Calcium-binding protein 39

<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>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

• kinase binding Source: BHF-UCL <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%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.9

    "Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation."
    Zeqiraj E., Filippi B.M., Deak M., Alessi D.R., van Aalten D.M.
    Science 326:1707-1711(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-341 IN COMPLEX WITH STK11/LKB1 AND STRADA, IDENTIFICATION IN A COMPLEX WITH STK11/LKB1 AND STRADA, FUNCTION, MUTAGENESIS OF ARG-240 AND PHE-243.
• protein kinase activator 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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.9

    "Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation."
    Zeqiraj E., Filippi B.M., Deak M., Alessi D.R., van Aalten D.M.
    Science 326:1707-1711(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-341 IN COMPLEX WITH STK11/LKB1 AND STRADA, IDENTIFICATION IN A COMPLEX WITH STK11/LKB1 AND STRADA, FUNCTION, MUTAGENESIS OF ARG-240 AND PHE-243.
• protein serine/threonine kinase activator activity Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • Ref.9

    "Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation."
    Zeqiraj E., Filippi B.M., Deak M., Alessi D.R., van Aalten D.M.
    Science 326:1707-1711(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-341 IN COMPLEX WITH STK11/LKB1 AND STRADA, IDENTIFICATION IN A COMPLEX WITH STK11/LKB1 AND STRADA, FUNCTION, MUTAGENESIS OF ARG-240 AND PHE-243.
  • "The WNK-regulated SPAK/OSR1 kinases directly phosphorylate and inhibit the K+-Cl- co-transporters."
    de Los Heros P., Alessi D.R., Gourlay R., Campbell D.G., Deak M., Macartney T.J., Kahle K.T., Zhang J.
    Biochem J 458:559-573(2014) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• cell cycle arrest Source: Reactome
• cellular hypotonic response Source: ParkinsonsUK-UCL <p>Inferred by Curator</p> <p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence<br />is available.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ic">GO evidence code guide</a></p> Inferred by curatorⁱ
  • "The WNK-regulated SPAK/OSR1 kinases directly phosphorylate and inhibit the K+-Cl- co-transporters."
    de Los Heros P., Alessi D.R., Gourlay R., Campbell D.G., Deak M., Macartney T.J., Kahle K.T., Zhang J.
    Biochem J 458:559-573(2014) [PubMed] [Europe PMC] [Abstract]
• intracellular signal transduction Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "The WNK-regulated SPAK/OSR1 kinases directly phosphorylate and inhibit the K+-Cl- co-transporters."
    de Los Heros P., Alessi D.R., Gourlay R., Campbell D.G., Deak M., Macartney T.J., Kahle K.T., Zhang J.
    Biochem J 458:559-573(2014) [PubMed] [Europe PMC] [Abstract]
• negative regulation of potassium ion transmembrane transport Source: ParkinsonsUK-UCLInferred by curatorⁱ
  • "The WNK-regulated SPAK/OSR1 kinases directly phosphorylate and inhibit the K+-Cl- co-transporters."
    de Los Heros P., Alessi D.R., Gourlay R., Campbell D.G., Deak M., Macartney T.J., Kahle K.T., Zhang J.
    Biochem J 458:559-573(2014) [PubMed] [Europe PMC] [Abstract]
• negative regulation of potassium ion transmembrane transporter activity Source: ParkinsonsUK-UCLInferred by curatorⁱ
  • "The WNK-regulated SPAK/OSR1 kinases directly phosphorylate and inhibit the K+-Cl- co-transporters."
    de Los Heros P., Alessi D.R., Gourlay R., Campbell D.G., Deak M., Macartney T.J., Kahle K.T., Zhang J.
    Biochem J 458:559-573(2014) [PubMed] [Europe PMC] [Abstract]
• neutrophil degranulation Source: Reactome
• peptidyl-serine phosphorylation Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "The WNK-regulated SPAK/OSR1 kinases directly phosphorylate and inhibit the K+-Cl- co-transporters."
    de Los Heros P., Alessi D.R., Gourlay R., Campbell D.G., Deak M., Macartney T.J., Kahle K.T., Zhang J.
    Biochem J 458:559-573(2014) [PubMed] [Europe PMC] [Abstract]
• positive regulation of peptidyl-threonine phosphorylation Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "The WNK-regulated SPAK/OSR1 kinases directly phosphorylate and inhibit the K+-Cl- co-transporters."
    de Los Heros P., Alessi D.R., Gourlay R., Campbell D.G., Deak M., Macartney T.J., Kahle K.T., Zhang J.
    Biochem J 458:559-573(2014) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein serine/threonine kinase activity Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • Ref.9

