CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005482
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Radixin 
Protein Synonyms/Alias
 ESP10 
Gene Name
 Rdx 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
35QLFDQVVKTVGLREVacetylation[1]
35QLFDQVVKTVGLREVubiquitination[2, 3, 4]
60KGYSTWLKLNKKVTQacetylation[1, 5]
71KVTQQDVKKENPLQFacetylation[5]
72VTQQDVKKENPLQFKubiquitination[2, 6]
79KENPLQFKFRAKFFPubiquitination[2, 3, 6]
83LQFKFRAKFFPEDVSacetylation[1, 7]
83LQFKFRAKFFPEDVSsuccinylation[7]
83LQFKFRAKFFPEDVSubiquitination[2, 3, 4, 6]
139AKYGDYNKEIHKPGYubiquitination[2, 6]
143DYNKEIHKPGYLANDubiquitination[2]
162QRVLEQHKLTKEQWEubiquitination[2, 3, 4, 6]
165LEQHKLTKEQWEERIubiquitination[2]
209GVNYFEIKNKKGTELubiquitination[2, 4, 6]
237HDDKLTPKIGFPWSEubiquitination[3, 6]
253RNISFNDKKFVIKPIubiquitination[6]
254NISFNDKKFVIKPIDubiquitination[3]
262FVIKPIDKKAPDFVFubiquitination[6]
263VIKPIDKKAPDFVFYubiquitination[3, 6]
296ELYMRRRKPDTIEVQubiquitination[6]
306TIEVQQMKAQAREEKubiquitination[6]
360QIEEQTVKAQKELEEubiquitination[2]
363EQTVKAQKELEEQTRubiquitination[2]
400RRAAEEAKSAIAKQAubiquitination[2]
405EAKSAIAKQAADQMKubiquitination[2]
435IALLEEAKKKKEEEAubiquitination[2]
448EATEWQHKAFAAQEDubiquitination[2]
458AAQEDLEKTKEELKTubiquitination[2]
520ERVTETQKNERVKKQubiquitination[2]
526QKNERVKKQLQALSSubiquitination[2]
543AQARDETKKTQNDVLubiquitination[2]
544QARDETKKTQNDVLHubiquitination[2]
556VLHAENVKAGRDKYKubiquitination[2, 6]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] 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]
 [4] 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]
 [5] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [6] 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]
 [7] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
 Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. 
Sequence Annotation
 DOMAIN 5 295 FERM.
 REGION 60 63 Phosphatidylinositol binding.
 BINDING 278 278 Phosphatidylinositol.
 MOD_RES 270 270 Phosphotyrosine.
 MOD_RES 564 564 Phosphothreonine; by ROCK2.  
Keyword
 3D-structure; Actin capping; Actin-binding; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 583 AA 
Protein Sequence
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTVGLR EVWFFGLQYV DSKGYSTWLK 60
LNKKVTQQDV KKENPLQFKF RAKFFPEDVS EELIQEITQR LFFLQVKEAI LNDEIYCPPE 120
TAVLLASYAV QAKYGDYNKE IHKPGYLAND RLLPQRVLEQ HKLTKEQWEE RIQNWHEEHR 180
GMLREDSMME YLKIAQDLEM YGVNYFEIKN KKGTELWLGV DALGLNIYEH DDKLTPKIGF 240
PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI 300
EVQQMKAQAR EEKHQKQLER AQLENEKKKR EIAEKEKERI EREKEELMER LRQIEEQTVK 360
AQKELEEQTR KALELEQERQ RAKEEAERLD RERRAAEEAK SAIAKQAADQ MKNQEQLAAE 420
LAEFTAKIAL LEEAKKKKEE EATEWQHKAF AAQEDLEKTK EELKTVMSAP PPPPPPPVIP 480
PTENEHDEQD ENSAEASAEL SSEGVMNHRS EEERVTETQK NERVKKQLQA LSSELAQARD 540
ETKKTQNDVL HAENVKAGRD KYKTLRQIRQ GNTKQRIDEF EAM 583 
Gene Ontology
 GO:0045177; C:apical part of cell; IDA:MGI.
 GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0019898; C:extrinsic to membrane; IEA:InterPro.
 GO:0030175; C:filopodium; IDA:MGI.
 GO:0005925; C:focal adhesion; IEA:Compara.
 GO:0030027; C:lamellipodium; IDA:MGI.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0001726; C:ruffle; IDA:MGI.
 GO:0032420; C:stereocilium; IDA:MGI.
 GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
 GO:0045176; P:apical protein localization; IMP:MGI.
 GO:0030033; P:microvillus assembly; IMP:MGI. 
Interpro
 IPR019749; Band_41_domain.
 IPR019750; Band_41_fam.
 IPR011174; ERM.
 IPR011259; ERM_C_dom.
 IPR000798; Ez/rad/moesin_like.
 IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
 IPR019748; FERM_central.
 IPR019747; FERM_CS.
 IPR000299; FERM_domain.
 IPR018979; FERM_N.
 IPR018980; FERM_PH-like_C.
 IPR008954; Moesin.
 IPR011993; PH_like_dom. 
Pfam
 PF00769; ERM
 PF09380; FERM_C
 PF00373; FERM_M
 PF09379; FERM_N 
SMART
 SM00295; B41 
PROSITE
 PS00660; FERM_1
 PS00661; FERM_2
 PS50057; FERM_3 
PRINTS
 PR00935; BAND41.
 PR00661; ERMFAMILY.