dbPTM

TPIS_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TPIS_DROME
UniProt AC	P29613
Protein Name	Triosephosphate isomerase
Gene Name	Tpi
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	247
Subcellular Localization
Protein Description
Protein Sequence	MSRKFCVGGNWKMNGDQKSIAEIAKTLSSAALDPNTEVVIGCPAIYLMYARNLLPCELGLAGQNAYKVAKGAFTGEISPAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKDWKNVVVAYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPEFVDIINARQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
Oops, there are no PTM records of TPIS_DROME !!

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_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TPIS_DROME !!

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_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HSP83_DROME	Hsp83	genetic	20727972
PSB1_DROME	Prosbeta6	genetic	18458110
HSP7D_DROME	Hsc70-4	genetic	20727972
HSP83_DROME	Hsp83	physical	20727972
TPIS_DROME	Tpi	physical	27031109

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TPIS_DROME

Related Literatures of Post-Translational Modification