E41L1_MOUSE - dbPTM
E41L1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID E41L1_MOUSE
UniProt AC Q9Z2H5
Protein Name Band 4.1-like protein 1
Gene Name Epb41l1
Organism Mus musculus (Mouse).
Sequence Length 879
Subcellular Localization Cytoplasm, cytoskeleton.
Protein Description May function to confer stability and plasticity to neuronal membrane via multiple interactions, including the spectrin-actin-based cytoskeleton, integral membrane channels and membrane-associated guanylate kinases..
Protein Sequence MTTETGPDSEVKKAQEETPQQPEAAAAVTTPVTPAGHSHPETNSNEKHLTQQDTRPAEQSLDMDDKDYSEADGLSERTTPSKAQKSPQKIAKKFKSAICRVTLLDASEYECEVEKHGRGQVLFDLVCEHLNLLEKDYFGLTFCDADSQKNWLDPSKEIKKQIRSSPWNFAFTVKFYPPDPAQLTEDITRYYLCLQLRADIITGRLPCSFVTHALLGSYAVQAELGDYDAEEHVGNYVSELRFAPNQTRELEERIMELHKTYRGMTPGEAEIHFLENAKKLSMYGVDLHHAKDSEGIDIMLGVCANGLLIYRDRLRINRFAWPKILKISYKRSNFYIKIRPGEYEQFESTIGFKLPNHRSAKRLWKVCIEHHTFFRLVSPEPPPKGFLVMGSKFRYSGRTQAQTRQASALIDRPAPFFERSSSKRYTMSRSLDGAEFSRPASVSENHDAGPEGDKREDDAESGGRRSEAEEGEVRTPTKIKELKPEQETTPRHKQEFLDKPEDVLLKHQASINELKRTLKEPNSKLIHRDRDWDRERRLPSSPASPSPKGTPEKASERAGLREGSEEKVKPPRPRAPESDMGDEDQDQERDAVFLKDNHLAIERKCSSITVSSTSSLEAEVDFTVIGDYHGGAFEDFSRSLPELDRDKSDSETEGLVFAQDLKGPSSQEDESGGLEDSPDRGACSTPEMPQFESVKAETMTVSSLAIRKKIEPEAMLQSRVSAADSTQVDGGTPMVKDFMTTPPCITTETISTTMENSLKSGKGAAAMIPGPQTVATEIRSLSPIIGKDVLTSTYGATAETLSTSTTTHVTKTVKGGFSETRIEKRIIITGDEDVDQDQALALAIKEAKLQHPDMLVTKAVVYRETDPSPEERDKKPQES
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
29PhosphorylationPEAAAAVTTPVTPAG
CHHHHHCCCCCCCCC		22.2123684622
30PhosphorylationEAAAAVTTPVTPAGH
HHHHHCCCCCCCCCC		14.7925521595
33PhosphorylationAAVTTPVTPAGHSHP
HHCCCCCCCCCCCCC		14.5025521595
38PhosphorylationPVTPAGHSHPETNSN
CCCCCCCCCCCCCCC		39.5630372032
42PhosphorylationAGHSHPETNSNEKHL
CCCCCCCCCCCCCCC		48.6923684622
44PhosphorylationHSHPETNSNEKHLTQ
CCCCCCCCCCCCCCC		54.5120415495
50PhosphorylationNSNEKHLTQQDTRPA
CCCCCCCCCCCCCHH		24.7320415495
54PhosphorylationKHLTQQDTRPAEQSL
CCCCCCCCCHHHHCC		33.9326239621
60PhosphorylationDTRPAEQSLDMDDKD
CCCHHHHCCCCCCCC		20.1722324799
68PhosphorylationLDMDDKDYSEADGLS
CCCCCCCHHHCCCCC		17.7225521595
69PhosphorylationDMDDKDYSEADGLSE
CCCCCCHHHCCCCCC		36.1227180971
75PhosphorylationYSEADGLSERTTPSK
HHHCCCCCCCCCCCH		30.4825521595
78PhosphorylationADGLSERTTPSKAQK
CCCCCCCCCCCHHCC		38.7225521595
79PhosphorylationDGLSERTTPSKAQKS
CCCCCCCCCCHHCCC		31.6126239621
81PhosphorylationLSERTTPSKAQKSPQ
CCCCCCCCHHCCCHH		38.2329899451
86PhosphorylationTPSKAQKSPQKIAKK
CCCHHCCCHHHHHHH		22.0829899451
149UbiquitinationFCDADSQKNWLDPSK
ECCCCCCCCCCCCCH		54.78-
261PhosphorylationIMELHKTYRGMTPGE
HHHHHHHHCCCCCCC		15.2425338131
265PhosphorylationHKTYRGMTPGEAEIH
HHHHCCCCCCCCEEH		30.8521183079
281PhosphorylationLENAKKLSMYGVDLH
HHHHHHHEEECCCCC		20.8821183079
335PhosphorylationSYKRSNFYIKIRPGE
EEECCCEEEEECCCC		12.93-
343PhosphorylationIKIRPGEYEQFESTI
EEECCCCCCEECCCC		22.4229899451
372PhosphorylationKVCIEHHTFFRLVSP
HHHHHHCCEEEECCC		26.7822324799
378PhosphorylationHTFFRLVSPEPPPKG
CCEEEECCCCCCCCC		28.3025521595
391PhosphorylationKGFLVMGSKFRYSGR
CCEEEECCCCEECCC		15.5529514104
395PhosphorylationVMGSKFRYSGRTQAQ
EECCCCEECCCCHHH		20.7121454597
396PhosphorylationMGSKFRYSGRTQAQT
ECCCCEECCCCHHHH		19.9718388127
399PhosphorylationKFRYSGRTQAQTRQA
CCEECCCCHHHHHHH		31.6129514104
403PhosphorylationSGRTQAQTRQASALI
CCCCHHHHHHHHHHC		27.9729514104
407PhosphorylationQAQTRQASALIDRPA
HHHHHHHHHHCCCCC		18.4422324799
422PhosphorylationPFFERSSSKRYTMSR
CCCCCCCCCCEEECC		23.5429514104
425PhosphorylationERSSSKRYTMSRSLD
CCCCCCCEEECCCCC		15.55-
426PhosphorylationRSSSKRYTMSRSLDG
CCCCCCEEECCCCCC		16.8327717184
430PhosphorylationKRYTMSRSLDGAEFS
CCEEECCCCCCCCCC		24.4127087446
437PhosphorylationSLDGAEFSRPASVSE
CCCCCCCCCCCCCCC		28.9427087446
441PhosphorylationAEFSRPASVSENHDA
CCCCCCCCCCCCCCC		28.9427087446
443PhosphorylationFSRPASVSENHDAGP
CCCCCCCCCCCCCCC		30.1325619855
461PhosphorylationKREDDAESGGRRSEA
CCHHHHHCCCCCCCH		48.5525521595
466PhosphorylationAESGGRRSEAEEGEV
HHCCCCCCCHHCCCC		39.5425521595
475PhosphorylationAEEGEVRTPTKIKEL
HHCCCCCCCCCHHHC		40.2525521595
475 (in isoform 2)Phosphorylation-40.2526824392
475 (in isoform 3)Phosphorylation-40.2526824392
477PhosphorylationEGEVRTPTKIKELKP
CCCCCCCCCHHHCCC		44.8025521595
488PhosphorylationELKPEQETTPRHKQE
HCCCCCCCCHHHHHH		41.6222324799
489PhosphorylationLKPEQETTPRHKQEF
CCCCCCCCHHHHHHH		19.9925521595
498 (in isoform 2)Phosphorylation-70.5526824392
498 (in isoform 3)Phosphorylation-70.5526824392
510PhosphorylationVLLKHQASINELKRT
HHHHHHHHHHHHHHH		21.2625521595
515MethylationQASINELKRTLKEPN
HHHHHHHHHHHHCCC		36.84-
515UbiquitinationQASINELKRTLKEPN
HHHHHHHHHHHHCCC		36.84-
532 (in isoform 3)Phosphorylation-13.8827841257
534 (in isoform 3)Phosphorylation-34.7627841257
538 (in isoform 3)Phosphorylation-6.3827841257
540PhosphorylationDRERRLPSSPASPSP
HHHCCCCCCCCCCCC		54.2524925903
541PhosphorylationRERRLPSSPASPSPK
HHCCCCCCCCCCCCC		23.6525521595
544PhosphorylationRLPSSPASPSPKGTP
CCCCCCCCCCCCCCH		29.3325521595
546PhosphorylationPSSPASPSPKGTPEK
CCCCCCCCCCCCHHH		36.4325521595
550PhosphorylationASPSPKGTPEKASER
CCCCCCCCHHHHHHH		34.1125521595
564PhosphorylationRAGLREGSEEKVKPP
HHCCCCCCCCCCCCC		37.5225521595
578PhosphorylationPRPRAPESDMGDEDQ
CCCCCCCCCCCCCCC		31.6621149613
580PhosphorylationPRAPESDMGDEDQDQ
CCCCCCCCCCCCCHH		11.53-
639PhosphorylationAFEDFSRSLPELDRD
HHHHHHHHCCCCCCC		47.2625521595
648PhosphorylationPELDRDKSDSETEGL
CCCCCCCCCCCCCCE		51.1325521595
650PhosphorylationLDRDKSDSETEGLVF
CCCCCCCCCCCCEEE		54.2118388127
652PhosphorylationRDKSDSETEGLVFAQ
CCCCCCCCCCEEEEE		39.0327087446
665PhosphorylationAQDLKGPSSQEDESG
EECCCCCCCCCCCCC		54.0125521595
666PhosphorylationQDLKGPSSQEDESGG
ECCCCCCCCCCCCCC		40.5025521595
671PhosphorylationPSSQEDESGGLEDSP
CCCCCCCCCCCCCCC		50.9425521595
677PhosphorylationESGGLEDSPDRGACS
CCCCCCCCCCCCCCC		21.2325521595
684PhosphorylationSPDRGACSTPEMPQF
CCCCCCCCCCCCCCC		46.6025521595
685PhosphorylationPDRGACSTPEMPQFE
CCCCCCCCCCCCCCC		24.1325521595
693PhosphorylationPEMPQFESVKAETMT
CCCCCCCCCCEEEEE		30.1525619855
698PhosphorylationFESVKAETMTVSSLA
CCCCCEEEEEHHHHH		24.0121183079
700PhosphorylationSVKAETMTVSSLAIR
CCCEEEEEHHHHHHH		25.3428066266
702PhosphorylationKAETMTVSSLAIRKK
CEEEEEHHHHHHHHC		15.5228066266
703PhosphorylationAETMTVSSLAIRKKI
EEEEEHHHHHHHHCC		19.9321183079
721O-linked_GlycosylationAMLQSRVSAADSTQV
