TKT1_YEAST - dbPTM
TKT1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TKT1_YEAST
UniProt AC P23254
Protein Name Transketolase 1
Gene Name TKL1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 680
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 MTQFTDIDKLAVSTIRILAVDTVSKANSGHPGAPLGMAPAAHVLWSQMRMNPTNPDWINRDRFVLSNGHAVALLYSMLHLTGYDLSIEDLKQFRQLGSRTPGHPEFELPGVEVTTGPLGQGISNAVGMAMAQANLAATYNKPGFTLSDNYTYVFLGDGCLQEGISSEASSLAGHLKLGNLIAIYDDNKITIDGATSISFDEDVAKRYEAYGWEVLYVENGNEDLAGIAKAIAQAKLSKDKPTLIKMTTTIGYGSLHAGSHSVHGAPLKADDVKQLKSKFGFNPDKSFVVPQEVYDHYQKTILKPGVEANNKWNKLFSEYQKKFPELGAELARRLSGQLPANWESKLPTYTAKDSAVATRKLSETVLEDVYNQLPELIGGSADLTPSNLTRWKEALDFQPPSSGSGNYSGRYIRYGIREHAMGAIMNGISAFGANYKPYGGTFLNFVSYAAGAVRLSALSGHPVIWVATHDSIGVGEDGPTHQPIETLAHFRSLPNIQVWRPADGNEVSAAYKNSLESKHTPSIIALSRQNLPQLEGSSIESASKGGYVLQDVANPDIILVATGSEVSLSVEAAKTLAAKNIKARVVSLPDFFTFDKQPLEYRLSVLPDNVPIMSVEVLATTCWGKYAHQSFGIDRFGASGKAPEVFKFFGFTPEGVAERAQKTIAFYKGDKLISPLKKAF
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
2Phosphorylation------MTQFTDIDK
------CCCCCHHHH		32.1828889911
9UbiquitinationTQFTDIDKLAVSTIR
CCCCHHHHHHHHEEE		38.3815699485
24PhosphorylationILAVDTVSKANSGHP
EEEEECHHHCCCCCC		28.3023749301
28PhosphorylationDTVSKANSGHPGAPL
ECHHHCCCCCCCCCC		43.2522369663
46PhosphorylationPAAHVLWSQMRMNPT
HHHHHHHHHCCCCCC		15.2222369663
86PhosphorylationHLTGYDLSIEDLKQF
HHHCCCCCHHHHHHH		22.4927017623
2352-HydroxyisobutyrylationAKAIAQAKLSKDKPT
HHHHHHHHHCCCCCC		41.01-
235SuccinylationAKAIAQAKLSKDKPT
HHHHHHHHHCCCCCC		41.0123954790
248PhosphorylationPTLIKMTTTIGYGSL
CCEEEEEEEECCCCC		16.9617287358
249PhosphorylationTLIKMTTTIGYGSLH
CEEEEEEEECCCCCC		11.8424961812
254PhosphorylationTTTIGYGSLHAGSHS
EEEECCCCCCCCCCC		14.4321440633
259PhosphorylationYGSLHAGSHSVHGAP
CCCCCCCCCCCCCCC		17.2424961812
261PhosphorylationSLHAGSHSVHGAPLK
CCCCCCCCCCCCCCC		19.9420377248
268AcetylationSVHGAPLKADDVKQL
CCCCCCCCHHHHHHH		49.0324489116
273AcetylationPLKADDVKQLKSKFG
CCCHHHHHHHHHHHC		57.8324489116
278AcetylationDVKQLKSKFGFNPDK
HHHHHHHHHCCCCCC		48.1724489116
285UbiquitinationKFGFNPDKSFVVPQE
HHCCCCCCCCCCCHH		47.2323749301
285AcetylationKFGFNPDKSFVVPQE
HHCCCCCCCCCCCHH		47.2324489116
286PhosphorylationFGFNPDKSFVVPQEV
HCCCCCCCCCCCHHH		30.5622369663
299AcetylationEVYDHYQKTILKPGV
HHHHHHHHHCCCCCH		30.3024489116
299UbiquitinationEVYDHYQKTILKPGV
HHHHHHHHHCCCCCH		30.3017644757
300PhosphorylationVYDHYQKTILKPGVE
HHHHHHHHCCCCCHH		18.9328889911
303AcetylationHYQKTILKPGVEANN
HHHHHCCCCCHHHCH		35.5624489116
303SuccinylationHYQKTILKPGVEANN
HHHHHCCCCCHHHCH		35.5623954790
303UbiquitinationHYQKTILKPGVEANN
HHHHHCCCCCHHHCH		35.5623749301
311UbiquitinationPGVEANNKWNKLFSE
CCHHHCHHHHHHHHH		52.5317644757
311AcetylationPGVEANNKWNKLFSE
CCHHHCHHHHHHHHH		52.5324489116
314AcetylationEANNKWNKLFSEYQK
HHCHHHHHHHHHHHH		50.2024489116
317PhosphorylationNKWNKLFSEYQKKFP
HHHHHHHHHHHHHCH		45.9221440633
321SuccinylationKLFSEYQKKFPELGA
HHHHHHHHHCHHHHH		56.3223954790
321UbiquitinationKLFSEYQKKFPELGA
HHHHHHHHHCHHHHH		56.3215699485
321AcetylationKLFSEYQKKFPELGA
HHHHHHHHHCHHHHH		56.3222865919
322AcetylationLFSEYQKKFPELGAE
HHHHHHHHCHHHHHH		51.1024489116
322UbiquitinationLFSEYQKKFPELGAE
HHHHHHHHCHHHHHH		51.1015699485
335PhosphorylationAELARRLSGQLPANW
HHHHHHHCCCCCCCH		23.7622369663
345UbiquitinationLPANWESKLPTYTAK
CCCCHHHCCCCCCCC		47.1517644757
345AcetylationLPANWESKLPTYTAK
CCCCHHHCCCCCCCC		47.1524489116
352SuccinylationKLPTYTAKDSAVATR
CCCCCCCCCCHHHHH		44.4023954790
352UbiquitinationKLPTYTAKDSAVATR
CCCCCCCCCCHHHHH		44.4023749301
3522-HydroxyisobutyrylationKLPTYTAKDSAVATR
CCCCCCCCCCHHHHH		44.40-
352AcetylationKLPTYTAKDSAVATR
CCCCCCCCCCHHHHH		44.4024489116
354PhosphorylationPTYTAKDSAVATRKL
CCCCCCCCHHHHHHH		24.7628889911
360UbiquitinationDSAVATRKLSETVLE
CCHHHHHHHHHHHHH		52.6023749301
362PhosphorylationAVATRKLSETVLEDV
HHHHHHHHHHHHHHH		33.9722369663
364PhosphorylationATRKLSETVLEDVYN
HHHHHHHHHHHHHHH		27.3222369663
370PhosphorylationETVLEDVYNQLPELI
HHHHHHHHHHCHHHH		14.9822369663
392UbiquitinationPSNLTRWKEALDFQP
HHHHHHHHHHHCCCC		29.8023749301
392AcetylationPSNLTRWKEALDFQP
HHHHHHHHHHHCCCC		29.8024489116
401PhosphorylationALDFQPPSSGSGNYS
HHCCCCCCCCCCCCC		54.7529734811
402PhosphorylationLDFQPPSSGSGNYSG
HCCCCCCCCCCCCCC		42.6328889911
404PhosphorylationFQPPSSGSGNYSGRY
CCCCCCCCCCCCCCE		26.3028889911
407PhosphorylationPSSGSGNYSGRYIRY
CCCCCCCCCCCEEEC		18.9427017623
408PhosphorylationSSGSGNYSGRYIRYG
CCCCCCCCCCEEECC		22.3121440633
438PhosphorylationFGANYKPYGGTFLNF
CCCCCCCCCCCHHHH		24.8422369663
441PhosphorylationNYKPYGGTFLNFVSY
CCCCCCCCHHHHHHH		22.1622369663
447PhosphorylationGTFLNFVSYAAGAVR
CCHHHHHHHHHHCHH		12.6222369663
448PhosphorylationTFLNFVSYAAGAVRL
CHHHHHHHHHHCHHH		8.6522369663
492PhosphorylationETLAHFRSLPNIQVW
HHHHHHHCCCCEEEE		47.4322369663
512UbiquitinationNEVSAAYKNSLESKH
CCCCHHHHHCCCCCC		35.0224961812
518AcetylationYKNSLESKHTPSIIA
HHHCCCCCCCCHHHE		41.9724489116
522PhosphorylationLESKHTPSIIALSRQ
CCCCCCCHHHEEECC		27.9921440633
527PhosphorylationTPSIIALSRQNLPQL
CCHHHEEECCCCCCC		23.8528889911
579SuccinylationAAKTLAAKNIKARVV
HHHHHHHCCCEEEEE		54.3123954790
5792-HydroxyisobutyrylationAAKTLAAKNIKARVV
HHHHHHHCCCEEEEE		54.31-
579AcetylationAAKTLAAKNIKARVV
HHHHHHHCCCEEEEE		54.3125381059
596AcetylationPDFFTFDKQPLEYRL
CCCCCCCCCCCEEEE		50.0124489116
625UbiquitinationLATTCWGKYAHQSFG
EEECCCHHHHHHHHC		18.1117644757
630PhosphorylationWGKYAHQSFGIDRFG
CHHHHHHHHCCCCCC		18.6424961812
639PhosphorylationGIDRFGASGKAPEVF
CCCCCCCCCCCCHHH		41.0028889911
641UbiquitinationDRFGASGKAPEVFKF
CCCCCCCCCCHHHHH		59.2723749301
641SuccinylationDRFGASGKAPEVFKF
CCCCCCCCCCHHHHH		59.2723954790
641AcetylationDRFGASGKAPEVFKF
CCCCCCCCCCHHHHH		59.2724489116
647UbiquitinationGKAPEVFKFFGFTPE
CCCCHHHHHCCCCHH		44.9824961812
647SuccinylationGKAPEVFKFFGFTPE
CCCCHHHHHCCCCHH		44.9823954790
647AcetylationGKAPEVFKFFGFTPE
CCCCHHHHHCCCCHH		44.9824489116
652PhosphorylationVFKFFGFTPEGVAER
HHHHCCCCHHHHHHH		22.3221440633
662AcetylationGVAERAQKTIAFYKG
HHHHHHHHEEEEEEC		40.7022865919
662SuccinylationGVAERAQKTIAFYKG
HHHHHHHHEEEEEEC		40.7023954790
6622-HydroxyisobutyrylationGVAERAQKTIAFYKG
HHHHHHHHEEEEEEC		40.70-
663PhosphorylationVAERAQKTIAFYKGD
HHHHHHHEEEEEECC		12.8819779198
667PhosphorylationAQKTIAFYKGDKLIS
HHHEEEEEECCEECH		12.6819779198
668AcetylationQKTIAFYKGDKLISP
HHEEEEEECCEECHH		54.9324489116
668SuccinylationQKTIAFYKGDKLISP
HHEEEEEECCEECHH		54.9323954790
6682-HydroxyisobutyrylationQKTIAFYKGDKLISP
HHEEEEEECCEECHH		54.93-
668UbiquitinationQKTIAFYKGDKLISP
HHEEEEEECCEECHH		54.9323749301
671AcetylationIAFYKGDKLISPLKK
EEEEECCEECHHHHH		57.2824489116
671UbiquitinationIAFYKGDKLISPLKK
EEEEECCEECHHHHH		57.2822817900
674PhosphorylationYKGDKLISPLKKAF-
EECCEECHHHHHCC-		34.3221440633
677SuccinylationDKLISPLKKAF----
CEECHHHHHCC----		45.5023954790
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 TKT1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TKT1_YEAST !!
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 TKT1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
G6PD_YEASTZWF1genetic
8299150
TKT2_YEASTTKL2physical
16554755
SSB2_YEASTSSB2physical
19536198
TKT2_YEASTTKL2genetic
18408719
G6PD_YEASTZWF1genetic
19129474
G6PD_YEASTZWF1genetic
16941010
TKT2_YEASTTKL2genetic
16941010
UBI4P_YEASTUBI4physical
20694217
TKT2_YEASTTKL2genetic
7916691
TKT1_YEASTTKL1physical
15178335
KCS1_YEASTKCS1genetic
21623372
ERG6_YEASTERG6genetic
21623372
BAP2_YEASTBAP2genetic
21623372
THDH_YEASTILV1genetic
21623372
6PGD1_YEASTGND1genetic
21623372
ARO1_YEASTARO1genetic
21623372
RPE_YEASTRPE1genetic
21623372
THRC_YEASTTHR4genetic
21623372
TRPG_YEASTTRP3genetic
21623372
RM01_YEASTMRPL1genetic
27708008
PIN4_YEASTPIN4genetic
27708008
BAP2_YEASTBAP2genetic
27708008
SNF5_YEASTSNF5genetic
27708008
RV161_YEASTRVS161genetic
27708008
OCA4_YEASTOCA4genetic
27708008
DHE2_YEASTGDH2genetic
27708008
OCA6_YEASTOCA6genetic
27708008
WDR59_YEASTMTC5genetic
27708008
SAC3_YEASTSAC3genetic
27708008
UME6_YEASTUME6genetic
27708008
LSM6_YEASTLSM6genetic
27708008
STP1_YEASTSTP1genetic
27708008
MIG1_YEASTMIG1genetic
27708008
SGF73_YEASTSGF73genetic
27708008
AIM14_YEASTAIM14genetic
27708008
PEX31_YEASTPEX31genetic
27708008
UPF3_YEASTUPF3genetic
27708008
VMA21_YEASTVMA21genetic
27708008
SNF6_YEASTSNF6genetic
27708008
NMD2_YEASTNMD2genetic
27708008
STB5_YEASTSTB5genetic
27708008
SDS3_YEASTSDS3genetic
27708008
DAL81_YEASTDAL81genetic
27708008
YJQ3_YEASTYJL163Cgenetic
27708008
LST4_YEASTLST4genetic
27708008
ALY1_YEASTALY1genetic
27708008
ERG3_YEASTERG3genetic
27708008
VRP1_YEASTVRP1genetic
27708008
ERG6_YEASTERG6genetic
27708008
SOK2_YEASTSOK2genetic
27708008
SUB1_YEASTSUB1genetic
27708008
SAP30_YEASTSAP30genetic
27708008
GAS1_YEASTGAS1genetic
27708008
EAF7_YEASTEAF7genetic
27708008
SIN3_YEASTSIN3genetic
27708008
IRA2_YEASTIRA2genetic
27708008
HRK1_YEASTHRK1genetic
27708008
TGS1_YEASTTGS1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TKT1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-402; SER-492AND SER-639, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248 AND SER-335, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND MASSSPECTROMETRY.

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