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PREX1 Antibody (Center) Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession Q8TCU6
Peptide ID 90723104
Additional Information
Other Names Phosphatidylinositol 3, 5-trisphosphate-dependent Rac exchanger 1 protein, P-Rex1, PtdIns(3, 5)-dependent Rac exchanger 1, PREX1, KIAA1415
Format Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name PREX1
Synonyms KIAA1415
Function 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.
Cellular Location Cytoplasm, cytosol. Cell membrane. Note=Mainly cytosolic. Some amount is apparently associated to the plasma membrane
Tissue Location Mainly expressed in peripheral blood leukocytes and brain. Expressed at intermediate level in spleen and lymph nodes, and weakly expressed in other tissues EMBL; AJ320261; CAC86401.1; -; mRNA EMBL; AL136579; CAB66514.1; -; mRNA EMBL; AL035106; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AL133342; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AL445192; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL; AB037836; BAA92653.2; -; mRNA EMBL; CH471077; EAW75684.1; -; Genomic_DNA EMBL; CH471077; EAW75685.1; -; Genomic_DNA EMBL; BC053616; AAH53616.1; -; mRNA EMBL; AL832913; CAH10614.1; -; mRNA CCDS; CCDS13410.1; -. [Q8TCU6-1] RefSeq; NP_065871.2; NM_020820.3 UniGene; Hs.153310; - PDB; 3QIK; X-ray; 2.28 A; A=607-706 PDB; 4YON; X-ray; 1.95 A; A=1-404 PDB; 5D27; X-ray; 1.92 A; A=245-408 PDB; 5D3V; X-ray; 1.85 A; A/B=245-408 PDB; 5D3W; X-ray; 1.85 A; A/B=245-408 PDB; 5D3X; X-ray; 1.69 A; A/B=245-408 PDB; 5D3Y; X-ray; 1.95 A; A/B=245-408 PDB; 5FI0; X-ray; 3.28 A; A/C/E/G=38-408 PDB; 5FI1; X-ray; 3.20 A; A=38-408 PDBsum; 3QIK; - PDBsum; 4YON; - PDBsum; 5D27; - PDBsum; 5D3V; - PDBsum; 5D3W; - PDBsum; 5D3X; - PDBsum; 5D3Y; - PDBsum; 5FI0; - PDBsum; 5FI1; - ProteinModelPortal; Q8TCU6; - SMR; Q8TCU6; - BioGrid; 121633; 9 DIP; DIP-46975N; - IntAct; Q8TCU6; 15 STRING; 9606.ENSP00000361009; - iPTMnet; Q8TCU6; - PhosphoSitePlus; Q8TCU6; - BioMuta; PREX1; - DMDM; 148886999; - EPD; Q8TCU6; - MaxQB; Q8TCU6; - PaxDb; Q8TCU6; - PeptideAtlas; Q8TCU6; - PRIDE; Q8TCU6; - ProteomicsDB; 74175; - ProteomicsDB; 74176; -. [Q8TCU6-2] ProteomicsDB; 74177; -. [Q8TCU6-3] Ensembl; ENST00000371941; ENSP00000361009; ENSG00000124126. [Q8TCU6-1] GeneID; 57580; - KEGG; hsa:57580; - UCSC; uc002xtw.2; human. [Q8TCU6-1] CTD; 57580; - DisGeNET; 57580; - EuPathDB; HostDB:ENSG00000124126.13; - GeneCards; PREX1; - H-InvDB; HIX0138059; - HGNC; HGNC:32594; PREX1 HPA; HPA001927; - MIM; 606905; gene neXtProt; NX_Q8TCU6; - OpenTargets; ENSG00000124126; - PharmGKB; PA164725018; - eggNOG; ENOG410ITRX; Eukaryota eggNOG; ENOG410Z6ZS; LUCA GeneTree; ENSGT00920000148946; - HOVERGEN; HBG053677; - InParanoid; Q8TCU6; - KO; K12365; - OMA; MQATDIM; - OrthoDB; EOG091G00MJ; - PhylomeDB; Q8TCU6; - TreeFam; TF328639; - Reactome; R-HSA-193648; NRAGE