TKT_HUMAN - dbPTM
TKT_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TKT_HUMAN
UniProt AC P29401
Protein Name Transketolase
Gene Name TKT
Organism Homo sapiens (Human).
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 MESYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLNLRKISSDLDGHPVPKQAFTDVATGSLGQGLGAACGMAYTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNLVAILDINRLGQSDPAPLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKHQPTAIIAKTFKGRGITGVEDKESWHGKPLPKNMAEQIIQEIYSQIQSKKKILATPPQEDAPSVDIANIRMPSLPSYKVGDKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTSRPENAIIYNNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATKGRILTVEDHYYEGGIGEAVSSAVVGEPGITVTHLAVNRVPRSGKPAELLKMFGIDRDAIAQAVRGLITKA
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-------MESYHKPD
-------CCCCCCCC
7.5222814378
1Sulfoxidation-------MESYHKPD
-------CCCCCCCC
7.5228183972
3Phosphorylation-----MESYHKPDQQ
-----CCCCCCCCHH
31.1023401153
3 (in isoform 2)Phosphorylation-31.1027251275
4Phosphorylation----MESYHKPDQQK
----CCCCCCCCHHH
10.6823186163
4 (in isoform 2)Phosphorylation-10.6827642862
62-Hydroxyisobutyrylation--MESYHKPDQQKLQ
--CCCCCCCCHHHHH
41.90-
6Acetylation--MESYHKPDQQKLQ
--CCCCCCCCHHHHH
41.9019608861
6Malonylation--MESYHKPDQQKLQ
--CCCCCCCCHHHHH
41.9026320211
6Ubiquitination--MESYHKPDQQKLQ
--CCCCCCCCHHHHH
41.9019608861
11UbiquitinationYHKPDQQKLQALKDT
CCCCCHHHHHHHHHH
36.6121890473
11UbiquitinationYHKPDQQKLQALKDT
CCCCCHHHHHHHHHH
36.6121890473
112-HydroxyisobutyrylationYHKPDQQKLQALKDT
CCCCCHHHHHHHHHH
36.61-
11AcetylationYHKPDQQKLQALKDT
CCCCCHHHHHHHHHH
36.6119608861
11MalonylationYHKPDQQKLQALKDT
CCCCCHHHHHHHHHH
36.6126320211
11UbiquitinationYHKPDQQKLQALKDT
CCCCCHHHHHHHHHH
36.6119608861
16UbiquitinationQQKLQALKDTANRLR
HHHHHHHHHHHHHHH
56.9221890473
16UbiquitinationQQKLQALKDTANRLR
HHHHHHHHHHHHHHH
56.9221890473
162-HydroxyisobutyrylationQQKLQALKDTANRLR
HHHHHHHHHHHHHHH
56.92-
16AcetylationQQKLQALKDTANRLR
HHHHHHHHHHHHHHH
56.9225953088
16MalonylationQQKLQALKDTANRLR
HHHHHHHHHHHHHHH
56.9226320211
16UbiquitinationQQKLQALKDTANRLR
HHHHHHHHHHHHHHH
56.92-
39PhosphorylationAAGSGHPTSCCSAAE
CCCCCCCCCCCCHHH
28.8121082442
40PhosphorylationAGSGHPTSCCSAAEI
CCCCCCCCCCCHHHH
19.9921082442
55PhosphorylationMAVLFFHTMRYKSQD
HHHHHHHHCCCCCCC
9.7422210691
592-HydroxyisobutyrylationFFHTMRYKSQDPRNP
HHHHCCCCCCCCCCC
31.13-
59AcetylationFFHTMRYKSQDPRNP
HHHHCCCCCCCCCCC
31.1326210075
70MethylationPRNPHNDRFVLSKGH
CCCCCCCCEEEECCC
28.96115918541
1022-HydroxyisobutyrylationAELLNLRKISSDLDG
HHHHCHHHCCCCCCC
50.54-
102UbiquitinationAELLNLRKISSDLDG
HHHHCHHHCCCCCCC
50.54-
104PhosphorylationLLNLRKISSDLDGHP
HHCHHHCCCCCCCCC
22.3428355574
104 (in isoform 2)Phosphorylation-22.3427251275
105PhosphorylationLNLRKISSDLDGHPV
HCHHHCCCCCCCCCC
45.7423927012
114UbiquitinationLDGHPVPKQAFTDVA
CCCCCCCCHHHCCCC
55.26-
122PhosphorylationQAFTDVATGSLGQGL
HHHCCCCCCCCCCHH
27.4421712546
124PhosphorylationFTDVATGSLGQGLGA
HCCCCCCCCCCHHHH
25.6021712546
133GlutathionylationGQGLGAACGMAYTGK
CCHHHHHCCHHHCCC
3.6722555962
135SulfoxidationGLGAACGMAYTGKYF
HHHHHCCHHHCCCCC
2.3130846556
140AcetylationCGMAYTGKYFDKASY
CCHHHCCCCCCCCCE
34.6426051181
140UbiquitinationCGMAYTGKYFDKASY
CCHHHCCCCCCCCCE
34.64-
1442-HydroxyisobutyrylationYTGKYFDKASYRVYC
HCCCCCCCCCEEEEE
29.36-
144AcetylationYTGKYFDKASYRVYC
HCCCCCCCCCEEEEE
29.3619608861
144SuccinylationYTGKYFDKASYRVYC
HCCCCCCCCCEEEEE
29.3623954790
144UbiquitinationYTGKYFDKASYRVYC
HCCCCCCCCCEEEEE
29.3619608861
174UbiquitinationMAFASIYKLDNLVAI
HHHHHHHCHHCEEEE
47.93-
190PhosphorylationDINRLGQSDPAPLQH
EHHHCCCCCCCCCHH
43.7023911959
199SulfoxidationPAPLQHQMDIYQKRC
CCCCHHHHHHHHHHH
2.9530846556
202PhosphorylationLQHQMDIYQKRCEAF
CHHHHHHHHHHHHHH
12.0628152594
204UbiquitinationHQMDIYQKRCEAFGW
HHHHHHHHHHHHHCC
41.8821890473
2042-HydroxyisobutyrylationHQMDIYQKRCEAFGW
HHHHHHHHHHHHHCC
41.88-
204AcetylationHQMDIYQKRCEAFGW
HHHHHHHHHHHHHCC
41.8819608861
204MethylationHQMDIYQKRCEAFGW
HHHHHHHHHHHHHCC
41.8819608861
204UbiquitinationHQMDIYQKRCEAFGW
HHHHHHHHHHHHHCC
41.8821890473
212UbiquitinationRCEAFGWHAIIVDGH
HHHHHCCEEEEECCC
13.8721890473
212AcetylationRCEAFGWHAIIVDGH
HHHHHCCEEEEECCC
13.8719608861
212UbiquitinationRCEAFGWHAIIVDGH
HHHHHCCEEEEECCC
13.8719608861
232UbiquitinationCKAFGQAKHQPTAII
HHHHCCCCCCCCEEE
34.5821890473
2322-HydroxyisobutyrylationCKAFGQAKHQPTAII
HHHHCCCCCCCCEEE
34.58-
232AcetylationCKAFGQAKHQPTAII
HHHHCCCCCCCCEEE
34.5816916647
232MalonylationCKAFGQAKHQPTAII
HHHHCCCCCCCCEEE
34.5826320211
232UbiquitinationCKAFGQAKHQPTAII
HHHHCCCCCCCCEEE
34.58-
240UbiquitinationHQPTAIIAKTFKGRG
CCCCEEEEEECCCCC
9.9521890473
2412-HydroxyisobutyrylationQPTAIIAKTFKGRGI
CCCEEEEEECCCCCC
44.05-
241AcetylationQPTAIIAKTFKGRGI
CCCEEEEEECCCCCC
44.0519608861
241UbiquitinationQPTAIIAKTFKGRGI
CCCEEEEEECCCCCC
44.0521906983
244UbiquitinationAIIAKTFKGRGITGV
EEEEEECCCCCCCCC
53.59-
246MethylationIAKTFKGRGITGVED
EEEECCCCCCCCCCC
33.65115918529
249AcetylationTFKGRGITGVEDKES
ECCCCCCCCCCCCCC
37.6919608861
249PhosphorylationTFKGRGITGVEDKES
ECCCCCCCCCCCCCC
37.6920873877
249UbiquitinationTFKGRGITGVEDKES
ECCCCCCCCCCCCCC
37.6919608861
254UbiquitinationGITGVEDKESWHGKP
CCCCCCCCCCCCCCC
39.8921890473
2542-HydroxyisobutyrylationGITGVEDKESWHGKP
CCCCCCCCCCCCCCC
39.89-
254AcetylationGITGVEDKESWHGKP
CCCCCCCCCCCCCCC
39.8923954790
254MalonylationGITGVEDKESWHGKP
CCCCCCCCCCCCCCC
39.8926320211
254UbiquitinationGITGVEDKESWHGKP
CCCCCCCCCCCCCCC
39.8919608861
256PhosphorylationTGVEDKESWHGKPLP
CCCCCCCCCCCCCCC
30.0720873877
260UbiquitinationDKESWHGKPLPKNMA
CCCCCCCCCCCHHHH
30.4121890473
2602-HydroxyisobutyrylationDKESWHGKPLPKNMA
CCCCCCCCCCCHHHH
30.41-
260AcetylationDKESWHGKPLPKNMA
CCCCCCCCCCCHHHH
30.4119608861
260MalonylationDKESWHGKPLPKNMA
CCCCCCCCCCCHHHH
30.4126320211
260UbiquitinationDKESWHGKPLPKNMA
CCCCCCCCCCCHHHH
30.4119608861
262UbiquitinationESWHGKPLPKNMAEQ
CCCCCCCCCHHHHHH
12.2821890473
262AcetylationESWHGKPLPKNMAEQ
CCCCCCCCCHHHHHH
12.2819608861
262UbiquitinationESWHGKPLPKNMAEQ
CCCCCCCCCHHHHHH
12.2819608861
264UbiquitinationWHGKPLPKNMAEQII
CCCCCCCHHHHHHHH
68.02-
264 (in isoform 2)Phosphorylation-68.0227251275
266SulfoxidationGKPLPKNMAEQIIQE
CCCCCHHHHHHHHHH
5.6128183972
268UbiquitinationPLPKNMAEQIIQEIY
CCCHHHHHHHHHHHH
31.3821890473
268AcetylationPLPKNMAEQIIQEIY
CCCHHHHHHHHHHHH
31.3819608861
268UbiquitinationPLPKNMAEQIIQEIY
CCCHHHHHHHHHHHH
31.3819608861
275PhosphorylationEQIIQEIYSQIQSKK
HHHHHHHHHHHHHCC
8.1827273156
276PhosphorylationQIIQEIYSQIQSKKK
HHHHHHHHHHHHCCC
26.8625159151
280PhosphorylationEIYSQIQSKKKILAT
HHHHHHHHCCCCCCC
48.3323663014
2812-HydroxyisobutyrylationIYSQIQSKKKILATP
HHHHHHHCCCCCCCC
41.53-
281AcetylationIYSQIQSKKKILATP
HHHHHHHCCCCCCCC
41.5323954790
281UbiquitinationIYSQIQSKKKILATP
HHHHHHHCCCCCCCC
41.5321906983
282UbiquitinationYSQIQSKKKILATPP
HHHHHHCCCCCCCCC
50.74-
283UbiquitinationSQIQSKKKILATPPQ
HHHHHCCCCCCCCCC
46.8421890473
2832-HydroxyisobutyrylationSQIQSKKKILATPPQ
HHHHHCCCCCCCCCC
46.84-
283UbiquitinationSQIQSKKKILATPPQ
HHHHHCCCCCCCCCC
46.8421906983
283 (in isoform 2)Phosphorylation-46.8427642862
287PhosphorylationSKKKILATPPQEDAP
HCCCCCCCCCCCCCC
31.8629255136
288 (in isoform 2)Phosphorylation-23.9927251275
291UbiquitinationILATPPQEDAPSVDI
CCCCCCCCCCCCCCC
63.0121890473
295PhosphorylationPPQEDAPSVDIANIR
CCCCCCCCCCCCCCC
33.8629255136
295 (in isoform 2)Phosphorylation-33.8627251275
303SulfoxidationVDIANIRMPSLPSYK
CCCCCCCCCCCCCCC
2.0428183972
303 (in isoform 2)Phosphorylation-2.0427251275
305PhosphorylationIANIRMPSLPSYKVG
CCCCCCCCCCCCCCC
43.5021406692
308PhosphorylationIRMPSLPSYKVGDKI
CCCCCCCCCCCCCCH
