ADDG_MOUSE - dbPTM
ADDG_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADDG_MOUSE
UniProt AC Q9QYB5
Protein Name Gamma-adducin
Gene Name Add3
Organism Mus musculus (Mouse).
Sequence Length 706
Subcellular Localization Cytoplasm, cytoskeleton. Cell membrane
Peripheral membrane protein
Cytoplasmic side.
Protein Description Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Plays a role in actin filament capping. Binds to calmodulin..
Protein Sequence MSSDTSPAVVTTPPPPSMPHKERYFDRINESDPEYLRERNMSPDLRQDFNMMEQRKRVTQILQSPAFREDLECLIQEQMKKGHNPSGLLALQQIADYIVTSSFSGFSSPSLSLGMVTPINDLPGADTSSYVKGEKLTRCKLASLYRLADLFGWAHLANTYISVRISKEQDHIIIIPRGLSFSEATASTLVKVNIIGEVVDQGSTDLKIDHTGFSPHAAIYSTRPDVKCVIHIHTLATAAVSSMKCGILPISQESLILGDVAYYDYQGSLDEEEERIELQKVLGPSCKVLVLRNHGMVALGETLEEAFHYIFNVQMACEIQVQAVAGAGGVDNLLVLDLQKYKAFTHGVAMSGGGGVNMASHQKWKVGEIEFEGLMRTLDNLGYRTGYAYRHPLVREKPRHKSDVEIPATVTAFSFEDDSAPLSPLKFMAQRQQREKTRWLNSPNTYMKVNVPEESRNGETSPRTKITWMKAEDSSKVSSGTPIKIEDPNQFVPLNTNPTEVLEKRNKIREQNRYDLKTAGPQSQLLAGIVVDKPPSTMQFDDDDQGPPAPPNPFSHLLEGELEEYTKTIERKQQGLDDAEQGSLSDDAASVSQIQSQTQSPQSVPERLEENHELFSKSFTSMDAPVMIMNGKDEMHDVEDELAQRVSRLTTSTTIENIEITIKSPERTEEVLSPDGSPSKSPSKKKKKFRTPSFLKKNKKKEKVEA
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
2Phosphorylation------MSSDTSPAV
------CCCCCCCCE		36.6025619855
2Acetylation------MSSDTSPAV
------CCCCCCCCE		36.60-
3Phosphorylation-----MSSDTSPAVV
-----CCCCCCCCEE		43.5425619855
5Phosphorylation---MSSDTSPAVVTT
---CCCCCCCCEECC		38.2625619855
6Phosphorylation--MSSDTSPAVVTTP
--CCCCCCCCEECCC		18.8225619855
11PhosphorylationDTSPAVVTTPPPPSM
CCCCCEECCCCCCCC		27.3023684622
12PhosphorylationTSPAVVTTPPPPSMP
CCCCEECCCCCCCCC		23.3726824392
17PhosphorylationVTTPPPPSMPHKERY
ECCCCCCCCCCHHHH		51.2025619855
21UbiquitinationPPPSMPHKERYFDRI
CCCCCCCHHHHHHHC		37.71-
24PhosphorylationSMPHKERYFDRINES
CCCCHHHHHHHCCCC		15.7829514104
31PhosphorylationYFDRINESDPEYLRE
HHHHCCCCCHHHHHH		54.7125521595
35PhosphorylationINESDPEYLRERNMS
CCCCCHHHHHHCCCC		19.2226026062
42PhosphorylationYLRERNMSPDLRQDF
HHHHCCCCHHHHHHH		20.8625521595
59PhosphorylationMEQRKRVTQILQSPA
HHHHHHHHHHHHCHH		17.5826643407
64PhosphorylationRVTQILQSPAFREDL
HHHHHHHCHHHHHHH		18.1022942356
138MethylationVKGEKLTRCKLASLY
CCCCCCHHHHHHHHH		26.47-
376MethylationIEFEGLMRTLDNLGY
EEHHHHHHHHHHHCC		36.86-
384MethylationTLDNLGYRTGYAYRH
HHHHHCCCCCCCCCC		21.63-
401UbiquitinationVREKPRHKSDVEIPA
CCCCCCCCCCCCCCC		50.02-
402PhosphorylationREKPRHKSDVEIPAT
CCCCCCCCCCCCCCE		40.5424925903
409PhosphorylationSDVEIPATVTAFSFE
CCCCCCCEEEEEECC		17.0325619855
411PhosphorylationVEIPATVTAFSFEDD
CCCCCEEEEEECCCC		20.0325619855
414PhosphorylationPATVTAFSFEDDSAP
CCEEEEEECCCCCCC		25.8424925903
419PhosphorylationAFSFEDDSAPLSPLK
EEECCCCCCCCCHHH		44.0725619855
423PhosphorylationEDDSAPLSPLKFMAQ
CCCCCCCCHHHHHHH		27.4224925903
426UbiquitinationSAPLSPLKFMAQRQQ
CCCCCHHHHHHHHHH		36.16-
442PhosphorylationEKTRWLNSPNTYMKV
HHHHHCCCCCCEEEE		19.8421082442
445PhosphorylationRWLNSPNTYMKVNVP
HHCCCCCCEEEEECC		28.5128066266
446PhosphorylationWLNSPNTYMKVNVPE
HCCCCCCEEEEECCH		11.1126643407
455PhosphorylationKVNVPEESRNGETSP
EEECCHHHCCCCCCC		29.4126160508
460PhosphorylationEESRNGETSPRTKIT
HHHCCCCCCCCCEEE		45.4927087446
461PhosphorylationESRNGETSPRTKITW
HHCCCCCCCCCEEEE		14.2127087446
464PhosphorylationNGETSPRTKITWMKA
CCCCCCCCEEEEEEE		30.1326745281
478PhosphorylationAEDSSKVSSGTPIKI
ECCCCCCCCCCCCCC		27.1326643407
479PhosphorylationEDSSKVSSGTPIKIE
CCCCCCCCCCCCCCC		50.0723984901
481PhosphorylationSSKVSSGTPIKIEDP
CCCCCCCCCCCCCCC		24.6426643407
484UbiquitinationVSSGTPIKIEDPNQF
CCCCCCCCCCCCCCC		41.04-
496PhosphorylationNQFVPLNTNPTEVLE
CCCCCCCCCHHHHHH		50.7025777480
499PhosphorylationVPLNTNPTEVLEKRN
CCCCCCHHHHHHHHH		40.5725777480
514PhosphorylationKIREQNRYDLKTAGP
HHHHHHCCCCCCCCC		32.9329514104
572 (in isoform 2)Ubiquitination-33.90-
583PhosphorylationLDDAEQGSLSDDAAS
CCHHHCCCCCCCHHH		25.1328833060
585PhosphorylationDAEQGSLSDDAASVS
HHHCCCCCCCHHHHH		34.8321082442
590PhosphorylationSLSDDAASVSQIQSQ
CCCCCHHHHHHHHHH		24.8328833060
592PhosphorylationSDDAASVSQIQSQTQ
CCCHHHHHHHHHHCC		21.04-
598PhosphorylationVSQIQSQTQSPQSVP
HHHHHHHCCCCCCHH		35.94-
600PhosphorylationQIQSQTQSPQSVPER
HHHHHCCCCCCHHHH		28.44-
603PhosphorylationSQTQSPQSVPERLEE
HHCCCCCCHHHHHHH		42.9219854140
616PhosphorylationEENHELFSKSFTSMD
HHHHHHHHHCCCCCC		39.7619854140
618PhosphorylationNHELFSKSFTSMDAP
HHHHHHHCCCCCCCC		32.3425521595
620PhosphorylationELFSKSFTSMDAPVM
HHHHHCCCCCCCCEE		30.1722817900
621PhosphorylationLFSKSFTSMDAPVMI
HHHHCCCCCCCCEEE		16.8029138967
647PhosphorylationDELAQRVSRLTTSTT
HHHHHHHHHHCCCCE		24.6219367708
650PhosphorylationAQRVSRLTTSTTIEN
HHHHHHHCCCCEEEE		20.0021883323
651PhosphorylationQRVSRLTTSTTIENI
HHHHHHCCCCEEEEE		28.7721883331
652PhosphorylationRVSRLTTSTTIENIE
HHHHHCCCCEEEEEE		20.5122360483
653PhosphorylationVSRLTTSTTIENIEI
HHHHCCCCEEEEEEE		29.69204023921
654PhosphorylationSRLTTSTTIENIEIT
HHHCCCCEEEEEEEE		26.5151458459
661PhosphorylationTIENIEITIKSPERT
EEEEEEEEECCCCCC		15.0129899451
664PhosphorylationNIEITIKSPERTEEV
EEEEEECCCCCCEEC		28.3025619855
668PhosphorylationTIKSPERTEEVLSPD
EECCCCCCEECCCCC		34.5325619855
673PhosphorylationERTEEVLSPDGSPSK
CCCEECCCCCCCCCC		26.5625521595
677PhosphorylationEVLSPDGSPSKSPSK
ECCCCCCCCCCCCCH		33.1224925903
679PhosphorylationLSPDGSPSKSPSKKK
CCCCCCCCCCCCHHC		47.6825521595
681PhosphorylationPDGSPSKSPSKKKKK
CCCCCCCCCCHHCCC		38.4524925903
683PhosphorylationGSPSKSPSKKKKKFR
CCCCCCCCHHCCCCC		65.2924925903
691PhosphorylationKKKKKFRTPSFLKKN
HHCCCCCCHHHHHHC		26.8127742792
693PhosphorylationKKKFRTPSFLKKNKK
CCCCCCHHHHHHCCH		42.4725521595
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 ADDG_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADDG_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 ADDG_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ADDG_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ADDG_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-681, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; SER-677 ANDSER-681, 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-673 AND SER-681, ANDMASS SPECTROMETRY.

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