TAL1_YEAST - dbPTM
TAL1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TAL1_YEAST
UniProt AC P15019
Protein Name Transaldolase
Gene Name TAL1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 335
Subcellular Localization
Protein Description Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway..
Protein Sequence MSEPAQKKQKVANNSLEQLKASGTVVVADTGDFGSIAKFQPQDSTTNPSLILAAAKQPTYAKLIDVAVEYGKKHGKTTEEQVENAVDRLLVEFGKEILKIVPGRVSTEVDARLSFDTQATIEKARHIIKLFEQEGVSKERVLIKIASTWEGIQAAKELEEKDGIHCNLTLLFSFVQAVACAEAQVTLISPFVGRILDWYKSSTGKDYKGEADPGVISVKKIYNYYKKYGYKTIVMGASFRSTDEIKNLAGVDYLTISPALLDKLMNSTEPFPRVLDPVSAKKEAGDKISYISDESKFRFDLNEDAMATEKLSEGIRKFSADIVTLFDLIEKKVTA
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------MSEPAQKKQ
------CCHHHHHHH
52.899298649
7Acetylation-MSEPAQKKQKVANN
-CCHHHHHHHHHHCC
60.3125381059
15PhosphorylationKQKVANNSLEQLKAS
HHHHHCCCHHHHHHC
32.8430377154
30PhosphorylationGTVVVADTGDFGSIA
CEEEEECCCCCCCCE
28.9824961812
35PhosphorylationADTGDFGSIAKFQPQ
ECCCCCCCCEECCCC
21.2624961812
49PhosphorylationQDSTTNPSLILAAAK
CCCCCCHHHHHHHCC
30.0625752575
56UbiquitinationSLILAAAKQPTYAKL
HHHHHHCCCCCHHHH
52.6723749301
56SuccinylationSLILAAAKQPTYAKL
HHHHHHCCCCCHHHH
52.6723954790
56AcetylationSLILAAAKQPTYAKL
HHHHHHCCCCCHHHH
52.6724489116
72AcetylationDVAVEYGKKHGKTTE
HHHHHHHHHCCCCCH
40.4724489116
76UbiquitinationEYGKKHGKTTEEQVE
HHHHHCCCCCHHHHH
52.5823749301
95UbiquitinationRLLVEFGKEILKIVP
HHHHHHHHHHHHHCC
47.0723749301
95AcetylationRLLVEFGKEILKIVP
HHHHHHHHHHHHHCC
47.0724489116
99UbiquitinationEFGKEILKIVPGRVS
HHHHHHHHHCCCCCC
47.5222817900
99AcetylationEFGKEILKIVPGRVS
HHHHHHHHHCCCCCC
47.5224489116
123UbiquitinationDTQATIEKARHIIKL
CCHHHHHHHHHHHHH
47.0423749301
1232-HydroxyisobutyrylationDTQATIEKARHIIKL
CCHHHHHHHHHHHHH
47.04-
129AcetylationEKARHIIKLFEQEGV
HHHHHHHHHHHHCCC
46.6624489116
138AcetylationFEQEGVSKERVLIKI
HHHCCCCHHHHHHHH
47.3224489116
1382-HydroxyisobutyrylationFEQEGVSKERVLIKI
HHHCCCCHHHHHHHH
47.32-
138UbiquitinationFEQEGVSKERVLIKI
HHHCCCCHHHHHHHH
47.3223749301
138SuccinylationFEQEGVSKERVLIKI
HHHCCCCHHHHHHHH
47.3223954790
144UbiquitinationSKERVLIKIASTWEG
CHHHHHHHHHHHHHH
28.2323749301
156AcetylationWEGIQAAKELEEKDG
HHHHHHHHHHHHCCC
66.8924489116
156UbiquitinationWEGIQAAKELEEKDG
HHHHHHHHHHHHCCC
66.8923749301
200AcetylationGRILDWYKSSTGKDY
HHHHHHHHHCCCCCC
33.4124489116
200SuccinylationGRILDWYKSSTGKDY
HHHHHHHHHCCCCCC
33.4123954790
2002-HydroxyisobutyrylationGRILDWYKSSTGKDY
HHHHHHHHHCCCCCC
33.41-
205AcetylationWYKSSTGKDYKGEAD
HHHHCCCCCCCCCCC
58.9524489116
205SuccinylationWYKSSTGKDYKGEAD
HHHHCCCCCCCCCCC
58.9523954790
2052-HydroxyisobutyrylationWYKSSTGKDYKGEAD
HHHHCCCCCCCCCCC
58.95-
208AcetylationSSTGKDYKGEADPGV
HCCCCCCCCCCCCCC
61.4824489116
208SuccinylationSSTGKDYKGEADPGV
HCCCCCCCCCCCCCC
61.4823954790
219SuccinylationDPGVISVKKIYNYYK
CCCCEEHHHHHHHHH
27.0223954790
226SuccinylationKKIYNYYKKYGYKTI
HHHHHHHHHHCCEEE
29.2023954790
231AcetylationYYKKYGYKTIVMGAS
HHHHHCCEEEEECCC
27.6722865919
238PhosphorylationKTIVMGASFRSTDEI
EEEEECCCCCCHHHH
18.5722369663
246UbiquitinationFRSTDEIKNLAGVDY
CCCHHHHHHHCCCCE
43.8123749301
246AcetylationFRSTDEIKNLAGVDY
CCCHHHHHHHCCCCE
43.8124489116
246SuccinylationFRSTDEIKNLAGVDY
CCCHHHHHHHCCCCE
43.8123954790
279PhosphorylationPRVLDPVSAKKEAGD
CCCCCCCCCCCCCCC
39.5021440633
2812-HydroxyisobutyrylationVLDPVSAKKEAGDKI
CCCCCCCCCCCCCCC
43.57-
281SuccinylationVLDPVSAKKEAGDKI
CCCCCCCCCCCCCCC
43.5723954790
281AcetylationVLDPVSAKKEAGDKI
CCCCCCCCCCCCCCC
43.5725381059
282AcetylationLDPVSAKKEAGDKIS
CCCCCCCCCCCCCCE
53.1424489116
287AcetylationAKKEAGDKISYISDE
CCCCCCCCCEEECCC
32.4124489116
287SuccinylationAKKEAGDKISYISDE
CCCCCCCCCEEECCC
32.4123954790
2872-HydroxyisobutyrylationAKKEAGDKISYISDE
CCCCCCCCCEEECCC
32.41-
289PhosphorylationKEAGDKISYISDESK
CCCCCCCEEECCCCC
23.3523749301
292PhosphorylationGDKISYISDESKFRF
CCCCEEECCCCCCCC
27.3922369663
295PhosphorylationISYISDESKFRFDLN
CEEECCCCCCCCCCC
41.9322369663
2962-HydroxyisobutyrylationSYISDESKFRFDLNE
EEECCCCCCCCCCCC
38.21-
296UbiquitinationSYISDESKFRFDLNE
EEECCCCCCCCCCCC
38.2123749301
296AcetylationSYISDESKFRFDLNE
EEECCCCCCCCCCCC
38.2124489116
310UbiquitinationEDAMATEKLSEGIRK
CCHHHHHHHHHHHHH
53.6223749301
324PhosphorylationKFSADIVTLFDLIEK
HHHHHHHHHHHHHHH
23.2622369663

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 TAL1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TAL1_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 TAL1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TKT1_YEASTTKL1genetic
8299150
G6PD_YEASTZWF1genetic
8299150
TAL2_YEASTNQM1physical
16554755
SSB1_YEASTSSB1physical
19536198
TAL2_YEASTNQM1genetic
18408719
TAL2_YEASTNQM1genetic
16941010
G6PD_YEASTZWF1genetic
16941010
POP7_YEASTPOP7genetic
27708008
ACT_YEASTACT1genetic
27708008
DBF2_YEASTDBF2genetic
27708008
TAF1_YEASTTAF1genetic
27708008
STS1_YEASTSTS1genetic
27708008
DPB11_YEASTDPB11genetic
27708008
IF2A_YEASTSUI2genetic
27708008
GPI2_YEASTGPI2genetic
27708008
IF6_YEASTTIF6genetic
27708008
MRX3_YEASTYBL095Wgenetic
27708008
ECM8_YEASTECM8genetic
27708008
SLX5_YEASTSLX5genetic
27708008
CYK3_YEASTCYK3genetic
27708008
SWF1_YEASTSWF1genetic
27708008
RAV2_YEASTRAV2genetic
27708008
SNX41_YEASTSNX41genetic
27708008
YE16_YEASTYER186Cgenetic
27708008
RL24A_YEASTRPL24Agenetic
27708008
SKI8_YEASTSKI8genetic
27708008
SLX9_YEASTSLX9genetic
27708008
CGS6_YEASTCLB6genetic
27708008
YHI9_YEASTYHI9genetic
27708008
SNX4_YEASTSNX4genetic
27708008
YJH0_YEASTYJL070Cgenetic
27708008
SA185_YEASTSAP185genetic
27708008
FEN1_YEASTRAD27genetic
27708008
MEH1_YEASTMEH1genetic
27708008
BCH2_YEASTBCH2genetic
27708008
YL012_YEASTYLR012Cgenetic
27708008
IOC4_YEASTIOC4genetic
27708008
NTH2_YEASTNTG2genetic
27708008
RTC1_YEASTRTC1genetic
27708008
PRM4_YEASTPRM4genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TAL1_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins.";
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.;
Electrophoresis 18:1347-1360(1997).
Cited for: ACETYLATION AT SER-2.
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-238, AND MASSSPECTROMETRY.

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