signals death through JNK Reactome; R-HSA-194840; Rho GTPase cycle Reactome; R-HSA-416482; G alpha (12/13) signalling events ChiTaRS; PREX1; human EvolutionaryTrace; Q8TCU6; - GeneWiki; PREX1; - GenomeRNAi; 57580; - PRO; PR:Q8TCU6; - Proteomes; UP000005640; Chromosome 20 Bgee; ENSG00000124126; - ExpressionAtlas; Q8TCU6; baseline and differential Genevisible; Q8TCU6; HS GO; GO:0005829; C:cytosol; IDA:UniProtKB GO; GO:0043198; C:dendritic shaft; IEA:Ensembl GO; GO:0030426; C:growth cone; IEA:Ensembl GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl GO; GO:0005886; C:plasma membrane; TAS:UniProtKB GO; GO:0019899; F:enzyme binding; TAS:UniProtKB GO; GO:0005096; F:GTPase activator activity; TAS:UniProtKB GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB GO; GO:0030676; F:Rac guanyl-nucleotide exchange factor activity; IBA:GO_Central GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; TAS:UniProtKB GO; GO:0030041; P:actin filament polymerization; TAS:UniProtKB GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IBA:GO_Central GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro GO; GO:0006469; P:negative regulation of protein kinase activity; IBA:GO_Central GO; GO:0032007; P:negative regulation of TOR signaling; IBA:GO_Central GO; GO:0042119; P:neutrophil activation; TAS:UniProtKB GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl GO; GO:0030833; P:regulation of actin filament polymerization; IEA:Ensembl GO; GO:0050773; P:regulation of dendrite development; IEA:Ensembl GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome GO; GO:0006801; P:superoxide metabolic process; TAS:UniProtKB GO; GO:0030217; P:T cell differentiation; IEA:Ensembl CDD; cd00160; RhoGEF; 1 Gene3D; 1.10.10.10; -; 2 Gene3D; 1.20.900.10; -; 1 Gene3D; 2.30.29.30; -; 1 InterPro; IPR035899; DBL_dom_sf InterPro; IPR000591; DEP_dom InterPro; IPR000219; DH-domain InterPro; IPR001331; GDS_CDC24_CS InterPro; IPR001478; PDZ InterPro; IPR036034; PDZ_sf InterPro; IPR011993; PH-like_dom_sf InterPro; IPR001849; PH_domain InterPro; IPR036388; WH-like_DNA-bd_sf InterPro; IPR036390; WH_DNA-bd_sf Pfam; PF00610; DEP; 2 Pfam; PF00621; RhoGEF; 1 SMART; SM00049; DEP; 2 SMART; SM00228; PDZ; 2 SMART; SM00233; PH; 1 SMART; SM00325; RhoGEF; 1 SUPFAM; SSF46785; SSF46785; 2 SUPFAM; SSF48065; SSF48065; 1 SUPFAM; SSF50156; SSF50156; 2 PROSITE; PS50186; DEP; 2 PROSITE; PS00741; DH_1; 1 PROSITE; PS50010; DH_2; 1 PROSITE; PS50106; PDZ; 1 PROSITE; PS50003; PH_DOMAIN; 1 1: Evidence at protein level; 3D-structure; Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Guanine-nucleotide releasing factor; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat CHAIN 1 1659 Phosphatidylinositol 3,4,5-trisphosphate- dependent Rac exchanger 1 protein /FTId=PRO_0000080965 DOMAIN 49 240 DH. {ECO:0000255|PROSITE- ProRule:PRU00062} DOMAIN 271 392 