UniProtKB - Q9H4L5 (OSBL3_HUMAN)
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- BLAST>sp|Q9H4L5|OSBL3_HUMAN Oxysterol-binding protein-related protein 3 OS=Homo sapiens OX=9606 GN=OSBPL3 PE=1 SV=1 MMSDEKNLGVSQKLVSPSRSTSSCSSKQGSRQDSWEVVEGLRGEMNYTQEPPVQKGFLLK KRKWPLKGWHKRFFYLDKGILKYAKSQTDIEREKLHGCIDVGLSVMSVKKSSKCIDLDTE EHIYHLKVKSEEVFDEWVSKLRHHRMYRQNEIAMFPHEVNHFFSGSTITDSSSGVFDSIS SRKRSSISKQNLFQTGSNVSFSCGGETRVPLWLQSSEDMEKCSKDLAHCHAYLVEMSQLL QSMDVLHRTYSAPAINAIQGGSFESPKKEKRSHRRWRSRAIGKDAKGTLQVPKPFSGPVR LHSSNPNLSTLDFGEEKNYSDGSETSSEFSKMQEDLCHIAHKVYFTLRSAFNIMSAEREK LKQLMEQDASSSPSAQVIGLKNALSSALAQNTDLKERLRRIHAESLLLDSPAVAKSGDNL AEENSRDENRALVHQLSNESRLSITDSLSEFFDAQEVLLSPSSSENEISDDDSYVSDISD NLSLDNLSNDLDNERQTLGPVLDSGREAKSRRRTCLPAPCPSSSNISLWNILRNNIGKDL SKVAMPVELNEPLNTLQRLCEELEYSELLDKAAQIPSPLERMVYVAAFAISAYASSYYRA GSKPFNPVLGETYECIREDKGFQFFSEQVSHHPPISACHAESRNFVFWQDVRWKNKFWGK SMEIVPIGTTHVTLPVFGDHFEWNKVTSCIHNILSGQRWIEHYGEIVIKNLHDDSCYCKV NFIKAKYWSTNAHEIEGTVFDRSGKAVHRLFGKWHESIYCGGGSSSACVWRANPMPKGYE QYYSFTQFALELNEMDPSSKSLLPPTDTRFRPDQRFLEEGNLEEAEIQKQRIEQLQRERR RVLEENHVEHQPRFFRKSDDDSWVSNGTYLELRKDLGFSKLDHPVLW
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Protein
Oxysterol-binding protein-related protein 3
Gene
OSBPL3
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
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
Phosphoinositide-binding protein which associates with both cell and endoplasmic reticulum (ER) membranes (PubMed:16143324). Can bind to the ER membrane protein VAPA and recruit VAPA to plasma membrane sites, thus linking these intracellular compartments (PubMed:25447204). The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface (PubMed:18270267, PubMed:25447204). With VAPA, may regulate ER morphology (PubMed:16143324). Has a role in regulation of the actin cytoskeleton, cell polarity and cell adhesion (PubMed:18270267). Binds to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3 (PubMed:16143324). Also binds 25-hydroxycholesterol and cholesterol (PubMed:17428193).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.12"Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants."
Lehto M., Hynynen R., Karjalainen K., Kuismanen E., Hyvaerinen K., Olkkonen V.M.
Exp. Cell Res. 310:445-462(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, PH DOMAIN, FFAT MOTIF, MUTAGENESIS OF LYS-60; LYS-61; LYS-71; ARG-72; GLY-97 AND 451-PHE--ASP-453. - Ref.13"The mammalian oxysterol-binding protein-related proteins (ORPs) bind 25-hydroxycholesterol in an evolutionarily conserved pocket."
Suchanek M., Hynynen R., Wohlfahrt G., Lehto M., Johansson M., Saarinen H., Radzikowska A., Thiele C., Olkkonen V.M.
Biochem. J. 405:473-480(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.14"The R-Ras interaction partner ORP3 regulates cell adhesion."
Lehto M., Maeyraenpaeae M.I., Pellinen T., Ihalmo P., Lehtonen S., Kovanen P.T., Groop P.H., Ivaska J., Olkkonen V.M.
J. Cell Sci. 121:695-705(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RRAS, DOMAIN PH, AND PHOSPHORYLATION. - Ref.25"OSBP-related protein 3 (ORP3) coupling with VAMP-associated protein A regulates R-Ras activity."
Weber-Boyvat M., Kentala H., Lilja J., Vihervaara T., Hanninen R., Zhou Y., Peranen J., Nyman T.A., Ivaska J., Olkkonen V.M.
Exp. Cell Res. 331:278-291(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, DOMAIN FFAT MOTIF, PHOSPHORYLATION AT SER-251; SER-265; SER-304; SER-320; SER-323; SER-371; SER-372; SER-410 AND SER-437, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 162-PHE--THR-167 AND 451-PHE--ASP-453.
<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
- cholesterol binding Source: BHF-UCL <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
- sterol transporter activity Source: Reactome
<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
- bile acid biosynthetic process Source: Reactome
<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
| Biological process | Lipid transport, Transport |
| Ligand | Lipid-binding |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-192105 Synthesis of bile acids and bile salts |
<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: Oxysterol-binding protein-related protein 3Short name: ORP-3 Short name: OSBP-related protein 3 |
| <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:OSBPL3 Synonyms:KIAA0704, ORP3, OSBP3 |
| <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:ENSG00000070882.12 |
Human Gene Nomenclature Database More...HGNCi | HGNC:16370 OSBPL3 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 606732 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9H4L5 |
<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
Plasma membrane
- Cell membrane 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.11"Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues: the expression and intracellular localization of ORP3, ORP6, and ORP7."
Lehto M., Tienari J., Lehtonen S., Lehtonen E., Olkkonen V.M.
Cell Tissue Res. 315:39-57(2004) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. - Ref.12"Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants."
Lehto M., Hynynen R., Karjalainen K., Kuismanen E., Hyvaerinen K., Olkkonen V.M.
Exp. Cell Res. 310:445-462(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, PH DOMAIN, FFAT MOTIF, MUTAGENESIS OF LYS-60; LYS-61; LYS-71; ARG-72; GLY-97 AND 451-PHE--ASP-453. - Ref.14"The R-Ras interaction partner ORP3 regulates cell adhesion."
Lehto M., Maeyraenpaeae M.I., Pellinen T., Ihalmo P., Lehtonen S., Kovanen P.T., Groop P.H., Ivaska J., Olkkonen V.M.
J. Cell Sci. 121:695-705(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RRAS, DOMAIN PH, AND PHOSPHORYLATION. - Ref.25"OSBP-related protein 3 (ORP3) coupling with VAMP-associated protein A regulates R-Ras activity."
Weber-Boyvat M., Kentala H., Lilja J., Vihervaara T., Hanninen R., Zhou Y., Peranen J., Nyman T.A., Ivaska J., Olkkonen V.M.
Exp. Cell Res. 331:278-291(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, DOMAIN FFAT MOTIF, PHOSPHORYLATION AT SER-251; SER-265; SER-304; SER-320; SER-323; SER-371; SER-372; SER-410 AND SER-437, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 162-PHE--THR-167 AND 451-PHE--ASP-453.
<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"Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues: the expression and intracellular localization of ORP3, ORP6, and ORP7."
Lehto M., Tienari J., Lehtonen S., Lehtonen E., Olkkonen V.M.
Cell Tissue Res. 315:39-57(2004) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. - Ref.12"Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants."
Lehto M., Hynynen R., Karjalainen K., Kuismanen E., Hyvaerinen K., Olkkonen V.M.
Exp. Cell Res. 310:445-462(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, PH DOMAIN, FFAT MOTIF, MUTAGENESIS OF LYS-60; LYS-61; LYS-71; ARG-72; GLY-97 AND 451-PHE--ASP-453. - Ref.14"The R-Ras interaction partner ORP3 regulates cell adhesion."
Lehto M., Maeyraenpaeae M.I., Pellinen T., Ihalmo P., Lehtonen S., Kovanen P.T., Groop P.H., Ivaska J., Olkkonen V.M.
J. Cell Sci. 121:695-705(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RRAS, DOMAIN PH, AND PHOSPHORYLATION. - Ref.25"OSBP-related protein 3 (ORP3) coupling with VAMP-associated protein A regulates R-Ras activity."
Weber-Boyvat M., Kentala H., Lilja J., Vihervaara T., Hanninen R., Zhou Y., Peranen J., Nyman T.A., Ivaska J., Olkkonen V.M.
Exp. Cell Res. 331:278-291(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, DOMAIN FFAT MOTIF, PHOSPHORYLATION AT SER-251; SER-265; SER-304; SER-320; SER-323; SER-371; SER-372; SER-410 AND SER-437, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 162-PHE--THR-167 AND 451-PHE--ASP-453.
- Cell membrane 4 Publications
Nucleus
- Nucleus membrane 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.12"Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants."
Lehto M., Hynynen R., Karjalainen K., Kuismanen E., Hyvaerinen K., Olkkonen V.M.
Exp. Cell Res. 310:445-462(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, PH DOMAIN, FFAT MOTIF, MUTAGENESIS OF LYS-60; LYS-61; LYS-71; ARG-72; GLY-97 AND 451-PHE--ASP-453.
- Nucleus membrane 1 Publication
Endoplasmic reticulum
- Endoplasmic reticulum membrane 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.12"Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants."
Lehto M., Hynynen R., Karjalainen K., Kuismanen E., Hyvaerinen K., Olkkonen V.M.
Exp. Cell Res. 310:445-462(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, PH DOMAIN, FFAT MOTIF, MUTAGENESIS OF LYS-60; LYS-61; LYS-71; ARG-72; GLY-97 AND 451-PHE--ASP-453.
<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.12"Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants."
Lehto M., Hynynen R., Karjalainen K., Kuismanen E., Hyvaerinen K., Olkkonen V.M.
Exp. Cell Res. 310:445-462(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, PH DOMAIN, FFAT MOTIF, MUTAGENESIS OF LYS-60; LYS-61; LYS-71; ARG-72; GLY-97 AND 451-PHE--ASP-453.
- Endoplasmic reticulum membrane 1 Publication
Cytosol
- cytosol 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.12"Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants."
Lehto M., Hynynen R., Karjalainen K., Kuismanen E., Hyvaerinen K., Olkkonen V.M.
Exp. Cell Res. 310:445-462(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, PH DOMAIN, FFAT MOTIF, MUTAGENESIS OF LYS-60; LYS-61; LYS-71; ARG-72; GLY-97 AND 451-PHE--ASP-453.
- cytosol 1 Publication
Other locations
- filopodium tip 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.14"The R-Ras interaction partner ORP3 regulates cell adhesion."
Lehto M., Maeyraenpaeae M.I., Pellinen T., Ihalmo P., Lehtonen S., Kovanen P.T., Groop P.H., Ivaska J., Olkkonen V.M.
J. Cell Sci. 121:695-705(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RRAS, DOMAIN PH, AND PHOSPHORYLATION.
- filopodium tip 1 Publication
Cytosol
- cytosol Source: BHF-UCL <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
Endoplasmic reticulum
- endoplasmic reticulum membrane Source: UniProtKB-SubCell
- perinuclear endoplasmic reticulum Source: BHF-UCL <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
Nucleus
- nuclear membrane Source: BHF-UCL <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
- plasma membrane Source: BHF-UCL <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
Other locations
- filopodium tip Source: UniProtKB-SubCell
- membrane Source: UniProtKBInferred from high throughput direct assayi
<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 membrane, Cell projection, Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus<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
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 | 60 | K → I: Abolishes plasma membrane targeting and nuclear localization. 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 | 61 | K → A: Abolishes plasma membrane targeting and nuclear localization. 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 | 71 | K → A: Abolishes plasma membrane targeting and nuclear localization. 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 | 72 | R → I: Abolishes plasma membrane targeting and nuclear localization. 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 | 97 | G → E: Decreases plasma membrane targeting and nuclear localization. 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 | 162 – 167 | FFSGST → AAAAAA: No effect on interaction with VAPA. 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
| 6 | |
| <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 | 451 – 453 | FFD → VVV: Reduces VAPA binding. Abolishes association with endoplasmic reticulum. 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
| 3 |
Organism-specific databases
DisGeNET More...DisGeNETi | 26031 |
Open Targets More...OpenTargetsi | ENSG00000070882 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA32828 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | OSBPL3 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 20139176 |
<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_0000100371 | 1 – 887 | Oxysterol-binding protein-related protein 3Add BLAST | 887 |
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 | 16 | PhosphoserineCombined 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
| 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 | 34 | PhosphoserineCombined 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
| 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 | 200 | PhosphoserineCombined 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
| 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 | 251 | PhosphoserineCombined 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
| 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 | 265 | PhosphoserineCombined 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
<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 | 304 | PhosphoserineCombined 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
<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 | 309 | PhosphoserineCombined 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
| 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 | 320 | PhosphoserineCombined 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
<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 | 323 | 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 | 371 | 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 | 372 | PhosphoserineCombined 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
<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 | 410 | PhosphoserineCombined 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
<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 | 425 | PhosphoserineCombined 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
| 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 | 437 | PhosphoserineCombined 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
<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 | 440 | PhosphoserineCombined 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
| 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
Phosphorylation is enhanced in vitro by phorbol-12-myristate-13-acetate (PMA), forskolin and calcium ionophore A23187 (PubMed:25447204). Phosphorylation seems to be stimulated in conditions of low cell-cell (or cell-matrix) adhesion (PubMed:18270267).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
- Ref.14"The R-Ras interaction partner ORP3 regulates cell adhesion."
Lehto M., Maeyraenpaeae M.I., Pellinen T., Ihalmo P., Lehtonen S., Kovanen P.T., Groop P.H., Ivaska J., Olkkonen V.M.
J. Cell Sci. 121:695-705(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RRAS, DOMAIN PH, AND PHOSPHORYLATION. - Ref.25"OSBP-related protein 3 (ORP3) coupling with VAMP-associated protein A regulates R-Ras activity."
Weber-Boyvat M., Kentala H., Lilja J., Vihervaara T., Hanninen R., Zhou Y., Peranen J., Nyman T.A., Ivaska J., Olkkonen V.M.
Exp. Cell Res. 331:278-291(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, DOMAIN FFAT MOTIF, PHOSPHORYLATION AT SER-251; SER-265; SER-304; SER-320; SER-323; SER-371; SER-372; SER-410 AND SER-437, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 162-PHE--THR-167 AND 451-PHE--ASP-453.
<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
PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9H4L5 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9H4L5 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9H4L5 |
PeptideAtlas More...PeptideAtlasi | Q9H4L5 |
PRoteomics IDEntifications database More...PRIDEi | Q9H4L5 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 80852 80853 [Q9H4L5-2] 80854 [Q9H4L5-3] 80855 [Q9H4L5-4] 80856 [Q9H4L5-5] 80857 [Q9H4L5-6] 80858 [Q9H4L5-7] 80859 [Q9H4L5-8] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9H4L5 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9H4L5 |
<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
Expressed in a subset of small lymphocytes (at protein level). Expressed at high concentration in kidney, lymph node and thymus. Expressed at moderate concentration in stomach, jejunum, ileum, appendix, spleen, leukocytes, trachea, lung and thyroid gland. Expressed at low concentration in whole brain, esophagus, duodenum, ileocecum, colon, skeletal muscle, bone marrow, placenta and mammary gland (PubMed:14593528). Isoform 1a, isoform 1b, isoform 1c and isoform 1d are highly expressed in brain, bone marrow, colon, kidney, lung, skeletal muscle, spleen, thymus and thyroid. Not expressed in heart and liver. Isoform 2a, isoform 2b, isoform 2c and isoform 2d are expressed in brain, bone marrow, kidney, skeletal muscle, spleen, thymus and thyroid. Not expressed in heart, liver and lung (PubMed:12590732).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
- Ref.3"ORP3 splice variants and their expression in human tissues and hematopoietic cells."
Collier F.M., Gregorio-King C.C., Apostolopoulos J., Walder K., Kirkland M.A.
DNA Cell Biol. 22:1-9(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B; 1C; 1D; 2A; 2B; 2C AND 2D), TISSUE SPECIFICITY. - Ref.11"Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues: the expression and intracellular localization of ORP3, ORP6, and ORP7."
Lehto M., Tienari J., Lehtonen S., Lehtonen E., Olkkonen V.M.
Cell Tissue Res. 315:39-57(2004) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei
Expressed in several fetal tissues including kidney, thymus, spleen and lung.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.11"Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues: the expression and intracellular localization of ORP3, ORP6, and ORP7."
Lehto M., Tienari J., Lehtonen S., Lehtonen E., Olkkonen V.M.
Cell Tissue Res. 315:39-57(2004) [PubMed] [Europe PMC] [Abstract]Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000070882 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9H4L5 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9H4L5 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA000691 HPA048401 |
<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
Homodimer (PubMed:16143324). Interacts with RRAS (PubMed:18270267). Interacts (phosphorylated form) with VAPA (PubMed:16143324, PubMed:25447204).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.12"Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants."
Lehto M., Hynynen R., Karjalainen K., Kuismanen E., Hyvaerinen K., Olkkonen V.M.
Exp. Cell Res. 310:445-462(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, PH DOMAIN, FFAT MOTIF, MUTAGENESIS OF LYS-60; LYS-61; LYS-71; ARG-72; GLY-97 AND 451-PHE--ASP-453. - Ref.14"The R-Ras interaction partner ORP3 regulates cell adhesion."
Lehto M., Maeyraenpaeae M.I., Pellinen T., Ihalmo P., Lehtonen S., Kovanen P.T., Groop P.H., Ivaska J., Olkkonen V.M.
J. Cell Sci. 121:695-705(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RRAS, DOMAIN PH, AND PHOSPHORYLATION. - Ref.25"OSBP-related protein 3 (ORP3) coupling with VAMP-associated protein A regulates R-Ras activity."
Weber-Boyvat M., Kentala H., Lilja J., Vihervaara T., Hanninen R., Zhou Y., Peranen J., Nyman T.A., Ivaska J., Olkkonen V.M.
Exp. Cell Res. 331:278-291(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, DOMAIN FFAT MOTIF, PHOSPHORYLATION AT SER-251; SER-265; SER-304; SER-320; SER-323; SER-371; SER-372; SER-410 AND SER-437, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 162-PHE--THR-167 AND 451-PHE--ASP-453.
<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 |
|---|---|---|---|---|
| ORF | Q9Q2G4 | 5 | EBI-1051317,EBI-6248094 | From Human immunodeficiency virus 1. |
| YWHAB | P31946 | 2 | EBI-1051317,EBI-359815 | |
| YWHAG | P61981 | 2 | EBI-1051317,EBI-359832 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 117497, 40 interactors |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q9H4L5 |
Protein interaction database and analysis system More...IntActi | Q9H4L5, 42 interactors |
Molecular INTeraction database More...MINTi | Q9H4L5 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000315410 |
<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
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9H4L5 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9H4L5 |
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
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 51 – 146 | PHPROSITE-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 Add BLAST | 96 |
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 | 161 – 167 | FFAT 11 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
| 7 | |
| <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 | 450 – 454 | FFAT 21 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 ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
The FFAT 2 motif is required for interaction with VAPA and regulation of the endoplasmic reticulum targeting of ORP3. The FFAT 1 motif may contribute to VAPA binding.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
- Ref.12"Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants."
Lehto M., Hynynen R., Karjalainen K., Kuismanen E., Hyvaerinen K., Olkkonen V.M.
Exp. Cell Res. 310:445-462(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, PH DOMAIN, FFAT MOTIF, MUTAGENESIS OF LYS-60; LYS-61; LYS-71; ARG-72; GLY-97 AND 451-PHE--ASP-453. - Ref.25"OSBP-related protein 3 (ORP3) coupling with VAMP-associated protein A regulates R-Ras activity."
Weber-Boyvat M., Kentala H., Lilja J., Vihervaara T., Hanninen R., Zhou Y., Peranen J., Nyman T.A., Ivaska J., Olkkonen V.M.
Exp. Cell Res. 331:278-291(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, DOMAIN FFAT MOTIF, PHOSPHORYLATION AT SER-251; SER-265; SER-304; SER-320; SER-323; SER-371; SER-372; SER-410 AND SER-437, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 162-PHE--THR-167 AND 451-PHE--ASP-453.
The PH domain binds phosphoinositides, with a preference for PI(3,4)P2 and PI(3,4,5)P3. The PH domain mediates targeting to the plasma membrane (PubMed:18270267).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
- Ref.12"Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants."
Lehto M., Hynynen R., Karjalainen K., Kuismanen E., Hyvaerinen K., Olkkonen V.M.
Exp. Cell Res. 310:445-462(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBUNIT, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, PH DOMAIN, FFAT MOTIF, MUTAGENESIS OF LYS-60; LYS-61; LYS-71; ARG-72; GLY-97 AND 451-PHE--ASP-453. - Ref.14"The R-Ras interaction partner ORP3 regulates cell adhesion."
Lehto M., Maeyraenpaeae M.I., Pellinen T., Ihalmo P., Lehtonen S., Kovanen P.T., Groop P.H., Ivaska J., Olkkonen V.M.
J. Cell Sci. 121:695-705(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RRAS, DOMAIN PH, AND PHOSPHORYLATION.
<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
Belongs to the OSBP family.Curated
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1737 Eukaryota ENOG410XP9E LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000119155 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG058934 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9H4L5 |
KEGG Orthology (KO) More...KOi | K20463 |
Identification of Orthologs from Complete Genome Data More...OMAi | TCVWRAN |
Database of Orthologous Groups More...OrthoDBi | EOG091G0DJB |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9H4L5 |
TreeFam database of animal gene trees More...TreeFami | TF320922 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.30.29.30, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR037239 OSBP_sf IPR000648 Oxysterol-bd IPR018494 Oxysterol-bd_CS IPR011993 PH-like_dom_sf IPR001849 PH_domain |
The PANTHER Classification System More...PANTHERi | PTHR10972 PTHR10972, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF01237 Oxysterol_BP, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00233 PH, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF144000 SSF144000, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS01013 OSBP, 1 hit PS50003 PH_DOMAIN, 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>Sequences (8)i
<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.
This entry describes 8 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
Isoform 1a (identifier: Q9H4L5-1) [UniParc]FASTAAdd to basketAdded to basketShow »
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MMSDEKNLGV SQKLVSPSRS TSSCSSKQGS RQDSWEVVEG LRGEMNYTQE
60 70 80 90 100
PPVQKGFLLK KRKWPLKGWH KRFFYLDKGI LKYAKSQTDI EREKLHGCID
110 120 130 140 150
VGLSVMSVKK SSKCIDLDTE EHIYHLKVKS EEVFDEWVSK LRHHRMYRQN
160 170 180 190 200
EIAMFPHEVN HFFSGSTITD SSSGVFDSIS SRKRSSISKQ NLFQTGSNVS
210 220 230 240 250
FSCGGETRVP LWLQSSEDME KCSKDLAHCH AYLVEMSQLL QSMDVLHRTY
260 270 280 290 300
SAPAINAIQG GSFESPKKEK RSHRRWRSRA IGKDAKGTLQ VPKPFSGPVR
310 320 330 340 350
LHSSNPNLST LDFGEEKNYS DGSETSSEFS KMQEDLCHIA HKVYFTLRSA
360 370 380 390 400
FNIMSAEREK LKQLMEQDAS SSPSAQVIGL KNALSSALAQ NTDLKERLRR
410 420 430 440 450
IHAESLLLDS PAVAKSGDNL AEENSRDENR ALVHQLSNES RLSITDSLSE
460 470 480 490 500
FFDAQEVLLS PSSSENEISD DDSYVSDISD NLSLDNLSND LDNERQTLGP
510 520 530 540 550
VLDSGREAKS RRRTCLPAPC PSSSNISLWN ILRNNIGKDL SKVAMPVELN
560 570 580 590 600
EPLNTLQRLC EELEYSELLD KAAQIPSPLE RMVYVAAFAI SAYASSYYRA
610 620 630 640 650
GSKPFNPVLG ETYECIREDK GFQFFSEQVS HHPPISACHA ESRNFVFWQD
660 670 680 690 700
VRWKNKFWGK SMEIVPIGTT HVTLPVFGDH FEWNKVTSCI HNILSGQRWI
710 720 730 740 750
EHYGEIVIKN LHDDSCYCKV NFIKAKYWST NAHEIEGTVF DRSGKAVHRL
760 770 780 790 800
FGKWHESIYC GGGSSSACVW RANPMPKGYE QYYSFTQFAL ELNEMDPSSK
810 820 830 840 850
SLLPPTDTRF RPDQRFLEEG NLEEAEIQKQ RIEQLQRERR RVLEENHVEH
860 870 880
QPRFFRKSDD DSWVSNGTYL ELRKDLGFSK LDHPVLW
Length:887
Mass (Da):101,224
Last modified:March 1, 2001 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i12E16912BD3F2E99
Isoform 1b (identifier: Q9H4L5-2) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
259-289: Missing.
10 20 30 40 50
MMSDEKNLGV SQKLVSPSRS TSSCSSKQGS RQDSWEVVEG LRGEMNYTQE
60 70 80 90 100
PPVQKGFLLK KRKWPLKGWH KRFFYLDKGI LKYAKSQTDI EREKLHGCID
110 120 130 140 150
VGLSVMSVKK SSKCIDLDTE EHIYHLKVKS EEVFDEWVSK LRHHRMYRQN
160 170 180 190 200
EIAMFPHEVN HFFSGSTITD SSSGVFDSIS SRKRSSISKQ NLFQTGSNVS
210 220 230 240 250
FSCGGETRVP LWLQSSEDME KCSKDLAHCH AYLVEMSQLL QSMDVLHRTY
260 270 280 290 300
SAPAINAIQV PKPFSGPVRL HSSNPNLSTL DFGEEKNYSD GSETSSEFSK
310 320 330 340 350
MQEDLCHIAH KVYFTLRSAF NIMSAEREKL KQLMEQDASS SPSAQVIGLK
360 370 380 390 400
NALSSALAQN TDLKERLRRI HAESLLLDSP AVAKSGDNLA EENSRDENRA
410 420 430 440 450
LVHQLSNESR LSITDSLSEF FDAQEVLLSP SSSENEISDD DSYVSDISDN
460 470 480 490 500
LSLDNLSNDL DNERQTLGPV LDSGREAKSR RRTCLPAPCP SSSNISLWNI
510 520 530 540 550
LRNNIGKDLS KVAMPVELNE PLNTLQRLCE ELEYSELLDK AAQIPSPLER
560 570 580 590 600
MVYVAAFAIS AYASSYYRAG SKPFNPVLGE TYECIREDKG FQFFSEQVSH
610 620 630 640 650
HPPISACHAE SRNFVFWQDV RWKNKFWGKS MEIVPIGTTH VTLPVFGDHF
660 670 680 690 700
EWNKVTSCIH NILSGQRWIE HYGEIVIKNL HDDSCYCKVN FIKAKYWSTN
710 720 730 740 750
AHEIEGTVFD RSGKAVHRLF GKWHESIYCG GGSSSACVWR ANPMPKGYEQ
760 770 780 790 800
YYSFTQFALE LNEMDPSSKS LLPPTDTRFR PDQRFLEEGN LEEAEIQKQR
810 820 830 840 850
IEQLQRERRR VLEENHVEHQ PRFFRKSDDD SWVSNGTYLE LRKDLGFSKL
DHPVLW
Length:856
Mass (Da):97,687
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i1D56185E3FB98744
Isoform 1c (identifier: Q9H4L5-3) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
387-422: Missing.
10 20 30 40 50
MMSDEKNLGV SQKLVSPSRS TSSCSSKQGS RQDSWEVVEG LRGEMNYTQE
60 70 80 90 100
PPVQKGFLLK KRKWPLKGWH KRFFYLDKGI LKYAKSQTDI EREKLHGCID
110 120 130 140 150
VGLSVMSVKK SSKCIDLDTE EHIYHLKVKS EEVFDEWVSK LRHHRMYRQN
160 170 180 190 200
EIAMFPHEVN HFFSGSTITD SSSGVFDSIS SRKRSSISKQ NLFQTGSNVS
210 220 230 240 250
FSCGGETRVP LWLQSSEDME KCSKDLAHCH AYLVEMSQLL QSMDVLHRTY
260 270 280 290 300
SAPAINAIQG GSFESPKKEK RSHRRWRSRA IGKDAKGTLQ VPKPFSGPVR
310 320 330 340 350
LHSSNPNLST LDFGEEKNYS DGSETSSEFS KMQEDLCHIA HKVYFTLRSA
360 370 380 390 400
FNIMSAEREK LKQLMEQDAS SSPSAQVIGL KNALSSENSR DENRALVHQL
410 420 430 440 450
SNESRLSITD SLSEFFDAQE VLLSPSSSEN EISDDDSYVS DISDNLSLDN
460 470 480 490 500
LSNDLDNERQ TLGPVLDSGR EAKSRRRTCL PAPCPSSSNI SLWNILRNNI
510 520 530 540 550
GKDLSKVAMP VELNEPLNTL QRLCEELEYS ELLDKAAQIP SPLERMVYVA
560 570 580 590 600
AFAISAYASS YYRAGSKPFN PVLGETYECI REDKGFQFFS EQVSHHPPIS
610 620 630 640 650
ACHAESRNFV FWQDVRWKNK FWGKSMEIVP IGTTHVTLPV FGDHFEWNKV
660 670 680 690 700
TSCIHNILSG QRWIEHYGEI VIKNLHDDSC YCKVNFIKAK YWSTNAHEIE
710 720 730 740 750
GTVFDRSGKA VHRLFGKWHE SIYCGGGSSS ACVWRANPMP KGYEQYYSFT
760 770 780 790 800
QFALELNEMD PSSKSLLPPT DTRFRPDQRF LEEGNLEEAE IQKQRIEQLQ
810 820 830 840 850
RERRRVLEEN HVEHQPRFFR KSDDDSWVSN GTYLELRKDL GFSKLDHPVL
W
Length:851
Mass (Da):97,325
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iDA08C319F2BAEDCE
Isoform 1d (identifier: Q9H4L5-4) [UniParc]FASTAAdd to basketAdded to basketShow »
The sequence of this isoform differs from the canonical sequence as follows:
259-289: Missing.
387-422: Missing.
10 20 30 40 50
MMSDEKNLGV SQKLVSPSRS TSSCSSKQGS RQDSWEVVEG LRGEMNYTQE
60 70 80 90 100
PPVQKGFLLK KRKWPLKGWH KRFFYLDKGI LKYAKSQTDI EREKLHGCID
110 120 130 140 150
VGLSVMSVKK SSKCIDLDTE EHIYHLKVKS EEVFDEWVSK LRHHRMYRQN
160 170 180 190 200
EIAMFPHEVN HFFSGSTITD SSSGVFDSIS SRKRSSISKQ NLFQTGSNVS
210 220 230 240 250
FSCGGETRVP LWLQSSEDME KCSKDLAHCH AYLVEMSQLL QSMDVLHRTY
260 270 280 290 300
SAPAINAIQV PKPFSGPVRL HSSNPNLSTL DFGEEKNYSD GSETSSEFSK
310 320 330 340 350
MQEDLCHIAH KVYFTLRSAF NIMSAEREKL KQLMEQDASS SPSAQVIGLK
360 370 380 390 400
NALSSENSRD ENRALVHQLS NESRLSITDS LSEFFDAQEV LLSPSSSENE
410 420 430 440 450
ISDDDSYVSD ISDNLSLDNL SNDLDNERQT LGPVLDSGRE AKSRRRTCLP
460 470 480 490 500
APCPSSSNIS LWNILRNNIG KDLSKVAMPV ELNEPLNTLQ RLCEELEYSE
510 520 530 540 550
LLDKAAQIPS PLERMVYVAA FAISAYASSY YRAGSKPFNP VLGETYECIR
560 570 580 590 600
EDKGFQFFSE QVSHHPPISA CHAESRNFVF WQDVRWKNKF WGKSMEIVPI
610 620 630 640 650
GTTHVTLPVF GDHFEWNKVT SCIHNILSGQ RWIEHYGEIV IKNLHDDSCY
660 670 680 690 700
CKVNFIKAKY WSTNAHEIEG TVFDRSGKAV HRLFGKWHES IYCGGGSSSA
710 720 730 740 750
CVWRANPMPK GYEQYYSFTQ FALELNEMDP SSKSLLPPTD TRFRPDQRFL
760 770 780 790 800
EEGNLEEAEI QKQRIEQLQR ERRRVLEENH VEHQPRFFRK SDDDSWVSNG
810 820
TYLELRKDLG FSKLDHPVLW
Length:820
Mass (Da):93,788
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i3D0A8947F6EE4DC5
Isoform 2a (identifier: Q9H4L5-5) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
584-631: YVAAFAISAY...FQFFSEQVSH → RSQPSLATVQ...SSAWLFPVTL
632-887: Missing.
10 20 30 40 50
MMSDEKNLGV SQKLVSPSRS TSSCSSKQGS RQDSWEVVEG LRGEMNYTQE
60 70 80 90 100
PPVQKGFLLK KRKWPLKGWH KRFFYLDKGI LKYAKSQTDI EREKLHGCID
110 120 130 140 150
VGLSVMSVKK SSKCIDLDTE EHIYHLKVKS EEVFDEWVSK LRHHRMYRQN
160 170 180 190 200
EIAMFPHEVN HFFSGSTITD SSSGVFDSIS SRKRSSISKQ NLFQTGSNVS
210 220 230 240 250
FSCGGETRVP LWLQSSEDME KCSKDLAHCH AYLVEMSQLL QSMDVLHRTY
260 270 280 290 300
SAPAINAIQG GSFESPKKEK RSHRRWRSRA IGKDAKGTLQ VPKPFSGPVR
310 320 330 340 350
LHSSNPNLST LDFGEEKNYS DGSETSSEFS KMQEDLCHIA HKVYFTLRSA
360 370 380 390 400
FNIMSAEREK LKQLMEQDAS SSPSAQVIGL KNALSSALAQ NTDLKERLRR
410 420 430 440 450
IHAESLLLDS PAVAKSGDNL AEENSRDENR ALVHQLSNES RLSITDSLSE
460 470 480 490 500
FFDAQEVLLS PSSSENEISD DDSYVSDISD NLSLDNLSND LDNERQTLGP
510 520 530 540 550
VLDSGREAKS RRRTCLPAPC PSSSNISLWN ILRNNIGKDL SKVAMPVELN
560 570 580 590 600
EPLNTLQRLC EELEYSELLD KAAQIPSPLE RMVRSQPSLA TVQPRSPSHE
610 620 630 640
AIHGAHQRDS PCSLRFHFDC SVNRFITQSC LASSAWLFPV TL
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »Length:642
Mass (Da):72,211
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i7AC19EA7AE07E5E4
Isoform 2b (identifier: Q9H4L5-6) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
259-289: Missing.
584-631: YVAAFAISAY...FQFFSEQVSH → RSQPSLATVQ...SSAWLFPVTL
632-887: Missing.
10 20 30 40 50
MMSDEKNLGV SQKLVSPSRS TSSCSSKQGS RQDSWEVVEG LRGEMNYTQE
60 70 80 90 100
PPVQKGFLLK KRKWPLKGWH KRFFYLDKGI LKYAKSQTDI EREKLHGCID
110 120 130 140 150
VGLSVMSVKK SSKCIDLDTE EHIYHLKVKS EEVFDEWVSK LRHHRMYRQN
160 170 180 190 200
EIAMFPHEVN HFFSGSTITD SSSGVFDSIS SRKRSSISKQ NLFQTGSNVS
210 220 230 240 250
FSCGGETRVP LWLQSSEDME KCSKDLAHCH AYLVEMSQLL QSMDVLHRTY
260 270 280 290 300
SAPAINAIQV PKPFSGPVRL HSSNPNLSTL DFGEEKNYSD GSETSSEFSK
310 320 330 340 350
MQEDLCHIAH KVYFTLRSAF NIMSAEREKL KQLMEQDASS SPSAQVIGLK
360 370 380 390 400
NALSSALAQN TDLKERLRRI HAESLLLDSP AVAKSGDNLA EENSRDENRA
410 420 430 440 450
LVHQLSNESR LSITDSLSEF FDAQEVLLSP SSSENEISDD DSYVSDISDN
460 470 480 490 500
LSLDNLSNDL DNERQTLGPV LDSGREAKSR RRTCLPAPCP SSSNISLWNI
510 520 530 540 550
LRNNIGKDLS KVAMPVELNE PLNTLQRLCE ELEYSELLDK AAQIPSPLER
560 570 580 590 600
MVRSQPSLAT VQPRSPSHEA IHGAHQRDSP CSLRFHFDCS VNRFITQSCL
610
ASSAWLFPVT L
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »Length:611
Mass (Da):68,674
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i1A92347357A219CE
Isoform 2c (identifier: Q9H4L5-7) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
387-422: Missing.
584-631: YVAAFAISAY...FQFFSEQVSH → RSQPSLATVQ...SSAWLFPVTL
632-887: Missing.
10 20 30 40 50
MMSDEKNLGV SQKLVSPSRS TSSCSSKQGS RQDSWEVVEG LRGEMNYTQE
60 70 80 90 100
PPVQKGFLLK KRKWPLKGWH KRFFYLDKGI LKYAKSQTDI EREKLHGCID
110 120 130 140 150
VGLSVMSVKK SSKCIDLDTE EHIYHLKVKS EEVFDEWVSK LRHHRMYRQN
160 170 180 190 200
EIAMFPHEVN HFFSGSTITD SSSGVFDSIS SRKRSSISKQ NLFQTGSNVS
210 220 230 240 250
FSCGGETRVP LWLQSSEDME KCSKDLAHCH AYLVEMSQLL QSMDVLHRTY
260 270 280 290 300
SAPAINAIQG GSFESPKKEK RSHRRWRSRA IGKDAKGTLQ VPKPFSGPVR
310 320 330 340 350
LHSSNPNLST LDFGEEKNYS DGSETSSEFS KMQEDLCHIA HKVYFTLRSA
360 370 380 390 400
FNIMSAEREK LKQLMEQDAS SSPSAQVIGL KNALSSENSR DENRALVHQL
410 420 430 440 450
SNESRLSITD SLSEFFDAQE VLLSPSSSEN EISDDDSYVS DISDNLSLDN
460 470 480 490 500
LSNDLDNERQ TLGPVLDSGR EAKSRRRTCL PAPCPSSSNI SLWNILRNNI
510 520 530 540 550
GKDLSKVAMP VELNEPLNTL QRLCEELEYS ELLDKAAQIP SPLERMVRSQ
560 570 580 590 600
PSLATVQPRS PSHEAIHGAH QRDSPCSLRF HFDCSVNRFI TQSCLASSAW
LFPVTL
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »Length:606
Mass (Da):68,313
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iEA72B4600CF3C1B8
Isoform 2d (identifier: Q9H4L5-8) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
259-289: Missing.
387-422: Missing.
584-631: YVAAFAISAY...FQFFSEQVSH → RSQPSLATVQ...SSAWLFPVTL
632-887: Missing.
10 20 30 40 50
MMSDEKNLGV SQKLVSPSRS TSSCSSKQGS RQDSWEVVEG LRGEMNYTQE
60 70 80 90 100
PPVQKGFLLK KRKWPLKGWH KRFFYLDKGI LKYAKSQTDI EREKLHGCID
110 120 130 140 150
VGLSVMSVKK SSKCIDLDTE EHIYHLKVKS EEVFDEWVSK LRHHRMYRQN
160 170 180 190 200
EIAMFPHEVN HFFSGSTITD SSSGVFDSIS SRKRSSISKQ NLFQTGSNVS
210 220 230 240 250
FSCGGETRVP LWLQSSEDME KCSKDLAHCH AYLVEMSQLL QSMDVLHRTY
260 270 280 290 300
SAPAINAIQV PKPFSGPVRL HSSNPNLSTL DFGEEKNYSD GSETSSEFSK
310 320 330 340 350
MQEDLCHIAH KVYFTLRSAF NIMSAEREKL KQLMEQDASS SPSAQVIGLK
360 370 380 390 400
NALSSENSRD ENRALVHQLS NESRLSITDS LSEFFDAQEV LLSPSSSENE
410 420 430 440 450
ISDDDSYVSD ISDNLSLDNL SNDLDNERQT LGPVLDSGRE AKSRRRTCLP
460 470 480 490 500
APCPSSSNIS LWNILRNNIG KDLSKVAMPV ELNEPLNTLQ RLCEELEYSE
510 520 530 540 550
LLDKAAQIPS PLERMVRSQP SLATVQPRSP SHEAIHGAHQ RDSPCSLRFH
560 570
FDCSVNRFIT QSCLASSAWL FPVTL
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »Length:575
Mass (Da):64,776
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iCD8F92033643E963
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
The sequence BAA31679 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
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_053548 | 354 | M → V. Corresponds to variant dbSNP:rs11768296Ensembl. | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_008219 | 259 – 289 | Missing in isoform 1b, isoform 1d, isoform 2b and isoform 2d. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 31 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_008220 | 387 – 422 | Missing in isoform 1c, isoform 1d, isoform 2c and isoform 2d. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 36 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_008221 | 584 – 631 | YVAAF…EQVSH → RSQPSLATVQPRSPSHEAIH GAHQRDSPCSLRFHFDCSVN RFITQSCLASSAWLFPVTL in isoform 2a, isoform 2b, isoform 2c and isoform 2d. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 48 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_008222 | 632 – 887 | Missing in isoform 2a, isoform 2b, isoform 2c and isoform 2d. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 256 |
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 | AY008372 mRNA Translation: AAG23400.1 AF392444 mRNA Translation: AAL40657.1 AF491781 mRNA Translation: AAM27386.1 AF491782 mRNA Translation: AAM27387.1 AF491783 mRNA Translation: AAM27388.1 AF491784 mRNA Translation: AAM27389.1 AF491785 mRNA Translation: AAM27390.1 AF491786 mRNA Translation: AAM27391.1 AF515639 mRNA Translation: AAM74165.1 AF515640 mRNA Translation: AAM74166.1 AB014604 mRNA Translation: BAA31679.2 Different initiation. AC003093 Genomic DNA Translation: AAB83939.1 AC004008 Genomic DNA No translation available. AC004016 Genomic DNA Translation: AAC26986.2 AC004239 Genomic DNA No translation available. CH236948 Genomic DNA Translation: EAL24240.1 CH236948 Genomic DNA Translation: EAL24241.1 CH236948 Genomic DNA Translation: EAL24242.1 CH236948 Genomic DNA Translation: EAL24243.1 CH236948 Genomic DNA Translation: EAL24244.1 CH236948 Genomic DNA Translation: EAL24245.1 CH471073 Genomic DNA Translation: EAW93816.1 CH471073 Genomic DNA Translation: EAW93817.1 CH471073 Genomic DNA Translation: EAW93818.1 CH471073 Genomic DNA Translation: EAW93819.1 CH471073 Genomic DNA Translation: EAW93820.1 CH471073 Genomic DNA Translation: EAW93821.1 BC017731 mRNA Translation: AAH17731.1 AF323727 mRNA Translation: AAG53408.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS47564.1 [Q9H4L5-4] CCDS5390.1 [Q9H4L5-1] CCDS5391.1 [Q9H4L5-2] CCDS5392.1 [Q9H4L5-3] |
NCBI Reference Sequences More...RefSeqi | NP_056365.1, NM_015550.3 [Q9H4L5-1] NP_663160.1, NM_145320.2 [Q9H4L5-2] NP_663161.1, NM_145321.2 [Q9H4L5-3] NP_663162.1, NM_145322.2 [Q9H4L5-4] XP_005249755.1, XM_005249698.3 [Q9H4L5-1] XP_006715744.1, XM_006715681.3 [Q9H4L5-2] XP_006715745.1, XM_006715682.3 [Q9H4L5-3] XP_006715746.1, XM_006715683.3 [Q9H4L5-4] XP_011513560.1, XM_011515258.2 [Q9H4L5-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.520259 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000313367; ENSP00000315410; ENSG00000070882 [Q9H4L5-1] ENST00000396429; ENSP00000379706; ENSG00000070882 [Q9H4L5-3] ENST00000396431; ENSP00000379708; ENSG00000070882 [Q9H4L5-2] ENST00000409069; ENSP00000386953; ENSG00000070882 [Q9H4L5-4] ENST00000409452; ENSP00000386801; ENSG00000070882 [Q9H4L5-5] ENST00000409555; ENSP00000386990; ENSG00000070882 [Q9H4L5-8] ENST00000409759; ENSP00000386325; ENSG00000070882 [Q9H4L5-7] ENST00000409863; ENSP00000386429; ENSG00000070882 [Q9H4L5-6] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 26031 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:26031 |
UCSC genome browser More...UCSCi | uc003sxf.5 human [Q9H4L5-1] |
<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 - Coding sequence diversityi
Alternative splicing, 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 | |
|---|---|---|---|---|---|
| Q9H4L5 | Oxysterol-binding protein | 887 | |||
| Oxysterol-binding protein | 887 | ||||
| Q9H4L5-2 | Oxysterol-binding protein | 856 | |||
| Oxysterol-binding protein | 856 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9H4L5 | Oxysterol-binding protein | 887 | |||
| Oxysterol-binding protein | 887 | ||||
| UPI000BB7BC9C | 947 | ||||
| Oxysterol-binding protein (Fragment) | 911 | ||||
| Oxysterol-binding protein (Fragment) | 911 | ||||
| +97 | |||||
| Q9H4L5-2 | Oxysterol-binding protein | 856 | |||
| Oxysterol-binding protein | 856 | ||||
| UPI0004BE14BC | 911 | ||||
| UPI0001795E86 | 855 | ||||
| UPI000CA0102B | 861 | ||||
| +66 | |||||
| Q9H4L5-3 | UPI0004BD0F4E | 906 | |||
| UPI0001795E87 | 850 | ||||
| UPI000C9FFE8F | 856 | ||||
| UPI00063EE2F1 | 856 | ||||
| Oxysterol-binding protein | 854 | ||||
| +70 | |||||
| Q9H4L5-4 | Oxysterol-binding protein | 820 | |||
| UPI0004BDD079 | 875 | ||||
| UPI0001795E88 | 819 | ||||
| UPI0001D37378 | 823 | ||||
| UPI00098261C7 | 822 | ||||
| +58 | |||||
| Q9H4L5-5 | OSBPL3 isoform 6 (Fragment) | 643 | |||
| OSBPL3 isoform 6 | 642 | ||||
| Q9H4L5-6 | OSBPL3 isoform 9 (Fragment) | 612 | |||
| OSBPL3 isoform 9 | 611 | ||||
| Q9H4L5-7 | OSBPL3 isoform 11 (Fragment) | 607 | |||
| OSBPL3 isoform 11 | 606 | ||||
| Q9H4L5-8 | OSBPL3 isoform 10 (Fragment) | 576 | |||
| OSBPL3 isoform 7 | 575 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| Q9H4L5 | Oxysterol-binding protein | 887 | |||
| Oxysterol-binding protein | 887 | ||||
| UPI000BB7BC9C | 947 | ||||
| Oxysterol-binding protein (Fragment) | 911 | ||||
| Oxysterol-binding protein (Fragment) | 911 | ||||
| +396 | |||||
| Q9H4L5-3 | UPI0004BD0F4E | 906 | |||
| UPI0001795E87 | 850 | ||||
| UPI000C9FFE8F | 856 | ||||
| UPI00063EE2F1 | 856 | ||||
| Oxysterol-binding protein | 854 | ||||
| +247 | |||||
| Q9H4L5-4 | UPI0004BD0F4E | 906 | |||
| UPI0001795E87 | 850 | ||||
| UPI000C9FFE8F | 856 | ||||
| UPI00063EE2F1 | 856 | ||||
| Oxysterol-binding protein | 854 | ||||
| +247 | |||||
| Q9H4L5-5 | OSBPL3 isoform 6 (Fragment) | 643 | |||
| OSBPL3 isoform 6 | 642 | ||||
| UPI0005292FB8 | 694 | ||||
| Oxysterol-binding protein | 637 | ||||
| Oxysterol-binding protein (Fragment) | 614 | ||||
| +6 | |||||
| Q9H4L5-6 | OSBPL3 isoform 6 (Fragment) | 643 | |||
| OSBPL3 isoform 6 | 642 | ||||
| UPI0005292FB8 | 694 | ||||
| Oxysterol-binding protein | 637 | ||||
| Oxysterol-binding protein (Fragment) | 614 | ||||
| +6 | |||||
| Q9H4L5-7 | OSBPL3 isoform 6 (Fragment) | 643 | |||
| OSBPL3 isoform 6 | 642 | ||||
| UPI0005292FB8 | 694 | ||||
| Oxysterol-binding protein | 637 | ||||
| Oxysterol-binding protein (Fragment) | 614 | ||||
| +6 | |||||
| Q9H4L5-8 | OSBPL3 isoform 10 (Fragment) | 576 | |||
| OSBPL3 isoform 7 | 575 | ||||
<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
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 | AY008372 mRNA Translation: AAG23400.1 AF392444 mRNA Translation: AAL40657.1 AF491781 mRNA Translation: AAM27386.1 AF491782 mRNA Translation: AAM27387.1 AF491783 mRNA Translation: AAM27388.1 AF491784 mRNA Translation: AAM27389.1 AF491785 mRNA Translation: AAM27390.1 AF491786 mRNA Translation: AAM27391.1 AF515639 mRNA Translation: AAM74165.1 AF515640 mRNA Translation: AAM74166.1 AB014604 mRNA Translation: BAA31679.2 Different initiation. AC003093 Genomic DNA Translation: AAB83939.1 AC004008 Genomic DNA No translation available. AC004016 Genomic DNA Translation: AAC26986.2 AC004239 Genomic DNA No translation available. CH236948 Genomic DNA Translation: EAL24240.1 CH236948 Genomic DNA Translation: EAL24241.1 CH236948 Genomic DNA Translation: EAL24242.1 CH236948 Genomic DNA Translation: EAL24243.1 CH236948 Genomic DNA Translation: EAL24244.1 CH236948 Genomic DNA Translation: EAL24245.1 CH471073 Genomic DNA Translation: EAW93816.1 CH471073 Genomic DNA Translation: EAW93817.1 CH471073 Genomic DNA Translation: EAW93818.1 CH471073 Genomic DNA Translation: EAW93819.1 CH471073 Genomic DNA Translation: EAW93820.1 CH471073 Genomic DNA Translation: EAW93821.1 BC017731 mRNA Translation: AAH17731.1 AF323727 mRNA Translation: AAG53408.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS47564.1 [Q9H4L5-4] CCDS5390.1 [Q9H4L5-1] CCDS5391.1 [Q9H4L5-2] CCDS5392.1 [Q9H4L5-3] |
NCBI Reference Sequences More...RefSeqi | NP_056365.1, NM_015550.3 [Q9H4L5-1] NP_663160.1, NM_145320.2 [Q9H4L5-2] NP_663161.1, NM_145321.2 [Q9H4L5-3] NP_663162.1, NM_145322.2 [Q9H4L5-4] XP_005249755.1, XM_005249698.3 [Q9H4L5-1] XP_006715744.1, XM_006715681.3 [Q9H4L5-2] XP_006715745.1, XM_006715682.3 [Q9H4L5-3] XP_006715746.1, XM_006715683.3 [Q9H4L5-4] XP_011513560.1, XM_011515258.2 [Q9H4L5-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.520259 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9H4L5 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9H4L5 |
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 | 117497, 40 interactors |
The Eukaryotic Linear Motif resource for Functional Sites in Proteins More...ELMi | Q9H4L5 |
Protein interaction database and analysis system More...IntActi | Q9H4L5, 42 interactors |
Molecular INTeraction database More...MINTi | Q9H4L5 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000315410 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9H4L5 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9H4L5 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | OSBPL3 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 20139176 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9H4L5 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9H4L5 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9H4L5 |
PeptideAtlas More...PeptideAtlasi | Q9H4L5 |
PRoteomics IDEntifications database More...PRIDEi | Q9H4L5 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 80852 80853 [Q9H4L5-2] 80854 [Q9H4L5-3] 80855 [Q9H4L5-4] 80856 [Q9H4L5-5] 80857 [Q9H4L5-6] 80858 [Q9H4L5-7] 80859 [Q9H4L5-8] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000313367; ENSP00000315410; ENSG00000070882 [Q9H4L5-1] ENST00000396429; ENSP00000379706; ENSG00000070882 [Q9H4L5-3] ENST00000396431; ENSP00000379708; ENSG00000070882 [Q9H4L5-2] ENST00000409069; ENSP00000386953; ENSG00000070882 [Q9H4L5-4] ENST00000409452; ENSP00000386801; ENSG00000070882 [Q9H4L5-5] ENST00000409555; ENSP00000386990; ENSG00000070882 [Q9H4L5-8] ENST00000409759; ENSP00000386325; ENSG00000070882 [Q9H4L5-7] ENST00000409863; ENSP00000386429; ENSG00000070882 [Q9H4L5-6] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 26031 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:26031 |
UCSC genome browser More...UCSCi | uc003sxf.5 human [Q9H4L5-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 26031 |
DisGeNET More...DisGeNETi | 26031 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000070882.12 |
GeneCards: human genes, protein and diseases More...GeneCardsi | OSBPL3 |
Human Gene Nomenclature Database More...HGNCi | HGNC:16370 OSBPL3 |
Human Protein Atlas More...HPAi | HPA000691 HPA048401 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 606732 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9H4L5 |
Open Targets More...OpenTargetsi | ENSG00000070882 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA32828 |
Human Unidentified Gene-Encoded large proteins database More...HUGEi | Search... |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1737 Eukaryota ENOG410XP9E LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000119155 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG058934 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9H4L5 |
KEGG Orthology (KO) More...KOi | K20463 |
Identification of Orthologs from Complete Genome Data More...OMAi | TCVWRAN |
Database of Orthologous Groups More...OrthoDBi | EOG091G0DJB |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9H4L5 |
TreeFam database of animal gene trees More...TreeFami | TF320922 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-192105 Synthesis of bile acids and bile salts |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | OSBPL3 human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | OSBPL3 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 26031 |
Protein Ontology More...PROi | PR:Q9H4L5 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000070882 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9H4L5 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9H4L5 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.30.29.30, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR037239 OSBP_sf IPR000648 Oxysterol-bd IPR018494 Oxysterol-bd_CS IPR011993 PH-like_dom_sf IPR001849 PH_domain |
The PANTHER Classification System More...PANTHERi | PTHR10972 PTHR10972, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF01237 Oxysterol_BP, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00233 PH, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF144000 SSF144000, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS01013 OSBP, 1 hit PS50003 PH_DOMAIN, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | OSBL3_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q9H4L5Primary (citable) accession number: Q9H4L5 Secondary accession number(s): A4D167 , A4D168, A4D169, A4D170, A4D171, A4D172, B8ZZ79, B8ZZP0, O14591, O43357, O43358, Q8N702, Q8N703, Q8N704, Q8NFH0, Q8NFH1, Q8NI12, Q8NI13, Q9BZF4, Q9UED6 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 11, 2002 |
| Last sequence update: | March 1, 2001 | |
| Last modified: | July 18, 2018 | |
| This is version 146 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<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 - Technical termi
Complete proteome, Reference proteomeDocuments
- Human chromosome 7
Human chromosome 7: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families
