UniProtKB - P08100 (OPSD_HUMAN)
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- BLAST>sp|P08100|OPSD_HUMAN Rhodopsin OS=Homo sapiens OX=9606 GN=RHO PE=1 SV=1 MNGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLY VTVQHKKLRTPLNYILLNLAVADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLEGFFATLG GEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLAGWSRYIP EGLQCSCGIDYYTLKPEVNNESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQES ATTQKAEKEVTRMVIIMVIAFLICWVPYASVAFYIFTHQGSNFGPIFMTIPAFFAKSAAI YNPVIYIMMNKQFRNCMLTTICCGKNPLGDDEASATVSKTETSQVAPA
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Rhodopsin
RHO
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.7"Molecular assembly of rhodopsin with G protein-coupled receptor kinases."
He Y., Gao X., Goswami D., Hou L., Pal K., Yin Y., Zhao G., Ernst O.P., Griffin P., Melcher K., Xu H.E.
Cell Res. 27:728-747(2017) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GRK1 AND SAG, FUNCTION, MUTAGENESIS OF GLU-113 AND MET-257.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.8"Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser."
Kang Y., Zhou X.E., Gao X., He Y., Liu W., Ishchenko A., Barty A., White T.A., Yefanov O., Han G.W., Xu Q., de Waal P.W., Ke J., Tan M.H., Zhang C., Moeller A., West G.M., Pascal B.D. , Van Eps N., Caro L.N., Vishnivetskiy S.A., Lee R.J., Suino-Powell K.M., Gu X., Pal K., Ma J., Zhi X., Boutet S., Williams G.J., Messerschmidt M., Gati C., Zatsepin N.A., Wang D., James D., Basu S., Roy-Chowdhury S., Conrad C.E., Coe J., Liu H., Lisova S., Kupitz C., Grotjohann I., Fromme R., Jiang Y., Tan M., Yang H., Li J., Wang M., Zheng Z., Li D., Howe N., Zhao Y., Standfuss J., Diederichs K., Dong Y., Potter C.S., Carragher B., Caffrey M., Jiang H., Chapman H.N., Spence J.C., Fromme P., Weierstall U., Ernst O.P., Katritch V., Gurevich V.V., Griffin P.R., Hubbell W.L., Stevens R.C., Cherezov V., Melcher K., Xu H.E.
Nature 523:561-567(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF MUTANT GLN-113 AND TYR-257 IN COMPLEX WITH SAG, INTERACTION WITH SAG AND GNAT1, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-113 AND MET-257, TOPOLOGY, DISULFIDE BONDS. - Ref.9"Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors."
Zhou X.E., He Y., de Waal P.W., Gao X., Kang Y., Van Eps N., Yin Y., Pal K., Goswami D., White T.A., Barty A., Latorraca N.R., Chapman H.N., Hubbell W.L., Dror R.O., Stevens R.C., Cherezov V., Gurevich V.V. , Griffin P.R., Ernst O.P., Melcher K., Xu H.E.
Cell 170:457-469(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH SAG, FUNCTION, TOPOLOGY, GLYCOSYLATION AT ASN-15, PHOSPHORYLATION AT SER-334; THR-336 AND SER-338, DISULFIDE BOND, MUTAGENESIS OF 336-THR--THR-340; 336-THR--SER-338 AND SER-343. - Ref.13"Mutations within the rhodopsin gene in patients with autosomal dominant retinitis pigmentosa."
Dryja T.P., McGee T.L., Hahn L.B., Cowley G.S., Olsson J.E., Reichel E., Sandberg M.A., Berson E.L.
N. Engl. J. Med. 323:1302-1307(1990) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS RP4 HIS-23; ARG-58; LEU-347 AND SER-347, FUNCTION. - Ref.31"Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness."
Rao V.R., Cohen G.B., Oprian D.D.
Nature 367:639-642(1994) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT CSNBAD1 ASP-90, FUNCTION. - Ref.34"Dark-light: model for nightblindness from the human rhodopsin Gly-90-->Asp mutation."
Sieving P.A., Richards J.E., Naarendorp F., Bingham E.L., Scott K., Alpern M.
Proc. Natl. Acad. Sci. U.S.A. 92:880-884(1995) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT CSNBAD1 ASP-90, FUNCTION. - Ref.38"Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa."
Noorwez S.M., Kuksa V., Imanishi Y., Zhu L., Filipek S., Palczewski K., Kaushal S.
J. Biol. Chem. 278:14442-14450(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT RP4 HIS-23, FUNCTION, SUBCELLULAR LOCATION.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 113 | Plays an important role in the conformation switch to the active conformation1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 201 | ZincBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 279 | ZincBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- 11-cis retinal binding Source: UniProtKB
- G-protein coupled photoreceptor activity Source: UniProtKB
- G-protein coupled receptor activity Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- metal ion binding Source: UniProtKB-KW
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- absorption of visible light Source: AgBase
- G-protein coupled receptor signaling pathway Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- photoreceptor cell maintenance Source: Ensembl
- phototransduction, visible light Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- protein-chromophore linkage Source: UniProtKB-KW
- protein phosphorylation Source: Ensembl
- regulation of rhodopsin mediated signaling pathway Source: Reactome
- retina development in camera-type eye Source: Ensembl
- retinoid metabolic process Source: Reactome
- rhodopsin mediated signaling pathway Source: UniProtKB
- visual perception Source: UniProtKB-KW
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | G-protein coupled receptor, Photoreceptor protein, Receptor, Retinal protein, Transducer |
| Biological process | Sensory transduction, Vision |
| Ligand | Chromophore, Metal-binding, Zinc |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2453902 The canonical retinoid cycle in rods (twilight vision) R-HSA-2485179 Activation of the phototransduction cascade R-HSA-2514859 Inactivation, recovery and regulation of the phototransduction cascade R-HSA-418594 G alpha (i) signalling events R-HSA-419771 Opsins R-HSA-5620916 VxPx cargo-targeting to cilium |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P08100 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P08100 |
Protein family/group databases
Transport Classification Database More...TCDBi | 9.A.14.1.2 the g-protein-coupled receptor (gpcr) family |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: RhodopsinAlternative name(s): Opsin-2 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:RHO Synonyms:OPN2 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000163914.4 |
Human Gene Nomenclature Database More...HGNCi | HGNC:10012 RHO |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 180380 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P08100 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Other locations
- Membrane 5 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Ultrastructural visualization of trans-ciliary rhodopsin cargoes in mammalian rods."
Chuang J.Z., Hsu Y.C., Sung C.H.
Cilia 4:4-4(2015) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION. - Ref.8"Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser."
Kang Y., Zhou X.E., Gao X., He Y., Liu W., Ishchenko A., Barty A., White T.A., Yefanov O., Han G.W., Xu Q., de Waal P.W., Ke J., Tan M.H., Zhang C., Moeller A., West G.M., Pascal B.D. , Van Eps N., Caro L.N., Vishnivetskiy S.A., Lee R.J., Suino-Powell K.M., Gu X., Pal K., Ma J., Zhi X., Boutet S., Williams G.J., Messerschmidt M., Gati C., Zatsepin N.A., Wang D., James D., Basu S., Roy-Chowdhury S., Conrad C.E., Coe J., Liu H., Lisova S., Kupitz C., Grotjohann I., Fromme R., Jiang Y., Tan M., Yang H., Li J., Wang M., Zheng Z., Li D., Howe N., Zhao Y., Standfuss J., Diederichs K., Dong Y., Potter C.S., Carragher B., Caffrey M., Jiang H., Chapman H.N., Spence J.C., Fromme P., Weierstall U., Ernst O.P., Katritch V., Gurevich V.V., Griffin P.R., Hubbell W.L., Stevens R.C., Cherezov V., Melcher K., Xu H.E.
Nature 523:561-567(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF MUTANT GLN-113 AND TYR-257 IN COMPLEX WITH SAG, INTERACTION WITH SAG AND GNAT1, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-113 AND MET-257, TOPOLOGY, DISULFIDE BONDS. - Ref.9"Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors."
Zhou X.E., He Y., de Waal P.W., Gao X., Kang Y., Van Eps N., Yin Y., Pal K., Goswami D., White T.A., Barty A., Latorraca N.R., Chapman H.N., Hubbell W.L., Dror R.O., Stevens R.C., Cherezov V., Gurevich V.V. , Griffin P.R., Ernst O.P., Melcher K., Xu H.E.
Cell 170:457-469(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH SAG, FUNCTION, TOPOLOGY, GLYCOSYLATION AT ASN-15, PHOSPHORYLATION AT SER-334; THR-336 AND SER-338, DISULFIDE BOND, MUTAGENESIS OF 336-THR--THR-340; 336-THR--SER-338 AND SER-343. - Ref.38"Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa."
Noorwez S.M., Kuksa V., Imanishi Y., Zhu L., Filipek S., Palczewski K., Kaushal S.
J. Biol. Chem. 278:14442-14450(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT RP4 HIS-23, FUNCTION, SUBCELLULAR LOCATION. - Ref.39"A dual role for EDEM1 in the processing of rod opsin."
Kosmaoglou M., Kanuga N., Aguila M., Garriga P., Cheetham M.E.
J. Cell Sci. 122:4465-4472(2009) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT RP4 HIS-23, SUBCELLULAR LOCATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.8"Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser."
Kang Y., Zhou X.E., Gao X., He Y., Liu W., Ishchenko A., Barty A., White T.A., Yefanov O., Han G.W., Xu Q., de Waal P.W., Ke J., Tan M.H., Zhang C., Moeller A., West G.M., Pascal B.D. , Van Eps N., Caro L.N., Vishnivetskiy S.A., Lee R.J., Suino-Powell K.M., Gu X., Pal K., Ma J., Zhi X., Boutet S., Williams G.J., Messerschmidt M., Gati C., Zatsepin N.A., Wang D., James D., Basu S., Roy-Chowdhury S., Conrad C.E., Coe J., Liu H., Lisova S., Kupitz C., Grotjohann I., Fromme R., Jiang Y., Tan M., Yang H., Li J., Wang M., Zheng Z., Li D., Howe N., Zhao Y., Standfuss J., Diederichs K., Dong Y., Potter C.S., Carragher B., Caffrey M., Jiang H., Chapman H.N., Spence J.C., Fromme P., Weierstall U., Ernst O.P., Katritch V., Gurevich V.V., Griffin P.R., Hubbell W.L., Stevens R.C., Cherezov V., Melcher K., Xu H.E.
Nature 523:561-567(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF MUTANT GLN-113 AND TYR-257 IN COMPLEX WITH SAG, INTERACTION WITH SAG AND GNAT1, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-113 AND MET-257, TOPOLOGY, DISULFIDE BONDS. - Ref.9"Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors."
Zhou X.E., He Y., de Waal P.W., Gao X., Kang Y., Van Eps N., Yin Y., Pal K., Goswami D., White T.A., Barty A., Latorraca N.R., Chapman H.N., Hubbell W.L., Dror R.O., Stevens R.C., Cherezov V., Gurevich V.V. , Griffin P.R., Ernst O.P., Melcher K., Xu H.E.
Cell 170:457-469(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH SAG, FUNCTION, TOPOLOGY, GLYCOSYLATION AT ASN-15, PHOSPHORYLATION AT SER-334; THR-336 AND SER-338, DISULFIDE BOND, MUTAGENESIS OF 336-THR--THR-340; 336-THR--SER-338 AND SER-343. - Ref.39"A dual role for EDEM1 in the processing of rod opsin."
Kosmaoglou M., Kanuga N., Aguila M., Garriga P., Cheetham M.E.
J. Cell Sci. 122:4465-4472(2009) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT RP4 HIS-23, SUBCELLULAR LOCATION.
- photoreceptor outer segment 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Ultrastructural visualization of trans-ciliary rhodopsin cargoes in mammalian rods."
Chuang J.Z., Hsu Y.C., Sung C.H.
Cilia 4:4-4(2015) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
Note: Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to disk membranes in the rod outer segment (OS) photosensory cilia.1 Publication- Membrane 5 Publications
- Ref.6"Ultrastructural visualization of trans-ciliary rhodopsin cargoes in mammalian rods."
Chuang J.Z., Hsu Y.C., Sung C.H.
Cilia 4:4-4(2015) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Golgi apparatus
- Golgi apparatus Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- Golgi membrane Source: Reactome
Plasma Membrane
- ciliary membrane Source: Reactome
- integral component of plasma membrane Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- photoreceptor disc membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- photoreceptor inner segment membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- photoreceptor outer segment membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- plasma membrane Source: LIFEdb
Other locations
- cell-cell junction Source: Ensembl
- Golgi-associated vesicle membrane Source: Reactome
- integral component of membrane Source: UniProtKB
- photoreceptor inner segment Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- photoreceptor outer segment Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 1 – 36 | Extracellular2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 36 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 37 – 61 | Helical; Name=12 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 25 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 62 – 73 | Cytoplasmic2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 12 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 74 – 96 | Helical; Name=22 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 23 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 97 – 110 | Extracellular2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 14 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 111 – 133 | Helical; Name=32 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 23 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 134 – 152 | Cytoplasmic2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 19 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 153 – 173 | Helical; Name=42 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 174 – 202 | Extracellular2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 29 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 203 – 224 | Helical; Name=52 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 22 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 225 – 252 | Cytoplasmic2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 28 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 253 – 274 | Helical; Name=62 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 22 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 275 – 284 | Extracellular2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 10 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 285 – 309 | Helical; Name=72 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 25 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 310 – 348 | Cytoplasmic2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 39 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cell projection, Membrane<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Retinitis pigmentosa 4 (RP4)26 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.11"Autosomal dominant retinitis pigmentosa: absence of the rhodopsin proline-->histidine substitution (codon 23) in pedigrees from Europe."
Farrar G.J., Kenna P., Redmond R., McWilliam P., Bradley D.G., Humphries M.M., Sharp E.M., Inglehearn C.F., Bashir R., Jay M., Watty A., Ludwig M., Schinzel A., Samanns C., Gal A., Bhattacharya S.S., Humphries P.
Am. J. Hum. Genet. 47:941-945(1990) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS RP4. - Ref.12"A point mutation of the rhodopsin gene in one form of retinitis pigmentosa."
Dryja T.P., McGee T.L., Reichei E., Hahn L.B., Cowley G.S., Yandell D.W., Sandberg M.A., Berson E.L.
Nature 343:364-366(1990) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT RP4 HIS-23. - Ref.13"Mutations within the rhodopsin gene in patients with autosomal dominant retinitis pigmentosa."
Dryja T.P., McGee T.L., Hahn L.B., Cowley G.S., Olsson J.E., Reichel E., Sandberg M.A., Berson E.L.
N. Engl. J. Med. 323:1302-1307(1990) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS RP4 HIS-23; ARG-58; LEU-347 AND SER-347, FUNCTION. - Ref.14"A 3-bp deletion in the rhodopsin gene in a family with autosomal dominant retinitis pigmentosa."
Inglehearn C.F., Bashir R., Lester D.H., Jay M., Bird A.C., Bhattacharya S.S.
Am. J. Hum. Genet. 48:26-30(1991) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT RP4 ILE-255 DEL. - Ref.15"Identification of novel rhodopsin mutations associated with retinitis pigmentosa by GC-clamped denaturing gradient gel electrophoresis."
Sheffield V.C., Fishman G.A., Beck J.S., Kimura A.E., Stone E.M.
Am. J. Hum. Genet. 49:699-706(1991) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS RP4 MET-17; HIS-23; ARG-58; SER-182 AND LEU-267. - Ref.16"Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant retinitis pigmentosa."
Gal A., Artlich A., Ludwig M., Niemeyer G., Olek K., Schwinger E., Schinzel A.
Genomics 11:468-470(1991) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT RP4 ARG-347. - Ref.17"Rhodopsin mutations in autosomal dominant retinitis pigmentosa."
Sung C.H., Davenport C.M., Hennessey J.C., Maumenee I.H., Jacobson S.G., Heckenlively J.R., Nowakowski R., Fishman G., Gouras P., Nathans J.
Proc. Natl. Acad. Sci. U.S.A. 88:6481-6485(1991) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS RP4. - Ref.18"Mutation spectrum of the rhodopsin gene among patients with autosomal dominant retinitis pigmentosa."
Dryja T.P., Hahn L.B., Cowley G.S., McGee T.L., Berson E.L.
Proc. Natl. Acad. Sci. U.S.A. 88:9370-9374(1991) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS RP4. - Ref.19"Autosomal dominant retinitis pigmentosa: a novel mutation in the rhodopsin gene in the original 3q linked family."
Farrar G.J., Findlay J.B.C., Kumar-Singh R., Kenna P., Humphries M.M., Sharpe E., Humphries P.
Hum. Mol. Genet. 1:769-771(1992) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT RP4 ARG-207. - Ref.20"Point mutations of rhodopsin gene found in Japanese families with autosomal dominant retinitis pigmentosa (ADRP)."
Fujiki K., Hotta Y., Hayakawa M., Sakuma H., Shiono T., Noro M., Sakuma T., Tamai M., Hikiji K., Kawaguchi R., Hoshi A., Nakajima A., Kanai A.
Jpn. J. Hum. Genet. 37:125-132(1992) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS RP4 MET-17 AND LEU-347. - Ref.21"Identification of novel rhodopsin mutations responsible for retinitis pigmentosa: implications for the structure and function of rhodopsin."
Macke J.P., Davenport C.M., Jacobson S.G., Hennessey J.C., Gonzalez-Fernandez F., Conway B.P., Heckenlively J., Palmer R., Maumenee I.H., Sieving P., Gouras P., Good W., Nathans J.
Am. J. Hum. Genet. 53:80-89(1993) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS RP4 ARG-106; GLY-135; SER-140; GLU-188 AND ARG-211, VARIANTS ALA-51; ILE-104 AND MET-209. - Ref.22"Autosomal dominant 'sector' retinitis pigmentosa due to a point mutation predicting an Asn-15-Ser substitution of rhodopsin."
Kranich H., Bartkowski S., Denton M.J., Krey S., Dickinson P., Duvigneau C., Gal A.
Hum. Mol. Genet. 2:813-814(1993) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT RP4 SER-15. - Ref.24"Further screening of the rhodopsin gene in patients with autosomal dominant retinitis pigmentosa."
Vaithinathan R., Berson E.L., Dryja T.P.
Genomics 21:461-463(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS RP4. - Ref.25"Identification of a novel rhodopsin mutation (Met-44-Thr) in a simplex case of retinitis pigmentosa."
Reig C., Antich J., Gean E., Garcia-Sandoval B., Ramos C., Ayuso C., Carballo M.
Hum. Genet. 94:283-286(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT RP4 THR-44. - Ref.26"Three novel rhodopsin mutations (C110F, L131P, A164V) in patients with autosomal dominant retinitis pigmentosa."
Fuchs S., Kranich H., Denton M.J., Zrenner E., Bhattacharya S.S., Humphries P., Gal A.
Hum. Mol. Genet. 3:1203-1203(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS RP4 PHE-110; PRO-131 AND VAL-164. - Ref.27"Identification of a new mutation at codon 171 of rhodopsin gene causing autosomal dominant retinitis pigmentosa."
Antinolo G., Sanchez B., Borrego S., Rueda T., Chaparro P., Cabeza J.C.
Hum. Mol. Genet. 3:1421-1421(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT RP4 GLN-171. - Ref.28"Five novel missense mutations of the rhodopsin gene in autosomal dominant retinitis pigmentosa."
Souied E., Gerber S., Rozet J.-M., Bonneau D., Dufier J.-L., Ghazi I., Philip N., Soubrane G., Coscas G., Munnich A.
Hum. Mol. Genet. 3:1433-1434(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS RP4 PHE-127; PRO-131; ASN-178; ARG-267 AND ARG-297. - Ref.29"Two new rhodopsin transversion mutations (L40R; M216K) in families with autosomal dominant retinitis pigmentosa."
Al-Maghtheh M., Inglehearn C., Lunt P., Jay M., Bird A., Bhattacharya S.
Hum. Mutat. 3:409-410(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS RP4 ARG-40 AND LYS-216. - Ref.30"Autosomal dominant retinitis pigmentosa in a large family: a clinical and molecular genetic study."
Rosas D.J., Roman A.J., Weissbrod P., Macke J.P., Nathans J.
Invest. Ophthalmol. Vis. Sci. 35:3134-3144(1994) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT RP4 LEU-345. - Ref.33"Rhodopsin mutation proline347-to-alanine in a family with autosomal dominant retinitis pigmentosa indicates an important role for proline at position 347."
Macke J.P., Hennessey J.C., Nathans J.
Hum. Mol. Genet. 4:775-776(1995) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT RP4 ALA-347. - Ref.35"Retinitis punctata albescens associated with the Arg135Trp mutation in the rhodopsin gene."
Souied E., Soubrane G., Benlian P., Coscas G.J., Gerber S., Munnich A., Kaplan J.
Am. J. Ophthalmol. 121:19-25(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT RP4 TRP-135. - Ref.36"Rhodopsin mutation G109R in a family with autosomal dominant retinitis pigmentosa."
Goliath R., Bardien S., September A., Martin R., Ramesar R., Greenberg J.
Hum. Mutat. Suppl. 1:S40-S41(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT RP4 ARG-109. - Ref.38"Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa."
Noorwez S.M., Kuksa V., Imanishi Y., Zhu L., Filipek S., Palczewski K., Kaushal S.
J. Biol. Chem. 278:14442-14450(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT RP4 HIS-23, FUNCTION, SUBCELLULAR LOCATION. - Ref.39"A dual role for EDEM1 in the processing of rod opsin."
Kosmaoglou M., Kanuga N., Aguila M., Garriga P., Cheetham M.E.
J. Cell Sci. 122:4465-4472(2009) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT RP4 HIS-23, SUBCELLULAR LOCATION. - Ref.40"A homozygous p.Glu150Lys mutation in the opsin gene of two Pakistani families with autosomal recessive retinitis pigmentosa."
Azam M., Khan M.I., Gal A., Hussain A., Shah S.T., Khan M.S., Sadeque A., Bokhari H., Collin R.W., Orth U., van Genderen M.M., den Hollander A.I., Cremers F.P., Qamar R.
Mol. Vis. 15:2526-2534(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT RP4 LYS-150. - Ref.41"Next-generation genetic testing for retinitis pigmentosa."
Neveling K., Collin R.W., Gilissen C., van Huet R.A., Visser L., Kwint M.P., Gijsen S.J., Zonneveld M.N., Wieskamp N., de Ligt J., Siemiatkowska A.M., Hoefsloot L.H., Buckley M.F., Kellner U., Branham K.E., den Hollander A.I., Hoischen A., Hoyng C. , Klevering B.J., van den Born L.I., Veltman J.A., Cremers F.P., Scheffer H.
Hum. Mutat. 33:963-972(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS RP4 TRP-135; SER-180 AND ASN-214.
Farrar G.J., Kenna P., Redmond R., McWilliam P., Bradley D.G., Humphries M.M., Sharp E.M., Inglehearn C.F., Bashir R., Jay M., Watty A., Ludwig M., Schinzel A., Samanns C., Gal A., Bhattacharya S.S., Humphries P.
Am. J. Hum. Genet. 47:941-945(1990) [PubMed] [Europe PMC] [Abstract]
Dryja T.P., McGee T.L., Reichei E., Hahn L.B., Cowley G.S., Yandell D.W., Sandberg M.A., Berson E.L.
Nature 343:364-366(1990) [PubMed] [Europe PMC] [Abstract]
Dryja T.P., McGee T.L., Hahn L.B., Cowley G.S., Olsson J.E., Reichel E., Sandberg M.A., Berson E.L.
N. Engl. J. Med. 323:1302-1307(1990) [PubMed] [Europe PMC] [Abstract]
Inglehearn C.F., Bashir R., Lester D.H., Jay M., Bird A.C., Bhattacharya S.S.
Am. J. Hum. Genet. 48:26-30(1991) [PubMed] [Europe PMC] [Abstract]
Sheffield V.C., Fishman G.A., Beck J.S., Kimura A.E., Stone E.M.
Am. J. Hum. Genet. 49:699-706(1991) [PubMed] [Europe PMC] [Abstract]
Gal A., Artlich A., Ludwig M., Niemeyer G., Olek K., Schwinger E., Schinzel A.
Genomics 11:468-470(1991) [PubMed] [Europe PMC] [Abstract]
Sung C.H., Davenport C.M., Hennessey J.C., Maumenee I.H., Jacobson S.G., Heckenlively J.R., Nowakowski R., Fishman G., Gouras P., Nathans J.
Proc. Natl. Acad. Sci. U.S.A. 88:6481-6485(1991) [PubMed] [Europe PMC] [Abstract]
Dryja T.P., Hahn L.B., Cowley G.S., McGee T.L., Berson E.L.
Proc. Natl. Acad. Sci. U.S.A. 88:9370-9374(1991) [PubMed] [Europe PMC] [Abstract]
Farrar G.J., Findlay J.B.C., Kumar-Singh R., Kenna P., Humphries M.M., Sharpe E., Humphries P.
Hum. Mol. Genet. 1:769-771(1992) [PubMed] [Europe PMC] [Abstract]
Fujiki K., Hotta Y., Hayakawa M., Sakuma H., Shiono T., Noro M., Sakuma T., Tamai M., Hikiji K., Kawaguchi R., Hoshi A., Nakajima A., Kanai A.
Jpn. J. Hum. Genet. 37:125-132(1992) [PubMed] [Europe PMC] [Abstract]
Macke J.P., Davenport C.M., Jacobson S.G., Hennessey J.C., Gonzalez-Fernandez F., Conway B.P., Heckenlively J., Palmer R., Maumenee I.H., Sieving P., Gouras P., Good W., Nathans J.
Am. J. Hum. Genet. 53:80-89(1993) [PubMed] [Europe PMC] [Abstract]
Kranich H., Bartkowski S., Denton M.J., Krey S., Dickinson P., Duvigneau C., Gal A.
Hum. Mol. Genet. 2:813-814(1993) [PubMed] [Europe PMC] [Abstract]
Vaithinathan R., Berson E.L., Dryja T.P.
Genomics 21:461-463(1994) [PubMed] [Europe PMC] [Abstract]
Reig C., Antich J., Gean E., Garcia-Sandoval B., Ramos C., Ayuso C., Carballo M.
Hum. Genet. 94:283-286(1994) [PubMed] [Europe PMC] [Abstract]
Fuchs S., Kranich H., Denton M.J., Zrenner E., Bhattacharya S.S., Humphries P., Gal A.
Hum. Mol. Genet. 3:1203-1203(1994) [PubMed] [Europe PMC] [Abstract]
Antinolo G., Sanchez B., Borrego S., Rueda T., Chaparro P., Cabeza J.C.
Hum. Mol. Genet. 3:1421-1421(1994) [PubMed] [Europe PMC] [Abstract]
Souied E., Gerber S., Rozet J.-M., Bonneau D., Dufier J.-L., Ghazi I., Philip N., Soubrane G., Coscas G., Munnich A.
Hum. Mol. Genet. 3:1433-1434(1994) [PubMed] [Europe PMC] [Abstract]
Al-Maghtheh M., Inglehearn C., Lunt P., Jay M., Bird A., Bhattacharya S.
Hum. Mutat. 3:409-410(1994) [PubMed] [Europe PMC] [Abstract]
Rosas D.J., Roman A.J., Weissbrod P., Macke J.P., Nathans J.
Invest. Ophthalmol. Vis. Sci. 35:3134-3144(1994) [PubMed] [Europe PMC] [Abstract]
Macke J.P., Hennessey J.C., Nathans J.
Hum. Mol. Genet. 4:775-776(1995) [PubMed] [Europe PMC] [Abstract]
Souied E., Soubrane G., Benlian P., Coscas G.J., Gerber S., Munnich A., Kaplan J.
Am. J. Ophthalmol. 121:19-25(1996) [PubMed] [Europe PMC] [Abstract]
Goliath R., Bardien S., September A., Martin R., Ramesar R., Greenberg J.
Hum. Mutat. Suppl. 1:S40-S41(1998) [PubMed] [Europe PMC] [Abstract]
Noorwez S.M., Kuksa V., Imanishi Y., Zhu L., Filipek S., Palczewski K., Kaushal S.
J. Biol. Chem. 278:14442-14450(2003) [PubMed] [Europe PMC] [Abstract]
Kosmaoglou M., Kanuga N., Aguila M., Garriga P., Cheetham M.E.
J. Cell Sci. 122:4465-4472(2009) [PubMed] [Europe PMC] [Abstract]
Azam M., Khan M.I., Gal A., Hussain A., Shah S.T., Khan M.S., Sadeque A., Bokhari H., Collin R.W., Orth U., van Genderen M.M., den Hollander A.I., Cremers F.P., Qamar R.
Mol. Vis. 15:2526-2534(2009) [PubMed] [Europe PMC] [Abstract]
Neveling K., Collin R.W., Gilissen C., van Huet R.A., Visser L., Kwint M.P., Gijsen S.J., Zonneveld M.N., Wieskamp N., de Ligt J., Siemiatkowska A.M., Hoefsloot L.H., Buckley M.F., Kellner U., Branham K.E., den Hollander A.I., Hoischen A., Hoyng C. , Klevering B.J., van den Born L.I., Veltman J.A., Cremers F.P., Scheffer H.
Hum. Mutat. 33:963-972(2012) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004765 | 4 | T → K in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004766 | 15 | N → S in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004767 | 17 | T → M in RP4. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004768 | 23 | P → H in RP4; most common variant; impairs protein folding; leads to interaction with EDEM1 followed by degradation by the ERAD system. 5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004769 | 23 | P → L in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004770 | 28 | Q → H in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004771 | 40 | L → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004772 | 44 | M → T in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004773 | 45 | F → L in RP4. Corresponds to variant dbSNP:rs104893770EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004774 | 46 | L → R in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004776 | 51 | G → R in RP4. Corresponds to variant dbSNP:rs104893792EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004777 | 51 | G → V in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004778 | 53 | P → R in RP4. Corresponds to variant dbSNP:rs28933395EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004779 | 58 | T → R in RP4. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004780 | 68 – 71 | Missing in RP4. | 4 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004781 | 87 | V → D in RP4. Corresponds to variant dbSNP:rs104893771EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004782 | 89 | G → D in RP4. Corresponds to variant dbSNP:rs104893772EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004786 | 106 | G → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004787 | 106 | G → W in RP4. Corresponds to variant dbSNP:rs104893773EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004788 | 109 | G → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004789 | 110 | C → F in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004790 | 110 | C → Y in RP4. Corresponds to variant dbSNP:rs104893787EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004791 | 114 | G → D in RP4. Corresponds to variant dbSNP:rs104893788EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004792 | 125 | L → R in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004793 | 127 | S → F in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004794 | 131 | L → P in RP4. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004795 | 135 | R → G in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004796 | 135 | R → L in RP4. Corresponds to variant dbSNP:rs104893774EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004797 | 135 | R → W in RP4. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004798 | 140 | C → S in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004799 | 150 | E → K in RP4; autosomal recessive. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004800 | 164 | A → E in RP4. Corresponds to variant dbSNP:rs104893793EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004801 | 164 | A → V in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004802 | 167 | C → R in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004803 | 171 | P → L in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004804 | 171 | P → Q in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004805 | 171 | P → S in RP4. Corresponds to variant dbSNP:rs104893794EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004806 | 178 | Y → C in RP4. Corresponds to variant dbSNP:rs104893776EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004807 | 178 | Y → N in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_068359 | 180 | P → S in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004808 | 181 | E → K in RP4. Corresponds to variant dbSNP:rs775557680EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004809 | 182 | G → S in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004810 | 186 | S → P in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004811 | 188 | G → E in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004812 | 188 | G → R in RP4. Corresponds to variant dbSNP:rs527236100EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004814 | 190 | D → G in RP4. Corresponds to variant dbSNP:rs104893777EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004813 | 190 | D → N in RP4. Corresponds to variant dbSNP:rs104893779EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004815 | 190 | D → Y in RP4. Corresponds to variant dbSNP:rs104893779EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004816 | 207 | M → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004818 | 211 | H → P in RP4. Corresponds to variant dbSNP:rs28933993EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004819 | 211 | H → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_068360 | 214 | I → N in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004820 | 216 | M → K in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004821 | 220 | F → C in RP4. Corresponds to variant dbSNP:rs766161322Ensembl. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004822 | 222 | C → R in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004823 | 255 | Missing in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004824 | 264 | Missing in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004825 | 267 | P → L in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004826 | 267 | P → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004828 | 296 | K → E in RP4. Corresponds to variant dbSNP:rs29001653EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004829 | 297 | S → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004830 | 342 | T → M in RP4. Corresponds to variant dbSNP:rs183318466Ensembl. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004831 | 345 | V → L in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004832 | 345 | V → M in RP4. Corresponds to variant dbSNP:rs104893795EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004833 | 347 | P → A in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004834 | 347 | P → L in RP4; common variant. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004835 | 347 | P → Q in RP4. Corresponds to variant dbSNP:rs29001566EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004836 | 347 | P → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004837 | 347 | P → S in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Night blindness, congenital stationary, autosomal dominant 1 (CSNBAD1)4 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.23"Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness."