PH. {ECO:0000255|PROSITE- ProRule:PRU00145} DOMAIN 421 496 DEP 1. {ECO:0000255|PROSITE- ProRule:PRU00066} DOMAIN 523 597 DEP 2. {ECO:0000255|PROSITE- ProRule:PRU00066} DOMAIN 625 703 PDZ. {ECO:0000255|PROSITE- ProRule:PRU00143} MOD_RES 319 319 Phosphoserine MOD_RES 1001 1001 Phosphoserine {ECO:0000250|UniProtKB:Q69ZK0} MOD_RES 1195 1195 Phosphoserine {ECO:0000250|UniProtKB:Q69ZK0} MOD_RES 1200 1200 Phosphoserine VAR_SEQ 1 703 Missing (in isoform 2) /FTId=VSP_001818 VAR_SEQ 704 708 TKAKE -> MGLEQ (in isoform 2) /FTId=VSP_001819 VAR_SEQ 1471 1561 VLENVEGLPSPGSQAAEDLQQDINAQSLEKVQQYYRKLRAF YLERSNLPTDASTTAVKIDQLIRPINALDELCRLMKSFVHP KPGAAGSVG -> GELQAWGREDHGGRAKATKHTGSQPPAR PRHLPSQCWRTWRGCLLQAARPRRICSRTSTRSPWRKFSSI TANSGHFTWSGLTCPRMPAPRR (in isoform 3) /FTId=VSP_015090 VAR_SEQ 1562 1659 Missing (in isoform 3). /FTId=VSP_015091 VARIANT 659 659 V -> M (in dbSNP:rs55904123) /FTId=VAR_061798 VARIANT 696 696 R -> C (in dbSNP:rs7271583) /FTId=VAR_057191 VARIANT 786 786 Q -> H (in dbSNP:rs41283558) /FTId=VAR_061799 VARIANT 1118 1118 A -> T (in dbSNP:rs6012504) /FTId=VAR_057192 VARIANT 1240 1240 V -> I (in dbSNP:rs16993997) /FTId=VAR_023210 VARIANT 1340 1340 K -> E (in dbSNP:rs2664521) {ECO:0000269|PubMed:10718198, ECO:0000269|PubMed:11955434, ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005, ECO:0000269|Ref.4} /FTId=VAR_023211 VARIANT 1559 1559 S -> T (in dbSNP:rs3936192) /FTId=VAR_023212 CONFLICT 910 910 A -> V (in Ref. 2; CAB66514) HELIX 36 74 {ECO:0000244|PDB:4YON} HELIX 76 81 {ECO:0000244|PDB:4YON} HELIX 83 88 {ECO:0000244|PDB:4YON} HELIX 93 100 {ECO:0000244|PDB:4YON} HELIX 103 120 {ECO:0000244|PDB:4YON} HELIX 132 138 {ECO:0000244|PDB:4YON} HELIX 139 143 {ECO:0000244|PDB:4YON} HELIX 144 162 {ECO:0000244|PDB:4YON} HELIX 166 178 {ECO:0000244|PDB:4YON} STRAND 183 185 {ECO:0000244|PDB:5FI1} HELIX 188 199 {ECO:0000244|PDB:4YON} HELIX 202 211 {ECO:0000244|PDB:4YON} HELIX 245 254 {ECO:0000244|PDB:5D3X} STRAND 257 259 {ECO:0000244|PDB:5FI0} HELIX 265 268 {ECO:0000244|PDB:5D3X} STRAND 272 282 {ECO:0000244|PDB:5D3X} STRAND 285 294 {ECO:0000244|PDB:5D3X} STRAND 297 303 {ECO:0000244|PDB:5D3X} STRAND 320 322 {ECO:0000244|PDB:5D27} STRAND 325 332 {ECO:0000244|PDB:5D3X} HELIX 333 335 {ECO:0000244|PDB:5D3X} STRAND 336 340 {ECO:0000244|PDB:5D3X} STRAND 345 347 {ECO:0000244|PDB:5D27} HELIX 348 350 {ECO:0000244|PDB:5D3X} STRAND 356 363 {ECO:0000244|PDB:5D3X} TURN 364 367 {ECO:0000244|PDB:5D3X} STRAND 368 373 {ECO:0000244|PDB:5D3X} HELIX 377 405 {ECO:0000244|PDB:5D3X} HELIX 607 620 {ECO:0000244|PDB:3QIK} STRAND 623 628 {ECO:0000244|PDB:3QIK} STRAND 632 642 {ECO:0000244|PDB:3QIK} STRAND 645 651 {ECO:0000244|PDB:3QIK} HELIX 656 660 {ECO:0000244|PDB:3QIK} STRAND 667 671 {ECO:0000244|PDB:3QIK} STRAND 674 676 {ECO:0000244|PDB:3QIK} HELIX 681 693 {ECO:0000244|PDB:3QIK} STRAND 698 703 {ECO:0000244|PDB:3QIK} SEQUENCE 1659 AA; 186203 MW; 159419355ED0F00F