UniProtKB - P31645 (SC6A4_HUMAN)
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- BLAST>sp|P31645|SC6A4_HUMAN Sodium-dependent serotonin transporter OS=Homo sapiens OX=9606 GN=SLC6A4 PE=1 SV=1 METTPLNSQKQLSACEDGEDCQENGVLQKVVPTPGDKVESGQISNGYSAVPSPGAGDDTR HSIPATTTTLVAELHQGERETWGKKVDFLLSVIGYAVDLGNVWRFPYICYQNGGGAFLLP YTIMAIFGGIPLFYMELALGQYHRNGCISIWRKICPIFKGIGYAICIIAFYIASYYNTIM AWALYYLISSFTDQLPWTSCKNSWNTGNCTNYFSEDNITWTLHSTSPAEEFYTRHVLQIH RSKGLQDLGGISWQLALCIMLIFTVIYFSIWKGVKTSGKVVWVTATFPYIILSVLLVRGA TLPGAWRGVLFYLKPNWQKLLETGVWIDAAAQIFFSLGPGFGVLLAFASYNKFNNNCYQD ALVTSVVNCMTSFVSGFVIFTVLGYMAEMRNEDVSEVAKDAGPSLLFITYAEAIANMPAS TFFAIIFFLMLITLGLDSTFAGLEGVITAVLDEFPHVWAKRRERFVLAVVITCFFGSLVT LTFGGAYVVKLLEEYATGPAVLTVALIEAVAVSWFYGITQFCRDVKEMLGFSPGWFWRIC WVAISPLFLLFIICSFLMSPPQLRLFQYNYPYWSIILGYCIGTSSFICIPTYIAYRLIIT PGTFKERIIKSITPETPTEIPCGDIRLNAV
- Align
Sodium-dependent serotonin transporter
SLC6A4
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information 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"Plasma serotonin levels and the platelet serotonin transporter."
Brenner B., Harney J.T., Ahmed B.A., Jeffus B.C., Unal R., Mehta J.L., Kilic F.
J. Neurochem. 102:206-215(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.13"Serotonin transamidates Rab4 and facilitates its binding to the C terminus of serotonin transporter."
Ahmed B.A., Jeffus B.C., Bukhari S.I., Harney J.T., Unal R., Lupashin V.V., van der Sluijs P., Kilic F.
J. Biol. Chem. 283:9388-9398(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RAB4, SUBCELLULAR LOCATION, INDUCTION BY SEROTONIN. - Ref.14"The cellular distribution of serotonin transporter is impeded on serotonin-altered vimentin network."
Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S., Ziu E., Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D., Kilic F.
PLoS ONE 4:E4730-E4730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH VIM, SUBCELLULAR LOCATION, INDUCTION BY SEROTONIN, MUTAGENESIS OF SER-611; THR-613 AND THR-616, PHOSPHORYLATION AT SER-611; THR-613 AND THR-616. - Ref.16"X-ray structures and mechanism of the human serotonin transporter."
Coleman J.A., Green E.M., Gouaux E.
Nature 532:334-339(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.14 ANGSTROMS) OF 76-618 IN COMPLEXES WITH SODIUM IONS AND THE ANTIDEPRESSANTS CITALOPRAM AND PAROXETINE, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-208 AND ASN-217, DISULFIDE BONDS.
Miscellaneous
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 94 | Sodium 1; via carbonyl oxygenBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 96 | Sodium 2; via carbonyl oxygen1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 97 | Sodium 1; via carbonyl oxygenBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 101 | Sodium 21 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 336 | Sodium 21 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 368 | Sodium 21 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 434 | Sodium 1; via carbonyl oxygenBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 437 | Sodium 1By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 438 | Sodium 1By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- actin filament binding Source: UniProtKB
- cocaine binding Source: Ensembl
- dopamine:sodium symporter activity Source: GO_Central
- metal ion binding Source: UniProtKB-KW
- monoamine transmembrane transporter activity Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- myosin binding Source: Ensembl
- nitric-oxide synthase binding Source: Ensembl
- protein homodimerization activity Source: Ensembl
- Rab GTPase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- serotonin:sodium symporter activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- serotonin transmembrane transporter activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- syntaxin-1 binding Source: Ensembl
<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
- brain morphogenesis Source: BHF-UCL
- cellular response to cGMP Source: Ensembl
- cellular response to retinoic acid Source: Ensembl
- circadian rhythm Source: Ensembl
- dopamine uptake involved in synaptic transmission Source: GO_Central
- memory Source: Ensembl
- monoamine transport Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- negative regulation of cerebellar granule cell precursor proliferation Source: Ensembl
- negative regulation of neuron differentiation Source: Ensembl
- negative regulation of organ growth Source: BHF-UCL
- negative regulation of synaptic transmission, dopaminergic Source: Ensembl
- neurotransmitter biosynthetic process Source: Reactome
- positive regulation of cell cycle Source: Ensembl
- positive regulation of gene expression Source: Ensembl
- positive regulation of serotonin secretion Source: Ensembl
- protein complex oligomerization Source: UniProtKB
- protein homooligomerization Source: Ensembl
