EZRI_MOUSE - dbPTM
EZRI_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EZRI_MOUSE
UniProt AC P26040
Protein Name Ezrin
Gene Name Ezr
Organism Mus musculus (Mouse).
Sequence Length 586
Subcellular Localization Apical cell membrane
Peripheral membrane protein
Cytoplasmic side . Cell projection . Cell projection, microvillus membrane
Peripheral membrane protein
Cytoplasmic side . Cell projection, ruffle membrane
Peripheral membrane protein
Cytoplasmic
Protein Description Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis (By similarity)..
Protein Sequence MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLQYVDNKGFPTWLKLDKKVSAQEVRKENPVQFKFRAKFYPEDVAEELIQDITQKLFFLQVKDGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEMHKSGYLSSERLIPQRVMDQHKLSRDQWEDRIQVWHAEHRGMLKDSAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMLREKEELMLRLQDYEQKTKRAEKELSEQIEKALQLEEERRRAQEEAERLEADRMAALRAKEELERQAQDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVNYHVQEGLQDEGAEPMGYSAELSSEGILDDRNEEKRITEAEKNERVQRQLLTLSNELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAM
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
35AcetylationQLFDQVVKTIGLREV
HHHHHHHHHHCCCHH
35.2522826441
57PhosphorylationVDNKGFPTWLKLDKK
ECCCCCCCEEECCCC
40.9622817900
60AcetylationKGFPTWLKLDKKVSA
CCCCCEEECCCCCCH
46.32-
60PhosphoglycerylationKGFPTWLKLDKKVSA
CCCCCEEECCCCCCH
46.32-
72UbiquitinationVSAQEVRKENPVQFK
CCHHHHHHHCCCCEE
68.0022790023
79UbiquitinationKENPVQFKFRAKFYP
HHCCCCEEEEECCCC
19.4922790023
83UbiquitinationVQFKFRAKFYPEDVA
CCEEEEECCCCHHHH
40.97-
139UbiquitinationAKFGDYNKEMHKSGY
HHHCCCCHHHHHCCC
50.6222790023
143UbiquitinationDYNKEMHKSGYLSSE
CCCHHHHHCCCCCCC
44.2422790023
144PhosphorylationYNKEMHKSGYLSSER
CCHHHHHCCCCCCCC
20.2828973931
146PhosphorylationKEMHKSGYLSSERLI
HHHHHCCCCCCCCCC
15.5322817900
148PhosphorylationMHKSGYLSSERLIPQ
HHHCCCCCCCCCCCH
22.9728973931
162UbiquitinationQRVMDQHKLSRDQWE
HHHHHHHCCCHHHHH
42.3922790023
184UbiquitinationAEHRGMLKDSAMLEY
HHHCCCCCCHHHHHH
40.5222790023
191PhosphorylationKDSAMLEYLKIAQDL
CCHHHHHHHHHHHHH
14.88-
209UbiquitinationGINYFEIKNKKGTDL
CCCEEEEECCCCCCE
56.3622790023
235PhosphorylationYEKDDKLTPKIGFPW
EECCCCCCCCCCCCH
28.4222817900
237UbiquitinationKDDKLTPKIGFPWSE
CCCCCCCCCCCCHHH
50.6722790023
237AcetylationKDDKLTPKIGFPWSE
CCCCCCCCCCCCHHH
50.6722826441
249PhosphorylationWSEIRNISFNDKKFV
HHHHCCCCCCCCEEE
22.8828285833
253UbiquitinationRNISFNDKKFVIKPI
CCCCCCCCEEEEEEC
49.57-
253MalonylationRNISFNDKKFVIKPI
CCCCCCCCEEEEEEC
49.5726320211
253AcetylationRNISFNDKKFVIKPI
CCCCCCCCEEEEEEC
49.5723236377
254MalonylationNISFNDKKFVIKPID
CCCCCCCEEEEEECC
47.9626320211
254AcetylationNISFNDKKFVIKPID
CCCCCCCEEEEEECC
47.9622826441
258AcetylationNDKKFVIKPIDKKAP
