TPIS_YEAST - dbPTM
TPIS_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPIS_YEAST
UniProt AC P00942
Protein Name Triosephosphate isomerase
Gene Name TPI1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 248
Subcellular Localization
Protein Description
Protein Sequence MARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENSVDQIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDWTNVVVAYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPEFVDIINSRN
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
4Phosphorylation----MARTFFVGGNF
----CCCEEEECCCE		16.3422369663
12AcetylationFFVGGNFKLNGSKQS
EEECCCEEECCCHHH		45.0724489116
12UbiquitinationFFVGGNFKLNGSKQS
EEECCCEEECCCHHH		45.0723749301
16PhosphorylationGNFKLNGSKQSIKEI
CCEEECCCHHHHHHH		26.8422369663
17SuccinylationNFKLNGSKQSIKEIV
CEEECCCHHHHHHHH		49.8423954790
17UbiquitinationNFKLNGSKQSIKEIV
CEEECCCHHHHHHHH		49.8422817900
172-HydroxyisobutyrylationNFKLNGSKQSIKEIV
CEEECCCHHHHHHHH		49.84-
19PhosphorylationKLNGSKQSIKEIVER
EECCCHHHHHHHHHH		39.0922369663
212-HydroxyisobutyrylationNGSKQSIKEIVERLN
CCCHHHHHHHHHHHC		46.78-
21SuccinylationNGSKQSIKEIVERLN
CCCHHHHHHHHHHHC		46.7823954790
21UbiquitinationNGSKQSIKEIVERLN
CCCHHHHHHHHHHHC		46.7822817900
21AcetylationNGSKQSIKEIVERLN
CCCHHHHHHHHHHHC		46.7824489116
29PhosphorylationEIVERLNTASIPENV
HHHHHHCCCCCCCCE		26.7721551504
31PhosphorylationVERLNTASIPENVEV
HHHHCCCCCCCCEEE		36.3221551504
52PhosphorylationTYLDYSVSLVKKPQV
EECEEEEEEEECCEE		22.8521551504
55UbiquitinationDYSVSLVKKPQVTVG
EEEEEEEECCEEECC		65.1217644757
562-HydroxyisobutyrylationYSVSLVKKPQVTVGA
EEEEEEECCEEECCC		32.95-
56AcetylationYSVSLVKKPQVTVGA
EEEEEEECCEEECCC		32.9517397211
56UbiquitinationYSVSLVKKPQVTVGA
EEEEEEECCEEECCC		32.9523749301
60PhosphorylationLVKKPQVTVGAQNAY
EEECCEEECCCCEEE		14.1521082442
67PhosphorylationTVGAQNAYLKASGAF
ECCCCEEEEEECCCC		19.1123749301
69SuccinylationGAQNAYLKASGAFTG
CCCEEEEEECCCCCC		28.0323954790
69UbiquitinationGAQNAYLKASGAFTG
CCCEEEEEECCCCCC		28.0323749301
692-HydroxyisobutyrylationGAQNAYLKASGAFTG
CCCEEEEEECCCCCC		28.03-
69AcetylationGAQNAYLKASGAFTG
CCCEEEEEECCCCCC		28.0324489116
71PhosphorylationQNAYLKASGAFTGEN
CEEEEEECCCCCCCC		29.1222369663
75PhosphorylationLKASGAFTGENSVDQ
EEECCCCCCCCCHHH		42.9522369663
79PhosphorylationGAFTGENSVDQIKDV
CCCCCCCCHHHHHHH		23.8322369663
84UbiquitinationENSVDQIKDVGAKWV
CCCHHHHHHHCCCEE		40.5023749301
842-HydroxyisobutyrylationENSVDQIKDVGAKWV
CCCHHHHHHHCCCEE		40.50-
84AcetylationENSVDQIKDVGAKWV
CCCHHHHHHHCCCEE		40.5024489116
