ALDOC_MOUSE - dbPTM
ALDOC_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ALDOC_MOUSE
UniProt AC P05063
Protein Name Fructose-bisphosphate aldolase C
Gene Name Aldoc
Organism Mus musculus (Mouse).
Sequence Length 363
Subcellular Localization
Protein Description
Protein Sequence MPHSYPALSAEQKKELSDIALRIVTPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCPLPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQGRYEGSGDGGAAAQSLYIANHAY
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
4Phosphorylation----MPHSYPALSAE
----CCCCCCCCCHH		27.2655443871
5Phosphorylation---MPHSYPALSAEQ
---CCCCCCCCCHHH		6.8926643407
9PhosphorylationPHSYPALSAEQKKEL
CCCCCCCCHHHHHHH		31.6926643407
14UbiquitinationALSAEQKKELSDIAL
CCCHHHHHHHCCCCC		64.6827667366
25PhosphorylationDIALRIVTPGKGILA
CCCCEEECCCCCHHH		24.7751459485
28UbiquitinationLRIVTPGKGILAADE
CEEECCCCCHHHCCC		43.9427667366
36PhosphorylationGILAADESVGSMAKR
CHHHCCCHHHHHHHH		32.1225521595
39PhosphorylationAADESVGSMAKRLSQ
HCCCHHHHHHHHHHH		17.2625521595
42UbiquitinationESVGSMAKRLSQIGV
CHHHHHHHHHHHHCC		45.2727667366
42MalonylationESVGSMAKRLSQIGV
CHHHHHHHHHHHHCC		45.2726320211
45PhosphorylationGSMAKRLSQIGVENT
HHHHHHHHHHCCCCC		24.6422324799
65PhosphorylationLYRQVLFSADDRVKK
HHHHHHHCCHHHHHH		26.9928059163
71UbiquitinationFSADDRVKKCIGGVI
HCCHHHHHHHHCEEE		42.70-
101UbiquitinationFVRTIQDKGILVGIK
EEEEECCCCEEEEEE		31.32-
108UbiquitinationKGILVGIKVDKGVVP
CCEEEEEEECCCCEE		38.15-
111UbiquitinationLVGIKVDKGVVPLAG
EEEEEECCCCEECCC		57.5027667366
111AcetylationLVGIKVDKGVVPLAG
EEEEEECCCCEECCC		57.50-
119PhosphorylationGVVPLAGTDGETTTQ
CCEECCCCCCCCCHH		34.91-
135S-nitrosylationLDGLLERCAQYKKDG
HHHHHHHHHHHCCCC		1.7021278135
135S-nitrosocysteineLDGLLERCAQYKKDG
HHHHHHHHHHHCCCC		1.70-
139AcetylationLERCAQYKKDGADFA
HHHHHHHCCCCCCHH		32.1022361413
140UbiquitinationERCAQYKKDGADFAK
HHHHHHCCCCCCHHE		57.3627667366
147UbiquitinationKDGADFAKWRCVLKI
CCCCCHHEEEEEEEE		34.8527667366
147AcetylationKDGADFAKWRCVLKI
CCCCCHHEEEEEEEE		34.8522826441
153UbiquitinationAKWRCVLKISDRTPS
HEEEEEEEECCCCHH		21.55-
158PhosphorylationVLKISDRTPSALAIL
EEEECCCCHHHHHHH		26.9622817900
160PhosphorylationKISDRTPSALAILEN
EECCCCHHHHHHHHC		34.9922817900
174PhosphorylationNANVLARYASICQQN
CHHHHHHHHHHHHHC		10.0926239621
176PhosphorylationNVLARYASICQQNGI
HHHHHHHHHHHHCCC		18.2481018239
178S-nitrosylationLARYASICQQNGIVP
HHHHHHHHHHCCCCC		2.9322588120
178S-nitrosocysteineLARYASICQQNGIVP
HHHHHHHHHHCCCCC		2.93-
200UbiquitinationPDGDHDLKRCQYVTE
CCCCCCHHHHHHHHH		58.13-
200AcetylationPDGDHDLKRCQYVTE
CCCCCCHHHHHHHHH		58.1323236377
202S-nitrosocysteineGDHDLKRCQYVTEKV
CCCCHHHHHHHHHHH		3.06-
202S-nitrosylationGDHDLKRCQYVTEKV
CCCCHHHHHHHHHHH		3.0621278135
204PhosphorylationHDLKRCQYVTEKVLA
CCHHHHHHHHHHHHH		16.9925521595
208UbiquitinationRCQYVTEKVLAAVYK
HHHHHHHHHHHHHHH		32.93-
214PhosphorylationEKVLAAVYKALSDHH
HHHHHHHHHHHCCCC		5.9428542873
218PhosphorylationAAVYKALSDHHVYLE
HHHHHHHCCCCEEEE		39.4946162133
223PhosphorylationALSDHHVYLEGTLLK
HHCCCCEEEECEEEC		8.4865333
227PhosphorylationHHVYLEGTLLKPNMV
CCEEEECEEECCCCC		21.3946162145
230UbiquitinationYLEGTLLKPNMVTPG
EEECEEECCCCCCCC		37.14-
230AcetylationYLEGTLLKPNMVTPG
EEECEEECCCCCCCC		37.1423806337
235PhosphorylationLLKPNMVTPGHACPI
EECCCCCCCCCCCCC		16.8826060331
260PhosphorylationTVTALRRTVPPAVPG
HHHHHHHCCCCCCCC		30.8125777480
269PhosphorylationPPAVPGVTFLSGGQS
CCCCCCEEEECCCCC		25.4425777480
272PhosphorylationVPGVTFLSGGQSEEE
CCCEEEECCCCCHHH		36.3625777480
276PhosphorylationTFLSGGQSEEEASLN
EEECCCCCHHHHHCC		50.6925777480
281PhosphorylationGQSEEEASLNLNAIN
CCCHHHHHCCCCCCC		22.5225777480
290S-nitrosocysteineNLNAINRCPLPRPWA
CCCCCCCCCCCCCEE		3.34-
290S-nitrosylationNLNAINRCPLPRPWA
CCCCCCCCCCCCCEE		3.3424895380
301PhosphorylationRPWALTFSYGRALQA
CCEEEEEEHHHHHHH		22.8026643407
330UbiquitinationAATEEFIKRAEMNGL
CCCHHHHHHHHHCCC		51.3727667366
355PhosphorylationDGGAAAQSLYIANHA
CCCHHHHHEEEECCC		20.5825367039
357PhosphorylationGAAAQSLYIANHAY-
CHHHHHEEEECCCC-		11.84154451
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 ALDOC_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of ALDOC_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ALDOC_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-39, AND MASSSPECTROMETRY.

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