42.7625307156
309PhosphorylationRMPSLPSYKVGDKIA
CCCCCCCCCCCCCHH
14.0421406692
310UbiquitinationMPSLPSYKVGDKIAT
CCCCCCCCCCCCHHH
44.0421890473
310AcetylationMPSLPSYKVGDKIAT
CCCCCCCCCCCCHHH
44.0425953088
310UbiquitinationMPSLPSYKVGDKIAT
CCCCCCCCCCCCHHH
44.0421890473
313 (in isoform 2)Phosphorylation-42.0227251275
3142-HydroxyisobutyrylationPSYKVGDKIATRKAY
CCCCCCCCHHHHHHH
28.45-
314AcetylationPSYKVGDKIATRKAY
CCCCCCCCHHHHHHH
28.4523749302
314UbiquitinationPSYKVGDKIATRKAY
CCCCCCCCHHHHHHH
28.4519608861
318UbiquitinationVGDKIATRKAYGQAL
CCCCHHHHHHHHHHH
16.7621890473
319UbiquitinationGDKIATRKAYGQALA
CCCHHHHHHHHHHHH
41.4221890473
3192-HydroxyisobutyrylationGDKIATRKAYGQALA
CCCHHHHHHHHHHHH
41.42-
319UbiquitinationGDKIATRKAYGQALA
CCCHHHHHHHHHHHH
41.4221906983
321PhosphorylationKIATRKAYGQALAKL
CHHHHHHHHHHHHHH
16.8928152594
322AcetylationIATRKAYGQALAKLG
HHHHHHHHHHHHHHC
15.9019608861
327UbiquitinationAYGQALAKLGHASDR
HHHHHHHHHCCCCCC
56.7121890473
3272-HydroxyisobutyrylationAYGQALAKLGHASDR
HHHHHHHHHCCCCCC
56.71-
327AcetylationAYGQALAKLGHASDR
HHHHHHHHHCCCCCC
56.7123954790
327UbiquitinationAYGQALAKLGHASDR
HHHHHHHHHCCCCCC
56.7121906983
334MethylationKLGHASDRIIALDGD
HHCCCCCCEEEEECC
21.51115918533
342PhosphorylationIIALDGDTKNSTFSE
EEEEECCCCCCCHHH
37.3421815630
3432-HydroxyisobutyrylationIALDGDTKNSTFSEI
EEEECCCCCCCHHHH
54.35-
343AcetylationIALDGDTKNSTFSEI
EEEECCCCCCCHHHH
54.3523954790
343SumoylationIALDGDTKNSTFSEI
EEEECCCCCCCHHHH
54.35-
343UbiquitinationIALDGDTKNSTFSEI
EEEECCCCCCCHHHH
54.3521906983
345PhosphorylationLDGDTKNSTFSEIFK
EECCCCCCCHHHHHH
32.1725159151
346PhosphorylationDGDTKNSTFSEIFKK
ECCCCCCCHHHHHHH
40.3421712546
348PhosphorylationDTKNSTFSEIFKKEH
CCCCCCHHHHHHHHC
29.8525159151
350 (in isoform 2)Phosphorylation-6.2527251275
3522-HydroxyisobutyrylationSTFSEIFKKEHPDRF
CCHHHHHHHHCCCCE
64.01-
352AcetylationSTFSEIFKKEHPDRF
CCHHHHHHHHCCCCE
64.0123954790
352SuccinylationSTFSEIFKKEHPDRF
CCHHHHHHHHCCCCE
64.0123954790
352SumoylationSTFSEIFKKEHPDRF
CCHHHHHHHHCCCCE
64.0128112733
352UbiquitinationSTFSEIFKKEHPDRF
CCHHHHHHHHCCCCE
64.01-
353AcetylationTFSEIFKKEHPDRFI
CHHHHHHHHCCCCEE
50.9725953088
353UbiquitinationTFSEIFKKEHPDRFI
CHHHHHHHHCCCCEE
50.97-
382PhosphorylationGCATRNRTVPFCSTF
CCCCCCCCCCCHHHH
35.76-
386S-nitrosylationRNRTVPFCSTFAAFF
CCCCCCCHHHHHHHH
2.8325040305
386S-palmitoylationRNRTVPFCSTFAAFF
CCCCCCCHHHHHHHH
2.8329575903
387PhosphorylationNRTVPFCSTFAAFFT
CCCCCCHHHHHHHHH
27.26-
406PhosphorylationQIRMAAISESNINLC
HHHHHHHCCCCCCCC
30.1928176443
408PhosphorylationRMAAISESNINLCGS
HHHHHCCCCCCCCCC
35.9028176443
415PhosphorylationSNINLCGSHCGVSIG
CCCCCCCCCCCCCCC
18.0128176443
420PhosphorylationCGSHCGVSIGEDGPS
CCCCCCCCCCCCCCC
15.3428176443
427PhosphorylationSIGEDGPSQMALEDL
CCCCCCCCHHHHHHH
37.8128176443
439PhosphorylationEDLAMFRSVPTSTVF
HHHHHHHCCCCCEEE
22.6021712546
442PhosphorylationAMFRSVPTSTVFYPS
HHHHCCCCCEEECCC
34.5721712546
444PhosphorylationFRSVPTSTVFYPSDG
HHCCCCCEEECCCCC
19.6728152594
447PhosphorylationVPTSTVFYPSDGVAT
CCCCEEECCCCCCCC
9.4828152594
449PhosphorylationTSTVFYPSDGVATEK
CCEEECCCCCCCCHH
35.3028152594
454PhosphorylationYPSDGVATEKAVELA
CCCCCCCCHHHHHHH
35.3028152594
4562-HydroxyisobutyrylationSDGVATEKAVELAAN
CCCCCCHHHHHHHHC
54.07-
456AcetylationSDGVATEKAVELAAN
CCCCCCHHHHHHHHC
54.0726051181
456UbiquitinationSDGVATEKAVELAAN
CCCCCCHHHHHHHHC
54.0721906983
465UbiquitinationVELAANTKGICFIRT
HHHHHCCCCEEEEEC
46.1921890473
4652-HydroxyisobutyrylationVELAANTKGICFIRT
HHHHHCCCCEEEEEC
46.19-
465AcetylationVELAANTKGICFIRT
HHHHHCCCCEEEEEC
46.1926051181
465UbiquitinationVELAANTKGICFIRT
HHHHHCCCCEEEEEC
46.1921890473
468S-palmitoylationAANTKGICFIRTSRP
HHCCCCEEEEECCCC
2.9429575903
472PhosphorylationKGICFIRTSRPENAI
CCEEEEECCCCCCEE
25.0321712546
473UbiquitinationGICFIRTSRPENAII
CEEEEECCCCCCEEE
35.6721890473
481PhosphorylationRPENAIIYNNNEDFQ
CCCCEEEECCCCCCC
13.0128152594
489 (in isoform 2)Phosphorylation-6.5727642862
4932-HydroxyisobutyrylationDFQVGQAKVVLKSKD
CCCCCEEEEEEECCC
25.62-
493AcetylationDFQVGQAKVVLKSKD
CCCCCEEEEEEECCC
25.6227452117
493UbiquitinationDFQVGQAKVVLKSKD
CCCCCEEEEEEECCC
25.62-
497AcetylationGQAKVVLKSKDDQVT
CEEEEEEECCCCCEE
43.8025953088
497UbiquitinationGQAKVVLKSKDDQVT
CEEEEEEECCCCCEE
43.80-
4992-HydroxyisobutyrylationAKVVLKSKDDQVTVI
EEEEEECCCCCEEEE
64.83-
499AcetylationAKVVLKSKDDQVTVI
EEEEEECCCCCEEEE
64.8323749302
499UbiquitinationAKVVLKSKDDQVTVI
EEEEEECCCCCEEEE
64.83-
5232-HydroxyisobutyrylationLAAAELLKKEKINIR
HHHHHHHHHCCCCEE
72.08-
523AcetylationLAAAELLKKEKINIR
HHHHHHHHHCCCCEE
72.0825953088
523UbiquitinationLAAAELLKKEKINIR
HHHHHHHHHCCCCEE
72.08-
5262-HydroxyisobutyrylationAELLKKEKINIRVLD
HHHHHHCCCCEEEEC
50.35-
538UbiquitinationVLDPFTIKPLDRKLI
EECCCCCCCCCCEEH
36.1521890473
5382-HydroxyisobutyrylationVLDPFTIKPLDRKLI
EECCCCCCCCCCEEH
36.15-
538AcetylationVLDPFTIKPLDRKLI
EECCCCCCCCCCEEH
36.1525953088
538SuccinylationVLDPFTIKPLDRKLI
EECCCCCCCCCCEEH
36.1523954790
538UbiquitinationVLDPFTIKPLDRKLI
EECCCCCCCCCCEEH
36.15-
543MalonylationTIKPLDRKLILDSAR
CCCCCCCEEHHHHCC
39.2826320211
543UbiquitinationTIKPLDRKLILDSAR
CCCCCCCEEHHHHCC
39.28-
546UbiquitinationPLDRKLILDSARATK
CCCCEEHHHHCCCCC
6.5321890473
548PhosphorylationDRKLILDSARATKGR
CCEEHHHHCCCCCCC
19.06-
563PhosphorylationILTVEDHYYEGGIGE
EEEEECCEECCCHHH
18.61-
564PhosphorylationLTVEDHYYEGGIGEA
EEEECCEECCCHHHH
12.51-
574PhosphorylationGIGEAVSSAVVGEPG
CHHHHHHHHCCCCCC
20.63-
595PhosphorylationAVNRVPRSGKPAELL
EECCCCCCCCHHHHH
45.1323911959
5972-HydroxyisobutyrylationNRVPRSGKPAELLKM
CCCCCCCCHHHHHHH
42.15-
597AcetylationNRVPRSGKPAELLKM
CCCCCCCCHHHHHHH
42.1519608861
597MalonylationNRVPRSGKPAELLKM
CCCCCCCCHHHHHHH
42.1526320211
597UbiquitinationNRVPRSGKPAELLKM
CCCCCCCCHHHHHHH
42.1519608861
6032-HydroxyisobutyrylationGKPAELLKMFGIDRD
CCHHHHHHHHCCCHH
44.82-
603AcetylationGKPAELLKMFGIDRD
CCHHHHHHHHCCCHH
44.8219608861
603SuccinylationGKPAELLKMFGIDRD
CCHHHHHHHHCCCHH
44.8223954790
604SulfoxidationKPAELLKMFGIDRDA
CHHHHHHHHCCCHHH
3.6221406390
605AcetylationPAELLKMFGIDRDAI
HHHHHHHHCCCHHHH
8.0919608861
605UbiquitinationPAELLKMFGIDRDAI
HHHHHHHHCCCHHHH
8.0919608861
609MethylationLKMFGIDRDAIAQAV
HHHHCCCHHHHHHHH
33.0866701869
611AcetylationMFGIDRDAIAQAVRG
HHCCCHHHHHHHHHH
10.4219608861

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
382TPhosphorylationKinaseAKT1P31749
PSP
387SPhosphorylationKinaseAKT1P31749
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TKT_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TKT_HUMANTKTphysical
9357955
TPIS_HUMANTPI1physical
22939629
UBC9_HUMANUBE2Iphysical
22939629
UFC1_HUMANUFC1physical
22939629
VDAC3_HUMANVDAC3physical
22939629
UGDH_HUMANUGDHphysical
22939629
UFM1_HUMANUFM1physical
22939629
UB2D1_HUMANUBE2D1physical
22939629
THIM_HUMANACAA2physical
26344197
PPAC_HUMANACP1physical
26344197
AK1A1_HUMANAKR1A1physical
26344197
ALDR_HUMANAKR1B1physical
26344197
AK1BF_HUMANAKR1B15physical
26344197
AK1C2_HUMANAKR1C2physical
26344197
AL4A1_HUMANALDH4A1physical
26344197
ALDOA_HUMANALDOAphysical
26344197
CALR_HUMANCALRphysical
26344197
COX17_HUMANCOX17physical
26344197
DUT_HUMANDUTphysical
26344197
ENOA_HUMANENO1physical
26344197
ENOG_HUMANENO2physical
26344197
ENOB_HUMANENO3physical
26344197
ESTD_HUMANESDphysical
26344197
FABP5_HUMANFABP5physical
26344197
FABP7_HUMANFABP7physical
26344197
FUMH_HUMANFHphysical
26344197
G3P_HUMANGAPDHphysical
26344197
GLRX1_HUMANGLRXphysical
26344197
G6PI_HUMANGPIphysical
26344197
GPX4_HUMANGPX4physical
26344197
HINT1_HUMANHINT1physical
26344197
HS74L_HUMANHSPA4Lphysical
26344197
CH10_HUMANHSPE1physical
26344197
IDHC_HUMANIDH1physical