Dryja T.P., Berson E.L., Rao V.R., Oprian D.D.
Nat. Genet. 4:280-283(1993) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT CSNBAD1 GLU-292. - Ref.31"Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness."
Rao V.R., Cohen G.B., Oprian D.D.
Nature 367:639-642(1994) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT CSNBAD1 ASP-90, FUNCTION. - Ref.34"Dark-light: model for nightblindness from the human rhodopsin Gly-90-->Asp mutation."
Sieving P.A., Richards J.E., Naarendorp F., Bingham E.L., Scott K., Alpern M.
Proc. Natl. Acad. Sci. U.S.A. 92:880-884(1995) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT CSNBAD1 ASP-90, FUNCTION. - Ref.37"A novel mutation within the rhodopsin gene (Thr-94-Ile) causing autosomal dominant congenital stationary night blindness."
Al-Jandal N., Farrar G.J., Kiang A.-S., Humphries M.M., Bannon N., Findlay J.B.C., Humphries P., Kenna P.F.
Hum. Mutat. 13:75-81(1999) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT CSNBAD1 ILE-94.
Dryja T.P., Berson E.L., Rao V.R., Oprian D.D.
Nat. Genet. 4:280-283(1993) [PubMed] [Europe PMC] [Abstract]
Rao V.R., Cohen G.B., Oprian D.D.
Nature 367:639-642(1994) [PubMed] [Europe PMC] [Abstract]
Sieving P.A., Richards J.E., Naarendorp F., Bingham E.L., Scott K., Alpern M.
Proc. Natl. Acad. Sci. U.S.A. 92:880-884(1995) [PubMed] [Europe PMC] [Abstract]
Al-Jandal N., Farrar G.J., Kiang A.-S., Humphries M.M., Bannon N., Findlay J.B.C., Humphries P., Kenna P.F.
Hum. Mutat. 13:75-81(1999) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004783 | 90 | G → D in CSNBAD1; constitutive activity in the absence of bound retinal. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004784 | 94 | T → I in CSNBAD1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004827 | 292 | A → E in CSNBAD1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 113 | E → Q: Induces a conformation change that promotes interaction with GRK1 and SAG; when associated with Y-257. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 257 | M → Y: Induces a conformation change that promotes interaction with GRK1 and SAG; when associated with Q-113. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 336 – 340 | TVSKT → AVAKA: Loss of phosphorylation sites and decreased interaction with SAG. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 5 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 336 – 338 | TVS → AVA: Loss of phosphorylation sites and decreased interaction with SAG; when associated with A-343. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 343 | S → A: Loss of phosphorylation sites and decreased interaction with SAG; when associated with 336-A--A-338. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Congenital stationary night blindness, Disease mutation, Retinitis pigmentosaOrganism-specific databases
DisGeNET More...DisGeNETi | 6010 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | RHO |
MalaCards human disease database More...MalaCardsi | RHO |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 610445 phenotype 613731 phenotype |
Open Targets More...OpenTargetsi | ENSG00000163914 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 215 Congenital stationary night blindness 791 Retinitis pigmentosa 52427 Retinitis punctata albescens |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA34390 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB04233 (Hydroxyethyloxy)Tri(Ethyloxy)Octane DB03152 B-2-Octylglucoside DB01159 Halothane DB04450 Heptyl 1-Thiohexopyranoside DB03381 Hexadecanal DB04147 Lauryl Dimethylamine-N-Oxide DB01646 N-Acetylmethionine DB03796 Palmitic Acid DB04522 Phosphonoserine DB02482 Phosphonothreonine |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | RHO |
Domain mapping of disease mutations (DMDM) More...DMDMi | 129207 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000197677 | 1 – 348 | RhodopsinAdd BLAST | 348 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 1 | N-acetylmethionineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 2 | N-linked (GlcNAc...) asparagineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 15 | N-linked (GlcNAc...) asparagine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 110 ↔ 187 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 296 | N6-(retinylidene)lysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 322 | S-palmitoyl cysteineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 323 | S-palmitoyl cysteineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 334 | Phosphoserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 336 | Phosphothreonine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 338 | Phosphoserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 340 | PhosphothreonineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 342 | PhosphothreonineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 343 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"Molecular assembly of rhodopsin with G protein-coupled receptor kinases."
He Y., Gao X., Goswami D., Hou L., Pal K., Yin Y., Zhao G., Ernst O.P., Griffin P., Melcher K., Xu H.E.
Cell Res. 27:728-747(2017) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GRK1 AND SAG, FUNCTION, MUTAGENESIS OF GLU-113 AND MET-257.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.38"Pharmacological chaperone-mediated in vivo folding and stabilization of the P23H-opsin mutant associated with autosomal dominant retinitis pigmentosa."
