THI3_YEAST - dbPTM
THI3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THI3_YEAST
UniProt AC Q07471
Protein Name Thiamine metabolism regulatory protein THI3
Gene Name THI3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 609
Subcellular Localization Nucleus .
Protein Description One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-acids). In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from leucine (4-methyl-2-oxopentanoate, also alpha-keto-isocaproate) and isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), whereas transaminated valine, transaminated aromatic amino acids, and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins. The enzyme is also positively regulating the thiamine metabolism by a molecular mechanism that may involve thiamine concentration sensing and signal transmission..
Protein Sequence MNSSYTQRYALPKCIAISDYLFHRLNQLNIHTIFGLSGEFSMPLLDKLYNIPNLRWAGNSNELNAAYAADGYSRLKGLGCLITTFGVGELSAINGVAGSYAEHVGILHIVGMPPTSAQTKQLLLHHTLGNGDFTVFHRIASDVACYTTLIIDSELCADEVDKCIKKAWIEQRPVYMGMPVNQVNLPIESARLNTPLDLQLHKNDPDVEKEVISRILSFIYKSQNPAIIVDACTSRQNLIEETKELCNRLKFPVFVTPMGKGTVNETDPQFGGVFTGSISAPEVREVVDFADFIIVIGCMLSEFSTSTFHFQYKTKNCALLYSTSVKLKNATYPDLSIKLLLQKILANLDESKLSYQPSEQPSMMVPRPYPAGNVLLRQEWVWNEISHWFQPGDIIITETGASAFGVNQTRFPVNTLGISQALWGSVGYTMGACLGAEFAVQEINKDKFPATKHRVILFMGDGAFQLTVQELSTIVKWGLTPYIFVMNNQGYSVDRFLHHRSDASYYDIQPWNYLGLLRVFGCTNYETKKIITVGEFRSMISDPNFATNDKIRMIEIMLPPRDVPQALLDRWVVEKEQSKQVQEENENSSAVNTPTPEFQPLLKKNQVGY
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
134PhosphorylationTLGNGDFTVFHRIAS
HCCCCCCEEEEHHHC		27.3128889911
482PhosphorylationVKWGLTPYIFVMNNQ
HHCCCCCEEEEECCC		11.1919779198
491PhosphorylationFVMNNQGYSVDRFLH
EEECCCCCEEEEEEC		8.8519779198
492PhosphorylationVMNNQGYSVDRFLHH
EECCCCCEEEEEECC		25.1119779198
588PhosphorylationVQEENENSSAVNTPT
HHHHHCCCCCCCCCC		17.3121551504
589PhosphorylationQEENENSSAVNTPTP
HHHHCCCCCCCCCCH		48.0623749301
593PhosphorylationENSSAVNTPTPEFQP
CCCCCCCCCCHHCHH		23.1823749301
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 THI3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THI3_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 THI3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCPB_YEASTCCT2physical
11805826
FYV8_YEASTFYV8physical
11805826
THI2_YEASTTHI2physical
16194233
PDC2_YEASTPDC2physical
19013460
THI7_YEASTTHI7genetic
21623372
TPS1_YEASTTPS1genetic
21623372
DS1P2_YEASTYSR3genetic
21623372
ERG6_YEASTERG6genetic
21623372
THI7_YEASTTHI7genetic
23209439
NRT1_YEASTNRT1genetic
23209439
THI72_YEASTTHI72genetic
23209439
DHAS_YEASTHOM2genetic
23111598
THI2_YEASTTHI2genetic
27015653
ERG27_YEASTERG27genetic
27708008
TAD3_YEASTTAD3genetic
27708008
RSC9_YEASTRSC9genetic
27708008
TIM50_YEASTTIM50genetic
27708008
DEP1_YEASTDEP1genetic
27708008
RXT2_YEASTRXT2genetic
27708008
MIG1_YEASTMIG1genetic
27708008
TPC1_YEASTTPC1genetic
27708008
SDS3_YEASTSDS3genetic
27708008
ILM1_YEASTILM1genetic
27708008
ERG3_YEASTERG3genetic
27708008
THI7_YEASTTHI7genetic
27708008
ERG6_YEASTERG6genetic
27708008
SAP30_YEASTSAP30genetic
27708008
PHO23_YEASTPHO23genetic
27708008
EAF7_YEASTEAF7genetic
27708008
CTI6_YEASTCTI6genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of THI3_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 THR-134, AND MASSSPECTROMETRY.

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