PICK1_HUMAN - dbPTM
PICK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PICK1_HUMAN
UniProt AC Q9NRD5
Protein Name PRKCA-binding protein
Gene Name PICK1
Organism Homo sapiens (Human).
Sequence Length 415
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-associ
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 MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGRSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKMELLDQKHVQDIVFQLQRLVSTMSKYYNDCYAVLRDADVFPIEVDLAHTTLAYGLNQEEFTDGEEEEEEEDTAAGEPSRDTRGAAGPLDKGGSWCDS
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 Orthologous
Protein Cluster
7Phosphorylation-MFADLDYDIEEDKL
-CCCCCCCCCCCCCC		26.5627642862
18PhosphorylationEDKLGIPTVPGKVTL
CCCCCCCCCCCEEEE		37.0921406692
82PhosphorylationGRSIKGKTKVEVAKM
CCCCCCCCHHHHHHH		49.3320403402
103UbiquitinationEVTIHYNKLQADPKQ
EEEEEEECCCCCCCC		34.51-
109UbiquitinationNKLQADPKQGMSLDI
ECCCCCCCCCCCHHH		61.09-
130PhosphorylationHRLVENMSSGTADAL
HHHHHCCCCCHHHHH		36.8823898821
131PhosphorylationRLVENMSSGTADALG
HHHHCCCCCHHHHHC		29.4223898821
133PhosphorylationVENMSSGTADALGLS
HHCCCCCHHHHHCCH		24.2623898821
140PhosphorylationTADALGLSRAILCND
HHHHHCCHHHHHCCC		20.1923898821
151UbiquitinationLCNDGLVKRLEELER
HCCCCHHHHHHHHHH		57.20-
164UbiquitinationERTAELYKGMTEHTK
HHHHHHHCHHHHHHH		55.63-
209UbiquitinationAASEAFVKFADAHRS
CHHHHHHHHHHHCHH		28.5121890473
209UbiquitinationAASEAFVKFADAHRS
CHHHHHHHHHHHCHH		28.5121890473
216PhosphorylationKFADAHRSIEKFGIR
HHHHHCHHHHHHHHH		25.8227174698
219UbiquitinationDAHRSIEKFGIRLLK
HHCHHHHHHHHHHHH		47.42-
285PhosphorylationIALGEPLYRVSTGNY
EEECCCEEEEECCCE		21.49-
292PhosphorylationYRVSTGNYEYRLILR
EEEECCCEEEEEEHH		18.71-
318UbiquitinationMRKDVLEKMELLDQK
HHHHHHHHHHHHCHH		33.25-
339PhosphorylationFQLQRLVSTMSKYYN
HHHHHHHHHHHHHHH		24.00-
342PhosphorylationQRLVSTMSKYYNDCY
HHHHHHHHHHHHHHH		20.00-
349PhosphorylationSKYYNDCYAVLRDAD
HHHHHHHHHHHHCCC		11.56-
367PhosphorylationIEVDLAHTTLAYGLN
EEEEEHHHHHHCCCC		20.2129496963
371PhosphorylationLAHTTLAYGLNQEEF
EHHHHHHCCCCHHHC		25.8428348404
379PhosphorylationGLNQEEFTDGEEEEE
CCCHHHCCCCCHHHH		46.5026657352
408UbiquitinationGAAGPLDKGGSWCDS
CCCCCCCCCCCCCCC		73.23-
411PhosphorylationGPLDKGGSWCDS---
CCCCCCCCCCCC---		32.9524719451
413S-palmitoylationLDKGGSWCDS-----
CCCCCCCCCC-----		3.84-
415PhosphorylationKGGSWCDS-------
CCCCCCCC-------		38.7024719451
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
342SPhosphorylationKinaseGSK3BP49841
PSP
415SPhosphorylationKinaseGSK3BP49841
PSP
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:17553932
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
82TPhosphorylation

20403402
413CPalmitoylation

-
