TPIS_MOUSE - dbPTM
TPIS_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPIS_MOUSE
UniProt AC P17751
Protein Name Triosephosphate isomerase
Gene Name Tpi1
Organism Mus musculus (Mouse).
Sequence Length 299
Subcellular Localization
Protein Description
Protein Sequence MEGKAEQQGAGLTMAEGGEKEEFCFTAIYISGQWREPCVCTDLQRLEPGTMAPTRKFFVGGNWKMNGRKKCLGELICTLNAANVPAGTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIKDLGATWVVLGHSERRHVFGESDELIGQKVSHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVNDGVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEFVDIINAKQ
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
13PhosphorylationEQQGAGLTMAEGGEK
HHCCCCEEECCCCCC		17.2630635358
14AcetylationQQGAGLTMAEGGEKE
HCCCCEEECCCCCCC		3.72-
56UbiquitinationGTMAPTRKFFVGGNW
CCCCCCCCEEECCCC		45.7027667366
56MalonylationGTMAPTRKFFVGGNW
CCCCCCCCEEECCCC		45.7026320211
56SuccinylationGTMAPTRKFFVGGNW
CCCCCCCCEEECCCC		45.70-
56AcetylationGTMAPTRKFFVGGNW
CCCCCCCCEEECCCC		45.7023806337
64AcetylationFFVGGNWKMNGRKKC
EEECCCCCCCCCCCH		26.8722826441
64UbiquitinationFFVGGNWKMNGRKKC
EEECCCCCCCCCCCH		26.8722790023
67S-nitrosylationGGNWKMNGRKKCLGE
CCCCCCCCCCCHHHH		39.0121278135
68NitrationGNWKMNGRKKCLGEL
CCCCCCCCCCHHHHH		30.2016800626
78PhosphorylationCLGELICTLNAANVP
HHHHHHHHHCCCCCC		18.9623649490
80PhosphorylationGELICTLNAANVPAG
HHHHHHHCCCCCCCC		20.89-
88PhosphorylationAANVPAGTEVVCAPP
CCCCCCCCEEEECCC		27.9323649490
105AcetylationYIDFARQKLDPKIAV
EHHHHHHHCCHHHHH		49.6723806337
106PhosphorylationIDFARQKLDPKIAVA
HHHHHHHCCHHHHHE		11.74-
109SuccinylationARQKLDPKIAVAAQN
HHHHCCHHHHHEECC		42.8623806337
109UbiquitinationARQKLDPKIAVAAQN
HHHHCCHHHHHEECC		42.86-
109AcetylationARQKLDPKIAVAAQN
HHHHCCHHHHHEECC		42.8623806337
117S-nitrosylationIAVAAQNCYKVTNGA
HHHEECCEEEEECCC		2.0124895380
117GlutathionylationIAVAAQNCYKVTNGA
HHHEECCEEEEECCC		2.0124333276
117S-nitrosocysteineIAVAAQNCYKVTNGA
HHHEECCEEEEECCC		2.01-
117S-palmitoylationIAVAAQNCYKVTNGA
HHHEECCEEEEECCC		2.0126165157
118Nitrated tyrosineAVAAQNCYKVTNGAF
HHEECCEEEEECCCC		18.95-
118PhosphorylationAVAAQNCYKVTNGAF
HHEECCEEEEECCCC		18.9527708245
118NitrationAVAAQNCYKVTNGAF
HHEECCEEEEECCCC		18.9516800626
119AcetylationVAAQNCYKVTNGAFT
HEECCEEEEECCCCC		44.7970217
119MalonylationVAAQNCYKVTNGAFT
HEECCEEEEECCCCC		44.7926320211
119UbiquitinationVAAQNCYKVTNGAFT
HEECCEEEEECCCCC		44.79-
121PhosphorylationAQNCYKVTNGAFTGE
ECCEEEEECCCCCCC		24.6327180971
126PhosphorylationKVTNGAFTGEISPGM
EEECCCCCCCCCCCH		33.1125777480
127S-nitrosylationVTNGAFTGEISPGMI
EECCCCCCCCCCCHH		24.6421278135
130PhosphorylationGAFTGEISPGMIKDL
CCCCCCCCCCHHCCC		15.8826824392
135AcetylationEISPGMIKDLGATWV
CCCCCHHCCCCCEEE		37.7022826441
140PhosphorylationMIKDLGATWVVLGHS
HHCCCCCEEEEEECC		19.5922210690
147PhosphorylationTWVVLGHSERRHVFG
EEEEEECCCCCCCCC		30.8828542873
149SuccinylationVVLGHSERRHVFGES
EEEECCCCCCCCCCC		36.7023806337
156SuccinylationRRHVFGESDELIGQK
CCCCCCCCHHHHHHH		36.4423806337
156PhosphorylationRRHVFGESDELIGQK
CCCCCCCCHHHHHHH		36.4425521595
156AcetylationRRHVFGESDELIGQK
CCCCCCCCHHHHHHH		36.4423806337
159PhosphorylationVFGESDELIGQKVSH
CCCCCHHHHHHHHHH		6.8221183079
165PhosphorylationELIGQKVSHALAEGL
HHHHHHHHHHHHHCC		15.3022210690
173PhosphorylationHALAEGLGVIACIGE
HHHHHCCCEEEEEEC		21.4621183079
177S-palmitoylationEGLGVIACIGEKLDE
HCCCEEEEEECCCCH		2.5626165157
177S-nitrosocysteineEGLGVIACIGEKLDE
HCCCEEEEEECCCCH		2.56-
177S-nitrosylationEGLGVIACIGEKLDE
HCCCEEEEEECCCCH		2.5624895380
181AcetylationVIACIGEKLDEREAG
EEEEEECCCCHHCCC		56.9022733758
192UbiquitinationREAGITEKVVFEQTK
HCCCCCCEEEEEEEE		34.7427667366
192AcetylationREAGITEKVVFEQTK
HCCCCCCEEEEEEEE		34.7422826441
192MalonylationREAGITEKVVFEQTK
HCCCCCCEEEEEEEE		34.7426320211
194AcetylationAGITEKVVFEQTKVI
CCCCCEEEEEEEEEE		6.9123806337
194SuccinylationAGITEKVVFEQTKVI
CCCCCEEEEEEEEEE		6.9123806337
194MethylationAGITEKVVFEQTKVI
CCCCCEEEEEEEEEE		6.91-
199MalonylationKVVFEQTKVIADNVK
EEEEEEEEEEECCCC		31.1926320211
199AcetylationKVVFEQTKVIADNVK
EEEEEEEEEEECCCC		31.1922826441
199SuccinylationKVVFEQTKVIADNVK
EEEEEEEEEEECCCC		31.19-
199UbiquitinationKVVFEQTKVIADNVK
EEEEEEEEEEECCCC		31.1927667366
206MalonylationKVIADNVKDWSKVVL
EEEECCCCCHHHEEE		60.7926320211
206UbiquitinationKVIADNVKDWSKVVL
EEEECCCCCHHHEEE		60.7927667366
206SuccinylationKVIADNVKDWSKVVL
EEEECCCCCHHHEEE		60.79-
206AcetylationKVIADNVKDWSKVVL
EEEECCCCCHHHEEE		60.7923806337
209NitrationADNVKDWSKVVLAYE
ECCCCCHHHEEEEEE		26.2116800626
209PhosphorylationADNVKDWSKVVLAYE
ECCCCCHHHEEEEEE		26.2125266776
210AcetylationDNVKDWSKVVLAYEP
CCCCCHHHEEEEEEE		31.9122826441
210UbiquitinationDNVKDWSKVVLAYEP
CCCCCHHHEEEEEEE		31.9122790023
212PhosphorylationVKDWSKVVLAYEPVW
CCCHHHEEEEEEEEE		2.6617242355
214PhosphorylationDWSKVVLAYEPVWAI
CHHHEEEEEEEEEEE		8.60-
218S-nitrosylationVVLAYEPVWAIGTGK
EEEEEEEEEEECCCC		3.4420925432
223PhosphorylationEPVWAIGTGKTATPQ
EEEEEECCCCCCCHH		29.4126643407
225UbiquitinationVWAIGTGKTATPQQA
EEEECCCCCCCHHHH		34.5227667366
225MalonylationVWAIGTGKTATPQQA
EEEECCCCCCCHHHH		34.5226320211
225AcetylationVWAIGTGKTATPQQA
EEEECCCCCCCHHHH		34.5223806337
226PhosphorylationWAIGTGKTATPQQAQ
EEECCCCCCCHHHHH		36.7924899341
228PhosphorylationIGTGKTATPQQAQEV
ECCCCCCCHHHHHHH		27.1925521595
238MalonylationQAQEVHEKLRGWLKS
HHHHHHHHHHHHHHH		28.7126320211
238AcetylationQAQEVHEKLRGWLKS
HHHHHHHHHHHHHHH		28.7122826441
238UbiquitinationQAQEVHEKLRGWLKS
HHHHHHHHHHHHHHH		28.7127667366
244MalonylationEKLRGWLKSNVNDGV
HHHHHHHHHCCCCCC		33.2126320211
244UbiquitinationEKLRGWLKSNVNDGV
HHHHHHHHHCCCCCC		33.2127667366
244SuccinylationEKLRGWLKSNVNDGV
HHHHHHHHHCCCCCC		33.21-
244AcetylationEKLRGWLKSNVNDGV
HHHHHHHHHCCCCCC		33.2123806337
244MethylationEKLRGWLKSNVNDGV
HHHHHHHHHCCCCCC		33.21-
245PhosphorylationKLRGWLKSNVNDGVA
HHHHHHHHCCCCCCC		43.7925521595
254PhosphorylationVNDGVAQSTRIIYGG
CCCCCCCCCEEEECC		15.2023684622
259Nitrated tyrosineAQSTRIIYGGSVTGA
CCCCEEEECCCCCCH		17.05-
259PhosphorylationAQSTRIIYGGSVTGA
CCCCEEEECCCCCCH		17.0522324799
259NitrationAQSTRIIYGGSVTGA
CCCCEEEECCCCCCH		17.0516800626
262PhosphorylationTRIIYGGSVTGATCK
CEEEECCCCCCHHHH		16.4925521595
264PhosphorylationIIYGGSVTGATCKEL
EEECCCCCCHHHHHH		23.8527742792
267PhosphorylationGGSVTGATCKELASQ
CCCCCCHHHHHHHCC		26.0028833060
268GlutathionylationGSVTGATCKELASQP
CCCCCHHHHHHHCCC		2.9824333276
268S-palmitoylationGSVTGATCKELASQP
CCCCCHHHHHHHCCC		2.9826165157
268S-nitrosocysteineGSVTGATCKELASQP
CCCCCHHHHHHHCCC		2.98-
273PhosphorylationATCKELASQPDVDGF
HHHHHHHCCCCCCCE		55.6722210690
288MalonylationLVGGASLKPEFVDII
EECCCCCCHHHHHHH		39.7526073543
288UbiquitinationLVGGASLKPEFVDII
EECCCCCCHHHHHHH		39.75-
288AcetylationLVGGASLKPEFVDII
EECCCCCCHHHHHHH		39.7522826441
298SuccinylationFVDIINAKQ------
HHHHHCCCC------		52.6423954790
298AcetylationFVDIINAKQ------
HHHHHCCCC------		52.6423954790
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 TPIS_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPIS_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 TPIS_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUX1_HUMANCUX1physical
26496610
CASP_HUMANCUX1physical
26496610
EEA1_HUMANEEA1physical
26496610
CAF1A_HUMANCHAF1Aphysical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPIS_MOUSE

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Related Literatures of Post-Translational Modification
Nitration
ReferencePubMed
"Endogenously nitrated proteins in mouse brain: links toneurodegenerative disease.";
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,Squier T.C., Bigelow D.J.;
Biochemistry 45:8009-8022(2006).
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-118 AND TYR-259, AND MASSSPECTROMETRY.

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