TKT_MOUSE - dbPTM
TKT_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TKT_MOUSE
UniProt AC P40142
Protein Name Transketolase
Gene Name Tkt
Organism Mus musculus (Mouse).
Sequence Length 623
Subcellular Localization
Protein Description Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate..
Protein Sequence MEGYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKALDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLPEAELLNLRKISSDLDGHPVPKQAFTDVATGSLGQGLGAACGMAYTGKYFDKASYRVYCMLGDGEVSEGSVWEAMAFAGIYKLDNLVAIFDINRLGQSDPAPLQHQVDIYQKRCEAFGWHTIIVDGHSVEELCKAFGQAKHQPTAIIAKTFKGRGITGIEDKEAWHGKPLPKNMAEQIIQEIYSQVQSKKKILATPPQEDAPSVDIANIRMPTPPSYKVGDKIATRKAYGLALAKLGHASDRIIALDGDTKNSTFSELFKKEHPDRFIECYIAEQNMVSIAVGCATRDRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPMSTVFYPSDGVATEKAVELAANTKGICFIRTSRPENAIIYSNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEALAAAESLKKDKISIRVLDPFTIKPLDRKLILDSARATKGRILTVEDHYYEGGIGEAVSAAVVGEPGVTVTRLAVSQVPRSGKPAELLKMFGIDKDAIVQAVKGLVTKG
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
1Acetylation-------MEGYHKPD
-------CCCCCCCC
8.9923806337
4Phosphorylation----MEGYHKPDQQK
----CCCCCCCCHHH
8.0525367039
6Acetylation--MEGYHKPDQQKLQ
--CCCCCCCCHHHHH
41.6323806337
6Malonylation--MEGYHKPDQQKLQ
--CCCCCCCCHHHHH
41.6326320211
6Ubiquitination--MEGYHKPDQQKLQ
--CCCCCCCCHHHHH
41.63-
11AcetylationYHKPDQQKLQALKDT
CCCCCHHHHHHHHHH
36.6123201123
16AcetylationQQKLQALKDTANRLR
HHHHHHHHHHHHHHH
56.9223806337
16MalonylationQQKLQALKDTANRLR
HHHHHHHHHHHHHHH
56.9226320211
16UbiquitinationQQKLQALKDTANRLR
HHHHHHHHHHHHHHH
56.9227667366
39PhosphorylationAAGSGHPTSCCSAAE
CCCCCCCCCCCCHHH
28.8120139300
40PhosphorylationAGSGHPTSCCSAAEI
CCCCCCCCCCCHHHH
19.9920139300
59MalonylationFFHTMRYKALDPRNP
HHHHHHCCCCCCCCC
31.9126320211
102MalonylationAELLNLRKISSDLDG
HHHHCHHHCCCCCCC
50.5426320211
102UbiquitinationAELLNLRKISSDLDG
HHHHCHHHCCCCCCC
50.54-
104PhosphorylationLLNLRKISSDLDGHP
HHCHHHCCCCCCCCC
22.3429176673
105PhosphorylationLNLRKISSDLDGHPV
HCHHHCCCCCCCCCC
45.7429176673
114UbiquitinationLDGHPVPKQAFTDVA
CCCCCCCCHHHCCCC
55.2622790023
133GlutathionylationGQGLGAACGMAYTGK
CCHHHHHCCHHHCCC
3.6724333276
144AcetylationYTGKYFDKASYRVYC
HCCCCCCCCCEEEEE
29.3622826441
144MalonylationYTGKYFDKASYRVYC
HCCCCCCCCCEEEEE
29.3626320211
144UbiquitinationYTGKYFDKASYRVYC
HCCCCCCCCCEEEEE
29.36-
204AcetylationHQVDIYQKRCEAFGW
HHHHHHHHHHHHHCC
41.8823236377
204MalonylationHQVDIYQKRCEAFGW
HHHHHHHHHHHHHCC
41.8826320211
204UbiquitinationHQVDIYQKRCEAFGW
HHHHHHHHHHHHHCC
41.8827667366
206GlutathionylationVDIYQKRCEAFGWHT
HHHHHHHHHHHCCEE
5.9524333276
232AcetylationCKAFGQAKHQPTAII
HHHHCCCCCCCCEEE
34.5823806337
232MalonylationCKAFGQAKHQPTAII
HHHHCCCCCCCCEEE
34.5826320211
232UbiquitinationCKAFGQAKHQPTAII
HHHHCCCCCCCCEEE
34.5827667366
241AcetylationQPTAIIAKTFKGRGI
CCCEEEEEECCCCCC
44.0522826441
241SuccinylationQPTAIIAKTFKGRGI
CCCEEEEEECCCCCC
44.0523954790
241UbiquitinationQPTAIIAKTFKGRGI
CCCEEEEEECCCCCC
44.05-
254AcetylationGITGIEDKEAWHGKP
CCCCCCCHHHHCCCC
36.2223236377
254MalonylationGITGIEDKEAWHGKP
CCCCCCCHHHHCCCC
36.2226320211
254UbiquitinationGITGIEDKEAWHGKP
CCCCCCCHHHHCCCC
36.2227667366
260AcetylationDKEAWHGKPLPKNMA
CHHHHCCCCCCHHHH
30.4123201123
260MalonylationDKEAWHGKPLPKNMA
CHHHHCCCCCCHHHH
30.4126320211
260UbiquitinationDKEAWHGKPLPKNMA
CHHHHCCCCCCHHHH
30.4127667366
264AcetylationWHGKPLPKNMAEQII
HCCCCCCHHHHHHHH
68.0223954790
264UbiquitinationWHGKPLPKNMAEQII
HCCCCCCHHHHHHHH
68.0222790023
275NitrationEQIIQEIYSQVQSKK
HHHHHHHHHHHHCCC
7.72-
275PhosphorylationEQIIQEIYSQVQSKK
HHHHHHHHHHHHCCC
7.7225177544
276PhosphorylationQIIQEIYSQVQSKKK
HHHHHHHHHHHCCCC
29.5426745281
280PhosphorylationEIYSQVQSKKKILAT
HHHHHHHCCCCCCCC
47.8126643407
281AcetylationIYSQVQSKKKILATP
HHHHHHCCCCCCCCC
40.78133965
281MalonylationIYSQVQSKKKILATP
HHHHHHCCCCCCCCC
40.7826073543
281UbiquitinationIYSQVQSKKKILATP
HHHHHHCCCCCCCCC
40.78-
282MalonylationYSQVQSKKKILATPP
HHHHHCCCCCCCCCC
50.7426073543
282UbiquitinationYSQVQSKKKILATPP
HHHHHCCCCCCCCCC
50.74-
283UbiquitinationSQVQSKKKILATPPQ
HHHHCCCCCCCCCCC
46.8422790023
287PhosphorylationSKKKILATPPQEDAP
CCCCCCCCCCCCCCC
31.8625521595
295PhosphorylationPPQEDAPSVDIANIR
CCCCCCCCCCCCCCC
33.8627180971
305PhosphorylationIANIRMPTPPSYKVG
CCCCCCCCCCCCCCC
38.1927180971
308PhosphorylationIRMPTPPSYKVGDKI
CCCCCCCCCCCCCHH
38.5026643407
309PhosphorylationRMPTPPSYKVGDKIA
CCCCCCCCCCCCHHH
18.5726643407
310AcetylationMPTPPSYKVGDKIAT
CCCCCCCCCCCHHHH
44.0422826441
310MalonylationMPTPPSYKVGDKIAT
CCCCCCCCCCCHHHH
44.0426320211
310UbiquitinationMPTPPSYKVGDKIAT
CCCCCCCCCCCHHHH
44.0427667366
314AcetylationPSYKVGDKIATRKAY
CCCCCCCHHHHHHHH
28.4523806337
314MalonylationPSYKVGDKIATRKAY
CCCCCCCHHHHHHHH
28.4526320211
314SuccinylationPSYKVGDKIATRKAY
CCCCCCCHHHHHHHH
28.4523806337
319AcetylationGDKIATRKAYGLALA
CCHHHHHHHHHHHHH
41.4222826441
319MalonylationGDKIATRKAYGLALA
CCHHHHHHHHHHHHH
41.4226320211
319UbiquitinationGDKIATRKAYGLALA
CCHHHHHHHHHHHHH
41.4227667366
327AcetylationAYGLALAKLGHASDR
HHHHHHHHHCCCCCC
56.7122826441
327UbiquitinationAYGLALAKLGHASDR
HHHHHHHHHCCCCCC
56.7122790023
342PhosphorylationIIALDGDTKNSTFSE
EEEECCCCCCCCHHH
37.3422817900
343AcetylationIALDGDTKNSTFSEL
EEECCCCCCCCHHHH
54.3522826441
343UbiquitinationIALDGDTKNSTFSEL
EEECCCCCCCCHHHH
54.3522790023
345PhosphorylationLDGDTKNSTFSELFK
ECCCCCCCCHHHHHH
32.1727180971
346PhosphorylationDGDTKNSTFSELFKK
CCCCCCCCHHHHHHH
40.3421743459
348PhosphorylationDTKNSTFSELFKKEH
CCCCCCHHHHHHHHC
33.2221743459
352AcetylationSTFSELFKKEHPDRF
CCHHHHHHHHCCCCE
70.6323954790
352SuccinylationSTFSELFKKEHPDRF
CCHHHHHHHHCCCCE
70.6323954790
352UbiquitinationSTFSELFKKEHPDRF
CCHHHHHHHHCCCCE
70.6327667366
386S-palmitoylationRDRTVPFCSTFAAFF
CCCCCCCHHHHHHHH
2.8326165157
387PhosphorylationDRTVPFCSTFAAFFT
CCCCCCHHHHHHHHH
27.2620139300
388PhosphorylationRTVPFCSTFAAFFTR
CCCCCHHHHHHHHHH
20.6220139300
444PhosphorylationFRSVPMSTVFYPSDG
HHCCCCEEEECCCCC
14.3720139300
447PhosphorylationVPMSTVFYPSDGVAT
CCCEEEECCCCCCCC
9.48-
449PhosphorylationMSTVFYPSDGVATEK
CEEEECCCCCCCCHH
35.3026525534
456UbiquitinationSDGVATEKAVELAAN
CCCCCCHHHHHHHHC
54.0722790023
468GlutathionylationAANTKGICFIRTSRP
HHCCCCEEEEECCCC
2.9424333276
482PhosphorylationPENAIIYSNNEDFQV
CCCEEEECCCCCCCC
23.8329899451
493UbiquitinationDFQVGQAKVVLKSKD
CCCCCEEEEEEECCC
25.6222790023
498PhosphorylationQAKVVLKSKDDQVTV
EEEEEEECCCCCEEE
36.8429899451
499AcetylationAKVVLKSKDDQVTVI
EEEEEECCCCCEEEE
64.8323201123
499MalonylationAKVVLKSKDDQVTVI
EEEEEECCCCCEEEE
64.8326073543
499UbiquitinationAKVVLKSKDDQVTVI
EEEEEECCCCCEEEE
64.83-
504PhosphorylationKSKDDQVTVIGAGVT
ECCCCCEEEEECCCC
10.7729899451
523AcetylationLAAAESLKKDKISIR
HHHHHHHCCCCCEEE
69.1123954790
528PhosphorylationSLKKDKISIRVLDPF
HHCCCCCEEEEECCC
15.3030387612
536PhosphorylationIRVLDPFTIKPLDRK
EEEECCCCCCCCCCE
33.2221454597
538AcetylationVLDPFTIKPLDRKLI
EECCCCCCCCCCEEH
36.1523806337
538UbiquitinationVLDPFTIKPLDRKLI
EECCCCCCCCCCEEH
36.1522790023
543AcetylationTIKPLDRKLILDSAR
CCCCCCCEEHHHHCC
39.2822826441
543MalonylationTIKPLDRKLILDSAR
CCCCCCCEEHHHHCC
39.2826320211
543UbiquitinationTIKPLDRKLILDSAR
CCCCCCCEEHHHHCC
39.28-
590PhosphorylationTVTRLAVSQVPRSGK
EEEEEEEECCCCCCC
21.6127180971
595PhosphorylationAVSQVPRSGKPAELL
EEECCCCCCCHHHHH
45.1322817900
597MalonylationSQVPRSGKPAELLKM
ECCCCCCCHHHHHHH
42.1526320211
597UbiquitinationSQVPRSGKPAELLKM
ECCCCCCCHHHHHHH
42.1527667366
603AcetylationGKPAELLKMFGIDKD
CCHHHHHHHHCCCHH
44.8223236377
609AcetylationLKMFGIDKDAIVQAV
HHHHCCCHHHHHHHH
47.3323806337
609MalonylationLKMFGIDKDAIVQAV
HHHHCCCHHHHHHHH
47.3326073543

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 TKT_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TKT_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 TKT_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TKT_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TKT_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275, AND MASSSPECTROMETRY.

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