THI4_SCHPO - dbPTM
THI4_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID THI4_SCHPO
UniProt AC P40998
Protein Name Thiamine thiazole synthase {ECO:0000255|HAMAP-Rule:MF_03158}
Gene Name thi2
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 328
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance..
Protein Sequence MAPATAVVTPQTAFKTDLPVEKTAHNTVVKSEMGALSKAYPTYSLDESFSFAPIRESTVSRAMTRRYFSDLDKYAESDIVIVGAGSAGLTAAYYIGTRRPDLKIAIIEASVAPGGGAWLGGQLFSAMVVRKPADLFLNEIGVPYEDEGDYVVVKHAALFTSTVMARTLALPNVKLFNATAVEDLIVKEGKDGKQRIAGVVTNWTLVSLNHGLQSCMDPNTINAHLVVSATGHDGPFGAFCVKRLASAQLVSNLHDMRPLDMNRAEDLIVKGTREVFPGMIVGGMELSEFDGANRMGPTFGGMMFSGIKAAQEALAIFDERKAVNEKYL
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
5Phosphorylation---MAPATAVVTPQT
---CCCCEEEECCCC
20.9424763107
9PhosphorylationAPATAVVTPQTAFKT
CCCEEEECCCCCCCC
11.7724763107
12PhosphorylationTAVVTPQTAFKTDLP
EEEECCCCCCCCCCC
34.9529996109
16PhosphorylationTPQTAFKTDLPVEKT
CCCCCCCCCCCCEEC
35.9925720772
23PhosphorylationTDLPVEKTAHNTVVK
CCCCCEECCCCHHHH
21.4624763107
27PhosphorylationVEKTAHNTVVKSEMG
CEECCCCHHHHHHHH
19.4621712547
31PhosphorylationAHNTVVKSEMGALSK
CCCHHHHHHHHHHHH
22.6229996109
40PhosphorylationMGALSKAYPTYSLDE
HHHHHHCCCCCCCCC
10.3929996109
42PhosphorylationALSKAYPTYSLDESF
HHHHCCCCCCCCCCC
17.0529996109
43PhosphorylationLSKAYPTYSLDESFS
HHHCCCCCCCCCCCC
11.6129996109
44PhosphorylationSKAYPTYSLDESFSF
HHCCCCCCCCCCCCC
31.6429996109
48PhosphorylationPTYSLDESFSFAPIR
CCCCCCCCCCCCCCC
26.3425720772
57PhosphorylationSFAPIRESTVSRAMT
CCCCCCHHHHHHHHH
25.0229996109
58PhosphorylationFAPIRESTVSRAMTR
CCCCCHHHHHHHHHH
20.1129996109
60PhosphorylationPIRESTVSRAMTRRY
CCCHHHHHHHHHHHH
17.8929996109
69PhosphorylationAMTRRYFSDLDKYAE
HHHHHHHCCHHHHCC
28.4725720772
215OtherLNHGLQSCMDPNTIN
CCCHHHHCCCCCCCC
2.01-
246PhosphorylationFCVKRLASAQLVSNL
HHHHHHHHHHHHHCC
22.5725720772
251PhosphorylationLASAQLVSNLHDMRP
HHHHHHHHCCHHCCC
42.1229996109
287PhosphorylationIVGGMELSEFDGANR
EECCEEHHHCCCCCC
23.9425720772
327PhosphorylationRKAVNEKYL------
HHHHHHHCC------
16.0925720772

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 THI4_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of THI4_SCHPO !!

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 THI4_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
THI4_SCHPOthi2physical
23695164
THI4_SCHPOthi2physical
26771498

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of THI4_SCHPO

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Related Literatures of Post-Translational Modification

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