RADI_MOUSE - dbPTM
RADI_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RADI_MOUSE
UniProt AC P26043
Protein Name Radixin
Gene Name Rdx
Organism Mus musculus (Mouse).
Sequence Length 583
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cell projection, microvillus . Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphas
Protein Description Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane..
Protein Sequence MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERAQLENEKKKREIAEKEKERIEREKEELMERLRQIEEQTVKAQKELEEQTRKALELEQERQRAKEEAERLDRERRAAEEAKSAIAKQAADQMKNQEQLAAELAEFTAKIALLEEAKKKKEEEATEWQHKAFAAQEDLEKTKEELKTVMSAPPPPPPPPVIPPTENEHDEQDENSAEASAELSSEGVMNHRSEEERVTETQKNERVKKQLQALSSELAQARDETKKTQNDVLHAENVKAGRDKYKTLRQIRQGNTKQRIDEFEAM
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
3Ubiquitination-----MPKPINVRVT
-----CCCCEEEEEE		58.17-
3Malonylation-----MPKPINVRVT
-----CCCCEEEEEE		58.1726320211
35AcetylationQLFDQVVKTVGLREV
HHHHHHHHHHCHHHE		38.3422826441
35UbiquitinationQLFDQVVKTVGLREV
HHHHHHHHHHCHHHE		38.34-
55PhosphorylationQYVDSKGYSTWLKLN
EEECCCCCHHHHHHC		13.4817242355
60AcetylationKGYSTWLKLNKKVTQ
CCCHHHHHHCCCCCH		41.3923864654
66PhosphorylationLKLNKKVTQQDVKKE
HHHCCCCCHHHHHHH		29.4118779572
71AcetylationKVTQQDVKKENPLQF
CCCHHHHHHHCCCCE		63.7623864654
72UbiquitinationVTQQDVKKENPLQFK
CCHHHHHHHCCCCEE		63.67-
72MalonylationVTQQDVKKENPLQFK
CCHHHHHHHCCCCEE		63.6726320211
79SuccinylationKENPLQFKFRAKFFP
HHCCCCEEEEECCCC		22.4523954790
79UbiquitinationKENPLQFKFRAKFFP
HHCCCCEEEEECCCC		22.45-
83AcetylationLQFKFRAKFFPEDVS
CCEEEEECCCCCCCC		43.1923806337
83SuccinylationLQFKFRAKFFPEDVS
CCEEEEECCCCCCCC		43.19-
83SuccinylationLQFKFRAKFFPEDVS
CCEEEEECCCCCCCC		43.1923806337
83UbiquitinationLQFKFRAKFFPEDVS
CCEEEEECCCCCCCC		43.19-
139UbiquitinationAKYGDYNKEIHKPGY
HHHCCCCCCCCCCCC		52.39-
143UbiquitinationDYNKEIHKPGYLAND
CCCCCCCCCCCCCCC		45.88-
143MalonylationDYNKEIHKPGYLAND
CCCCCCCCCCCCCCC		45.8826320211
162UbiquitinationQRVLEQHKLTKEQWE
HHHHHHHCCCHHHHH		58.51-
162MalonylationQRVLEQHKLTKEQWE
HHHHHHHCCCHHHHH		58.5126320211
165AcetylationLEQHKLTKEQWEERI
HHHHCCCHHHHHHHH		59.3423954790
165UbiquitinationLEQHKLTKEQWEERI
HHHHCCCHHHHHHHH		59.34-
209UbiquitinationGVNYFEIKNKKGTEL
CCEEEEEECCCCCEE		56.36-
211UbiquitinationNYFEIKNKKGTELWL
EEEEEECCCCCEEEE		47.80-
237UbiquitinationHDDKLTPKIGFPWSE
CCCCCCCCCCCCHHH		50.67-
249PhosphorylationWSEIRNISFNDKKFV
HHHHCCCCCCCCEEE		22.8828285833
253UbiquitinationRNISFNDKKFVIKPI
CCCCCCCCEEEEEEC		49.57-
253AcetylationRNISFNDKKFVIKPI
CCCCCCCCEEEEEEC		49.57129481
253MalonylationRNISFNDKKFVIKPI
CCCCCCCCEEEEEEC		49.5726320211
254AcetylationNISFNDKKFVIKPID
CCCCCCCEEEEEECC		47.963755477
254MalonylationNISFNDKKFVIKPID
CCCCCCCEEEEEECC		47.9626320211
254UbiquitinationNISFNDKKFVIKPID
CCCCCCCEEEEEECC		47.96-
262UbiquitinationFVIKPIDKKAPDFVF
EEEEECCCCCCCCEE		52.10-
263MalonylationVIKPIDKKAPDFVFY
EEEECCCCCCCCEEE		62.4926320211
263UbiquitinationVIKPIDKKAPDFVFY
EEEECCCCCCCCEEE		62.49-
270PhosphorylationKAPDFVFYAPRLRIN
CCCCCEEEECCHHCC		15.4729899451
291PhosphorylationCMGNHELYMRRRKPD
HCCCHHHHHCCCCCC		5.8926026062
296UbiquitinationELYMRRRKPDTIEVQ
HHHHCCCCCCCHHHH		45.49-
299PhosphorylationMRRRKPDTIEVQQMK
HCCCCCCCHHHHHHH		27.8025338131
306UbiquitinationTIEVQQMKAQAREEK
CHHHHHHHHHHHHHH		32.77-
358PhosphorylationLRQIEEQTVKAQKEL
HHHHHHHHHHHHHHH		27.5324719451
360MalonylationQIEEQTVKAQKELEE
HHHHHHHHHHHHHHH		48.7826320211
360UbiquitinationQIEEQTVKAQKELEE
HHHHHHHHHHHHHHH		48.78-
363UbiquitinationEQTVKAQKELEEQTR
HHHHHHHHHHHHHHH		69.95-
400MalonylationRRAAEEAKSAIAKQA
HHHHHHHHHHHHHHH		43.6426320211
400UbiquitinationRRAAEEAKSAIAKQA
HHHHHHHHHHHHHHH		43.64-
405MalonylationEAKSAIAKQAADQMK
HHHHHHHHHHHHHHC		34.0626320211
405UbiquitinationEAKSAIAKQAADQMK
HHHHHHHHHHHHHHC		34.06-
435SuccinylationIALLEEAKKKKEEEA
HHHHHHHHHHHHHHH		69.2923954790
435MalonylationIALLEEAKKKKEEEA
HHHHHHHHHHHHHHH		69.2926320211
435UbiquitinationIALLEEAKKKKEEEA
HHHHHHHHHHHHHHH		69.29-
448UbiquitinationEATEWQHKAFAAQED
HHHHHHHHHHHHHHH		30.05-
458UbiquitinationAAQEDLEKTKEELKT
HHHHHHHHHHHHHHH		72.67-
468PhosphorylationEELKTVMSAPPPPPP
HHHHHHHCCCCCCCC		33.0325338131
482PhosphorylationPPPVIPPTENEHDEQ
CCCCCCCCCCCCCCC		46.1923140645
493PhosphorylationHDEQDENSAEASAEL
CCCCCCCHHHHHHHH		25.9923140645
497PhosphorylationDENSAEASAELSSEG
CCCHHHHHHHHHHCC		17.4923140645
501PhosphorylationAEASAELSSEGVMNH
HHHHHHHHHCCCCCC		20.1823140645
502PhosphorylationEASAELSSEGVMNHR
HHHHHHHHCCCCCCC		51.5023140645
520UbiquitinationERVTETQKNERVKKQ
HHHCHHHHHHHHHHH		69.10-
526MalonylationQKNERVKKQLQALSS
HHHHHHHHHHHHHHH		54.0826320211
526UbiquitinationQKNERVKKQLQALSS
HHHHHHHHHHHHHHH		54.08-
532PhosphorylationKKQLQALSSELAQAR
HHHHHHHHHHHHHHH		25.4525521595
533PhosphorylationKQLQALSSELAQARD
HHHHHHHHHHHHHHH		37.1630352176
543UbiquitinationAQARDETKKTQNDVL
HHHHHHHHCHHHHHC		52.34-
544MalonylationQARDETKKTQNDVLH
HHHHHHHCHHHHHCH		63.8626320211
544UbiquitinationQARDETKKTQNDVLH
HHHHHHHCHHHHHCH		63.86-
556UbiquitinationVLHAENVKAGRDKYK
HCHHHHHHCCHHHHH		57.62-
556MalonylationVLHAENVKAGRDKYK
HCHHHHHHCCHHHHH		57.6226320211
562PhosphorylationVKAGRDKYKTLRQIR
HHCCHHHHHHHHHHH		17.3129514104
564PhosphorylationAGRDKYKTLRQIRQG
CCHHHHHHHHHHHCC		24.8822942356
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
564TPhosphorylationKinaseGRK2P25098
PSP
564TPhosphorylationKinasePRKCQQ02111
GPS
564TPhosphorylationKinaseROCK2P70336
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RADI_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of RADI_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CPNE1_HUMANCPNE1physical
12522145
CPNE4_HUMANCPNE4physical
12522145
NHRF2_HUMANSLC9A3R2physical
12499563
NHRF1_HUMANSLC9A3R1physical
12499563
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RADI_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Rho-kinase phosphorylates COOH-terminal threonines ofezrin/radixin/moesin (ERM) proteins and regulates their head-to-tailassociation.";
Matsui T., Maeda M., Doi Y., Yonemura S., Amano M., Kaibuchi K.,Tsukita S., Tsukita S.;
J. Cell Biol. 140:647-657(1998).
Cited for: PHOSPHORYLATION AT THR-564, AND ENZYME REGULATION.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-270, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory