DREB_MOUSE - dbPTM
DREB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DREB_MOUSE
UniProt AC Q9QXS6
Protein Name Drebrin
Gene Name Dbn1
Organism Mus musculus (Mouse).
Sequence Length 706
Subcellular Localization Cytoplasm . Cytoplasm, cell cortex . Cell junction . Cell projection . Cell projection, growth cone . In the absence of antigen, evenly distributed throughout subcortical regions of the T-cell membrane and cytoplasm. In the presence of antigen, distr
Protein Description Drebrins might play some role in cell migration, extension of neuronal processes and plasticity of dendrites. Required for actin polymerization at immunological synapses (IS) and for CXCR4 recruitment to IS..
Protein Sequence MAGVSFSGHRLELLAAYEEVIREESAADWALYTYEDGSDDLKLAASGEGGLQELSGHFENQKVMYGFCSVKDSQAALPKYVLINWVGEDVPDARKCACASHVAKVAEFFQGVDVIVNASSVEDIDAGAIGQRLSNGLARLSSPVLHRLRLREDENAEPVGTTYQKTDAAVEMKRINREQFWEQAKKEEELRKEEERKKALDARLRFEQERMEQERQEQEERERRYREREQQIEEHRRKQQSLEAEEAKRRLKEQSIFGDQRDEEEESQMKKSESEVEEAAAIIAQRPDNPREFFRQQERVASASGGSCDAPAPAPFNHRPGRPYCPFIKASDSGPSSSSSSSSSPPRTPFPYITCHRTPNLSSSLPCSHLDSHRRMAPTPIPTRSPSDSSTASTPIAEQIERALDEVTSSQPPPPPPPPPPTQEAQETTPSLDEELSKEAKVTAAPEVWAGCAAEPPQAQEPPLLQSSPLEDSMCTESPEQAALAAPAEPAASVTSVADVHAADTIETTTATTDTTIANNVTPAAASLIDLWPGNGEEASTLQAEPRVPTPPSGAEASLAEVPLLNEAAQEPLPPVGEGCANLLNFDELPEPPATFCDPEEEVGETLAASQVLTMPSALEEVDQVLEQELEPEPHLLTNGETTQKEGTQASEGYFSQSQEEEFAQSEEPCAKVPPPVFYNKPPEIDITCWDADPVPEEEEGFEGGD
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
2Acetylation------MAGVSFSGH
------CCCCCCCHH		27.39-
5Phosphorylation---MAGVSFSGHRLE
---CCCCCCCHHHHH		16.8726824392
7Phosphorylation-MAGVSFSGHRLELL
-CCCCCCCHHHHHHH		26.6126824392
73PhosphorylationGFCSVKDSQAALPKY
EEECHHCHHHCCCCE		18.9227841257
134PhosphorylationGAIGQRLSNGLARLS
CHHHHHHHHHHHHHC		30.9215648052
141PhosphorylationSNGLARLSSPVLHRL
HHHHHHHCCHHHHHH		27.3525521595
142PhosphorylationNGLARLSSPVLHRLR
HHHHHHCCHHHHHHH		24.5018388127
162PhosphorylationNAEPVGTTYQKTDAA
CCCCCCCCEECCHHH		20.30-
163PhosphorylationAEPVGTTYQKTDAAV
CCCCCCCEECCHHHH		14.0929514104
165AcetylationPVGTTYQKTDAAVEM
CCCCCEECCHHHHHH		37.658276043
173AcetylationTDAAVEMKRINREQF
CHHHHHHHHHCHHHH		36.308276053
241PhosphorylationEHRRKQQSLEAEEAK
HHHHHHHHHHHHHHH		26.1925521595
252AcetylationEEAKRRLKEQSIFGD
HHHHHHHHHHHHHCC		52.4722826441
255PhosphorylationKRRLKEQSIFGDQRD
HHHHHHHHHHCCCCC		22.4529899451
272PhosphorylationEESQMKKSESEVEEA
HHHHHHHCHHHHHHH		40.6225521595
274PhosphorylationSQMKKSESEVEEAAA
HHHHHCHHHHHHHHH		54.7726824392
326 (in isoform 3)Phosphorylation-28.31-
331PhosphorylationYCPFIKASDSGPSSS
CCCEEECCCCCCCCC		27.5720415495
333PhosphorylationPFIKASDSGPSSSSS
CEEECCCCCCCCCCC		50.5424899341
333 (in isoform 3)Phosphorylation-50.5429514104
336PhosphorylationKASDSGPSSSSSSSS
ECCCCCCCCCCCCCC		46.5124925903
337PhosphorylationASDSGPSSSSSSSSS
CCCCCCCCCCCCCCC		37.0624719451
338PhosphorylationSDSGPSSSSSSSSSP
CCCCCCCCCCCCCCC		38.2824925903
339PhosphorylationDSGPSSSSSSSSSPP
CCCCCCCCCCCCCCC		35.8729899451
340PhosphorylationSGPSSSSSSSSSPPR
CCCCCCCCCCCCCCC		35.8729899451
341PhosphorylationGPSSSSSSSSSPPRT
CCCCCCCCCCCCCCC		35.8724925903
342PhosphorylationPSSSSSSSSSPPRTP
CCCCCCCCCCCCCCC		36.4624925903
343PhosphorylationSSSSSSSSSPPRTPF
CCCCCCCCCCCCCCC		49.1424925903
344PhosphorylationSSSSSSSSPPRTPFP
CCCCCCCCCCCCCCC		40.6525521595
348PhosphorylationSSSSPPRTPFPYITC
CCCCCCCCCCCEEEE		34.7525521595
379PhosphorylationSHRRMAPTPIPTRSP
CCCCCCCCCCCCCCC		25.0624925903
383PhosphorylationMAPTPIPTRSPSDSS
CCCCCCCCCCCCCCC		44.4924925903
385PhosphorylationPTPIPTRSPSDSSTA
CCCCCCCCCCCCCCC		31.1025521595
387PhosphorylationPIPTRSPSDSSTAST
CCCCCCCCCCCCCCC		51.9025521595
389PhosphorylationPTRSPSDSSTASTPI
CCCCCCCCCCCCCHH		33.6524925903
390PhosphorylationTRSPSDSSTASTPIA
CCCCCCCCCCCCHHH		32.7425521595
391PhosphorylationRSPSDSSTASTPIAE
CCCCCCCCCCCHHHH		28.6924925903
393PhosphorylationPSDSSTASTPIAEQI
CCCCCCCCCHHHHHH		34.5025521595
394PhosphorylationSDSSTASTPIAEQIE
CCCCCCCCHHHHHHH		19.0925521595
429PhosphorylationTQEAQETTPSLDEEL
CHHHHHCCCCCCHHH		15.3229899451
431PhosphorylationEAQETTPSLDEELSK
HHHHCCCCCCHHHHH		46.4926824392
437PhosphorylationPSLDEELSKEAKVTA
CCCCHHHHHHCCCCC		31.5629899451
468PhosphorylationEPPLLQSSPLEDSMC
CCCCCCCCCCCCCCC		22.12-
550PhosphorylationQAEPRVPTPPSGAEA
CCCCCCCCCCCCCCC		45.00-
648PhosphorylationETTQKEGTQASEGYF
CCCCCCCCCCCCCCC		23.2724925903
651PhosphorylationQKEGTQASEGYFSQS
CCCCCCCCCCCCCCC		23.0323984901
654PhosphorylationGTQASEGYFSQSQEE
CCCCCCCCCCCCHHH		8.9424925903
656PhosphorylationQASEGYFSQSQEEEF
CCCCCCCCCCHHHHH		22.0424925903
658PhosphorylationSEGYFSQSQEEEFAQ
CCCCCCCCHHHHHHH		38.0625521595
666PhosphorylationQEEEFAQSEEPCAKV
HHHHHHHCCCCHHCC		40.2627149854
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
658SPhosphorylationKinaseATMQ13315
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of DREB_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DREB_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-142; SER-344 ANDSER-385, AND MASS SPECTROMETRY.
"Quantitative analysis of both protein expression and serine /threonine post-translational modifications through stable isotopelabeling with dithiothreitol.";
Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,Hart G.W., Burlingame A.L.;
Proteomics 5:388-398(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, AND MASSSPECTROMETRY.
"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-142, AND MASSSPECTROMETRY.
"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 SER-390 AND THR-394, ANDMASS SPECTROMETRY.

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