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Protein Page:
PREX1 (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
PREX1 Functions as a RAC guanine nucleotide exchange factor (GEF), which activates the Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol 3,4,5-trisphosphate and the beta gamma subunits of heterotrimeric G protein. May function downstream of heterotrimeric G proteins in neutrophils. Interacts preferentially with RAC2. Interacts with RAC1. Mainly expressed in peripheral blood leukocytes and brain. Expressed at intermediate level in spleen and lymph nodes, and weakly expressed in other tissues. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: GEFs, Rac/Rho; GEFs
Chromosomal Location of Human Ortholog: 20q13.13
Cellular Component: growth cone; intracellular membrane-bound organelle; perinuclear region of cytoplasm; cytoplasm; plasma membrane; dendritic shaft; cytosol
Molecular Function: protein binding; Rho guanyl-nucleotide exchange factor activity; enzyme binding; Rho GTPase activator activity; phospholipid binding
Biological Process: regulation of actin filament polymerization; neutrophil activation; actin filament polymerization; regulation of dendrite development; superoxide metabolic process; positive regulation of Rho GTPase activity
Reference #:  Q8TCU6 (UniProtKB)
Alt. Names/Synonyms: KIAA1415; P-Rex1; Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein; phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 1; PREX1; PtdIns(3,4,5)-dependent Rac exchanger 1
Gene Symbols: PREX1
Molecular weight: 186,203 Da
Basal Isoelectric point: 6.03  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PREX1

Protein Structure Not Found.


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Sites Implicated In
cell growth, induced: S1169‑p
activity, induced: S605‑p, S1169‑p
activity, inhibited: S313‑p, S319‑p

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

 
0 1 S174-p TVRAFLLsCMLLGGR
0 1 T308-p CKRKSRVtGsKKsTK
0 1 S310-p RKSRVtGsKKsTKRT
1 0 S313-p RVtGsKKsTKRTKsI
1 4 S319-p KsTKRTKsINGSLYI
0 1 T333-p IFRGRINtEVMEVEN
1 3 S436-p KDRRRKLstVPKCFL
0 1 T437-p DRRRKLstVPKCFLG
0 1 S512 SELEDIMSKGVRLYC
1 0 S605-p DEEMEGTsSKNKQLR
0 1 K624-ub LVENILAkRLLILPQ
0 5 K642-ac YGFDIEEkNKAVVVK
0 3 T704-p PLRLLVAtKAKEIIK
1 0 S805-p ARASQEAsTEDPSGE
1 0 S834-p LSLGPRLsLCEDSPM
1 15 S1001-p IRFGRKPsLIGLDPE
1 2 S1049-p GQGLHDGsFGPASGT
0 1 Y1096 ALKEMKQYVTQINRL
1 0 S1125-p ASLAEEAsSLPLVSE
0 2 L1127 LAEEAsSLPLVSEES
0 2 S1159-p AEEDQEDsGHDTMsy
1 0 S1165-p DsGHDTMsyRDsYSE
0 1 Y1166-p sGHDTMsyRDsYSEC
2 0 S1169-p DTMsyRDsYSECNSN
1 1 S1182-p SNRDSVLsYTSVRSN
0 1 S1185 DSVLsYTSVRSNSsY
1 0 S1191-p TSVRSNSsYLGsDEM
0 1 S1195-p SNSsYLGsDEMGsGD
1 5 S1200-p LGsDEMGsGDELPCD
0 1 Y1442-p QALKVIFyLDSYHFS
0 1 T1525-p LPTDASTtAVKIDQL
  mouse

 
S169 AVRAFLLSCMLLGGR
T303 CKRKSRVTGSKKSTK
S305 RKSRVTGSKKSTKRT
S308 RVTGSKKSTKRTKsI
S314-p KSTKRTKsINGSLYI
T328 IFRGRINTEVMEVEN
S431-p KDRRRKLsTVPKCFL
T432 DRRRKLsTVPKCFLG
S507-p SELEDIMsKGVRLYC
S600 DEEMEGTSSKNKQLR
K619 LVENILAKRLLIPPQ
K637 YGFDLEEKNKAVVVK
T699 PLRLLVATKAKETIK
P800 ARASQGAPDEDPQED
S824 LSLGPQLSLHEDSAV
S991-p IRFGRKPsLIGLDPE
S1038 GQGLNDSSYGSASGA
Y1085-p ALKEMKQyVTQINRL
S1116 PSLVEETSSsPPVSE
S1118-p LVEETSSsPPVSEES
S1150-p SEDEQEDsGHDTMSY
S1156 DsGHDTMSYRDSYSE
Y1157 sGHDTMSYRDSYSEC
S1160 DTMSYRDSYSECNSN
S1173-p SNRDSVLsYTsVRSN
S1176-p DSVLsYTsVRSNSSY
S1182 TsVRSNSSYLGsDEM
S1186-p SNSSYLGsDEMGsGD
S1191-p LGsDEMGsGDELPCD
Y1433 QALKVVFYLDGFHFS
T1516 LPTDAGATAVKIDQL
  rat

 
N101 AARAFLLNCMLLGGR
T235 CKRKSRVTGSKKSTK
S237 RKSRVTGSKKSTKRT
S240 RVTGSKKSTKRTKsI
S246-p KSTKRTKsINGSLYI
T260 IFRGRINTEVMEVEN
S363 KDRRRKLSTVPKCFL
T364 DRRRKLSTVPKCFLG
S439 SELEDIMSKGVRLYC
S532 DEEMEGTSSKNKQLR
K551 LVENILAKRLLIPPQ
K569 YGFDLEEKNKAVVVK
T631 PLRLLVATKAKETIK
P732 ARASQGAPDEDPQED
S753 LSLGPQLSLHEDSAV
S920 IRFGRKPSLIGLDPE
- under review  
Y1015 ALKEMKQYVTQINRL
- under review  
S1046 LVEETSSSPPASEES
S1078 SEDEQEDSGHDTMSY
S1084 DSGHDTMSYRDSYSE
Y1085 SGHDTMSYRDSYSEC
S1088 DTMSYRDSYSECNSN
S1101-p SNRDSVLsYTSVRSN
S1104 DSVLsYTSVRSNSSY
S1110 TSVRSNSSYLGSDET
S1114 SNSSYLGSDETGsGD
S1119-p LGSDETGsGDELPCD
Y1361 QALKVVFYLDGFHFS
T1444 LPTDATTTAVKIDQL
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