    "Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation."
    Zeqiraj E., Filippi B.M., Deak M., Alessi D.R., van Aalten D.M.
    Science 326:1707-1711(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-341 IN COMPLEX WITH STK11/LKB1 AND STRADA, IDENTIFICATION IN A COMPLEX WITH STK11/LKB1 AND STRADA, FUNCTION, MUTAGENESIS OF ARG-240 AND PHE-243.
  • "The WNK-regulated SPAK/OSR1 kinases directly phosphorylate and inhibit the K+-Cl- co-transporters."
    de Los Heros P., Alessi D.R., Gourlay R., Campbell D.G., Deak M., Macartney T.J., Kahle K.T., Zhang J.
    Biochem J 458:559-573(2014) [PubMed] [Europe PMC] [Abstract]
• response to activity Source: Ensembl
• response to thyroid hormone Source: Ensembl
• signal transduction Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "The WNK-regulated SPAK/OSR1 kinases directly phosphorylate and inhibit the K+-Cl- co-transporters."
    de Los Heros P., Alessi D.R., Gourlay R., Campbell D.G., Deak M., Macartney T.J., Kahle K.T., Zhang J.
    Biochem J 458:559-573(2014) [PubMed] [Europe PMC] [Abstract]

Enzyme and pathway databases

<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

Organism-specific databases

<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

• UniProt annotation
• GO - Cellular component

<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

<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

Organism-specific databases

Miscellaneous databases

Chemistry databases

Genetic variation databases

<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

Proteomic databases

PTM databases

<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

Gene expression databases

Organism-specific databases

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• kinase binding Source: BHF-UCLInferred from physical interactionⁱ
  • Ref.9

    "Structure of the LKB1-STRAD-MO25 complex reveals an allosteric mechanism of kinase activation."
    Zeqiraj E., Filippi B.M., Deak M., Alessi D.R., van Aalten D.M.
    Science 326:1707-1711(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-341 IN COMPLEX WITH STK11/LKB1 AND STRADA, IDENTIFICATION IN A COMPLEX WITH STK11/LKB1 AND STRADA, FUNCTION, MUTAGENESIS OF ARG-240 AND PHE-243.

Protein-protein interaction databases

Miscellaneous databases

<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

3D structure databases

Miscellaneous databases

<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

<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

Phylogenomic databases

Family and domain databases

<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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MPFPFGKSHK SPADIVKNLK ESMAVLEKQD ISDKKAEKAT EEVSKNLVAM 
        60         70         80         90        100
KEILYGTNEK EPQTEAVAQL AQELYNSGLL STLVADLQLI DFEGKKDVAQ 
       110        120        130        140        150
IFNNILRRQI GTRTPTVEYI CTQQNILFML LKGYESPEIA LNCGIMLREC 
       160        170        180        190        200
IRHEPLAKII LWSEQFYDFF RYVEMSTFDI ASDAFATFKD LLTRHKLLSA 
       210        220        230        240        250
EFLEQHYDRF FSEYEKLLHS ENYVTKRQSL KLLGELLLDR HNFTIMTKYI 
       260        270        280        290        300
SKPENLKLMM NLLRDKSRNI QFEAFHVFKV FVANPNKTQP ILDILLKNQA 
       310        320        330        340 
KLIEFLSKFQ NDRTEDEQFN DEKTYLVKQI RDLKRPAQQE A          

Sequence databases

Genome annotation databases

<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

• 100% Identity
• 90% Identity
• 50% Identity

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

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Genetic variation 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>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<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

Keywords - Technical termⁱ

Documents

1. Human chromosome 2
   Human chromosome 2: entries, gene names and cross-references to MIM
2. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
3. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
4. SIMILARITY comments
   Index of protein domains and families