84SuccinylationENSVDQIKDVGAKWV
CCCHHHHHHHCCCEE		40.5023954790
89SuccinylationQIKDVGAKWVILGHS
HHHHHCCCEEEEECC		35.7423954790
89AcetylationQIKDVGAKWVILGHS
HHHHHCCCEEEEECC		35.7424489116
892-HydroxyisobutyrylationQIKDVGAKWVILGHS
HHHHHCCCEEEEECC		35.74-
89UbiquitinationQIKDVGAKWVILGHS
HHHHHCCCEEEEECC		35.7417644757
96PhosphorylationKWVILGHSERRSYFH
CEEEEECCCCHHHCC		30.8822369663
100PhosphorylationLGHSERRSYFHEDDK
EECCCCHHHCCCCCC		38.0721082442
101PhosphorylationGHSERRSYFHEDDKF
ECCCCHHHCCCCCCC		13.7217330950
107SuccinylationSYFHEDDKFIADKTK
HHCCCCCCCHHCHHH		51.4923954790
1072-HydroxyisobutyrylationSYFHEDDKFIADKTK
HHCCCCCCCHHCHHH		51.49-
107AcetylationSYFHEDDKFIADKTK
HHCCCCCCCHHCHHH		51.4924489116
112AcetylationDDKFIADKTKFALGQ
CCCCHHCHHHHHCCC		44.5924489116
1122-HydroxyisobutyrylationDDKFIADKTKFALGQ
CCCCHHCHHHHHCCC		44.59-
114UbiquitinationKFIADKTKFALGQGV
CCHHCHHHHHCCCCC		34.0917644757
1142-HydroxyisobutyrylationKFIADKTKFALGQGV
CCHHCHHHHHCCCCC		34.09-
134UbiquitinationIGETLEEKKAGKTLD
ECCCCCHHHCCCCHH		38.2517644757
135UbiquitinationGETLEEKKAGKTLDV
CCCCCHHHCCCCHHH		66.7017644757
1382-HydroxyisobutyrylationLEEKKAGKTLDVVER
CCHHHCCCCHHHHHH		51.26-
138AcetylationLEEKKAGKTLDVVER
CCHHHCCCCHHHHHH		51.2624489116
139PhosphorylationEEKKAGKTLDVVERQ
CHHHCCCCHHHHHHH		27.5428889911
158PhosphorylationLEEVKDWTNVVVAYE
HHHHHHCCCEEEEEE		28.4122369663
164PhosphorylationWTNVVVAYEPVWAIG
CCCEEEEEEEEEEEC		14.7922369663
172PhosphorylationEPVWAIGTGLAATPE
EEEEEECCCCCCCHH		23.9422369663
187PhosphorylationDAQDIHASIRKFLAS
HHHHHHHHHHHHHHH		14.5722369663
190UbiquitinationDIHASIRKFLASKLG
HHHHHHHHHHHHHHC		42.9622817900
194PhosphorylationSIRKFLASKLGDKAA
HHHHHHHHHHCHHHH		30.4726447709
195UbiquitinationIRKFLASKLGDKAAS
HHHHHHHHHCHHHHH		51.3822817900
195SuccinylationIRKFLASKLGDKAAS
HHHHHHHHHCHHHHH		51.3823954790
195AcetylationIRKFLASKLGDKAAS
HHHHHHHHHCHHHHH		51.3824489116
1952-HydroxyisobutyrylationIRKFLASKLGDKAAS
HHHHHHHHHCHHHHH		51.38-
199UbiquitinationLASKLGDKAASELRI
HHHHHCHHHHHHEEE		44.0123749301
1992-HydroxyisobutyrylationLASKLGDKAASELRI
HHHHHCHHHHHHEEE		44.01-
199AcetylationLASKLGDKAASELRI
HHHHHCHHHHHHEEE		44.0124489116
208PhosphorylationASELRILYGGSANGS
HHHEEEEECCCCCCC		19.6429136822
211PhosphorylationLRILYGGSANGSNAV
EEEEECCCCCCCCCE		17.7522369663
215PhosphorylationYGGSANGSNAVTFKD
ECCCCCCCCCEEECC		22.7922369663
219PhosphorylationANGSNAVTFKDKADV
CCCCCCEEECCCCCC		23.6624961812
221SuccinylationGSNAVTFKDKADVDG
CCCCEEECCCCCCCC		49.2923954790
221AcetylationGSNAVTFKDKADVDG
CCCCEEECCCCCCCC		49.2924489116
2212-HydroxyisobutyrylationGSNAVTFKDKADVDG
CCCCEEECCCCCCCC		49.29-
223SuccinylationNAVTFKDKADVDGFL
CCEEECCCCCCCCEE		47.2623954790
223AcetylationNAVTFKDKADVDGFL
CCEEECCCCCCCCEE		47.2624489116
223UbiquitinationNAVTFKDKADVDGFL
CCEEECCCCCCCCEE		47.2623749301
235PhosphorylationGFLVGGASLKPEFVD
CEEECCCCCCHHHHH		39.9522369663
237UbiquitinationLVGGASLKPEFVDII
EECCCCCCHHHHHHH		39.7523793018
237AcetylationLVGGASLKPEFVDII
EECCCCCCHHHHHHH		39.7524489116
246PhosphorylationEFVDIINSRN-----
HHHHHHHCCC-----		23.8522369663
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_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPIS_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 TPIS_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NDH1_YEASTNDE1genetic
12039737
NDH2_YEASTNDE2genetic
12039737
GPDM_YEASTGUT2genetic
12039737
TPIS_YEASTTPI1physical
18439027
TPIS_YEASTTPI1physical
18300228
HSC82_YEASTHSC82physical
19536198
TPIS_YEASTTPI1physical
22949845
MOB2_YEASTMOB2genetic
27708008
CDC24_YEASTCDC24genetic
27708008
CND2_YEASTBRN1genetic
27708008
ORC2_YEASTORC2genetic
27708008
ENP1_YEASTENP1genetic
27708008
CDC53_YEASTCDC53genetic
27708008
RPB1_YEASTRPO21genetic
27708008
RMRP_YEASTSNM1genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC20_YEASTCDC20genetic
27708008
RRP4_YEASTRRP4genetic
27708008
IPI1_YEASTIPI1genetic
27708008
ORC6_YEASTORC6genetic
27708008
CDC23_YEASTCDC23genetic
27708008
PAN1_YEASTPAN1genetic
27708008
NU192_YEASTNUP192genetic
27708008
RFC2_YEASTRFC2genetic
27708008
CDC11_YEASTCDC11genetic
27708008
RPF2_YEASTRPF2genetic
27708008
CLF1_YEASTCLF1genetic
27708008
NEP1_YEASTEMG1genetic
27708008
GSP1_YEASTGSP1genetic
27708008
RU1C_YEASTYHC1genetic
27708008
TAD3_YEASTTAD3genetic
27708008
ORC1_YEASTORC1genetic
27708008
GPI12_YEASTGPI12genetic
27708008
RPC6_YEASTRPC34genetic
27708008
CH10_YEASTHSP10genetic
27708008
APC5_YEASTAPC5genetic
27708008
SEC63_YEASTSEC63genetic
27708008
RPA1_YEASTRPA190genetic
27708008
SEC62_YEASTSEC62genetic
27708008
HRR25_YEASTHRR25genetic
27708008
IPL1_YEASTIPL1genetic
27708008
IWS1_YEASTSPN1genetic
27708008
DPM1_YEASTDPM1genetic
27708008
ETR1_YEASTETR1genetic
27708008
VMA21_YEASTVMA21genetic
27708008
PMA2_YEASTPMA2genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPIS_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-71; SER-211 AND SER-215,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 SER-96 AND SER-100, AND MASSSPECTROMETRY.

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