TTKA_DROME - dbPTM
TTKA_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TTKA_DROME
UniProt AC P42282
Protein Name Protein tramtrack, alpha isoform
Gene Name ttk
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 813
Subcellular Localization Nucleus .
Protein Description Binds to a number of sites in the transcriptional regulatory region of ftz. Isoform alpha is required to repress genes that promote the R7 cell fate. Probable repressor of the transcription of the segmentation genes ftz, eve, h, odd, run, and en. May bind to the region 5'-AGGG[CT]GG-3'. Degradation of ttk is directed by binding of sinah or sina, via the adapter molecule phyl which binds to the BTB domain of ttk..
Protein Sequence MKMASQRFCLRWNNHQSNLLSVFDQLLHAETFTDVTLAVEGQHLKAHKMVLSACSPYFNTLFVSHPEKHPIVILKDVPYSDMKSLLDFMYRGEVSVDQERLTAFLRVAESLRIKGLTEVNDDKPSPAAAAAGAGATGSESTATTPQLQRIQPYLVPQRNRSQAGGLLASAANAGNTPTLPVQPSLLSSALMPKRKRGRPRKLSGSSNGTGNDYDDFDRENMMNDSSDLGNGKMCNESYSGNDDGSDDNQPNAGHTDDLNESRDSLPSKRSKNSKDHRVVSHHEDNSTSVTPTKATPELSQRLFGSSSTTISATAPGGSSTGPSETISLLEISDERESAPVHLPTILGLKIRAINTTTPAQQGSPQTPTKSKPKIRQATGSNNSNSLLKQQLRGGAKDPEVPPATRITGAVTPNAALNAEEQSKEMPKKNQDEVNACIGLHSLANAAEQQAAQVASTGNLHHQLLLHMAANNSMLNTTDYYQQQQQESPSSAGQFMDDDLELLSLNDQQDKSDEPDHEMVTLADENAGLPGYQGNEAEATPAQEDSPAAETATAPPPAPRSGKKGAKRPIQRRRVRRKAQSTLDDQAEHLTEMSVRGLDLFRYASVVEGVYRCTECAKENMQKTFKNKYSFQRHAFLYHEGKHRKVFPCPVCSKEFSRPDKMKNHLKMTHENFTPPKDIGAFSPLKYLISAAAAGDMHATIYQQQQDHYHRQLAEQLEQQNASFDSRDSSLILPDVKMEHAEDQDAEQEAELSDGGYDASNPAAAAAAMLSLQQDVIIKDEIQISPSPSPTPPASCAVAEGKSLALASTAQTAT
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
203PhosphorylationRGRPRKLSGSSNGTG
CCCCCCCCCCCCCCC
39.4022817900
205PhosphorylationRPRKLSGSSNGTGND
CCCCCCCCCCCCCCC
19.7722817900
206PhosphorylationPRKLSGSSNGTGNDY
CCCCCCCCCCCCCCC
42.6922817900
209PhosphorylationLSGSSNGTGNDYDDF
CCCCCCCCCCCCHHC
36.7429892262
682PhosphorylationPKDIGAFSPLKYLIS
CHHCCCCCHHHHHHH
28.8718327897
722PhosphorylationQLEQQNASFDSRDSS
HHHHHCCCCCCCCCC
36.8222817900

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
-KUbiquitinationE3 ubiquitin ligasesinaP21461
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TTKA_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 TTKA_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LOLAL_DROMElolalphysical
14605208
PP4C_DROMEPp4-19Cphysical
14605208
STAT_DROMEStat92Ephysical
14605208
DEI_DROMEtxphysical
14605208
ARRA_DROMEArr1physical
14605208
JMJD4_DROMECG7200physical
14605208
KU70_DROMEIrbpphysical
22036573
RFC1_DROMEGnf1physical
22036573
SINA_DROMEsinaphysical
12215542
PHYL_DROMEphylphysical
12215542
LOZEN_DROMElzgenetic
20003234
AFF4_DROMElilligenetic
11171404
UBPE_DROMEUbp64Egenetic
18160715
CHDM_DROMEMi-2genetic
11743021
CTBP_DROMECtBPgenetic
10978285
MPIP_DROMEstggenetic
12447387
GIANT_DROMEgtphysical
23935523
HANG_DROMEhangphysical
25242320
PHYL_DROMEphylphysical
9267026
OTP_DROMEotpphysical
25242320
DICH_DROMEDphysical
23935523
TTKB_DROMEttkphysical
23847101
TTKA_DROMEttkphysical
23847101
TTKB_DROMEttkphysical
12204250
TTKA_DROMEttkphysical
12204250
TTKB_DROMEttkphysical
12384587
TTKA_DROMEttkphysical
12384587

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TTKA_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-203; SER-205; SER-206;THR-209 AND SER-682, AND MASS SPECTROMETRY.

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