNASUi 6295.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000409110 ; ENSP00000386444 ; ENSG00000130561 .
GeneIDi 6295.
KEGGi hsa:6295.
UCSCi uc002vuh.2. human.

Organism-specific databases

CTDi 6295.
GeneCardsi GC02P234247.
GeneReviewsi SAG.
HGNCi HGNC:10521. SAG.
MIMi 181031. gene.
258100. phenotype.
613758. phenotype.
neXtProti NX_P10523.
Orphaneti 215. Congenital stationary night blindness.
75382. Oguchi disease.
791. Retinitis pigmentosa.
PharmGKBi PA34929.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG330592.
HOGENOMi HOG000231319.
HOVERGENi HBG002399.
InParanoidi P10523.
OMAi KEIYFHG.
PhylomeDBi P10523.
TreeFami TF314260.

Enzyme and pathway databases

Reactomei REACT_163919. Inactivation, recovery and regulation of the phototransduction cascade.
SignaLinki P10523.

Miscellaneous databases

GeneWikii SAG_(gene).
GenomeRNAii 6295.
NextBioi 24439.
PROi P10523.
SOURCEi Search...

Gene expression databases

ArrayExpressi P10523.
Bgeei P10523.
CleanExi HS_SAG.
Genevestigatori P10523.

Family and domain databases

Gene3Di 2.60.40.640. 1 hit.
2.60.40.840. 1 hit.
InterProi IPR000698. Arrestin.
IPR011021. Arrestin-like_N.
IPR014752. Arrestin_C.
IPR011022. Arrestin_C-like.
IPR017864. Arrestin_CS.
IPR014753. Arrestin_N.
IPR014756. Ig_E-set.
[Graphical view ]
PANTHERi PTHR11792. PTHR11792. 1 hit.
Pfami PF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view ]
PRINTSi PR00309. ARRESTIN.
SMARTi SM01017. Arrestin_C. 1 hit.
[Graphical view ]
SUPFAMi SSF81296. SSF81296. 2 hits.
PROSITEi PS00295. ARRESTINS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of human retinal S-antigen reveals similarities with alpha-transducin."
    Yamaki K., Tsuda M., Shinohara T.
    FEBS Lett. 234:39-43(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-403.
    Tissue: Retina.
  2. Erratum
    Yamaki K., Tsuda M., Shinohara T.
    FEBS Lett. 236:507-507(1988)
  3. "Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness."
    Yamamoto S., Sippel K.C., Berson E.L., Dryja T.P.
    Nat. Genet. 15:175-178(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-403.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 1-133.
    Tissue: Retina.
  6. "A homozygous 1-base pair deletion in the arrestin gene is a frequent cause of Oguchi disease in Japanese."
    Fuchs S., Nakazawa M., Maw M., Tamai M., Oguchi Y., Gal A.
    Nat. Genet. 10:360-362(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CSNBO1, VARIANT VAL-76.
  7. "Arrestin gene mutations in autosomal recessive retinitis pigmentosa."
    Nakazawa M., Wada Y., Tamai M.
    Arch. Ophthalmol. 116:498-501(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN RP47.
  8. "Robust self-association is a common feature of mammalian visual arrestin-1."
    Kim M., Hanson S.M., Vishnivetskiy S.A., Song X., Cleghorn W.M., Hubbell W.L., Gurevich V.V.
    Biochemistry 50:2235-2242(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  9. "Evaluation of the human arrestin gene in patients with retinitis pigmentosa and stationary night blindness."
    Sippel K.C., DeStefano J.D., Berson E.L., Dryja T.P.
    Invest. Ophthalmol. Vis. Sci. 39:665-670(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VAL-76; CYS-84; MET-125; LEU-364; ILE-378 AND CYS-384.

Entry informationi

Entry nameiARRS_HUMAN
AccessioniPrimary (citable) accession number: P10523
Secondary accession number(s): A0FDN6, Q53SV3, Q99858
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: June 27, 2006
Last modified: September 3, 2014
This is version 136 of the entry and version 3 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

Miscellaneous

Arrestin binds calcium.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

Dasty 3

Similar proteinsi