MOES_MOUSE - dbPTM
MOES_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MOES_MOUSE
UniProt AC P26041
Protein Name Moesin {ECO:0000303|PubMed:1429901}
Gene Name Msn {ECO:0000312|MGI:MGI:97167}
Organism Mus musculus (Mouse).
Sequence Length 577
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasm, cytoskeleton . Apical cell membrane
Peripheral membrane protein
Cytoplasmic side . Cell projection, microvillus membrane
Peripheral membrane protein
Cytoplasmic side . Cel
Protein Description Probably involved in connections of major cytoskeletal structures to the plasma membrane. Plays a role in regulating the proliferation, migration, and adhesion of human lymphoid cells and participates in immunologic synapse formation..
Protein Sequence MPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKAFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQMERALLENEKKKRELAEKEKEKIEREKEELMEKLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLASEMAELTARISQLEMARKKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEHDEQDENGAEASAELRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM
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
56PhosphorylationYQDTKAFSTWLKLNK
ECCCCHHHHHHHHCC		24.4328833060
57PhosphorylationQDTKAFSTWLKLNKK
CCCCHHHHHHHHCCC		28.5021082442
60UbiquitinationKAFSTWLKLNKKVTA
CHHHHHHHHCCCCCH		41.3922790023
60AcetylationKAFSTWLKLNKKVTA
CHHHHHHHHCCCCCH		41.3922826441
63AcetylationSTWLKLNKKVTAQDV
HHHHHHCCCCCHHHH		60.0822826441
64SuccinylationTWLKLNKKVTAQDVR
HHHHHCCCCCHHHHH		43.6823806337
64AcetylationTWLKLNKKVTAQDVR
HHHHHCCCCCHHHHH		43.6823806337
72UbiquitinationVTAQDVRKESPLLFK
CCHHHHHHHCCCEEE		63.49-
72SuccinylationVTAQDVRKESPLLFK
CCHHHHHHHCCCEEE		63.4923806337
72AcetylationVTAQDVRKESPLLFK
CCHHHHHHHCCCEEE		63.4923806337
74PhosphorylationAQDVRKESPLLFKFR
HHHHHHHCCCEEEEE		24.7126824392
79AcetylationKESPLLFKFRAKFYP
HHCCCEEEEEECCCC		33.6323806337
79UbiquitinationKESPLLFKFRAKFYP
HHCCCEEEEEECCCC		33.6327667366
79SuccinylationKESPLLFKFRAKFYP
HHCCCEEEEEECCCC		33.6323806337
83SuccinylationLLFKFRAKFYPEDVS
CEEEEEECCCCCCCC		40.97-
83SuccinylationLLFKFRAKFYPEDVS
CEEEEEECCCCCCCC		40.9722790023
83UbiquitinationLLFKFRAKFYPEDVS
CEEEEEECCCCCCCC		40.97-
116PhosphorylationGILNDDIYCPPETAV
CCCCCCCCCCHHHHH		13.0922817900
117S-nitrosocysteineILNDDIYCPPETAVL
CCCCCCCCCHHHHHH		4.65-
117GlutathionylationILNDDIYCPPETAVL
CCCCCCCCCHHHHHH		4.6524333276
117S-nitrosylationILNDDIYCPPETAVL
CCCCCCCCCHHHHHH		4.65-
133UbiquitinationASYAVQSKYGDFNKE
HHHHHHHHHCCCCHH		35.84-
139UbiquitinationSKYGDFNKEVHKSGY
HHHCCCCHHHHHCCC		62.1922790023
139AcetylationSKYGDFNKEVHKSGY
HHHCCCCHHHHHCCC		62.1922826441
143UbiquitinationDFNKEVHKSGYLAGD
CCCHHHHHCCCCCCC		51.2422790023
144PhosphorylationFNKEVHKSGYLAGDK
CCHHHHHCCCCCCCC		20.1428285833
146PhosphorylationKEVHKSGYLAGDKLL
HHHHHCCCCCCCCCC		10.64-
151SuccinylationSGYLAGDKLLPQRVL
CCCCCCCCCCHHHHH		51.5123806337
151AcetylationSGYLAGDKLLPQRVL
CCCCCCCCCCHHHHH		51.5123806337
162UbiquitinationQRVLEQHKLNKDQWE
HHHHHHHCCCHHHHH		54.1522790023
162AcetylationQRVLEQHKLNKDQWE
HHHHHHHCCCHHHHH		54.1523806337
165UbiquitinationLEQHKLNKDQWEERI
HHHHCCCHHHHHHHH		62.8322790023
165AcetylationLEQHKLNKDQWEERI
HHHHCCCHHHHHHHH		62.8323806337
209UbiquitinationGVNYFSIKNKKGSEL
CCEEEEEECCCCCEE		62.6122790023
211UbiquitinationNYFSIKNKKGSELWL
EEEEEECCCCCEEEE		54.21-
237UbiquitinationQNDRLTPKIGFPWSE
CCCCCCCCCCCCHHH		50.67-
249PhosphorylationWSEIRNISFNDKKFV
HHHHCCCCCCCCEEE		22.8828285833
253AcetylationRNISFNDKKFVIKPI
CCCCCCCCEEEEEEC		49.57129473
253UbiquitinationRNISFNDKKFVIKPI
CCCCCCCCEEEEEEC		49.57-
254AcetylationNISFNDKKFVIKPID
CCCCCCCEEEEEECC		47.963755473
263UbiquitinationVIKPIDKKAPDFVFY
EEEECCCCCCCCEEE		62.49-
270PhosphorylationKAPDFVFYAPRLRIN
CCCCCEEEECCHHCC		15.4729899451
284GlutathionylationNKRILALCMGNHELY
CHHHHHHHCCCHHHH		2.4624333276
291PhosphorylationCMGNHELYMRRRKPD
HCCCHHHHHCCCCCC		5.8926026062
299PhosphorylationMRRRKPDTIEVQQMK
HCCCCCCCHHHHHHH		27.8025338131
306UbiquitinationTIEVQQMKAQAREEK
CHHHHHHHHHHHHHH		32.77-
335SuccinylationKKRELAEKEKEKIER
HHHHHHHHHHHHHHH		69.3626388266
350UbiquitinationEKEELMEKLKQIEEQ
HHHHHHHHHHHHHHH		47.2022790023
352UbiquitinationEELMEKLKQIEEQTK
HHHHHHHHHHHHHHH		61.3722790023
360UbiquitinationQIEEQTKKAQQELEE
HHHHHHHHHHHHHHH		55.6122790023
384PhosphorylationQERKRAQSEAEKLAK
HHHHHHHHHHHHHHH		37.4824899341
400AcetylationRQEAEEAKEALLQAS
HHHHHHHHHHHHHHH		46.9623236377
407PhosphorylationKEALLQASRDQKKTQ
HHHHHHHHHHHHHHH		24.3525266776
412AcetylationQASRDQKKTQEQLAS
HHHHHHHHHHHHHHH		50.2123806337
419PhosphorylationKTQEQLASEMAELTA
HHHHHHHHHHHHHHH		36.1822817900
425PhosphorylationASEMAELTARISQLE
HHHHHHHHHHHHHHH		12.8524719451
429PhosphorylationAELTARISQLEMARK
HHHHHHHHHHHHHHH		24.1427180971
438AcetylationLEMARKKKESEAVEW
HHHHHHHHHHHHHHH		70.3022826441
440PhosphorylationMARKKKESEAVEWQQ
HHHHHHHHHHHHHHH		39.4724719451
448UbiquitinationEAVEWQQKAQMVQED
HHHHHHHHHHHHHHH		26.0322790023
458UbiquitinationMVQEDLEKTRAELKT
HHHHHHHHHHHHHHH		51.0822790023
458AcetylationMVQEDLEKTRAELKT
HHHHHHHHHHHHHHH		51.0822826441
464UbiquitinationEKTRAELKTAMSTPH
HHHHHHHHHHHCCCC		26.2422790023
465PhosphorylationKTRAELKTAMSTPHV
HHHHHHHHHHCCCCC		39.9727087446
468PhosphorylationAELKTAMSTPHVAEP
HHHHHHHCCCCCCCC		36.0027087446
469PhosphorylationELKTAMSTPHVAEPA
HHHHHHCCCCCCCCC		12.3430635358
491PhosphorylationDENGAEASAELRADA
CCCCHHHHHHHHHHH		17.4922942356
504PhosphorylationDAMAKDRSEEERTTE
HHHHCCCCHHHHCHH		60.5426824392
509PhosphorylationDRSEEERTTEAEKNE
CCCHHHHCHHHHHHH		32.0629550500
523UbiquitinationERVQKHLKALTSELA
HHHHHHHHHHHHHHH		40.8622790023
526PhosphorylationQKHLKALTSELANAR
HHHHHHHHHHHHHCC		25.6427180971
527PhosphorylationKHLKALTSELANARD
HHHHHHHHHHHHCCH		31.3127180971
536PhosphorylationLANARDESKKTANDM
HHHCCHHHHHHHHHH		43.6829176673
537UbiquitinationANARDESKKTANDMI
HHCCHHHHHHHHHHH		52.6922790023
538UbiquitinationNARDESKKTANDMIH
HCCHHHHHHHHHHHH		63.2522790023
556PhosphorylationMRLGRDKYKTLRQIR
HHCCHHHHHHHHHHH		17.3129514104
558PhosphorylationLGRDKYKTLRQIRQG
CCHHHHHHHHHHHCC		24.8819737918
576PhosphorylationQRIDEFESM------
HCHHHHHCC------		34.8027087446
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
558TPhosphorylationKinaseROCK1Q13464
PSP
558TPhosphorylationKinaseROCK2P70336
Uniprot
558TPhosphorylationKinaseLOKO55098
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
117COxidation

-
117CS-nitrosylation

-
558TPhosphorylation

9856983
558TPhosphorylation

9856983
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 MOES_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CATZ_HUMANCTSZphysical
26496610
FLOT2_HUMANFLOT2physical
26496610
GNS_HUMANGNSphysical
26496610
HD_HUMANHTTphysical
26496610
NDUV3_HUMANNDUFV3physical
26496610
PSMD2_HUMANPSMD2physical
26496610
RADI_HUMANRDXphysical
26496610
ELOC_HUMANTCEB1physical
26496610
EZRI_HUMANEZRphysical
26496610
USP9X_HUMANUSP9Xphysical
26496610
DYSF_HUMANDYSFphysical
26496610
ZMYM4_HUMANZMYM4physical
26496610
RPGF2_HUMANRAPGEF2physical
26496610
KI20A_HUMANKIF20Aphysical
26496610
PRDX3_HUMANPRDX3physical
26496610
HAUS7_HUMANHAUS7physical
26496610
ZF64A_HUMANZFP64physical
26496610
ZF64B_HUMANZFP64physical
26496610
ZN624_HUMANZNF624physical
26496610
DOCK6_HUMANDOCK6physical
26496610
ACD10_HUMANACAD10physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MOES_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND MASSSPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-558, AND MASSSPECTROMETRY.
"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-558, AND ENZYME REGULATION.
"Phosphorylation of moesin by rho-associated kinase (Rho-kinase) playsa crucial role in the formation of microvilli-like structures.";
Oshiro N., Fukata Y., Kaibuchi K.;
J. Biol. Chem. 273:34663-34666(1998).
Cited for: PHOSPHORYLATION AT THR-558, SUBCELLULAR LOCATION, AND MUTAGENESIS OFTHR-558.
"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-116, AND MASSSPECTROMETRY.

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