- regulation of thalamus size Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- response to estradiol Source: Ensembl
- response to hypoxia Source: Ensembl
- response to nutrient Source: Ensembl
- response to toxic substance Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- serotonin transport Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- serotonin uptake Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- social behavior Source: BHF-UCL
- sperm ejaculation Source: Ensembl
- vasoconstriction Source: Ensembl
<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 | Neurotransmitter transport, Symport, Transport |
| Ligand | Metal-binding, Sodium |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-380615 Serotonin clearance from the synaptic cleft |
SIGNOR Signaling Network Open Resource More...SIGNORi | P31645 |
Protein family/group databases
Transport Classification Database More...TCDBi | 2.A.22.1.1 the neurotransmitter:sodium symporter (nss) family |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Sodium-dependent serotonin transporterShort name: SERTBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi Alternative name(s): 5HT transporter Short name: 5HTT Solute carrier family 6 member 4 |
| <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:SLC6A4 Synonyms:HTT, SERT |
| <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:ENSG00000108576.9 |
Human Gene Nomenclature Database More...HGNCi | HGNC:11050 SLC6A4 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 182138 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P31645 |
<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
Endosome
- Endosome membrane 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.10"Subcellular redistribution of the serotonin transporter by secretory carrier membrane protein 2."
Mueller H.K., Wiborg O., Haase J.
J. Biol. Chem. 281:28901-28909(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SCAMP2, SUBCELLULAR LOCATION. - Ref.13"Serotonin transamidates Rab4 and facilitates its binding to the C terminus of serotonin transporter."
Ahmed B.A., Jeffus B.C., Bukhari S.I., Harney J.T., Unal R., Lupashin V.V., van der Sluijs P., Kilic F.
J. Biol. Chem. 283:9388-9398(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RAB4, SUBCELLULAR LOCATION, INDUCTION BY SEROTONIN.
- Endosome membrane 2 Publications
Plasma membrane
- Cell membrane 5 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Subcellular redistribution of the serotonin transporter by secretory carrier membrane protein 2."
Mueller H.K., Wiborg O., Haase J.
J. Biol. Chem. 281:28901-28909(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SCAMP2, SUBCELLULAR LOCATION. - Ref.11"Plasma serotonin levels and the platelet serotonin transporter."
Brenner B., Harney J.T., Ahmed B.A., Jeffus B.C., Unal R., Mehta J.L., Kilic F.
J. Neurochem. 102:206-215(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.13"Serotonin transamidates Rab4 and facilitates its binding to the C terminus of serotonin transporter."
Ahmed B.A., Jeffus B.C., Bukhari S.I., Harney J.T., Unal R., Lupashin V.V., van der Sluijs P., Kilic F.
J. Biol. Chem. 283:9388-9398(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RAB4, SUBCELLULAR LOCATION, INDUCTION BY SEROTONIN. - Ref.14"The cellular distribution of serotonin transporter is impeded on serotonin-altered vimentin network."
Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S., Ziu E., Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D., Kilic F.
PLoS ONE 4:E4730-E4730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH VIM, SUBCELLULAR LOCATION, INDUCTION BY SEROTONIN, MUTAGENESIS OF SER-611; THR-613 AND THR-616, PHOSPHORYLATION AT SER-611; THR-613 AND THR-616. - Ref.16"X-ray structures and mechanism of the human serotonin transporter."
Coleman J.A., Green E.M., Gouaux E.
Nature 532:334-339(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.14 ANGSTROMS) OF 76-618 IN COMPLEXES WITH SODIUM IONS AND THE ANTIDEPRESSANTS CITALOPRAM AND PAROXETINE, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-208 AND ASN-217, DISULFIDE BONDS.
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
1 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.16"X-ray structures and mechanism of the human serotonin transporter."
Coleman J.A., Green E.M., Gouaux E.
Nature 532:334-339(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.14 ANGSTROMS) OF 76-618 IN COMPLEXES WITH SODIUM IONS AND THE ANTIDEPRESSANTS CITALOPRAM AND PAROXETINE, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION AT ASN-208 AND ASN-217, DISULFIDE BONDS.
- Cell membrane 5 Publications
Other locations
- Endomembrane system 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.10"Subcellular redistribution of the serotonin transporter by secretory carrier membrane protein 2."
Mueller H.K., Wiborg O., Haase J.
J. Biol. Chem. 281:28901-28909(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SCAMP2, SUBCELLULAR LOCATION.
Note: Could be part of recycling endosomes (PubMed:18227069, PubMed:16870614). Density of transporter molecules on the plasma membrane is itself regulated by STX1A (By similarity). Density of transporter molecules on the plasma membrane is also regulated by serotonin (PubMed:17506858) (PubMed:18227069).By similarity- Endomembrane system 1 Publication
- Ref.10"Subcellular redistribution of the serotonin transporter by secretory carrier membrane protein 2."
Mueller H.K., Wiborg O., Haase J.
J. Biol. Chem. 281:28901-28909(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SCAMP2, SUBCELLULAR LOCATION. - Ref.11"Plasma serotonin levels and the platelet serotonin transporter."
Brenner B., Harney J.T., Ahmed B.A., Jeffus B.C., Unal R., Mehta J.L., Kilic F.
J. Neurochem. 102:206-215(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. - Ref.13"Serotonin transamidates Rab4 and facilitates its binding to the C terminus of serotonin transporter."
Ahmed B.A., Jeffus B.C., Bukhari S.I., Harney J.T., Unal R., Lupashin V.V., van der Sluijs P., Kilic F.
J. Biol. Chem. 283:9388-9398(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RAB4, SUBCELLULAR LOCATION, INDUCTION BY SEROTONIN.
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
3 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Cytosol
- cytosol Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Endosome
- endosome membrane Source: UniProtKB-SubCell
Plasma Membrane
- integral component of plasma membrane Source: GO_Central
- plasma membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- endomembrane system Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- membrane raft Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- neuron projection Source: GO_Central
- presynapse Source: GOC
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 1 – 87 | CytoplasmicCuratedAdd BLAST | 87 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 88 – 112 | Helical; Name=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
| 25 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 113 – 115 | ExtracellularCurated | 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 116 – 135 | Helical; Name=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
| 20 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 136 – 160 | CytoplasmicCuratedAdd BLAST | 25 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 161 – 186 | Helical; Name=31 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
| 26 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 187 – 252 | ExtracellularCuratedAdd BLAST | 66 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 253 – 271 | Helical; Name=41 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
| 19 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 272 – 277 | CytoplasmicCurated | 6 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 278 – 297 | Helical; Name=51 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
| 20 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 298 – 324 | ExtracellularCuratedAdd BLAST | 27 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 325 – 347 | Helical; Name=61 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
| 23 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 348 – 360 | CytoplasmicCuratedAdd BLAST | 13 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 361 – 380 | Helical; Name=71 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
| 20 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 381 – 421 | ExtracellularCuratedAdd BLAST | 41 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 422 – 443 | Helical; Name=81 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
| 22 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 444 – 463 | CytoplasmicCuratedAdd BLAST | 20 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 464 – 483 | Helical; Name=91 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
| 20 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 484 – 494 | ExtracellularCuratedAdd BLAST | 11 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 495 – 516 | Helical; Name=101 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
| 22 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 517 – 538 | CytoplasmicCuratedAdd BLAST | 22 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 539 – 558 | Helical; Name=111 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
| 20 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 559 – 574 | ExtracellularCuratedAdd BLAST | 16 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 575 – 595 | Helical; Name=121 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
| 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 596 – 630 | CytoplasmicCuratedAdd BLAST | 35 |
<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, Endosome, Membrane<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
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 | 611 | S → A: Loss of 10 % of serotonin uptake activity. Loss of 5 % of serotonin uptake activity; when associated with A-613 and A-616. 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 | 611 | S → D: Loss of 61 % of serotonin uptake activity. Loss of 95 % of serotonin uptake activity and lack of association between VIM and the plasma membrane; when associated with D-613 and D-616. 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 | 613 | T → A: Loss of 26 % of serotonin uptake activity. Loss of 5 % of serotonin uptake activity; when associated with A-611 and A-616. 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 | 613 | T → D: Loss of 26 % of serotonin uptake activity. Loss of 95 % of serotonin uptake activity and lack of association between VIM and the plasma membrane; when associated with D-611 and D-616. 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 | 616 | T → A: No change. Loss of 5 % of serotonin uptake activity; when associated with A-611 and A-613. 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 | 616 | T → D: No change. Loss of 95 % of serotonin uptake activity and lack of association between VIM and the plasma membrane; when associated with D-611 and D-613. 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 |
Organism-specific databases
DisGeNET More...DisGeNETi | 6532 |
MalaCards human disease database More...MalaCardsi | SLC6A4 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 103780 phenotype 164230 phenotype |
Open Targets More...OpenTargetsi | ENSG00000108576 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA312 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL228 |
Drug and drug target database More...DrugBanki | DB01472 4-Methoxyamphetamine DB04836 Amineptine DB00321 Amitriptyline DB00543 Amoxapine DB00182 Amphetamine DB00289 Atomoxetine DB04889 Bicifadine DB09016 Butriptyline DB01114 Chlorphenamine DB00215 Citalopram DB01242 Clomipramine DB00907 Cocaine DB05688 CRx-119 DB01151 Desipramine DB06700 Desvenlafaxine DB01191 Dexfenfluramine DB06701 Dexmethylphenidate DB00514 Dextromethorphan DB00988 Dopamine DB01142 Doxepin DB00476 Duloxetine DB01363 Ephedra DB01175 Escitalopram DB00574 Fenfluramine DB00472 Fluoxetine DB00176 Fluvoxamine DB00458 Imipramine DB08918 Levomilnacipran DB00408 Loxapine DB00579 Mazindol DB01577 Methamphetamine DB09543 Methyl salicylate DB00422 Methylphenidate DB06148 Mianserin DB04896 Milnacipran DB00805 Minaprine DB00370 Mirtazapine DB01442 MMDA DB01149 Nefazodone DB00540 Nortriptyline DB05422 OPC-14523 DB00715 Paroxetine DB00454 Pethidine DB00191 Phentermine DB00344 Protriptyline DB00852 Pseudoephedrine DB01104 Sertraline DB01105 Sibutramine DB06204 Tapentadol DB01079 Tegaserod DB00193 Tramadol DB00656 Trazodone DB00726 Trimipramine DB00285 Venlafaxine DB00661 Verapamil DB06684 Vilazodone DB09068 Vortioxetine DB04832 Zimelidine |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 928 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 400630 |
<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_0000214757 | 1 – 630 | Sodium-dependent serotonin transporterAdd BLAST | 630 |
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 | 47 | Phosphotyrosine1 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 | 142 | Phosphotyrosine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 200 ↔ 209 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 208 | N-linked (GlcNAc...) asparagineSequence analysis1 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/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 217 | N-linked (GlcNAc...) asparagineSequence analysis1 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 | 276 | Phosphothreonine; by PKG1 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 | 611 | 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 | 613 | Phosphothreonine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 616 | Phosphothreonine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information 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"Serotonin transporter phosphorylation by cGMP-dependent protein kinase is altered by a mutation associated with obsessive compulsive disorder."
Zhang Y.W., Gesmonde J., Ramamoorthy S., Rudnick G.
J. Neurosci. 27:10878-10886(2007) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT THR-276, VARIANT VAL-425. - Ref.14"The cellular distribution of serotonin transporter is impeded on serotonin-altered vimentin network."
Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S., Ziu E., Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D., Kilic F.
PLoS ONE 4:E4730-E4730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH VIM, SUBCELLULAR LOCATION, INDUCTION BY SEROTONIN, MUTAGENESIS OF SER-611; THR-613 AND THR-616, PHOSPHORYLATION AT SER-611; THR-613 AND THR-616. - Ref.15"Tyrosine phosphorylation of the human serotonin transporter: a role in the transporter stability and function."
Annamalai B., Mannangatti P., Arapulisamy O., Shippenberg T.S., Jayanthi L.D., Ramamoorthy S.
Mol. Pharmacol. 81:73-85(2012) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT TYR-47 AND TYR-142.
<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
Disulfide bond, Glycoprotein, PhosphoproteinProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P31645 |
PeptideAtlas More...PeptideAtlasi | P31645 |
PRoteomics IDEntifications database More...PRIDEi | P31645 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 54798 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P31645 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P31645 |
<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
<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"Plasma serotonin levels and the platelet serotonin transporter."
Brenner B., Harney J.T., Ahmed B.A., Jeffus B.C., Unal R., Mehta J.L., Kilic F.
J. Neurochem. 102:206-215(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<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.13"Serotonin transamidates Rab4 and facilitates its binding to the C terminus of serotonin transporter."
Ahmed B.A., Jeffus B.C., Bukhari S.I., Harney J.T., Unal R., Lupashin V.V., van der Sluijs P., Kilic F.
J. Biol. Chem. 283:9388-9398(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RAB4, SUBCELLULAR LOCATION, INDUCTION BY SEROTONIN. - Ref.14"The cellular distribution of serotonin transporter is impeded on serotonin-altered vimentin network."
Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S., Ziu E., Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D., Kilic F.
PLoS ONE 4:E4730-E4730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH VIM, SUBCELLULAR LOCATION, INDUCTION BY SEROTONIN, MUTAGENESIS OF SER-611; THR-613 AND THR-616, PHOSPHORYLATION AT SER-611; THR-613 AND THR-616.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000108576 |
CleanEx database of gene expression profiles More...CleanExi | HS_HTT HS_SLC6A4 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P31645 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P31645 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA071354 HPA074728 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information 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.9"Serotonin-, protein kinase C-, and Hic-5-associated redistribution of the platelet serotonin transporter."
Carneiro A.M.D., Blakely R.D.
J. Biol. Chem. 281:24769-24780(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TGFB1I1. - Ref.10"Subcellular redistribution of the serotonin transporter by secretory carrier membrane protein 2."
Mueller H.K., Wiborg O., Haase J.
J. Biol. Chem. 281:28901-28909(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SCAMP2, SUBCELLULAR LOCATION. - Ref.13"Serotonin transamidates Rab4 and facilitates its binding to the C terminus of serotonin transporter."
Ahmed B.A., Jeffus B.C., Bukhari S.I., Harney J.T., Unal R., Lupashin V.V., van der Sluijs P., Kilic F.
J. Biol. Chem. 283:9388-9398(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH RAB4, SUBCELLULAR LOCATION, INDUCTION BY SEROTONIN. - Ref.14"The cellular distribution of serotonin transporter is impeded on serotonin-altered vimentin network."
Ahmed B.A., Bukhari I.A., Jeffus B.C., Harney J.T., Thyparambil S., Ziu E., Fraer M., Rusch N.J., Zimniak P., Lupashin V., Tang D., Kilic F.
PLoS ONE 4:E4730-E4730(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH VIM, SUBCELLULAR LOCATION, INDUCTION BY SEROTONIN, MUTAGENESIS OF SER-611; THR-613 AND THR-616, PHOSPHORYLATION AT SER-611; THR-613 AND THR-616.
<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
- actin filament binding Source: UniProtKB
- myosin binding Source: Ensembl
- nitric-oxide synthase binding Source: Ensembl
- protein homodimerization activity Source: Ensembl
- Rab GTPase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- syntaxin-1 binding Source: Ensembl
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 112423, 11 interactors |
Protein interaction database and analysis system More...IntActi | P31645, 2 interactors |
Molecular INTeraction database More...MINTi | P31645 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000261707 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P31645 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 85 – 96 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 99 – 111 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 114 – 117 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 118 – 127 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 129 – 143 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 149 – 152 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 156 – 159 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 160 – 173 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 176 – 188 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 189 – 191 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 192 – 194 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 196 – 198 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 202 – 204 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 207 – 209 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 212 – 214 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 227 – 234 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 235 – 237 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 239 – 241 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 244 – 247 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 253 – 270 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 274 – 284 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 287 – 300 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 303 – 305 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 306 – 313 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 317 – 321 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 323 – 337 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 340 – 342 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 343 – 349 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 353 – 355 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 358 – 389 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 32 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 396 – 398 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 403 – 407 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 409 – 415 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 420 – 453 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 34 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 462 – 477 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 478 – 480 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 485 – 494 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 497 – 513 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 514 – 517 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 518 – 528 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 529 – 531 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 535 – 542 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 544 – 558 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 574 – 583 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 584 – 587 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 588 – 599 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 604 – 612 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 5I6X | X-ray | 3.14 | A | 76-618 | [»] | |
| 5I6Z | X-ray | 4.53 | A | 76-618 | [»] | |
| 5I71 | X-ray | 3.15 | A | 76-618 | [»] | |
| 5I73 | X-ray | 3.24 | A | 76-618 | [»] | |
| 5I74 | X-ray | 3.40 | A | 76-618 | [»] | |
| 5I75 | X-ray | 3.49 | A | 76-618 | [»] | |
| 6AWN | X-ray | 3.62 | A | 76-618 | [»] | |
| 6AWO | X-ray | 3.53 | A | 76-618 | [»] | |
| 6AWP | X-ray | 3.80 | A | 76-618 | [»] | |
| 6AWQ | X-ray | 4.05 | A | 76-618 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P31645 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P31645 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 611 – 630 | Required for serotonin uptake activity1 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
| 20 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 616 – 624 | Interaction with RAB4A | 9 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3659 Eukaryota COG0733 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118857 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000116406 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG071421 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P31645 |
KEGG Orthology (KO) More...KOi | K05037 |
Identification of Orthologs from Complete Genome Data More...OMAi | NMPAATF |
Database of Orthologous Groups More...OrthoDBi | EOG091G08PX |
Database for complete collections of gene phylogenies More...PhylomeDBi | P31645 |
TreeFam database of animal gene trees More...TreeFami | TF343812 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000175 Na/ntran_symport IPR013086 Na/ntran_symport_serotonin_N IPR037272 SNS_sf |
The PANTHER Classification System More...PANTHERi | PTHR11616 PTHR11616, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF03491 5HT_transport_N, 1 hit PF00209 SNF, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR01203 5HTTRANSPORT PR00176 NANEUSMPORT |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF161070 SSF161070, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00610 NA_NEUROTRAN_SYMP_1, 1 hit PS00754 NA_NEUROTRAN_SYMP_2, 1 hit PS50267 NA_NEUROTRAN_SYMP_3, 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 (2)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 2 <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
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
METTPLNSQK QLSACEDGED CQENGVLQKV VPTPGDKVES GQISNGYSAV
60 70 80 90 100
PSPGAGDDTR HSIPATTTTL VAELHQGERE TWGKKVDFLL SVIGYAVDLG
110 120 130 140 150
NVWRFPYICY QNGGGAFLLP YTIMAIFGGI PLFYMELALG QYHRNGCISI
160 170 180 190 200
WRKICPIFKG IGYAICIIAF YIASYYNTIM AWALYYLISS FTDQLPWTSC
210 220 230 240 250
KNSWNTGNCT NYFSEDNITW TLHSTSPAEE FYTRHVLQIH RSKGLQDLGG
260 270 280 290 300
ISWQLALCIM LIFTVIYFSI WKGVKTSGKV VWVTATFPYI ILSVLLVRGA
310 320 330 340 350
TLPGAWRGVL FYLKPNWQKL LETGVWIDAA AQIFFSLGPG FGVLLAFASY
360 370 380 390 400
NKFNNNCYQD ALVTSVVNCM TSFVSGFVIF TVLGYMAEMR NEDVSEVAKD
410 420 430 440 450
AGPSLLFITY AEAIANMPAS TFFAIIFFLM LITLGLDSTF AGLEGVITAV
460 470 480 490 500
LDEFPHVWAK RRERFVLAVV ITCFFGSLVT LTFGGAYVVK LLEEYATGPA
510 520 530 540 550
VLTVALIEAV AVSWFYGITQ FCRDVKEMLG FSPGWFWRIC WVAISPLFLL
560 570 580 590 600
FIICSFLMSP PQLRLFQYNY PYWSIILGYC IGTSSFICIP TYIAYRLIIT
610 620 630
PGTFKERIIK SITPETPTEI PCGDIRLNAV
The sequence of this isoform differs from the canonical sequence as follows:
1-1: M → MSQSRRVNPDDRELGGDLQIQAPRDQLGSLADGHQCHLLTSRM
10 20 30 40 50
MSQSRRVNPD DRELGGDLQI QAPRDQLGSL ADGHQCHLLT SRMETTPLNS
60 70 80 90 100
QKQLSACEDG EDCQENGVLQ KVVPTPGDKV ESGQISNGYS AVPSPGAGDD
110 120 130 140 150
TRHSIPATTT TLVAELHQGE RETWGKKVDF LLSVIGYAVD LGNVWRFPYI
160 170 180 190 200
CYQNGGGAFL LPYTIMAIFG GIPLFYMELA LGQYHRNGCI SIWRKICPIF
210 220 230 240 250
KGIGYAICII AFYIASYYNT IMAWALYYLI SSFTDQLPWT SCKNSWNTGN
260 270 280 290 300
CTNYFSEDNI TWTLHSTSPA EEFYTRHVLQ IHRSKGLQDL GGISWQLALC
310 320 330 340 350
IMLIFTVIYF SIWKGVKTSG KVVWVTATFP YIILSVLLVR GATLPGAWRG
360 370 380 390 400
VLFYLKPNWQ KLLETGVWID AAAQIFFSLG PGFGVLLAFA SYNKFNNNCY
410 420 430 440 450
QDALVTSVVN CMTSFVSGFV IFTVLGYMAE MRNEDVSEVA KDAGPSLLFI
460 470 480 490 500
TYAEAIANMP ASTFFAIIFF LMLITLGLDS TFAGLEGVIT AVLDEFPHVW
510 520 530 540 550
AKRRERFVLA VVITCFFGSL VTLTFGGAYV VKLLEEYATG PAVLTVALIE
560 570 580 590 600
AVAVSWFYGI TQFCRDVKEM LGFSPGWFWR ICWVAISPLF LLFIICSFLM
610 620 630 640 650
SPPQLRLFQY NYPYWSIILG YCIGTSSFIC IPTYIAYRLI ITPGTFKERI
660 670
IKSITPETPT EIPCGDIRLN AV
<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi
<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.20"Influence of life stress on depression: moderation by a polymorphism in the 5-HTT gene."
Caspi A., Sugden K., Moffitt T.E., Taylor A., Craig I.W., Harrington H., McClay J., Mill J., Martin J., Braithwaite A., Poulton R.
Science 301:386-389(2003) [PubMed] [Europe PMC] [Abstract]Cited for: POLYMORPHISM IN THE PROMOTER REGION.
Online Mendelian Inheritance in Man (OMIM)
More...MIMi:164230].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"Serotonin transporter phosphorylation by cGMP-dependent protein kinase is altered by a mutation associated with obsessive compulsive disorder."
Zhang Y.W., Gesmonde J., Ramamoorthy S., Rudnick G.
J. Neurosci. 27:10878-10886(2007) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT THR-276, VARIANT VAL-425. - Ref.18"Serotonin transporter missense mutation associated with a complex neuropsychiatric phenotype."
Ozaki N., Goldman D., Kaye W.H., Plotnicov K., Greenberg B.D., Lappalainen J., Rudnick G., Murphy D.L.
Mol. Psychiatry 8:933-936(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT VAL-425. - Ref.19"A human serotonin transporter mutation causes constitutive activation of transport activity."
Kilic F., Murphy D.L., Rudnick G.
Mol. Pharmacol. 64:440-446(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANT VAL-425.
Online Mendelian Inheritance in Man (OMIM)
More...MIMi:103780].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.21"Meta-analysis of the association of a functional serotonin transporter promoter polymorphism with alcohol dependence."
Feinn R., Nellissery M., Kranzler H.R.
Am. J. Med. Genet. B Neuropsychiatr. Genet. 133:79-84(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ALCOHOLISM.
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_014181 | 56 | G → A1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_029158 | 201 | K → N. Corresponds to variant dbSNP:rs2228673Ensembl. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_036788 | 425 | I → L. Corresponds to variant dbSNP:rs28914832EnsemblClinVar. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_026751 | 425 | I → V Polymorphism linked with susceptibility to obsessive-compulsive disorder; increased serotonin transport capacity. 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
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_036789 | 465 | F → L. Corresponds to variant dbSNP:rs28914833Ensembl. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_036790 | 550 | L → V. Corresponds to variant dbSNP:rs28914834Ensembl. | 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014182 | 605 | K → N1 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 |
Alternative sequence
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 | X70697 mRNA Translation: CAA50029.1 L05568 mRNA Translation: AAA35492.1 AY902473 mRNA Translation: AAW80933.1 EU099989 Genomic DNA Translation: ABV02581.1 BC069484 mRNA Translation: AAH69484.1 U79746 Genomic DNA Translation: AAB93475.1 AK308014 mRNA No translation available. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS11256.1 [P31645-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A47398 |
NCBI Reference Sequences More...RefSeqi | NP_001036.1, NM_001045.5 [P31645-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.134662 Hs.29792 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000261707; ENSP00000261707; ENSG00000108576 [P31645-1] ENST00000401766; ENSP00000385822; ENSG00000108576 [P31645-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6532 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6532 |
UCSC genome browser More...UCSCi | uc002hey.6 human [P31645-1] |
<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 | |
|---|---|---|---|---|---|
| P31645 | Transporter (Fragment) | 618 | |||
| Serotonin transporter (Fragment) | 164 | ||||
| Serotonin transporter (Fragment) | 164 | ||||
| Serotonin transporter (Fragment) | 164 | ||||
| Serotonin transporter (Fragment) | 164 | ||||
| +118 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P31645 | Transporter (Fragment) | 618 | |||
| Serotonin transporter (Fragment) | 164 | ||||
| Serotonin transporter (Fragment) | 164 | ||||
| Serotonin transporter (Fragment) | 164 | ||||
| Serotonin transporter (Fragment) | 164 | ||||
| +296 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| SHMPD The Singapore human mutation and polymorphism database |
| Wikipedia Serotonin transporter entry |
| Protein Spotlight Love, love, love... -Issue 123 of November 2010 |
| NIEHS-SNPs |
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 | X70697 mRNA Translation: CAA50029.1 L05568 mRNA Translation: AAA35492.1 AY902473 mRNA Translation: AAW80933.1 EU099989 Genomic DNA Translation: ABV02581.1 BC069484 mRNA Translation: AAH69484.1 U79746 Genomic DNA Translation: AAB93475.1 AK308014 mRNA No translation available. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS11256.1 [P31645-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A47398 |
NCBI Reference Sequences More...RefSeqi | NP_001036.1, NM_001045.5 [P31645-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.134662 Hs.29792 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 5I6X | X-ray | 3.14 | A | 76-618 | [»] | |
| 5I6Z | X-ray | 4.53 | A | 76-618 | [»] | |
| 5I71 | X-ray | 3.15 | A | 76-618 | [»] | |
| 5I73 | X-ray | 3.24 | A | 76-618 | [»] | |
| 5I74 | X-ray | 3.40 | A | 76-618 | [»] | |
| 5I75 | X-ray | 3.49 | A | 76-618 | [»] | |
| 6AWN | X-ray | 3.62 | A | 76-618 | [»] | |
| 6AWO | X-ray | 3.53 | A | 76-618 | [»] | |
| 6AWP | X-ray | 3.80 | A | 76-618 | [»] | |
| 6AWQ | X-ray | 4.05 | A | 76-618 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P31645 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P31645 | |||||
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 | 112423, 11 interactors |
Protein interaction database and analysis system More...IntActi | P31645, 2 interactors |
Molecular INTeraction database More...MINTi | P31645 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000261707 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P31645 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL228 |
Drug and drug target database More...DrugBanki | DB01472 4-Methoxyamphetamine DB04836 Amineptine DB00321 Amitriptyline DB00543 Amoxapine DB00182 Amphetamine DB00289 Atomoxetine DB04889 Bicifadine DB09016 Butriptyline DB01114 Chlorphenamine DB00215 Citalopram DB01242 Clomipramine DB00907 Cocaine DB05688 CRx-119 DB01151 Desipramine DB06700 Desvenlafaxine DB01191 Dexfenfluramine DB06701 Dexmethylphenidate DB00514 Dextromethorphan DB00988 Dopamine DB01142 Doxepin DB00476 Duloxetine DB01363 Ephedra DB01175 Escitalopram DB00574 Fenfluramine DB00472 Fluoxetine DB00176 Fluvoxamine DB00458 Imipramine DB08918 Levomilnacipran DB00408 Loxapine DB00579 Mazindol DB01577 Methamphetamine DB09543 Methyl salicylate DB00422 Methylphenidate DB06148 Mianserin DB04896 Milnacipran DB00805 Minaprine DB00370 Mirtazapine DB01442 MMDA DB01149 Nefazodone DB00540 Nortriptyline DB05422 OPC-14523 DB00715 Paroxetine DB00454 Pethidine DB00191 Phentermine DB00344 Protriptyline DB00852 Pseudoephedrine DB01104 Sertraline DB01105 Sibutramine DB06204 Tapentadol DB01079 Tegaserod DB00193 Tramadol DB00656 Trazodone DB00726 Trimipramine DB00285 Venlafaxine DB00661 Verapamil DB06684 Vilazodone DB09068 Vortioxetine DB04832 Zimelidine |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 928 |
Protein family/group databases
Transport Classification Database More...TCDBi | 2.A.22.1.1 the neurotransmitter:sodium symporter (nss) family |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P31645 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P31645 |
Polymorphism and mutation databases
Domain mapping of disease mutations (DMDM) More...DMDMi | 400630 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P31645 |
PeptideAtlas More...PeptideAtlasi | P31645 |
PRoteomics IDEntifications database More...PRIDEi | P31645 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 54798 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000261707; ENSP00000261707; ENSG00000108576 [P31645-1] ENST00000401766; ENSP00000385822; ENSG00000108576 [P31645-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6532 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6532 |
UCSC genome browser More...UCSCi | uc002hey.6 human [P31645-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 6532 |
DisGeNET More...DisGeNETi | 6532 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000108576.9 |
GeneCards: human genes, protein and diseases More...GeneCardsi | SLC6A4 |
Human Gene Nomenclature Database More...HGNCi | HGNC:11050 SLC6A4 |
Human Protein Atlas More...HPAi | HPA071354 HPA074728 |
MalaCards human disease database More...MalaCardsi | SLC6A4 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 103780 phenotype 164230 phenotype 182138 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P31645 |
Open Targets More...OpenTargetsi | ENSG00000108576 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA312 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3659 Eukaryota COG0733 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118857 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000116406 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG071421 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P31645 |
KEGG Orthology (KO) More...KOi | K05037 |
Identification of Orthologs from Complete Genome Data More...OMAi | NMPAATF |
Database of Orthologous Groups More...OrthoDBi | EOG091G08PX |
Database for complete collections of gene phylogenies More...PhylomeDBi | P31645 |
TreeFam database of animal gene trees More...TreeFami | TF343812 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-380615 Serotonin clearance from the synaptic cleft |
SIGNOR Signaling Network Open Resource More...SIGNORi | P31645 |
Miscellaneous databases
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Serotonin_transporter |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 6532 |
Protein Ontology More...PROi | PR:P31645 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000108576 |
CleanEx database of gene expression profiles More...CleanExi | HS_HTT HS_SLC6A4 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P31645 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P31645 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR000175 Na/ntran_symport IPR013086 Na/ntran_symport_serotonin_N IPR037272 SNS_sf |
The PANTHER Classification System More...PANTHERi | PTHR11616 PTHR11616, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF03491 5HT_transport_N, 1 hit PF00209 SNF, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR01203 5HTTRANSPORT PR00176 NANEUSMPORT |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF161070 SSF161070, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00610 NA_NEUROTRAN_SYMP_1, 1 hit PS00754 NA_NEUROTRAN_SYMP_2, 1 hit PS50267 NA_NEUROTRAN_SYMP_3, 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 | SC6A4_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 | P31645Primary (citable) accession number: P31645 Secondary accession number(s): Q5EE02 | |
| <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: | July 1, 1993 |
| Last sequence update: | July 1, 1993 | |
| Last modified: | June 20, 2018 | |
| This is version 180 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
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 17
Human chromosome 17: 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 - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
