CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024508
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 RanBP2-like and GRIP domain-containing protein 3 
Protein Synonyms/Alias
  
Gene Name
 RGPD3 
Gene Synonyms/Alias
 RGP3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
94VELNPTQKDLVLKIAubiquitination[1, 2, 3]
106KIAELLCKNDVTDGRubiquitination[2, 4]
123YWVERAAKLFPGSPAubiquitination[2, 4, 5]
133PGSPAIYKLKEQLLDubiquitination[2]
135SPAIYKLKEQLLDCEubiquitination[2, 6]
336RPKIKLIKGEAGQNLubiquitination[2]
380VVETFANKSGQSALYubiquitination[3]
608GRSVHYWKKVLPLLKubiquitination[2]
609RSVHYWKKVLPLLKIubiquitination[2]
615KKVLPLLKIIKKKNSubiquitination[5]
619PLLKIIKKKNSIPEPubiquitination[2]
620LLKIIKKKNSIPEPIubiquitination[2, 4]
734DSNLSVVKKLPVPLEubiquitination[3, 4, 5, 7]
735SNLSVVKKLPVPLESubiquitination[2]
785HSTPSPTKYSLSPSKubiquitination[2]
792KYSLSPSKSYKYSPKubiquitination[2]
799KSYKYSPKTPPRWAEubiquitination[2, 4]
924PVSADGFKFGISEPGubiquitination[2]
935SEPGNQEKKSEKPLEubiquitination[2]
1002GFSGAGEKLFSSQYGubiquitination[8]
1058VTGEEGEKVLYSQGVubiquitination[2]
1066VLYSQGVKLFRFDAEubiquitination[2, 3]
1086ERGLGNLKILKNEVNubiquitination[2, 5, 8, 9]
1089LGNLKILKNEVNGKVubiquitination[2]
1121ITTTMNLKPLSGSDRubiquitination[2]
1161PELAEEFKQKFEECQubiquitination[1, 2]
1163LAEEFKQKFEECQRLubiquitination[2]
1181IPLQTPHKLVDTGRAubiquitination[2, 9]
1199IQRAEEMKSGLKDFKubiquitination[2]
1203EEMKSGLKDFKTFLTubiquitination[2, 4]
1206KSGLKDFKTFLTNDQubiquitination[2, 5]
1304KSALSLSKSPAKLNQubiquitination[2]
1369AEFYRYDKDVGQWKEubiquitination[2]
1375DKDVGQWKERGIGDIubiquitination[2]
1383ERGIGDIKILQNYDNubiquitination[2, 5, 8]
1404MRRDQVLKLCANHRIubiquitination[1, 2]
1421DMSLQNMKGTERVWVubiquitination[1, 2, 4]
1449EHLAVRFKLQDVADSubiquitination[2, 5, 8]
1459DVADSFKKIFDEAKTubiquitination[2]
1465KKIFDEAKTAQEKDSubiquitination[2]
1470EAKTAQEKDSLITPHubiquitination[2]
1491PRESPCGKIAVAVLEubiquitination[2]
1547VFGSESVKRIFSSEKubiquitination[2]
1596AQSGSESKVEPKKCEubiquitination[1]
1606PKKCELSKNSDIEQSubiquitination[2]
1617IEQSSDSKVKNLSASubiquitination[2]
1691MEQIKLLKSEIRRLEubiquitination[2]
1714AANVEHLKNVLLQFIubiquitination[2]
1724LLQFIFLKPGSERERubiquitination[2]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [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]
 [7] 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]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] 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
Functional Description
  
Sequence Annotation
 REPEAT 60 93 TPR 1.
 REPEAT 584 617 TPR 2.
 DOMAIN 1037 1173 RanBD1 1.
 DOMAIN 1334 1470 RanBD1 2.
 DOMAIN 1703 1753 GRIP.
 MOD_RES 21 21 Phosphoserine (By similarity).  
Keyword
 Coiled coil; Complete proteome; Phosphoprotein; Reference proteome; Repeat; TPR repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1758 AA 
Protein Sequence
MSCSKAYGER YVASVQGSAP SPRKKSTRGF YFAKLYYEAK EYDLAKKYIC TYINVREMDP 60
RAHRFLGLLY ELEENTEKAV ECYRRSVELN PTQKDLVLKI AELLCKNDVT DGRAEYWVER 120
AAKLFPGSPA IYKLKEQLLD CEGEDGWNKL FDLIQSELYV RPDDVHVNIR LVELYRSTKR 180
LKDAVARCHE AERNIALRSS LEWNSCVVQT LKEYLESLQC LESDKSDWRA TNTDLLLAYA 240
NLMLLTLSTR DVQESRELLE SFDSALQSAK SSLGGNDELS ATFLEMKGHF YMHAGSLLLK 300
MGQHGNNVQW RALSELAALC YLIAFQVPRP KIKLIKGEAG QNLLEMMACD RLSQSGHMLL 360
NLSRGKQDFL KVVVETFANK SGQSALYDAL FSSQSPKDTS FLGSDDIGNI DVQEPELEDL 420
ARYDVGAIRA HNGSLQHLTW LGLQWNSLPA LPGIRKWLKQ LFHHLPQETS RLETNAPESI 480
CILDLEVFLL GVVYTSHLQL KEKCNSHHSS YQPLCLPLPV CKQLCTERQK SWWDAVCTLI 540
HRKAVPGNSA KLRLLVQHEI NTLRAQEKHG LQPALLVHWA KCLQKMGSGL NSFYDQREYI 600
GRSVHYWKKV LPLLKIIKKK NSIPEPIDPL FKHFHSVDIQ ASEIVEYEED AHVTFAILDA 660
VNGNIEDAMT AFESIKSVVS YWNLALIFHR KAEDIANDAL SPEEQEECKN YLRKTRGYLI 720
KILDDSDSNL SVVKKLPVPL ESVKEMLKSV MQELENYSEG GPLYKNGSLR NADSEIKHST 780
PSPTKYSLSP SKSYKYSPKT PPRWAEDQNS LLKMIRQEVK AIKEEMQELK LNSSKSASHH 840
RWPTENYGPD SVPDGYQGSQ TFHGAPLTVA TTGPSVYYSQ SPAYNSQYLL RPAANVTPTK 900
GSSNTEFKST KEGFSIPVSA DGFKFGISEP GNQEKKSEKP LENDTGLQAQ DISGRKKGRG 960
VIFGQTSSTF TFADVAKSTS GEGFQFGKKD LNFKGFSGAG EKLFSSQYGK MANKANTSGD 1020
FEKDDDAYKT EDSDDIHFEP VVQMPEKVEL VTGEEGEKVL YSQGVKLFRF DAEVSQWKER 1080
GLGNLKILKN EVNGKVRMLM QREQVLKVCA NHWITTTMNL KPLSGSDRAW MWSASDFSDG 1140
DAKLERLAAK FKTPELAEEF KQKFEECQRL LLDIPLQTPH KLVDTGRAAK LIQRAEEMKS 1200
GLKDFKTFLT NDQTKVAEEE NKGSGTGAAG ASDTTIKPNA ENTGPTLEWD NYDLREDALD 1260
DSVSSSSVHA SPLASSPVRK NLFHFDESTT GSNFSFKSAL SLSKSPAKLN QSGTSVGTDE 1320
ESDVTQEEER DGQYFEPVVP LPDLVEVSSG EENEQVVFSH RAEFYRYDKD VGQWKERGIG 1380
DIKILQNYDN KHVRILMRRD QVLKLCANHR ITPDMSLQNM KGTERVWVWT ACDFADGERK 1440
VEHLAVRFKL QDVADSFKKI FDEAKTAQEK DSLITPHVSR SSTPRESPCG KIAVAVLEET 1500
TRERTDVIQG DDVADAASEV EVSSTSETTT KAVVSPPKFV FGSESVKRIF SSEKSKPFAF 1560
GNSSATGSLF GFSFNAPLKS NNSETSSVAQ SGSESKVEPK KCELSKNSDI EQSSDSKVKN 1620
LSASFPTEES SINYTFKTPE KEPPLWYAEF TKEELVQKLS STTKSADHLN GLLREIEATN 1680
AVLMEQIKLL KSEIRRLERN QEQEVSAANV EHLKNVLLQF IFLKPGSERE RLLPVINTML 1740
QLSLEEKGKL AAVAQGEE 1758 
Gene Ontology
 GO:0000042; P:protein targeting to Golgi; IEA:InterPro. 
Interpro
 IPR000237; GRIP.
 IPR011993; PH_like_dom.
 IPR000156; Ran_bind_dom.
 IPR001440; TPR-1.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR019734; TPR_repeat. 
Pfam
 PF01465; GRIP
 PF00638; Ran_BP1
 PF00515; TPR_1 
SMART
 SM00755; Grip
 SM00160; RanBD 
PROSITE
 PS50913; GRIP
 PS50196; RANBD1
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS