PICK1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PICK1_RAT
• UniProt AC: Q9EP80
• Protein Name: PRKCA-binding protein
• Gene Name: Pick1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 416
• Subcellular Localization: Cytoplasm, perinuclear region . Membrane ; Peripheral membrane protein . Membrane; Lipid-anchor. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . Cell junction, synapse, synaptosome . Cytoplasm, cytoskeleton . Also membrane-
• Protein Description: 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 competetive 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..
• Protein Sequence: MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKMELLDQKHVQDIVFQLQRFVSTMSKYYNDCYAVLRDADVFPIEVDLAHTTLAYGPNQGGFTDGEDEEEEEEDGAAREVSKDARGATGPTDKGGSWCDS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
77	Phosphorylation	ITGVNGRSIKGKTKV EECCCCCCCCCCCHH	30.01	22129425
82	Phosphorylation	GRSIKGKTKVEVAKM CCCCCCCCHHHHHHH	49.33	20403402
167	Phosphorylation	AELYKGMTEHTKNLL HHHHCHHHHHHHHHH	33.03	16641100
170	Phosphorylation	YKGMTEHTKNLLRAF HCHHHHHHHHHHHHH	18.52	16641100
183	Phosphorylation	AFYELSQTHRAFGDV HHHHHHHHHHHHCCE	15.23	16641100
367	Phosphorylation	IEVDLAHTTLAYGPN EEEEECCEECCCCCC	20.21	22673903
368	Phosphorylation	EVDLAHTTLAYGPNQ EEEECCEECCCCCCC	10.26	22673903
371	Phosphorylation	LAHTTLAYGPNQGGF ECCEECCCCCCCCCC	35.91	22673903
379	Phosphorylation	GPNQGGFTDGEDEEE CCCCCCCCCCCCHHH	46.50	22673903
414	S-palmitoylation	TDKGGSWCDS----- CCCCCCCCCC-----	3.84	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
77	S	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
82	T	Phosphorylation	Phosphorylation at Thr-82 appears to inhibit the interaction with AMPA receptors.	-
414	C	Palmitoylation	Palmitoylation on Cys-414 is essential for long-term synaptic depression (LTD).	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PICK1_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BTG2_HUMAN	BTG2	physical	11237868

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.