CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018006
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein 
Protein Synonyms/Alias
 P-Rex1; PtdIns(3,4,5)-dependent Rac exchanger 1 
Gene Name
 PREX1 
Gene Synonyms/Alias
 KIAA1415 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
182CMLLGGRKTTDIPLEubiquitination[1]
201SPIQRICKYPLLLKEubiquitination[1]
241CSNINETKRQMEKLEubiquitination[1]
624LVENILAKRLLILPQubiquitination[1, 2, 3]
649KNKAVVVKSVQRGSLubiquitination[1]
707LLVATKAKEIIKIPDubiquitination[1]
926FRNICDTKLESIGQRubiquitination[1]
945QEFAAQLKSRVSPPFubiquitination[1]
1069RGLSFLLKQEDREIQubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 49 240 DH.
 DOMAIN 271 392 PH.
 DOMAIN 421 496 DEP 1.
 DOMAIN 523 597 DEP 2.
 DOMAIN 625 703 PDZ.  
Keyword
 3D-structure; Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Guanine-nucleotide releasing factor; Membrane; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1659 AA 
Protein Sequence
MEAPSGSEPG GDGAGDCAHP DPRAPGAAAP SSGPGPCAAA RESERQLRLR LCVLNEILGT 60
ERDYVGTLRF LQSAFLHRIR QNVADSVEKG LTEENVKVLF SNIEDILEVH KDFLAALEYC 120
LHPEPQSQHE LGNVFLKFKD KFCVYEEYCS NHEKALRLLV ELNKIPTVRA FLLSCMLLGG 180
RKTTDIPLEG YLLSPIQRIC KYPLLLKELA KRTPGKHPDH PAVQSALQAM KTVCSNINET 240
KRQMEKLEAL EQLQSHIEGW EGSNLTDICT QLLLQGTLLK ISAGNIQERA FFLFDNLLVY 300
CKRKSRVTGS KKSTKRTKSI NGSLYIFRGR INTEVMEVEN VEDGTADYHS NGYTVTNGWK 360
IHNTAKNKWF VCMAKTAEEK QKWLDAIIRE REQRESLKLG MERDAYVMIA EKGEKLYHMM 420
MNKKVNLIKD RRRKLSTVPK CFLGNEFVAW LLEIGEISKT EEGVNLGQAL LENGIIHHVS 480
DKHQFKNEQV MYRFRYDDGT YKARSELEDI MSKGVRLYCR LHSLYTPVIK DRDYHLKTYK 540
SVLPGSKLVD WLLAQGDCQT REEAVALGVG LCNNGFMHHV LEKSEFRDES QYFRFHADEE 600
MEGTSSKNKQ LRNDFKLVEN ILAKRLLILP QEEDYGFDIE EKNKAVVVKS VQRGSLAEVA 660
GLQVGRKIYS INEDLVFLRP FSEVESILNQ SFCSRRPLRL LVATKAKEII KIPDQPDTLC 720
FQIRGAAPPY VYAVGRGSEA MAAGLCAGQC ILKVNGSNVM NDGAPEVLEH FQAFRSRREE 780
ALGLYQWIYH THEDAQEARA SQEASTEDPS GEQAQEEDQA DSAFPLLSLG PRLSLCEDSP 840
MVTLTVDNVH LEHGVVYEYV STAGVRCHVL EKIVEPRGCF GLTAKILEAF AANDSVFVEN 900
CRRLMALSSA IVTMPHFEFR NICDTKLESI GQRIACYQEF AAQLKSRVSP PFKQAPLEPH 960
PLCGLDFCPT NCHINLMEVS YPKTTPSVGR SFSIRFGRKP SLIGLDPEQG HLNPMSYTQH 1020
CITTMAAPSW KCLPAAEGDP QGQGLHDGSF GPASGTLGQE DRGLSFLLKQ EDREIQDAYL 1080
QLFTKLDVAL KEMKQYVTQI NRLLSTITEP TSGGSCDASL AEEASSLPLV SEESEMDRSD 1140
HGGIKKVCFK VAEEDQEDSG HDTMSYRDSY SECNSNRDSV LSYTSVRSNS SYLGSDEMGS 1200
GDELPCDMRI PSDKQDKLHG CLEHLFNQVD SINALLKGPV MSRAFEETKH FPMNHSLQEF 1260
KQKEECTIRG RSLIQISIQE DPWNLPNSIK TLVDNIQRYV EDGKNQLLLA LLKCTDTELQ 1320
LRRDAIFCQA LVAAVCTFSK QLLAALGYRY NNNGEYEESS RDASRKWLEQ VAATGVLLHC 1380
QSLLSPATVK EERTMLEDIW VTLSELDNVT FSFKQLDENY VANTNVFYHI EGSRQALKVI 1440
FYLDSYHFSK LPSRLEGGAS LRLHTALFTK VLENVEGLPS PGSQAAEDLQ QDINAQSLEK 1500
VQQYYRKLRA FYLERSNLPT DASTTAVKID QLIRPINALD ELCRLMKSFV HPKPGAAGSV 1560
GAGLIPISSE LCYRLGACQM VMCGTGMQRS TLSVSLEQAA ILARSHGLLP KCIMQATDIM 1620
RKQGPRVEIL AKNLRVKDQM PQGAPRLYRL CQPPVDGDL 1659 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0043198; C:dendritic shaft; IEA:Compara.
 GO:0030426; C:growth cone; IEA:Compara.
 GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0005886; C:plasma membrane; TAS:UniProtKB.
 GO:0019899; F:enzyme binding; TAS:UniProtKB.
 GO:0005543; F:phospholipid binding; IDA:UniProtKB.
 GO:0005100; F:Rho GTPase activator activity; TAS:UniProtKB.
 GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; TAS:UniProtKB.
 GO:0030041; P:actin filament polymerization; TAS:UniProtKB.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0042119; P:neutrophil activation; TAS:UniProtKB.
 GO:0030833; P:regulation of actin filament polymerization; IEA:Compara.
 GO:0050773; P:regulation of dendrite development; IEA:Compara.
 GO:0006801; P:superoxide metabolic process; TAS:UniProtKB. 
Interpro
 IPR000591; DEP_dom.
 IPR000219; DH-domain.
 IPR001331; GDS_CDC24_CS.
 IPR001478; PDZ.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology.
 IPR011991; WHTH_DNA-bd_dom. 
Pfam
 PF00610; DEP
 PF00169; PH
 PF00621; RhoGEF 
SMART
 SM00049; DEP
 SM00228; PDZ
 SM00233; PH
 SM00325; RhoGEF 
PROSITE
 PS50186; DEP
 PS00741; DH_1
 PS50010; DH_2
 PS50106; PDZ
 PS50003; PH_DOMAIN 
PRINTS