CCCEEEEEECCCCCC
30.5322826441
262AcetylationFVIKPIDKKAPDFVF
EEEEECCCCCCCCEE
52.1022826441
263MalonylationVIKPIDKKAPDFVFY
EEEECCCCCCCCEEE
62.4926320211
263UbiquitinationVIKPIDKKAPDFVFY
EEEECCCCCCCCEEE
62.49-
263AcetylationVIKPIDKKAPDFVFY
EEEECCCCCCCCEEE
62.4922826441
270PhosphorylationKAPDFVFYAPRLRIN
CCCCCEEEECCHHCC
15.4729899451
291PhosphorylationCMGNHELYMRRRKPD
HCCCHHHHHCCCCCC
5.89-
299PhosphorylationMRRRKPDTIEVQQMK
HCCCCCCCHHHHHHH
27.8025338131
306UbiquitinationTIEVQQMKAQAREEK
CHHHHHHHHHHHHHH
32.7722790023
332PhosphorylationTEKKRRETVEREKEQ
HHHHHHHHHHHHHHH
26.3429899451
337UbiquitinationRETVEREKEQMLREK
HHHHHHHHHHHHHHH
60.5122790023
344UbiquitinationKEQMLREKEELMLRL
HHHHHHHHHHHHHHH
50.4822790023
354PhosphorylationLMLRLQDYEQKTKRA
HHHHHHHHHHHHHHH
13.8022817900
363UbiquitinationQKTKRAEKELSEQIE
HHHHHHHHHHHHHHH
64.0722790023
363AcetylationQKTKRAEKELSEQIE
HHHHHHHHHHHHHHH
64.0723806337
366PhosphorylationKRAEKELSEQIEKAL
HHHHHHHHHHHHHHH
28.66-
371UbiquitinationELSEQIEKALQLEEE
HHHHHHHHHHHHHHH
56.9022790023
412UbiquitinationRQAQDQIKSQEQLAA
HHHHHHHHHHHHHHH
40.2222790023
424PhosphorylationLAAELAEYTAKIALL
HHHHHHHHHHHHHHH
13.3428973931
438UbiquitinationLEEARRRKEDEVEEW
HHHHHHCCHHHHHHH
68.6422790023
450UbiquitinationEEWQHRAKEAQDDLV
HHHHHHHHHHHHHHH
54.2422790023
458UbiquitinationEAQDDLVKTKEELHL
HHHHHHHCCHHHHEE
62.2622790023
478PhosphorylationPPPPPPVYEPVNYHV
CCCCCCCCCCCCHHH
21.9322817900
483PhosphorylationPVYEPVNYHVQEGLQ
CCCCCCCHHHHCCCC
12.0022817900
523UbiquitinationKRITEAEKNERVQRQ
HCCCHHHHHHHHHHH
71.7722790023
533PhosphorylationRVQRQLLTLSNELSQ
HHHHHHHHHHHHHHH
36.4128285833
535PhosphorylationQRQLLTLSNELSQAR
HHHHHHHHHHHHHHH
24.0321082442
539PhosphorylationLTLSNELSQARDENK
HHHHHHHHHHHHHCC
18.6727600695
546UbiquitinationSQARDENKRTHNDII
HHHHHHCCCCHHHHC
57.5422790023
565PhosphorylationMRQGRDKYKTLRQIR
HHCCHHHHHHHHHHH
17.3129514104
567PhosphorylationQGRDKYKTLRQIRQG
CCHHHHHHHHHHHCC
24.8815196952

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
146YPhosphorylationKinasePDGFR-Uniprot
235TPhosphorylationKinaseCDK5P49615
PSP
354YPhosphorylationKinasePDGFR-Uniprot
478YPhosphorylationKinaseSRCP12931
PSP
567TPhosphorylationKinasePRKCIP41743
GPS
567TPhosphorylationKinasePRKCIQ62074
Uniprot
567TPhosphorylationKinaseROCK2P70336
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EZRI_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 EZRI_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MOES_HUMANMSNphysical
26496610
RADI_HUMANRDXphysical
26496610
SRRM2_HUMANSRRM2physical
26496610
IBTK_HUMANIBTKphysical
26496610
TBCD7_HUMANTBC1D7physical
26496610
TPPC9_HUMANTRAPPC9physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EZRI_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP