<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functionⁱ

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

1. calcium-activated potassium channel 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

   • 20006580

2. outward rectifier potassium channel activity 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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

1. cellular response to pH Source: Ensembl
2. potassium ion export Source: Ensembl
3. potassium ion 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

   • 20006580

<p>UniProtKB Keywords constitute a <a target="_top" href="/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 - Molecular functionⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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 - Biological processⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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 - Ligandⁱ

Enzyme and pathway databases

Protein family/group databases

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Topology

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	1 – 31	31	CytoplasmicSequence Analysis			Add BLAST
<p>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><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	32 – 52	21	HelicalSequence Analysis			Add BLAST
<p>Describes the extent of a region in a membrane, which does not cross it.</p><p><a href='../manual/intramem' target='_top'>More...</a></p>Intramembranei	114 – 140	27	Pore-forming; Name=Pore-forming 1Sequence Analysis			Add BLAST
<p>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><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	142 – 162	21	HelicalSequence Analysis			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	163 – 292	130	CytoplasmicSequence Analysis			Add BLAST
<p>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><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	293 – 313	21	HelicalSequence Analysis			Add BLAST
<p>Describes the extent of a region in a membrane, which does not cross it.</p><p><a href='../manual/intramem' target='_top'>More...</a></p>Intramembranei	326 – 340	15	Pore-forming; Name=Pore-forming 2Sequence Analysis			Add BLAST
<p>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><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	347 – 367	21	HelicalSequence Analysis			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	368 – 394	27	CytoplasmicSequence Analysis			Add BLAST

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

1. integral component of membrane Source: UniProtKB-KW
2. 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

   • 20006580

<p>UniProtKB Keywords constitute a <a target="_top" href="/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

<p>Provides information on the disease(s) and phenotype(s) associated with the deficiency of a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	83 – 83	1	N → Q: Strongly reduced current amplitude and localization to cell membrane. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.9 "N-linked glycosylation determines cell surface expression of two-pore-domain K+ channel TRESK." Egenberger B., Polleichtner G., Wischmeyer E., Doring F. Biochem. Biophys. Res. Commun. 391:1262-1267(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-83, MUTAGENESIS OF ASN-83.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	132 – 132	1	H → N: Insensitive to extracellular protons. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.6 "TRESK two-pore-domain K+ channels constitute a significant component of background potassium currents in murine dorsal root ganglion neurones." Dobler T., Springauf A., Tovornik S., Weber M., Schmitt A., Sedlmeier R., Wischmeyer E., Doring F. J. Physiol. (Lond.) 585:867-879(2007) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, MUTAGENESIS OF HIS-132.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	212 – 212	1	I → A: Loss of interaction with calcineurin and activation by elevated intracellular calcium; when associated with A-214.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	214 – 214	1	I → A: Strongly reduced activation by elevated intracellular calcium. Loss of interaction with calcineurin and activation by elevated intracellular calcium; when associated with A-212.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	264 – 264	1	S → A: Loss of interaction with YWHAH. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.7 "Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation." Czirjak G., Vuity D., Enyedi P. J. Biol. Chem. 283:15672-15680(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH YWHAH, MUTAGENESIS OF SER-264, PHOSPHORYLATION AT SER-264.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	276 – 276	1	S → A: Enhances basal channel activity and abolishes stimulation by calcineurin. 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.1 "The two-pore domain K+ channel, TRESK, is activated by the cytoplasmic calcium signal through calcineurin." Czirjak G., Toth Z.E., Enyedi P. J. Biol. Chem. 279:18550-18558(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF SER-276, PHOSPHORYLATION AT SER-276, TISSUE SPECIFICITY.

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini	1 – 394	394	Potassium channel subfamily K member 18		PRO_0000312501	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	83 – 83	1	N-linked (GlcNAc...)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.9 "N-linked glycosylation determines cell surface expression of two-pore-domain K+ channel TRESK." Egenberger B., Polleichtner G., Wischmeyer E., Doring F. Biochem. Biophys. Res. Commun. 391:1262-1267(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-83, MUTAGENESIS OF ASN-83.
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	264 – 264	1	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 Ref.7 "Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation." Czirjak G., Vuity D., Enyedi P. J. Biol. Chem. 283:15672-15680(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH YWHAH, MUTAGENESIS OF SER-264, PHOSPHORYLATION AT SER-264.
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	276 – 276	1	Phosphoserine1 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 Ref.1 "The two-pore domain K+ channel, TRESK, is activated by the cytoplasmic calcium signal through calcineurin." Czirjak G., Toth Z.E., Enyedi P. J. Biol. Chem. 279:18550-18558(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF SER-276, PHOSPHORYLATION AT SER-276, TISSUE SPECIFICITY.

<p>Describes post-translational modifications (PTMs). This subsection complements the information provided at the sequence level or describes modifications for which position-specific data is not yet available.</p><p><a href='../manual/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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

Proteomic databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>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 the protein level’.</p><p><a href='../manual/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

<p>Provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.</p><p><a href='../manual/developmental_stage' target='_top'>More...</a></p>Developmental stageⁱ

Gene expression databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>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 ‘Function’ section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

Protein-protein interaction databases

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	210 – 215	6	Interaction with calcineurin
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	261 – 266	6	Interaction with YWHAH

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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

Phylogenomic databases

Family and domain databases

<p>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 length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MEAEEPPEAR RCCPEALGKA RGCCPEALGK LLPGLCFLCC LVTYALVGAA 
        60         70         80         90        100
LFSAVEGRPD PEAEENPELK KFLDDLCNIL KCNLTVVEGS RKNLCEHLQH 
       110        120        130        140        150
LKPQWLKAPQ DWSFLSALFF CCTVFSTVGY GHMYPVTRLG KFLCMLYALF 
       160        170        180        190        200
GIPLMFLVLT DIGDILATIL SRAYSRFQAL LCLPHDIFKW RSLPLCRKQP 
       210        220        230        240        250
DSKPVEEAIP QIVIDAGVDE LLNPQPSKDP PSPSCNVELF ERLVAREKKN 
       260        270        280        290        300
KLQPPTRPVE RSNSCPELVL GRLSCSILSN LDEVGQQVER LDIPLPVIAL 
       310        320        330        340        350
VVFAYISCAA AILPFWETEL GFEDAFYFCF VTLTTIGFGD IVLVHPHFFL 
       360        370        380        390 
FFSIYIIVGM EILFIAFKLM QNRLLHTYKT LMLFVCQREV SLPW 

Experimental Info

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	228 – 228	1	K → R in AAI15706. (PubMed:15489334)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	228 – 228	1	K → R in AAI04133. (PubMed:15489334)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	251 – 251	1	K → E in AAI15706. (PubMed:15489334)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	251 – 251	1	K → E in AAI04133. (PubMed:15489334)Curated

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p> Cross-referencesⁱ

<p>Provides links to various web resources that are relevant for a specific protein.</p><p><a href='../manual/web_resource' target='_top'>More...</a></p> Web resourcesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsⁱ

1. "The two-pore domain K+ channel, TRESK, is activated by the cytoplasmic calcium signal through calcineurin."
   Czirjak G., Toth Z.E., Enyedi P.
   J. Biol. Chem. 279:18550-18558(2004) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF SER-276, PHOSPHORYLATION AT SER-276, TISSUE SPECIFICITY.
   Strain: NMRI.
   Tissue: Cerebellum.
   
2. "Species-specific differences in response to anesthetics and other modulators by the K2P channel TRESK."
   Keshavaprasad B., Liu C., Au J.D., Kindler C.H., Cotten J.F., Yost C.S.
   Anesth. Analg. 101:1042-1049(2005) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION.
   Strain: BALB/c.
   Tissue: Spinal cord.
   
3. "The transcriptional landscape of the mammalian genome."
   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.

   , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
   Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
   Strain: C57BL/6J.
   Tissue: Egg.
   
4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
   The MGC Project Team
   Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
5. "Targeting of calcineurin to an NFAT-like docking site is required for the calcium-dependent activation of the background K+ channel, TRESK."
   Czirjak G., Enyedi P.
   J. Biol. Chem. 281:14677-14682(2006) [PubMed] [Europe PMC] [Abstract]
   Cited for: INTERACTION WITH CALCINEURIN.
6. "TRESK two-pore-domain K+ channels constitute a significant component of background potassium currents in murine dorsal root ganglion neurones."
   Dobler T., Springauf A., Tovornik S., Weber M., Schmitt A., Sedlmeier R., Wischmeyer E., Doring F.
   J. Physiol. (Lond.) 585:867-879(2007) [PubMed] [Europe PMC] [Abstract]
   Cited for: TISSUE SPECIFICITY, MUTAGENESIS OF HIS-132.
7. "Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK regulation."
   Czirjak G., Vuity D., Enyedi P.
   J. Biol. Chem. 283:15672-15680(2008) [PubMed] [Europe PMC] [Abstract]
   Cited for: INTERACTION WITH YWHAH, MUTAGENESIS OF SER-264, PHOSPHORYLATION AT SER-264.
8. "Pungent agents from Szechuan peppers excite sensory neurons by inhibiting two-pore potassium channels."
   Bautista D.M., Sigal Y.M., Milstein A.D., Garrison J.L., Zorn J.A., Tsuruda P.R., Nicoll R.A., Julius D.
   Nat. Neurosci. 11:772-779(2008) [PubMed] [Europe PMC] [Abstract]
   Cited for: FUNCTION.
9. "N-linked glycosylation determines cell surface expression of two-pore-domain K+ channel TRESK."
   Egenberger B., Polleichtner G., Wischmeyer E., Doring F.
   Biochem. Biophys. Res. Commun. 391:1262-1267(2010) [PubMed] [Europe PMC] [Abstract]
   Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-83, MUTAGENESIS OF ASN-83.
10. "A dominant-negative mutation in the TRESK potassium channel is linked to familial migraine with aura."
    Lafreniere R.G., Cader M.Z., Poulin J.F., Andres-Enguix I., Simoneau M., Gupta N., Boisvert K., Lafreniere F., McLaughlan S., Dube M.P., Marcinkiewicz M.M., Ramagopalan S., Ansorge O., Brais B., Sequeiros J., Pereira-Monteiro J.M., Griffiths L.R., Tucker S.J., Ebers G., Rouleau G.A.
    Nat. Med. 16:1157-1160(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

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<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Miscellaneous

<p>UniProtKB Keywords constitute a <a target="_top" href="/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

Documents

1. MGD cross-references
   Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
2. Protein Spotlight
   Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
3. SIMILARITY comments
   Index of protein domains and families

External Data

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