PRKCA-binding protein

<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

Sites

<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 <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.11

    "Inhibition of Arp2/3-mediated actin polymerization by PICK1 regulates neuronal morphology and AMPA receptor endocytosis."
    Rocca D.L., Martin S., Jenkins E.L., Hanley J.G.
    Nat. Cell Biol. 10:259-271(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, ACTIN-BINDING, ASSOCIATION WITH THE ARP2/3 COMPLEX, MUTAGENESIS OF 251-LYS-LYS-252 AND TRP-413.
• Arp2/3 complex binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.11

    "Inhibition of Arp2/3-mediated actin polymerization by PICK1 regulates neuronal morphology and AMPA receptor endocytosis."
    Rocca D.L., Martin S., Jenkins E.L., Hanley J.G.
    Nat. Cell Biol. 10:259-271(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, ACTIN-BINDING, ASSOCIATION WITH THE ARP2/3 COMPLEX, MUTAGENESIS OF 251-LYS-LYS-252 AND TRP-413.
• cytoskeletal protein binding Source: RGD <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.11

    "Inhibition of Arp2/3-mediated actin polymerization by PICK1 regulates neuronal morphology and AMPA receptor endocytosis."
    Rocca D.L., Martin S., Jenkins E.L., Hanley J.G.
    Nat. Cell Biol. 10:259-271(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, ACTIN-BINDING, ASSOCIATION WITH THE ARP2/3 COMPLEX, MUTAGENESIS OF 251-LYS-LYS-252 AND TRP-413.
• enzyme binding Source: RGD
• ephrin receptor binding Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • "Molecular determinants for the complex binding specificity of the PDZ domain in PICK1."
    Madsen K.L., Beuming T., Niv M.Y., Chang C.W., Dev K.K., Weinstein H., Gether U.
    J Biol Chem 280:20539-20548(2005) [PubMed] [Europe PMC] [Abstract]
• G protein-coupled glutamate receptor binding Source: UniProtKBTraceable author statementⁱ
  • "Molecular determinants for the complex binding specificity of the PDZ domain in PICK1."
    Madsen K.L., Beuming T., Niv M.Y., Chang C.W., Dev K.K., Weinstein H., Gether U.
    J Biol Chem 280:20539-20548(2005) [PubMed] [Europe PMC] [Abstract]
• G protein-coupled receptor binding Source: ParkinsonsUK-UCLInferred from physical interactionⁱ
  • "The protein interacting with C-kinase (PICK1) interacts with and attenuates parkin-associated endothelial-like (PAEL) receptor-mediated cell death."
    Dutta P., O'Connell K.E., Ozkan S.B., Sailer A.W., Dev K.K.
    J Neurochem 130:360-373(2014) [PubMed] [Europe PMC] [Abstract]
• GTPase binding Source: UniProtKBTraceable author statementⁱ
  • "Molecular determinants for the complex binding specificity of the PDZ domain in PICK1."
    Madsen K.L., Beuming T., Niv M.Y., Chang C.W., Dev K.K., Weinstein H., Gether U.
    J Biol Chem 280:20539-20548(2005) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.1

    "Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1."
    Xia J., Zhang X., Staudinger J., Huganir R.L.
    Neuron 22:179-187(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GRIA2; GRIA3 AND ISOFORM 4C OF GRIA4, MUTAGENESIS OF 27-LYS-ASP-28.
• ionotropic glutamate receptor binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.7

    "NSF ATPase and alpha-/beta-SNAPs disassemble the AMPA receptor-PICK1 complex."
    Hanley J.G., Khatri L., Hanson P.I., Ziff E.B.
    Neuron 34:53-67(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH NAPA AND NAPB.
• membrane curvature sensor activity Source: RGD
• metal ion binding Source: UniProtKB-KW
• phospholipid binding Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• protein C-terminus binding Source: RGDInferred from physical interactionⁱ
  • "PICK1 interacts with and regulates PKC phosphorylation of mGLUR7."
    Dev K.K., Nakajima Y., Kitano J., Braithwaite S.P., Henley J.M., Nakanishi S.
    J Neurosci 20:7252-7257(2000) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: RGD <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%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "PICK1-ICA69 heteromeric BAR domain complex regulates synaptic targeting and surface expression of AMPA receptors."
    Cao M., Xu J., Shen C., Kam C., Huganir R.L., Xia J.
    J Neurosci 27:12945-12956(2007) [PubMed] [Europe PMC] [Abstract]
• protein kinase C binding Source: UniProtKBInferred from direct assayⁱ
  • "Molecular determinants for the complex binding specificity of the PDZ domain in PICK1."
    Madsen K.L., Beuming T., Niv M.Y., Chang C.W., Dev K.K., Weinstein H., Gether U.
    J Biol Chem 280:20539-20548(2005) [PubMed] [Europe PMC] [Abstract]
• receptor tyrosine kinase binding Source: UniProtKBTraceable author statementⁱ
  • "Molecular determinants for the complex binding specificity of the PDZ domain in PICK1."
    Madsen K.L., Beuming T., Niv M.Y., Chang C.W., Dev K.K., Weinstein H., Gether U.
    J Biol Chem 280:20539-20548(2005) [PubMed] [Europe PMC] [Abstract]
• signaling receptor binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.1

