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Details on Person UniProt:Q9NRD5 PICK1

Class:IdReferenceGeneProduct:61702
_chainChangeLogchain:1-415 added on Sat February 7 2015
_displayNameUniProt:Q9NRD5 PICK1
_timestamp2025-08-15 21:17:49
chainchain:1-415
checksumC569FD8AA5028B90
commentFUNCTION Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function.SUBUNIT Monomer and homodimer. Interacts with CXADR. Interacts presynaptically with the glutamate receptors GRIA2, GRIA3, GRIK3, isoform 3 of GRIA4, isoform A of GRM4, GRM7 and GRM8; with NAPA and NAPB; and with BTG2. The interaction with NAPA and NAPB disrupts the interaction with GRIA2, conducting to the internalization of GRIA2. Interacts with PRKCA; with the amine transporters SLC6A2 and SLC6A3; with the channels ASIC1 and ASIC2; with the GTP-binding proteins ARF1 and ARF3; with the ephrin receptor tyrosine kinases EPHA7, EPHB1 and EPHB2; with ERBB2 and through its PDZ domain with the C-terminal tail of PRLHR. Interacts with UNC5A. Interacts (via AH domain) with NCS1/FREQ; in a calcium-dependent manner. Interacts with F-actin and associates with the ARP2/3 complex. Interacts (via PDZ domain) with ARF1 (activated); the interaction blocks Arp2/3 complex inhibition. Interacts with SORCS3 (By similarity).INTERACTION Also membrane-associated, present at excitatory synapses.ALTERNATIVE PRODUCTS Ubiquitous.DOMAIN The AH domain mediates binding to F-actin.DOMAIN The unoccupied PDZ domain is probably involved in allosteric modulation by forming an intramolecular bridge with the AH domain leading to a 'closed' formation. Binding of a PDZ ligand, such as GRIA2, allows enhanced interactions with F-actin and the Arp2/3 complex thus enhanced inhibition of actin polymerization (By similarity).PTM Phosphorylation at Thr-82 appears to inhibit the interaction with AMPA receptors.PTM Palmitoylation on Cys-413 is essential for long-term synaptic depression (LTD).
descriptionrecommendedName: PRKCA-binding protein alternativeName: Protein interacting with C kinase 1 alternativeName: Protein kinase C-alpha-binding protein
geneNamePICK1
PRKCABP
identifierQ9NRD5
isSequenceChangedFALSE
keyword3D-structure
Actin-binding
Alternative splicing
Calcium
Cytoplasm
Cytoskeleton
Lipoprotein
Membrane
Metal-binding
Palmitate
Phosphoprotein
Proteomics identification
Reference proteome
Synapse
Synaptosome
Zinc
modified[InstanceEdit:9836292] Weiser, Joel, 2023-05-25
[InstanceEdit:9852000] Weiser, Joel, 2023-11-03
[InstanceEdit:9926675] Weiser, Joel, 2024-11-03
[InstanceEdit:9963647] Weiser, Joel, 2025-08-15
namePICK1
referenceDatabase[ReferenceDatabase:2] UniProt
referenceGene[ReferenceDNASequence:8991477] ENSEMBL:ENSG00000100151 PICK1 [Homo sapiens]
secondaryIdentifierPICK1_HUMAN
B3KS52
O95906
sequenceLength415
species[Species:48887] Homo sapiens
(isoformParent)[ReferenceIsoform:8973415] UniProt:Q9NRD5-1 PICK1 [Homo sapiens]
[ReferenceIsoform:8973416] UniProt:Q9NRD5-2 PICK1 [Homo sapiens]
(referenceEntity)[EntityWithAccessionedSequence:204316] PICK1 [cytosol] [Homo sapiens]
[EntityWithAccessionedSequence:416989] PICK1 [plasma membrane] [Homo sapiens]
[EntityWithAccessionedSequence:417017] PICK1 [endocytic vesicle membrane] [Homo sapiens]
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No pathways have been reviewed or authored by UniProt:Q9NRD5 PICK1 (61702)