SODC_MOUSE - dbPTM
SODC_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SODC_MOUSE
UniProt AC P08228
Protein Name Superoxide dismutase [Cu-Zn]
Gene Name Sod1
Organism Mus musculus (Mouse).
Sequence Length 154
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Destroys radicals which are normally produced within the cells and which are toxic to biological systems..
Protein Sequence MAMKAVCVLKGDGPVQGTIHFEQKASGEPVVLSGQITGLTEGQHGFHVHQYGDNTQGCTSAGPHFNPHSKKHGGPADEERHVGDLGNVTAGKDGVANVSIEDRVISLSGEHSIIGRTMVVHEKQDDLGKGGNEESTKTGNAGSRLACGVIGIAQ
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------MAMKAVCVL
------CCCEEEEEE		14.2623806337
4Succinylation----MAMKAVCVLKG
----CCCEEEEEEEC		28.29-
4Malonylation----MAMKAVCVLKG
----CCCEEEEEEEC		28.2926320211
4Succinylation----MAMKAVCVLKG
----CCCEEEEEEEC		28.2923806337
4Acetylation----MAMKAVCVLKG
----CCCEEEEEEEC		28.2923806337
7S-palmitoylation-MAMKAVCVLKGDGP
-CCCEEEEEEECCCC		3.3826165157
7S-nitrosylation-MAMKAVCVLKGDGP
-CCCEEEEEEECCCC		3.3824895380
7Glutathionylation-MAMKAVCVLKGDGP
-CCCEEEEEEECCCC		3.3824333276
10AcetylationMKAVCVLKGDGPVQG
CEEEEEEECCCCCCC		34.2621728379
10SuccinylationMKAVCVLKGDGPVQG
CEEEEEEECCCCCCC		34.26-
10UbiquitinationMKAVCVLKGDGPVQG
CEEEEEEECCCCCCC		34.26-
10MalonylationMKAVCVLKGDGPVQG
CEEEEEEECCCCCCC		34.2626320211
10SuccinylationMKAVCVLKGDGPVQG
CEEEEEEECCCCCCC		34.2623806337
18PhosphorylationGDGPVQGTIHFEQKA
CCCCCCCEEEEEECC		8.3222210690
33PhosphorylationSGEPVVLSGQITGLT
CCCCEEEEEEEECCC		19.6223649490
71AcetylationHFNPHSKKHGGPADE
CCCCCCCCCCCCCCC		50.9622826441
71UbiquitinationHFNPHSKKHGGPADE
CCCCCCCCCCCCCCC		50.9622790023
89PhosphorylationVGDLGNVTAGKDGVA
CCCCCCCCCCCCCCE		33.4225521595
92AcetylationLGNVTAGKDGVANVS
CCCCCCCCCCCEEEE		49.1723806337
92SuccinylationLGNVTAGKDGVANVS
CCCCCCCCCCCEEEE		49.17-
92UbiquitinationLGNVTAGKDGVANVS
CCCCCCCCCCCEEEE		49.17-
92MalonylationLGNVTAGKDGVANVS
CCCCCCCCCCCEEEE		49.1726320211
92SuccinylationLGNVTAGKDGVANVS
CCCCCCCCCCCEEEE		49.1723806337
99PhosphorylationKDGVANVSIEDRVIS
CCCCEEEEEEHEEEE		21.7726824392
106PhosphorylationSIEDRVISLSGEHSI
EEEHEEEEECCCCEE		17.3925521595
108PhosphorylationEDRVISLSGEHSIIG
EHEEEEECCCCEEEC		35.0326824392
112PhosphorylationISLSGEHSIIGRTMV
EEECCCCEEECEEEE		16.1726239621
123MalonylationRTMVVHEKQDDLGKG
EEEEEEECCCCCCCC		44.1226320211
123AcetylationRTMVVHEKQDDLGKG
EEEEEEECCCCCCCC		44.1223806337
123SuccinylationRTMVVHEKQDDLGKG
EEEEEEECCCCCCCC		44.12-
123UbiquitinationRTMVVHEKQDDLGKG
EEEEEEECCCCCCCC		44.1227667366
123SuccinylationRTMVVHEKQDDLGKG
EEEEEEECCCCCCCC		44.1223806337
129UbiquitinationEKQDDLGKGGNEEST
ECCCCCCCCCCCCCC		71.5827667366
129SuccinylationEKQDDLGKGGNEEST
ECCCCCCCCCCCCCC		71.5823954790
129AcetylationEKQDDLGKGGNEEST
ECCCCCCCCCCCCCC		71.5823201123
137UbiquitinationGGNEESTKTGNAGSR
CCCCCCCCCCCCCHH		64.8127667366
137MalonylationGGNEESTKTGNAGSR
CCCCCCCCCCCCCHH		64.8126073543
137SuccinylationGGNEESTKTGNAGSR
CCCCCCCCCCCCCHH		64.81-
137AcetylationGGNEESTKTGNAGSR
CCCCCCCCCCCCCHH		64.8123576753
137SuccinylationGGNEESTKTGNAGSR
CCCCCCCCCCCCCHH		64.8123806337
137GlutarylationGGNEESTKTGNAGSR
CCCCCCCCCCCCCHH		64.8124703693
138PhosphorylationGNEESTKTGNAGSRL
CCCCCCCCCCCCHHE		35.4423984901
143PhosphorylationTKTGNAGSRLACGVI
CCCCCCCHHEEEEEE		23.0123984901
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
-KUbiquitinationE3 ubiquitin ligaseRnf19aP50636
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseStub1Q9WUD1
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SODC_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 SODC_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SQSTM_MOUSESqstm1physical
19765191
SQSTM_MOUSESqstm1physical
17296612
PDIA2_MOUSEPdia2physical
16847061
SODC_MOUSESod1physical
23583391
DNJB2_HUMANDNAJB2physical
24023695
C4BPA_HUMANC4BPAphysical
26496610
FYN_HUMANFYNphysical
26496610
NCBP1_HUMANNCBP1physical
26496610
TRY1_HUMANPRSS1physical
26496610
RBBP6_HUMANRBBP6physical
26496610
YES_HUMANYES1physical
26496610
FL2D_HUMANWTAPphysical
26496610
CCS_HUMANCCSphysical
26496610
PDCD6_HUMANPDCD6physical
26496610
S27A4_HUMANSLC27A4physical
26496610
CPSF5_HUMANNUDT21physical
26496610
WWP2_HUMANWWP2physical
26496610
RRAS2_HUMANRRAS2physical
26496610
NCBP2_HUMANNCBP2physical
26496610
SK2L2_HUMANSKIV2L2physical
26496610
ZN346_HUMANZNF346physical
26496610
SRRT_HUMANSRRTphysical
26496610
GAR1_HUMANGAR1physical
26496610
MET14_HUMANMETTL14physical
26496610
P3H1_HUMANP3H1physical
26496610
ZCH18_HUMANZC3H18physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SODC_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-71, AND MASS SPECTROMETRY.

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