CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006453
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Radixin 
Protein Synonyms/Alias
  
Gene Name
 RDX 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
3*****MPKPINVRVTubiquitination[1]
35QLFDQVVKTVGLREVubiquitination[1]
79KENPLQFKFRAKFFPubiquitination[1]
83LQFKFRAKFFPEDVSubiquitination[1, 2]
139AKYGDYNKEIHKPGYubiquitination[2]
162QRVLEQHKLTKEQWEubiquitination[1, 2, 3, 4, 5]
209GVNYFEIKNKKGTELubiquitination[2, 3, 6]
253RNISFNDKKFVIKPIubiquitination[1]
352EELMERLKQIEEQTIubiquitination[2]
360QIEEQTIKAQKELEEubiquitination[4]
526QKNERVKKQLQALSSubiquitination[1, 2, 4, 6, 7, 8]
Reference
 [1] 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]
 [2] 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]
 [3] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [4] 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]
 [5] 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]
 [6] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [7] 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]
 [8] 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
 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 (By
 BINDING 278 278 Phosphatidylinositol (By similarity).
 MOD_RES 270 270 Phosphotyrosine (By similarity).
 MOD_RES 564 564 Phosphothreonine; by ROCK2 (By  
Keyword
 Actin capping; Actin-binding; Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Deafness; Disease mutation; Membrane; Non-syndromic deafness; Phosphoprotein; Polymorphism; 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 LKQIEEQTIK 360
AQKELEEQTR KALELDQERK RAKEEAERLE KERRAAEEAK SAIAKQAADQ MKNQEQLAAE 420
LAEFTAKIAL LEEAKKKKEE EATEWQHKAF AAQEDLEKTK EELKTVMSAP PPPPPPPVIP 480
PTENEHDEHD ENNAEASAEL SNEGVMNHRS EEERVTETQK NERVKKQLQA LSSELAQARD 540
ETKKTQNDVL HAENVKAGRD KYKTLRQIRQ GNTKQRIDEF EAM 583 
Gene Ontology
 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:0005886; C:plasma membrane; IDA:HPA.
 GO:0051693; P:actin filament capping; IEA:UniProtKB-KW. 
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.