Noorwez S.M., Kuksa V., Imanishi Y., Zhu L., Filipek S., Palczewski K., Kaushal S.
J. Biol. Chem. 278:14442-14450(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT RP4 HIS-23, FUNCTION, SUBCELLULAR LOCATION.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, PhosphoproteinProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P08100 |
PeptideAtlas More...PeptideAtlasi | P08100 |
PRoteomics IDEntifications database More...PRIDEi | P08100 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 52066 |
PTM databases
GlyConnect protein glycosylation platform More...GlyConnecti | 525 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P08100 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P08100 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P08100 |
UniCarbKB; an annotated and curated database of glycan structures More...UniCarbKBi | P08100 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000163914 |
CleanEx database of gene expression profiles More...CleanExi | HS_RHO |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P08100 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB022486 CAB034887 CAB034888 HPA013440 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
3 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"Molecular assembly of rhodopsin with G protein-coupled receptor kinases."
He Y., Gao X., Goswami D., Hou L., Pal K., Yin Y., Zhao G., Ernst O.P., Griffin P., Melcher K., Xu H.E.
Cell Res. 27:728-747(2017) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GRK1 AND SAG, FUNCTION, MUTAGENESIS OF GLU-113 AND MET-257. - Ref.8"Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser."
Kang Y., Zhou X.E., Gao X., He Y., Liu W., Ishchenko A., Barty A., White T.A., Yefanov O., Han G.W., Xu Q., de Waal P.W., Ke J., Tan M.H., Zhang C., Moeller A., West G.M., Pascal B.D. , Van Eps N., Caro L.N., Vishnivetskiy S.A., Lee R.J., Suino-Powell K.M., Gu X., Pal K., Ma J., Zhi X., Boutet S., Williams G.J., Messerschmidt M., Gati C., Zatsepin N.A., Wang D., James D., Basu S., Roy-Chowdhury S., Conrad C.E., Coe J., Liu H., Lisova S., Kupitz C., Grotjohann I., Fromme R., Jiang Y., Tan M., Yang H., Li J., Wang M., Zheng Z., Li D., Howe N., Zhao Y., Standfuss J., Diederichs K., Dong Y., Potter C.S., Carragher B., Caffrey M., Jiang H., Chapman H.N., Spence J.C., Fromme P., Weierstall U., Ernst O.P., Katritch V., Gurevich V.V., Griffin P.R., Hubbell W.L., Stevens R.C., Cherezov V., Melcher K., Xu H.E.
Nature 523:561-567(2015) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF MUTANT GLN-113 AND TYR-257 IN COMPLEX WITH SAG, INTERACTION WITH SAG AND GNAT1, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-113 AND MET-257, TOPOLOGY, DISULFIDE BONDS. - Ref.9"Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors."
Zhou X.E., He Y., de Waal P.W., Gao X., Kang Y., Van Eps N., Yin Y., Pal K., Goswami D., White T.A., Barty A., Latorraca N.R., Chapman H.N., Hubbell W.L., Dror R.O., Stevens R.C., Cherezov V., Gurevich V.V. , Griffin P.R., Ernst O.P., Melcher K., Xu H.E.
Cell 170:457-469(2017) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH SAG, FUNCTION, TOPOLOGY, GLYCOSYLATION AT ASN-15, PHOSPHORYLATION AT SER-334; THR-336 AND SER-338, DISULFIDE BOND, MUTAGENESIS OF 336-THR--THR-340; 336-THR--SER-338 AND SER-343.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ZFYVE9 | O95405 | 2 | EBI-1394177,EBI-296817 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 111942, 11 interactors |
Protein interaction database and analysis system More...IntActi | P08100, 4 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000296271 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 2 – 5 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 10 – 13 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 16 – 18 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 23 – 25 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 29 – 31 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 35 – 64 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 30 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 66 – 68 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 71 – 73 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 74 – 88 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 90 – 100 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 106 – 140 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 35 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 143 – 147 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 150 – 168 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 170 – 173 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 174 – 176 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 178 – 181 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 182 – 185 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 186 – 189 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 191 – 193 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 196 – 199 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 200 – 209 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 210 – 212 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 213 – 236 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 24 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 241 – 277 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 37 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 285 – 306 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 22 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 307 – 309 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 311 – 321 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 322 – 324 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 331 – 333 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 339 – 341 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P08100 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P08100 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 330 – 348 | Interaction with SAG2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 19 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 134 – 136 | 'Ionic lock' involved in activated form stabilization1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 3 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3656 Eukaryota ENOG410XRW9 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118977 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000253932 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG107442 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P08100 |
KEGG Orthology (KO) More...KOi | K04250 |
Identification of Orthologs from Complete Genome Data More...OMAi | LAAYMFM |
Database of Orthologous Groups More...OrthoDBi | EOG091G0BDA |
Database for complete collections of gene phylogenies More...PhylomeDBi | P08100 |
TreeFam database of animal gene trees More...TreeFami | TF324998 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000276 GPCR_Rhodpsn IPR017452 GPCR_Rhodpsn_7TM IPR001760 Opsin IPR027430 Retinal_BS IPR000732 Rhodopsin IPR019477 Rhodopsin_N |
Pfam protein domain database More...Pfami | View protein in Pfam PF00001 7tm_1, 1 hit PF10413 Rhodopsin_N, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00237 GPCRRHODOPSN PR00238 OPSIN PR00579 RHODOPSIN |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01381 7TM_GPCR_Srsx, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00237 G_PROTEIN_RECEP_F1_1, 1 hit PS50262 G_PROTEIN_RECEP_F1_2, 1 hit PS00238 OPSIN, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
10 20 30 40 50
MNGTEGPNFY VPFSNATGVV RSPFEYPQYY LAEPWQFSML AAYMFLLIVL
60 70 80 90 100
GFPINFLTLY VTVQHKKLRT PLNYILLNLA VADLFMVLGG FTSTLYTSLH
110 120 130 140 150
GYFVFGPTGC NLEGFFATLG GEIALWSLVV LAIERYVVVC KPMSNFRFGE
160 170 180 190 200
NHAIMGVAFT WVMALACAAP PLAGWSRYIP EGLQCSCGID YYTLKPEVNN
210 220 230 240 250
ESFVIYMFVV HFTIPMIIIF FCYGQLVFTV KEAAAQQQES ATTQKAEKEV
260 270 280 290 300
TRMVIIMVIA FLICWVPYAS VAFYIFTHQG SNFGPIFMTI PAFFAKSAAI
310 320 330 340
YNPVIYIMMN KQFRNCMLTT ICCGKNPLGD DEASATVSKT ETSQVAPA
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004765 | 4 | T → K in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004766 | 15 | N → S in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004767 | 17 | T → M in RP4. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004768 | 23 | P → H in RP4; most common variant; impairs protein folding; leads to interaction with EDEM1 followed by degradation by the ERAD system. 5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004769 | 23 | P → L in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004770 | 28 | Q → H in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004771 | 40 | L → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004772 | 44 | M → T in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004773 | 45 | F → L in RP4. Corresponds to variant dbSNP:rs104893770EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004774 | 46 | L → R in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004775 | 51 | G → A1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004776 | 51 | G → R in RP4. Corresponds to variant dbSNP:rs104893792EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004777 | 51 | G → V in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004778 | 53 | P → R in RP4. Corresponds to variant dbSNP:rs28933395EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004779 | 58 | T → R in RP4. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004780 | 68 – 71 | Missing in RP4. | 4 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004781 | 87 | V → D in RP4. Corresponds to variant dbSNP:rs104893771EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004782 | 89 | G → D in RP4. Corresponds to variant dbSNP:rs104893772EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004783 | 90 | G → D in CSNBAD1; constitutive activity in the absence of bound retinal. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004784 | 94 | T → I in CSNBAD1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004785 | 104 | V → I Found in patients with pathologic myopia; unknown pathological significance. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004786 | 106 | G → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004787 | 106 | G → W in RP4. Corresponds to variant dbSNP:rs104893773EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004788 | 109 | G → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004789 | 110 | C → F in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004790 | 110 | C → Y in RP4. Corresponds to variant dbSNP:rs104893787EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004791 | 114 | G → D in RP4. Corresponds to variant dbSNP:rs104893788EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004792 | 125 | L → R in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004793 | 127 | S → F in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004794 | 131 | L → P in RP4. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004795 | 135 | R → G in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004796 | 135 | R → L in RP4. Corresponds to variant dbSNP:rs104893774EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004797 | 135 | R → W in RP4. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004798 | 140 | C → S in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004799 | 150 | E → K in RP4; autosomal recessive. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004800 | 164 | A → E in RP4. Corresponds to variant dbSNP:rs104893793EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004801 | 164 | A → V in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004802 | 167 | C → R in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004803 | 171 | P → L in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004804 | 171 | P → Q in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004805 | 171 | P → S in RP4. Corresponds to variant dbSNP:rs104893794EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004806 | 178 | Y → C in RP4. Corresponds to variant dbSNP:rs104893776EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004807 | 178 | Y → N in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_068359 | 180 | P → S in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004808 | 181 | E → K in RP4. Corresponds to variant dbSNP:rs775557680EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004809 | 182 | G → S in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004810 | 186 | S → P in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004811 | 188 | G → E in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004812 | 188 | G → R in RP4. Corresponds to variant dbSNP:rs527236100EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004814 | 190 | D → G in RP4. Corresponds to variant dbSNP:rs104893777EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004813 | 190 | D → N in RP4. Corresponds to variant dbSNP:rs104893779EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004815 | 190 | D → Y in RP4. Corresponds to variant dbSNP:rs104893779EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004816 | 207 | M → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004817 | 209 | V → M Found in a patient with retinitis pigmentosa; unknown pathological significance. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004818 | 211 | H → P in RP4. Corresponds to variant dbSNP:rs28933993EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004819 | 211 | H → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_068360 | 214 | I → N in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004820 | 216 | M → K in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004821 | 220 | F → C in RP4. Corresponds to variant dbSNP:rs766161322Ensembl. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004822 | 222 | C → R in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004823 | 255 | Missing in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004824 | 264 | Missing in RP4. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004825 | 267 | P → L in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004826 | 267 | P → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004827 | 292 | A → E in CSNBAD1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004828 | 296 | K → E in RP4. Corresponds to variant dbSNP:rs29001653EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004829 | 297 | S → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004830 | 342 | T → M in RP4. Corresponds to variant dbSNP:rs183318466Ensembl. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004831 | 345 | V → L in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004832 | 345 | V → M in RP4. Corresponds to variant dbSNP:rs104893795EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004833 | 347 | P → A in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004834 | 347 | P → L in RP4; common variant. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004835 | 347 | P → Q in RP4. Corresponds to variant dbSNP:rs29001566EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004836 | 347 | P → R in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004837 | 347 | P → S in RP4. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | U49742 Genomic DNA Translation: AAC31763.1 AB065668 Genomic DNA Translation: BAC05894.1 BX537381 mRNA Translation: CAD97623.1 BC112104 mRNA Translation: AAI12105.1 BC112106 mRNA Translation: AAI12107.1 U16824 Genomic DNA Translation: AAA97436.1 S81166 Genomic DNA Translation: AAB35906.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS3063.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A41200 OOHU |
NCBI Reference Sequences More...RefSeqi | NP_000530.1, NM_000539.3 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.247565 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000296271; ENSP00000296271; ENSG00000163914 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6010 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6010 |
UCSC genome browser More...UCSCi | uc003emt.4 human |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P08100 | Rhodopsin | 348 | |||
| Rhodopsin | 348 | ||||
| Rhodopsin | 348 | ||||
| Rhodopsin | 348 | ||||
| Rhodopsin | 348 |
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Mutations of the RHO gene Retina International's Scientific Newsletter |
| Wikipedia Rhodopsin entry |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | U49742 Genomic DNA Translation: AAC31763.1 AB065668 Genomic DNA Translation: BAC05894.1 BX537381 mRNA Translation: CAD97623.1 BC112104 mRNA Translation: AAI12105.1 BC112106 mRNA Translation: AAI12107.1 U16824 Genomic DNA Translation: AAA97436.1 S81166 Genomic DNA Translation: AAB35906.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS3063.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A41200 OOHU |
NCBI Reference Sequences More...RefSeqi | NP_000530.1, NM_000539.3 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.247565 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 4ZWJ | X-ray | 3.30 | A/B/C/D | 1-348 | [»] | |
| 5DGY | X-ray | 7.70 | A/B/C/D | 1-348 | [»] | |
| 5W0P | X-ray | 3.01 | A/B/C/D | 1-348 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P08100 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P08100 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 111942, 11 interactors |
Protein interaction database and analysis system More...IntActi | P08100, 4 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000296271 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB04233 (Hydroxyethyloxy)Tri(Ethyloxy)Octane |