CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013511
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Puratrophin-1 
Protein Synonyms/Alias
 Pleckstrin homology domain-containing family G member 4; PH domain-containing family G member 4; Purkinje cell atrophy-associated protein 1 
Gene Name
 PLEKHG4 
Gene Synonyms/Alias
 PRTPHN1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
405GRELTWLKQEVPEVTubiquitination[1, 2, 3, 4]
423DYRTAMDKADELYDRubiquitination[1, 3, 5]
511EQVRQGEKFLQPLTGubiquitination[1, 2, 3, 4]
608LPPAHFRKMWALATGubiquitination[3, 5]
642TWLALDQKLEASLKLubiquitination[3, 6]
648QKLEASLKLPPVGSTubiquitination[3]
674PAHPPLRKAYSFDRNubiquitination[3]
784HLFGNLEKLRDFHCHubiquitination[3]
844SYGHTFFKDKQQALGubiquitination[3]
846GHTFFKDKQQALGDHubiquitination[3, 5]
862DLASYLLKPIQRMGKubiquitination[1, 3]
869KPIQRMGKYALLLQEubiquitination[1, 2, 3, 6]
922QGCDVNLKEQGQLVRubiquitination[3, 6]
971GVDTFAYKRSFKMADubiquitination[1, 3, 5, 6]
975FAYKRSFKMADLGLTubiquitination[3]
1049VSMGVGNKAFRDIAPubiquitination[1, 2, 3]
1071RTVNYVLKCREVRSRubiquitination[3]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] 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]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
Functional Description
 Possible role in intracellular signaling and cytoskeleton dynamics at the Golgi. 
Sequence Annotation
 DOMAIN 732 908 DH.
 DOMAIN 920 1027 PH.
 MOD_RES 64 64 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Guanine-nucleotide releasing factor; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1191 AA 
Protein Sequence
MERPLENGDE SPDSQGHATD WRFAVCSFRD AWEEEEPASQ MHVKDPGPPR PPAGATQDEE 60
LQGSPLSRKF QLPPAADESG DAQRGTVESS SVLSEGPGPS GVESLLCPMS SHLSLAQGES 120
DTPGVGLVGD PGPSRAMPSG LSPGALDSDP VGLGDPLSEI SKLLEAAPSG SGLPKPADCL 180
LAQDLCWELL ASGMATLPGT RDVQGRAVLL LCAHSPAWLQ SECSSQELIR LLLYLRSIPR 240
PEVQALGLTV LVDARICAPS SSLFSGLSQL QEAAPGAVYQ VLLVGSTLLK EVPSGLQLEQ 300
LPSQSLLTHI PTAGLPTSLG GGLPYCHQAW LDFRRRLEAL LQNCQAACAL LQGAIESVKA 360
VPQPMEPGEV GQLLQQTEVL MQQVLDSPWL AWLQCQGGRE LTWLKQEVPE VTLSPDYRTA 420
MDKADELYDR VDGLLHQLTL QSNQRIQALE LVQTLEARES GLHQIEVWLQ QVGWPALEEA 480
GEPSLDMLLQ AQGSFQELYQ VAQEQVRQGE KFLQPLTGWE AAELDPPGAR FLALRAQLTE 540
FSRALAQRCQ RLADAERLFQ LFREALTWAE EGQRVLAELE QERPGVVLQQ LQLHWTRHPD 600
LPPAHFRKMW ALATGLGSEA IRQECRWAWA RCQDTWLALD QKLEASLKLP PVGSTASLCV 660
SQVPAAPAHP PLRKAYSFDR NLGQSLSEPA CHCHHAATIA ACRRPEAGGG ALPQASPTVP 720
PPGSSDPRSL NRLQLVLAEM VATEREYVRA LEYTMENYFP ELDRPDVPQG LRGQRAHLFG 780
NLEKLRDFHC HFFLRELEAC TRHPPRVAYA FLRHRVQFGM YALYSKNKPR SDALMSSYGH 840
TFFKDKQQAL GDHLDLASYL LKPIQRMGKY ALLLQELARA CGGPTQELSA LREAQSLVHF 900
QLRHGNDLLA MDAIQGCDVN LKEQGQLVRQ DEFVVRTGRH KSVRRIFLFE ELLLFSKPRH 960
GPTGVDTFAY KRSFKMADLG LTECCGNSNL RFEIWFRRRK ARDTFVLQAS SLAIKQAWTA 1020
DISHLLWRQA VHNKEVRMAE MVSMGVGNKA FRDIAPSEEA INDRTVNYVL KCREVRSRAS 1080
IAVAPFDHDS LYLGASNSLP GDPASCSVLG SLNLHLYRDP ALLGLRCPLY PSFPEEAALE 1140
AEAELGGQPS LTAEDSEISS QCPSASGSSG SDSSCVSGQA LGRGLEDLPC V 1191 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
 GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro. 
Interpro
 IPR000219; DH-domain.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology. 
Pfam
 PF00621; RhoGEF 
SMART
 SM00233; PH
 SM00325; RhoGEF 
PROSITE
 PS00741; DH_1
 PS50010; DH_2
 PS50003; PH_DOMAIN 
PRINTS