    "Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1."
    Xia J., Zhang X., Staudinger J., Huganir R.L.
    Neuron 22:179-187(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GRIA2; GRIA3 AND ISOFORM 4C OF GRIA4, MUTAGENESIS OF 27-LYS-ASP-28.
• SNAP receptor activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.7

    "NSF ATPase and alpha-/beta-SNAPs disassemble the AMPA receptor-PICK1 complex."
    Hanley J.G., Khatri L., Hanson P.I., Ziff E.B.
    Neuron 34:53-67(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH NAPA AND NAPB.

GO - Biological processⁱ

• cellular response to decreased oxygen levels Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.15

    "The antagonistic modulation of Arp2/3 activity by N-WASP, WAVE2 and PICK1 defines dynamic changes in astrocyte morphology."
    Murk K., Blanco Suarez E.M., Cockbill L.M., Banks P., Hanley J.G.
    J. Cell Sci. 126:3873-3883(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• cellular response to glucose starvation Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.15

    "The antagonistic modulation of Arp2/3 activity by N-WASP, WAVE2 and PICK1 defines dynamic changes in astrocyte morphology."
    Murk K., Blanco Suarez E.M., Cockbill L.M., Banks P., Hanley J.G.
    J. Cell Sci. 126:3873-3883(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• dendritic spine maintenance Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.11

    "Inhibition of Arp2/3-mediated actin polymerization by PICK1 regulates neuronal morphology and AMPA receptor endocytosis."
    Rocca D.L., Martin S., Jenkins E.L., Hanley J.G.
    Nat. Cell Biol. 10:259-271(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, ACTIN-BINDING, ASSOCIATION WITH THE ARP2/3 COMPLEX, MUTAGENESIS OF 251-LYS-LYS-252 AND TRP-413.
• dendritic spine organization Source: UniProtKBInferred from direct assayⁱ
  • Ref.13

    "PICK1 inhibition of the Arp2/3 complex controls dendritic spine size and synaptic plasticity."
    Nakamura Y., Wood C.L., Patton A.P., Jaafari N., Henley J.M., Mellor J.R., Hanley J.G.
    EMBO J. 30:719-730(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• dopamine transport Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#nas">GO evidence code guide</a></p> Non-traceable author statementⁱ
  • "Molecular determinants for the complex binding specificity of the PDZ domain in PICK1."
    Madsen K.L., Beuming T., Niv M.Y., Chang C.W., Dev K.K., Weinstein H., Gether U.
    J Biol Chem 280:20539-20548(2005) [PubMed] [Europe PMC] [Abstract]
• glial cell development Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.15

    "The antagonistic modulation of Arp2/3 activity by N-WASP, WAVE2 and PICK1 defines dynamic changes in astrocyte morphology."
    Murk K., Blanco Suarez E.M., Cockbill L.M., Banks P., Hanley J.G.
    J. Cell Sci. 126:3873-3883(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• intracellular protein transport Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• long-term synaptic depression Source: UniProtKBInferred from direct assayⁱ
  • Ref.13

    "PICK1 inhibition of the Arp2/3 complex controls dendritic spine size and synaptic plasticity."
    Nakamura Y., Wood C.L., Patton A.P., Jaafari N., Henley J.M., Mellor J.R., Hanley J.G.
    EMBO J. 30:719-730(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• monoamine transport Source: UniProtKB
• negative regulation of Arp2/3 complex-mediated actin nucleation Source: UniProtKBInferred from direct assayⁱ
  • Ref.11

    "Inhibition of Arp2/3-mediated actin polymerization by PICK1 regulates neuronal morphology and AMPA receptor endocytosis."
    Rocca D.L., Martin S., Jenkins E.L., Hanley J.G.
    Nat. Cell Biol. 10:259-271(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, ACTIN-BINDING, ASSOCIATION WITH THE ARP2/3 COMPLEX, MUTAGENESIS OF 251-LYS-LYS-252 AND TRP-413.
• negative regulation of cell death Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "The protein interacting with C-kinase (PICK1) interacts with and attenuates parkin-associated endothelial-like (PAEL) receptor-mediated cell death."
    Dutta P., O'Connell K.E., Ozkan S.B., Sailer A.W., Dev K.K.
    J Neurochem 130:360-373(2014) [PubMed] [Europe PMC] [Abstract]
• negative regulation of gene expression Source: ParkinsonsUK-UCLInferred from mutant phenotypeⁱ
  • "The protein interacting with C-kinase (PICK1) interacts with and attenuates parkin-associated endothelial-like (PAEL) receptor-mediated cell death."
    Dutta P., O'Connell K.E., Ozkan S.B., Sailer A.W., Dev K.K.
    J Neurochem 130:360-373(2014) [PubMed] [Europe PMC] [Abstract]
• positive regulation of receptor internalization Source: UniProtKBInferred from direct assayⁱ
  • Ref.11

    "Inhibition of Arp2/3-mediated actin polymerization by PICK1 regulates neuronal morphology and AMPA receptor endocytosis."
    Rocca D.L., Martin S., Jenkins E.L., Hanley J.G.
    Nat. Cell Biol. 10:259-271(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, ACTIN-BINDING, ASSOCIATION WITH THE ARP2/3 COMPLEX, MUTAGENESIS OF 251-LYS-LYS-252 AND TRP-413.
• protein kinase C-activating G protein-coupled receptor signaling pathway Source: UniProtKB
• protein phosphorylation Source: UniProtKBInferred from direct assayⁱ
  • Ref.3

    "Mitogen-stimulated TIS21 protein interacts with a protein-kinase-Calpha-binding protein rPICK1."
    Lin W.-J., Chang Y.-F., Wang W.-L., Huang C.-Y.F.
    Biochem. J. 354:635-643(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH BTG2.
• protein targeting Source: RGD
• receptor clustering Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.1

    "Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1."
    Xia J., Zhang X., Staudinger J., Huganir R.L.
    Neuron 22:179-187(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GRIA2; GRIA3 AND ISOFORM 4C OF GRIA4, MUTAGENESIS OF 27-LYS-ASP-28.
• regulation of Arp2/3 complex-mediated actin nucleation Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• regulation of insulin secretion Source: RGD
• regulation of postsynaptic neurotransmitter receptor internalization Source: SynGOInferred from direct assayⁱ
  • "PICK1 regulates AMPA receptor endocytosis via direct interactions with AP2 alpha-appendage and dynamin."
    Fiuza M., Rostosky C.M., Parkinson G.T., Bygrave A.M., Halemani N., Baptista M., Milosevic I., Hanley J.G.
    J Cell Biol 216:3323-3338(2017) [PubMed] [Europe PMC] [Abstract]

<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

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

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

<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

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Keywords - PTMⁱ

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

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

<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

• actin filament binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.11

    "Inhibition of Arp2/3-mediated actin polymerization by PICK1 regulates neuronal morphology and AMPA receptor endocytosis."
    Rocca D.L., Martin S., Jenkins E.L., Hanley J.G.
    Nat. Cell Biol. 10:259-271(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, ACTIN-BINDING, ASSOCIATION WITH THE ARP2/3 COMPLEX, MUTAGENESIS OF 251-LYS-LYS-252 AND TRP-413.
• cytoskeletal protein binding Source: RGDInferred from physical interactionⁱ
  • Ref.11

    "Inhibition of Arp2/3-mediated actin polymerization by PICK1 regulates neuronal morphology and AMPA receptor endocytosis."
    Rocca D.L., Martin S., Jenkins E.L., Hanley J.G.
    Nat. Cell Biol. 10:259-271(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, ACTIN-BINDING, ASSOCIATION WITH THE ARP2/3 COMPLEX, MUTAGENESIS OF 251-LYS-LYS-252 AND TRP-413.
• enzyme binding Source: RGD
• ephrin receptor binding Source: UniProtKBTraceable author statementⁱ
  • "Molecular determinants for the complex binding specificity of the PDZ domain in PICK1."
    Madsen K.L., Beuming T., Niv M.Y., Chang C.W., Dev K.K., Weinstein H., Gether U.
    J Biol Chem 280:20539-20548(2005) [PubMed] [Europe PMC] [Abstract]
• G protein-coupled glutamate receptor binding Source: UniProtKBTraceable author statementⁱ
  • "Molecular determinants for the complex binding specificity of the PDZ domain in PICK1."
    Madsen K.L., Beuming T., Niv M.Y., Chang C.W., Dev K.K., Weinstein H., Gether U.
    J Biol Chem 280:20539-20548(2005) [PubMed] [Europe PMC] [Abstract]
• G protein-coupled receptor binding Source: ParkinsonsUK-UCLInferred from physical interactionⁱ
  • "The protein interacting with C-kinase (PICK1) interacts with and attenuates parkin-associated endothelial-like (PAEL) receptor-mediated cell death."
    Dutta P., O'Connell K.E., Ozkan S.B., Sailer A.W., Dev K.K.
    J Neurochem 130:360-373(2014) [PubMed] [Europe PMC] [Abstract]
• GTPase binding Source: UniProtKBTraceable author statementⁱ
  • "Molecular determinants for the complex binding specificity of the PDZ domain in PICK1."
    Madsen K.L., Beuming T., Niv M.Y., Chang C.W., Dev K.K., Weinstein H., Gether U.
    J Biol Chem 280:20539-20548(2005) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.1

    "Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1."
    Xia J., Zhang X., Staudinger J., Huganir R.L.
    Neuron 22:179-187(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GRIA2; GRIA3 AND ISOFORM 4C OF GRIA4, MUTAGENESIS OF 27-LYS-ASP-28.
• ionotropic glutamate receptor binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.7

    "NSF ATPase and alpha-/beta-SNAPs disassemble the AMPA receptor-PICK1 complex."
    Hanley J.G., Khatri L., Hanson P.I., Ziff E.B.
    Neuron 34:53-67(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH NAPA AND NAPB.
• protein C-terminus binding Source: RGDInferred from physical interactionⁱ
  • "PICK1 interacts with and regulates PKC phosphorylation of mGLUR7."
    Dev K.K., Nakajima Y., Kitano J., Braithwaite S.P., Henley J.M., Nakanishi S.
    J Neurosci 20:7252-7257(2000) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: RGDInferred from mutant phenotypeⁱ
  • "PICK1-ICA69 heteromeric BAR domain complex regulates synaptic targeting and surface expression of AMPA receptors."
    Cao M., Xu J., Shen C., Kam C., Huganir R.L., Xia J.
    J Neurosci 27:12945-12956(2007) [PubMed] [Europe PMC] [Abstract]
• protein kinase C binding Source: UniProtKBInferred from direct assayⁱ
  • "Molecular determinants for the complex binding specificity of the PDZ domain in PICK1."
    Madsen K.L., Beuming T., Niv M.Y., Chang C.W., Dev K.K., Weinstein H., Gether U.
    J Biol Chem 280:20539-20548(2005) [PubMed] [Europe PMC] [Abstract]
• receptor tyrosine kinase binding Source: UniProtKBTraceable author statementⁱ
  • "Molecular determinants for the complex binding specificity of the PDZ domain in PICK1."
    Madsen K.L., Beuming T., Niv M.Y., Chang C.W., Dev K.K., Weinstein H., Gether U.
    J Biol Chem 280:20539-20548(2005) [PubMed] [Europe PMC] [Abstract]
• signaling receptor binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.1

    "Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1."
    Xia J., Zhang X., Staudinger J., Huganir R.L.
    Neuron 22:179-187(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GRIA2; GRIA3 AND ISOFORM 4C OF GRIA4, MUTAGENESIS OF 27-LYS-ASP-28.

Protein-protein interaction 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

Domains and Repeats

Compositional bias

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

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
MFADLDYDIE EDKLGIPTVP GKVTLQKDAQ NLIGISIGGG AQYCPCLYIV 
        60         70         80         90        100
QVFDNTPAAL DGTVAAGDEI TGVNGRSIKG KTKVEVAKMI QEVKGEVTIH 
       110        120        130        140        150
YNKLQADPKQ GMSLDIVLKK VKHRLVENMS SGTADALGLS RAILCNDGLV 
       160        170        180        190        200
KRLEELERTA ELYKGMTEHT KNLLRAFYEL SQTHRAFGDV FSVIGVREPQ 
       210        220        230        240        250
PAASEAFVKF ADAHRSIEKF GIRLLKTIKP MLTDLNTYLN KAIPDTRLTI 
       260        270        280        290        300
KKYLDVKFEY LSYCLKVKEM DDEEYSCIAL GEPLYRVSTG NYEYRLILRC 
       310        320        330        340        350
RQEARARFSQ MRKDVLEKME LLDQKHVQDI VFQLQRFVST MSKYYNDCYA 
       360        370        380        390        400
VLRDADVFPI EVDLAHTTLA YGPNQGGFTD GEDEEEEEED GAAREVSKDA 
       410 
RGATGPTDKG GSWCDS                                      

Experimental Info

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

• 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

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous 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. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references