TRA2_DROME - dbPTM
TRA2_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRA2_DROME
UniProt AC P19018
Protein Name Transformer-2 sex-determining protein
Gene Name tra2
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 264
Subcellular Localization
Protein Description Required for female sex determination in somatic cells and for spermatogenesis in male germ cells. Positive regulator of female-specific splicing and/or polyadenylation of doublesex (dsx) pre-mRNA. Splicing requires an enhancer complex, dsxRE (dsx repeat element: which contains six copies of a 13-nucleotide repeat and a purine-rich enhancer (PRE)). DsxRE is formed through cooperative interactions between tra, tra2 and the sr proteins, and these interactions require both the repeat sequences and PRE. PRE is required for specific binding of tra2 to the dsxRE. Protein-RNA and protein-protein interactions are involved in tra-2 dependent activation and repression of alternative splicing. Together with tra-2, plays a role in switching fru splicing from the male-specific pattern to the female-specific pattern through activation of the female-specific fru 5'-splice site..
Protein Sequence MDREPLSSGRLHCSARYKHKRSASSSSAGTTSSGHKDRRSDYDYCGSRRHQRSSSRRRSRSRSSSESPPPEPRHRSGRSSRDRERMHKSREHPQASRCIGVFGLNTNTSQHKVRELFNKYGPIERIQMVIDAQTQRSRGFCFIYFEKLSDARAAKDSCSGIEVDGRRIRVDFSITQRAHTPTPGVYLGRQPRGKAPRSFSPRRGRRVYHDRSASPYDNYRDRYDYRNDRYDRNLRRSPSRNRYTRNRSYSRSRSPQLRRTSSRY
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
40PhosphorylationSGHKDRRSDYDYCGS
CCCCCCCCCCCCCCH
41.2219429919
180PhosphorylationSITQRAHTPTPGVYL
EEECCCCCCCCCEEE
28.0719429919
182PhosphorylationTQRAHTPTPGVYLGR
ECCCCCCCCCEEECC
33.5519429919
198PhosphorylationPRGKAPRSFSPRRGR
CCCCCCCCCCCCCCC
29.0825749252
200PhosphorylationGKAPRSFSPRRGRRV
CCCCCCCCCCCCCCE
20.8122668510
212PhosphorylationRRVYHDRSASPYDNY
CCEECCCCCCCCCCC
38.8719429919
214PhosphorylationVYHDRSASPYDNYRD
EECCCCCCCCCCCHH
25.8219429919
219PhosphorylationSASPYDNYRDRYDYR
CCCCCCCCHHHCCCC
15.8225749252
237PhosphorylationYDRNLRRSPSRNRYT
CCCCCCCCCCCCHHH
22.3125749252
239PhosphorylationRNLRRSPSRNRYTRN
CCCCCCCCCCHHHCC
43.3525749252
248PhosphorylationNRYTRNRSYSRSRSP
CHHHCCCCCCCCCCH
30.8922817900
254PhosphorylationRSYSRSRSPQLRRTS
CCCCCCCCHHHHHHC
20.468124712

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 TRA2_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRA2_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 TRA2_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DOA_DROMEDoaphysical
14605208
RBP1_DROMERbp1physical
14605208
SRR55_DROMEB52physical
14605208
Y2199_DROMECG2199physical
14605208
SRR55_DROMEB52genetic
7565780
TRA2_DROMEtra2physical
8124712
TRSF_DROMEtraphysical
8124712
DSX_DROMEdsxphysical
1518835
DSX_DROMEdsxphysical
1674449
DSX_DROMEdsxphysical
8124712

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRA2_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-40; THR-180; SER-212;SER-214 AND SER-254, AND MASS SPECTROMETRY.

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