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Protein Page:
PIST (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PIST a ubiquitously expressed peripheral membrane protein that contains a PDZ domain and two coiled-coil regions. Associates with the Golgi apparatus and plasma membrane, regulating intracellular protein trafficking and degradation. May play a role in autophagy, and regulate the intracellular trafficking of the ADRB1 receptor. Interacts with GOLGA3 and STX6. The PDZ domain is known to mediate interactions with CLCN3-iso2, ACCN3, CFTR, SSTR5, FDZ5, ADRB1, FZD8, GRID2, mGluR5, mGluR1. Mutations of PDZ residues S302D, T304E, K348D, K350E abrogates the ability of PIST to interact with the CFTR C terminus. May regulate CFTR chloride currents and acid-induced ACCN3 currents by modulating cell surface expression of both channels. Overexpression results in CFTR intracellular retention and degradation in the lysosomes. Enriched in synaptosomal and postsynaptic densities (PSD) fractions. Expressed in cell bodies and dendrites of Purkinje cells. Localized at the trans-Golgi network (TGN) of spermatids and the medulla of round spermatides. An oncogenic fusion protein between PIST (aka FIG) and the receptor tyrosine kinase ROS is found in glioblastoma multiform. Unlike other fusion RTK oncogenes, he mechanism of activation of PIST-ROS does not appear to be dimerization. Rather, activation of the fused ROS kinase appears to depend upon translocation to the golgi apparatus: deletion of 2nd coiled-coil region, crucial for Golgi localization, appears to eliminate the transformation capacity of PIST-ROS. Three alternatively spliced human isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, peripheral
Cellular Component: Golgi membrane; Golgi apparatus; postsynaptic membrane; trans-Golgi network transport vesicle; protein complex; membrane; postsynaptic density; dendrite; cytoplasm; plasma membrane; cell junction
Molecular Function: protein C-terminus binding; protein binding; protein homodimerization activity; frizzled binding; small GTPase regulator activity
Biological Process: Golgi to plasma membrane transport; ER to Golgi vesicle-mediated transport; protein transport; apical protein localization; regulation of catalytic activity; spermatid nuclear differentiation; protein homooligomerization; cytoplasmic sequestering of CFTR protein
Reference #:  Q9HD26 (UniProtKB)
Alt. Names/Synonyms: CAL; CFTR-associated ligand; dJ94G16.2; dJ94G16.2 PIST; FIG; Fused in glioblastoma; Golgi associated PDZ and coiled-coil motif containing protein; golgi-associated PDZ and coiled-coil motif containing; Golgi-associated PDZ and coiled-coil motif-containing protein; GOPC; GOPC1; PDZ protein interacting specifically with TC10; PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10; PIST
Gene Symbols: GOPC
Molecular weight: 50,520 Da
Basal Isoelectric point: 5.59  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PIST

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 K93-ac SVSQINHkLEAQLVD
0 1 K93 SVSQINHKLEAQLVD
0 3 K102-ub EAQLVDLkSELTETQ
0 1 T145 GQSADSGTIkAKLSG
0 1 K147-ub SADSGTIkAKLSGPS
0 1 S154 kAKLSGPSVEELERE
0 1 Y201-p AVLQAEVyGARLAAK
0 1 Y209-p GARLAAKyLDKELAG
0 2 S276-p PPGHDQDsLKKsQGV
0 2 S280-p DQDsLKKsQGVGPIR
0 1 K350 NLRDTKHKEAVTILS
0 13 S376-p YVAPEVDsDDENVEy
0 6 Y383-p sDDENVEyEDESGHR
0 1 G401 YLDELEGGGNPGAsC
0 1 P404 ELEGGGNPGAsCKDt
0 3 S407-p GGGNPGAsCKDtsGE
0 1 K409 GNPGAsCKDtsGEIK
0 1 T411-p PGAsCKDtsGEIKVL
0 1 S412-p GAsCKDtsGEIKVLQ
0 2 T441-p DLGTASEtPLDDGAS
0 1 T455-p SKLDDLHtLyHKKsy
0 38 Y457-p LDDLHtLyHKKsy__
0 4 S461-p HtLyHKKsy______
0 1 Y462-p tLyHKKsy_______
  PIST iso2  
K93 SVSQINHKLEAQLVD
K93 SVSQINHKLEAQLVD
K102 EAQLVDLKSELTETQ
T145-p GQSADSGtIKAKLER
K147 SADSGtIKAKLEREL
- gap
Y193 AVLQAEVYGARLAAK
Y201 GARLAAKYLDKELAG
S268 PPGHDQDSLKKSQGV
S272 DQDSLKKSQGVGPIR
K342 NLRDTKHKEAVTILS
S368 YVAPEVDSDDENVEY
Y375 SDDENVEYEDESGHR
G393 YLDELEGGGNPGASC
P396 ELEGGGNPGASCKDT
S399 GGGNPGASCKDTSGE
K401 GNPGASCKDTSGEIK
T403 PGASCKDTSGEIKVL
S404 GASCKDTSGEIKVLQ
T433 DLGTASETPLDDGAS
T447 SKLDDLHTLYHKKSY
Y449 LDDLHTLYHKKSY__
S453 HTLYHKKSY______
Y454 TLYHKKSY_______
  PIST iso3  
K93 SVSQINHKLEAQLVD
K93 SVSQINHKLEAQLVD
K102 EAQLVDLKSELTETQ
T145 GQSADSGTIKAKLSG
K147 SADSGTIKAKLSGPS
S154 KAKLSGPSVEELERE
Y201 AVLQAEVYGARLAAK
Y209 GARLAAKYLDKELAG
S276 PPGHDQDSLKKSQGV
S280 DQDSLKKSQGVGPIR
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
  mouse

 
K94 TVSQINHKLEAQLVD
K94-ub TVSQINHkLEAQLVD
R103 EAQLVDLRSELTETQ
A146 GQSVDSGAIKAKLSV
K148 SVDSGAIKAKLSVHs
S155-p KAKLSVHsVEDLERE
Y202 AVLQAEVYGARLAAK
Y210 GARLAAKYLDKELAG
S277 PPGHDQDSLKKSQGV
S281 DQDSLKKSQGVGPIR
K351-ub NLRDTKHkEAVTILS
S377-p YVAPEVDsDDENVEY
Y384 sDDENVEYEDESGHR
S402-p YLDELEGsGNsGAsC
S405-p ELEGsGNsGAsCkDS
S408-p GsGNsGAsCkDSSGE
K410-ub GNsGAsCkDSSGEMK
S412 sGAsCkDSSGEMKML
S413 GAsCkDSSGEMKMLQ
S442-p DVGAAGEsPLDDTAA
S456 ARAAHLHSLHQKKAY
H458 AAHLHSLHQKKAY__
A462 HSLHQKKAY______
Y463 SLHQKKAY_______
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