TCTP_DROME - dbPTM
TCTP_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TCTP_DROME
UniProt AC Q9VGS2
Protein Name Translationally-controlled tumor protein homolog
Gene Name Tctp
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 172
Subcellular Localization Cytoplasm.
Protein Description Involved in calcium binding and microtubule stabilization..
Protein Sequence MKIYKDIITGDEMFADTYKMKLVDDVIYEVYGKLITRQGDDIKLEGANASAEEADEGTDITSESGVDVVLNHRLTECFAFGDKKSYTLYLKDYMKKVLAKLEEKSPDQVDIFKTNMNKAMKDILGRFKELQFFTGESMDCDGMVALVEYREINGDSVPVLMFFKHGLEEEKC
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
19AcetylationEMFADTYKMKLVDDV
HHHHHHHHCCCHHHH
31.4821791702
21AcetylationFADTYKMKLVDDVIY
HHHHHHCCCHHHHHH
41.0021791702
28PhosphorylationKLVDDVIYEVYGKLI
CCHHHHHHHHHHHHH
10.1319429919
31PhosphorylationDDVIYEVYGKLITRQ
HHHHHHHHHHHHHCC
9.1519429919
50PhosphorylationKLEGANASAEEADEG
EEECCCCCHHHCCCC
35.7022817900
58PhosphorylationAEEADEGTDITSESG
HHHCCCCCCCCCCCC
23.3730478224
61PhosphorylationADEGTDITSESGVDV
CCCCCCCCCCCCCCE
29.2922817900
62PhosphorylationDEGTDITSESGVDVV
CCCCCCCCCCCCCEE
30.0529892262
84AcetylationCFAFGDKKSYTLYLK
EEECCCCCEEEEEHH
54.1321791702
91AcetylationKSYTLYLKDYMKKVL
CEEEEEHHHHHHHHH
33.0021791702
100AcetylationYMKKVLAKLEEKSPD
HHHHHHHHHHHHCHH
52.8821791702
104AcetylationVLAKLEEKSPDQVDI
HHHHHHHHCHHHHHH
58.8921791702
105PhosphorylationLAKLEEKSPDQVDIF
HHHHHHHCHHHHHHH
36.6722817900
113AcetylationPDQVDIFKTNMNKAM
HHHHHHHHHHHHHHH
39.0521791702
121AcetylationTNMNKAMKDILGRFK
HHHHHHHHHHHHHHH
46.6121791702

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 TCTP_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TCTP_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 TCTP_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DYL1_DROMEctpphysical
14605208
SAP47_DROMESap47physical
14605208
C1GLT_DROMEC1GalTAphysical
14605208
CCNE_DROMECycEgenetic
17301792
ATM_DROMEtefugenetic
24352200
RHEB_DROMERhebphysical
17301792
RPB1_DROMERpII215physical
27687497
RAD50_DROMErad50physical
24352200
BRM_DROMEbrmphysical
27687497
ATM_DROMEtefuphysical
24352200

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; THR-58 AND THR-61,AND MASS SPECTROMETRY.
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASSSPECTROMETRY.

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