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PICK1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRM7_HUMANGRM7physical
11007882
ERBB2_HUMANERBB2physical
11278603
GRIA4_HUMANGRIA4physical
11891216
GRIA2_HUMANGRIA2physical
11891216
GRIA3_HUMANGRIA3physical
11891216
ASIC1_HUMANASIC1physical
11802773
BNC1_HUMANBNC1physical
11802773
PRKN_HUMANPARK2physical
17553932
GPR37_HUMANGPR37physical
24749734
FHOD1_HUMANFHOD1physical
26186194
EPHA7_HUMANEPHA7physical
26186194
UACA_HUMANUACAphysical
26186194
ZNF24_HUMANZNF24physical
26186194
ICA1L_HUMANICA1Lphysical
26186194
ICA69_HUMANICA1physical
26186194
KLH11_HUMANKLHL11physical
26186194
CEP89_HUMANCEP89physical
26186194
F117A_HUMANFAM117Aphysical
26186194
GNPTA_HUMANGNPTABphysical
26186194
ITA6_HUMANITGA6physical
26186194
JAM1_HUMANF11Rphysical
26186194
QSOX2_HUMANQSOX2physical
26186194
ARFP1_HUMANARFIP1physical
26186194
AAED1_HUMANAAED1physical
26186194
EFNB1_HUMANEFNB1physical
26186194
PKD2_HUMANPKD2physical
26186194
NDRG3_HUMANNDRG3physical
26186194
VAS1_HUMANATP6AP1physical
26186194
NFS1_HUMANNFS1physical
26186194
GPTC2_HUMANGPATCH2physical
26186194
AT11A_HUMANATP11Aphysical
26186194
AMGO1_HUMANAMIGO1physical
26186194
NECT2_HUMANPVRL2physical
26186194
EFNB2_HUMANEFNB2physical
26186194
DSE_HUMANDSEphysical
26186194
CEGT_HUMANUGCGphysical
26186194
GRM7_HUMANGRM7physical
11891216
AAED1_HUMANAAED1physical
28514442
CEP89_HUMANCEP89physical
28514442
ICA69_HUMANICA1physical
28514442
ICA1L_HUMANICA1Lphysical
28514442
UACA_HUMANUACAphysical
28514442
KLH11_HUMANKLHL11physical
28514442
PKD2_HUMANPKD2physical
28514442
JAM1_HUMANF11Rphysical
28514442
GNPTA_HUMANGNPTABphysical
28514442
NDRG3_HUMANNDRG3physical
28514442
F117A_HUMANFAM117Aphysical
28514442
BIN3_HUMANBIN3physical
28514442
EPHA7_HUMANEPHA7physical
28514442
ZNF24_HUMANZNF24physical
28514442
AT11A_HUMANATP11Aphysical
28514442
ARFP1_HUMANARFIP1physical
28514442
AMGO1_HUMANAMIGO1physical
28514442
FHOD1_HUMANFHOD1physical
28514442
NFS1_HUMANNFS1physical
28514442
DSE_HUMANDSEphysical
28514442
EFNB1_HUMANEFNB1physical
28514442
GPTC2_HUMANGPATCH2physical
28514442
VAS1_HUMANATP6AP1physical
28514442
EFNB2_HUMANEFNB2physical
28514442
ITA6_HUMANITGA6physical
28514442
LDB1_HUMANLDB1physical
28514442
ILVBL_HUMANILVBLphysical
28514442
NECT2_HUMANPVRL2physical
28514442
QSOX2_HUMANQSOX2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PICK1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Threonine 82 at the PDZ domain of PICK1 is critical for AMPA receptorinteraction and localization.";
Shao X., Zhu L., Wang Y., Lu Y., Wang W., Zhu J., Shen Y., Xia J.,Luo J.;
Neurochem. Int. 56:962-970(2010).
Cited for: FUNCTION, AND PHOSPHORYLATION AT THR-82.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory