Q62083
uniprot
Q62083
canonical
amino_acid_sequence
MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGKSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIGPRRALYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKMELLDQKHVQDIVFQLQRFVSTMSKYYNDCYAVLQDADVFPIEVDLAHTTLAYGPNQGSFTDGEEEDEEEEDGAAREVSKDACGATGPTDKGGSWCDS
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:14976185, ECO:0000269|PubMed:20445062}.
uniprot
proteins
mass_dalton
46597
uniprot
proteins
mutagenesis
MUTAGEN 27..28; /note="KD->AA: Abolishes interaction with other proteins, but not with itself. Partial loss of the ASIC1/ASIC3 channel regulation by PKC."; /evidence="ECO:0000269|PubMed:14976185, ECO:0000269|PubMed:9405395"; MUTAGEN 27; /note="K->A: Does not abolish the interaction with PKCA."; /evidence="ECO:0000269|PubMed:14976185, ECO:0000269|PubMed:9405395"; MUTAGEN 414; /note="C->S: Fails to rescue cerebellar LTD in PICK1 knockouts."; /evidence="ECO:0000269|PubMed:24068808
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-82 appears to inhibit the interaction with AMPA receptors (By similarity). Phosphorylated on tyrosine residues by EPHB2 and on serine or threonine residues by PKC. {ECO:0000250, ECO:0000269|PubMed:7844141, ECO:0000269|PubMed:9883737}.; PTM: Palmitoylation on Cys-414 is essential for long-term synaptic depression (LTD). {ECO:0000269|PubMed:24068808}.
uniprot
proteins
pubmed
10340301
uniprot
proteins
pubmed
11278603
uniprot
proteins
pubmed
12065412
uniprot
proteins
pubmed
14976185
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20445062
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24068808
uniprot
proteins
pubmed
24069373
uniprot
proteins
pubmed
7844141
uniprot
proteins
pubmed
9405395
uniprot
proteins
pubmed
9883737
uniprot
proteins
sequence_length
416
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9EP80}. Membrane {ECO:0000250|UniProtKB:Q9EP80}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9EP80}. Membrane {ECO:0000269|PubMed:24068808}; Lipid-anchor {ECO:0000269|PubMed:24068808}. Postsynaptic density {ECO:0000269|PubMed:24069373}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q9EP80}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9EP80}. Note=Also membrane-associated, present at excitatory synapses. {ECO:0000250|UniProtKB:Q9EP80}.
uniprot
proteins