HHHHHCCCCCCCCCC		19.3430059200
721PhosphorylationAMLQSRVSAADSTQV
HHHHHCCCCCCCCCC		19.3419060867
725PhosphorylationSRVSAADSTQVDGGT
HCCCCCCCCCCCCCC		18.9328066266
726PhosphorylationRVSAADSTQVDGGTP
CCCCCCCCCCCCCCC		32.9128576409
732PhosphorylationSTQVDGGTPMVKDFM
CCCCCCCCCCCCCCC		17.4628066266
740PhosphorylationPMVKDFMTTPPCITT
CCCCCCCCCCCEEEE		35.8229899451
741PhosphorylationMVKDFMTTPPCITTE
CCCCCCCCCCEEEEE		17.2819060867
757PhosphorylationISTTMENSLKSGKGA
CCHHHHHHHHCCCCC		24.7029514104
773O-linked_GlycosylationAMIPGPQTVATEIRS
EECCCCHHHHHHHHH		18.4255411853
773PhosphorylationAMIPGPQTVATEIRS
EECCCCHHHHHHHHH		18.4226643407
776O-linked_GlycosylationPGPQTVATEIRSLSP
CCCHHHHHHHHHHCC		27.8455411877
776PhosphorylationPGPQTVATEIRSLSP
CCCHHHHHHHHHHCC		27.8426643407
780PhosphorylationTVATEIRSLSPIIGK
HHHHHHHHHCCCCCH		38.5724925903
782PhosphorylationATEIRSLSPIIGKDV
HHHHHHHCCCCCHHH		18.4625521595
791PhosphorylationIIGKDVLTSTYGATA
CCCHHHHHCCCCCEE		20.9026643407
792O-linked_GlycosylationIGKDVLTSTYGATAE
CCHHHHHCCCCCEEE		18.5730059200
792PhosphorylationIGKDVLTSTYGATAE
CCHHHHHCCCCCEEE		18.5726643407
793O-linked_GlycosylationGKDVLTSTYGATAET
CHHHHHCCCCCEEEE		22.2730059200
793PhosphorylationGKDVLTSTYGATAET
CHHHHHCCCCCEEEE		22.2725168779
794PhosphorylationKDVLTSTYGATAETL
HHHHHCCCCCEEEEE		12.4425168779
797O-linked_GlycosylationLTSTYGATAETLSTS
HHCCCCCEEEEECCC		22.2146205797
797PhosphorylationLTSTYGATAETLSTS
HHCCCCCEEEEECCC		22.2125168779
800O-linked_GlycosylationTYGATAETLSTSTTT
CCCCEEEEECCCCCE		24.4430059200
805PhosphorylationAETLSTSTTTHVTKT
EEEECCCCCEEEEEE		35.4829899451
812PhosphorylationTTTHVTKTVKGGFSE
CCEEEEEEECCCCCC		20.34-
818PhosphorylationKTVKGGFSETRIEKR
EEECCCCCCCEEEEE		41.1423375375
857PhosphorylationQHPDMLVTKAVVYRE
CCCCEEEEEEEEEEC		14.8822871156
862PhosphorylationLVTKAVVYRETDPSP
EEEEEEEEECCCCCH		8.9916452087
865PhosphorylationKAVVYRETDPSPEER
EEEEEECCCCCHHHH		44.1824925903
868PhosphorylationVYRETDPSPEERDKK
EEECCCCCHHHHCCC		47.9925521595
879PhosphorylationRDKKPQES-------
HCCCCCCC-------		40.0317622165
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

Oops, there are no upstream regulatory protein records of E41L1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of E41L1_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 E41L1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CADM3_MOUSECadm3physical
15893517
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of E41L1_MOUSE

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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-430; SER-510 ANDSER-639, AND MASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378; SER-650; SER-677AND THR-685, AND MASS SPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-865; SER-868 ANDSER-879, AND MASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546; THR-550 ANDSER-648, AND MASS SPECTROMETRY.
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; THR-475; SER-546;THR-550; SER-648 AND SER-650, AND MASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-685, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-343, AND MASSSPECTROMETRY.

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