26344197
ITPA_HUMANITPAphysical
26344197
LDHA_HUMANLDHAphysical
26344197
LDH6B_HUMANLDHAL6Bphysical
26344197
LDHB_HUMANLDHBphysical
26344197
LYPA2_HUMANLYPLA2physical
26344197
MIF_HUMANMIFphysical
26344197
SIAS_HUMANNANSphysical
26344197
NEDD8_HUMANNEDD8physical
26344197
NDKB_HUMANNME2physical
26344197
PDIA1_HUMANP4HBphysical
26344197
PCBP1_HUMANPCBP1physical
26344197
PIMT_HUMANPCMT1physical
26344197
PDCD6_HUMANPDCD6physical
26344197
PDC6I_HUMANPDCD6IPphysical
26344197
PGK1_HUMANPGK1physical
26344197
PGM2_HUMANPGM2physical
26344197
PIPNB_HUMANPITPNBphysical
26344197
PLST_HUMANPLS3physical
26344197
MYP2_HUMANPMP2physical
26344197
RAB10_HUMANRAB10physical
26344197
RPE_HUMANRPEphysical
26344197
SCYL2_HUMANSCYL2physical
26344197
SF01_HUMANSF1physical
26344197
SODM_HUMANSOD2physical
26344197
STAT4_HUMANSTAT4physical
26344197
STIP1_HUMANSTIP1physical
26344197
TALDO_HUMANTALDO1physical
26344197
TPIS_HUMANTPI1physical
26344197
UFM1_HUMANUFM1physical
26344197
TERA_HUMANVCPphysical
26344197
XRCC6_HUMANXRCC6physical
26344197
KHNYN_HUMANKHNYNphysical
28514442
GREB1_HUMANGREB1physical
28514442
SMG8_HUMANSMG8physical
28514442
FIGL1_HUMANFIGNL1physical
28514442
DPOA2_HUMANPOLA2physical
28514442
WDR54_HUMANWDR54physical
28514442
CE034_HUMANC5orf34physical
28514442
WDR19_HUMANWDR19physical
28514442
MOCOS_HUMANMOCOSphysical
28514442
POTEF_HUMANPOTEFphysical
28514442
WDR41_HUMANWDR41physical
28514442
STIL_HUMANSTILphysical
28514442
MED20_HUMANMED20physical
28514442
E2AK4_HUMANEIF2AK4physical
28514442
TBL1X_HUMANTBL1Xphysical
28514442
KCC2B_HUMANCAMK2Bphysical
28514442
TRI32_HUMANTRIM32physical
28514442
KDM5C_HUMANKDM5Cphysical
28514442
SPC25_HUMANSPC25physical
28514442
MED17_HUMANMED17physical
28514442
TYW4_HUMANLCMT2physical
28514442
PLEC_HUMANPLECphysical
28514442
DPP9_HUMANDPP9physical
28514442
EMAL4_HUMANEML4physical
28514442
HD_HUMANHTTphysical
28514442
TPPC8_HUMANTRAPPC8physical
28514442
ACSF4_HUMANAASDHphysical
28514442
TBCD4_HUMANTBC1D4physical
28514442

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

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-6; LYS-11; LYS-144;LYS-204; LYS-241; LYS-260; LYS-314; LYS-597 AND LYS-603, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
"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-232, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275 AND THR-287, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275, AND MASSSPECTROMETRY.

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