CRC64; MEAPSGSEPG GDGAGDCAHP DPRAPGAAAP SSGPGPCAAA RESERQLRLR LCVLNEILGT ERDYVGTLRF LQSAFLHRIR QNVADSVEKG LTEENVKVLF SNIEDILEVH KDFLAALEYC LHPEPQSQHE LGNVFLKFKD KFCVYEEYCS NHEKALRLLV ELNKIPTVRA FLLSCMLLGG RKTTDIPLEG YLLSPIQRIC KYPLLLKELA KRTPGKHPDH PAVQSALQAM KTVCSNINET KRQMEKLEAL EQLQSHIEGW EGSNLTDICT QLLLQGTLLK ISAGNIQERA FFLFDNLLVY CKRKSRVTGS KKSTKRTKSI NGSLYIFRGR INTEVMEVEN VEDGTADYHS NGYTVTNGWK IHNTAKNKWF VCMAKTAEEK QKWLDAIIRE REQRESLKLG MERDAYVMIA EKGEKLYHMM MNKKVNLIKD RRRKLSTVPK CFLGNEFVAW LLEIGEISKT EEGVNLGQAL LENGIIHHVS DKHQFKNEQV MYRFRYDDGT YKARSELEDI MSKGVRLYCR LHSLYTPVIK DRDYHLKTYK SVLPGSKLVD WLLAQGDCQT REEAVALGVG LCNNGFMHHV LEKSEFRDES QYFRFHADEE MEGTSSKNKQ LRNDFKLVEN ILAKRLLILP QEEDYGFDIE EKNKAVVVKS VQRGSLAEVA GLQVGRKIYS INEDLVFLRP FSEVESILNQ SFCSRRPLRL LVATKAKEII KIPDQPDTLC FQIRGAAPPY VYAVGRGSEA MAAGLCAGQC ILKVNGSNVM NDGAPEVLEH FQAFRSRREE ALGLYQWIYH THEDAQEARA SQEASTEDPS GEQAQEEDQA DSAFPLLSLG PRLSLCEDSP MVTLTVDNVH LEHGVVYEYV STAGVRCHVL EKIVEPRGCF GLTAKILEAF AANDSVFVEN CRRLMALSSA IVTMPHFEFR NICDTKLESI GQRIACYQEF AAQLKSRVSP PFKQAPLEPH PLCGLDFCPT NCHINLMEVS YPKTTPSVGR SFSIRFGRKP SLIGLDPEQG HLNPMSYTQH CITTMAAPSW KCLPAAEGDP QGQGLHDGSF GPASGTLGQE DRGLSFLLKQ EDREIQDAYL QLFTKLDVAL KEMKQYVTQI NRLLSTITEP TSGGSCDASL AEEASSLPLV SEESEMDRSD HGGIKKVCFK VAEEDQEDSG HDTMSYRDSY SECNSNRDSV LSYTSVRSNS SYLGSDEMGS GDELPCDMRI PSDKQDKLHG CLEHLFNQVD SINALLKGPV MSRAFEETKH FPMNHSLQEF KQKEECTIRG RSLIQISIQE DPWNLPNSIK TLVDNIQRYV EDGKNQLLLA LLKCTDTELQ LRRDAIFCQA LVAAVCTFSK QLLAALGYRY NNNGEYEESS RDASRKWLEQ VAATGVLLHC QSLLSPATVK EERTMLEDIW VTLSELDNVT FSFKQLDENY VANTNVFYHI EGSRQALKVI FYLDSYHFSK LPSRLEGGAS LRLHTALFTK VLENVEGLPS PGSQAAEDLQ QDINAQSLEK VQQYYRKLRA FYLERSNLPT DASTTAVKID QLIRPINALD ELCRLMKSFV HPKPGAAGSV GAGLIPISSE LCYRLGACQM VMCGTGMQRS TLSVSLEQAA ILARSHGLLP KCIMQATDIM RKQGPRVEIL AKNLRVKDQM PQGAPRLYRL CQPPVDGDL
Research Areas
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Background

The protein encoded by this gene acts as a guanine nucleotide exchange factor for the RHO family of small GTP-binding proteins (RACs). It has been shown to bind to and activate RAC1 by exchanging bound GDP for free GTP. The encoded protein, which is found mainly in the cytoplasm, is activated by phosphatidylinositol-3,4,5-trisphosphate and the beta-gamma subunits of heterotrimeric G proteins.

References

Carretero-Ortega, J., et al. Mol. Pharmacol. 77(3):435-442(2010)Ledezma-Sanchez, B.A., et al. Biochem. Biophys. Res. Commun. 391(4):1647-1652(2010)Takefuji, M., et al. J. Hum. Genet. 55(1):42-49(2010)Qin, J., et al. Oncogene 28(16):1853-1863(2009)Waters, J.E., et al. J. Cell. Sci. 121 (PT 17), 2892-2903 (2008)Sugiyama, N., et al. Mol. Cell Proteomics 6(6):1103-1109(2007)Weiner, O.D. Curr. Biol. 12 (12), R429-R431 (2002)

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Cat# BP9461c
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