ADRM1_DROME - dbPTM
ADRM1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADRM1_DROME
UniProt AC Q7K2G1
Protein Name Proteasomal ubiquitin receptor ADRM1 homolog
Gene Name Rpn13
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 389
Subcellular Localization Cytoplasm. Nucleus.
Protein Description May function as a proteasomal ubiquitin receptor. May promote the deubiquitinating activity associated with the 26S proteasome (By similarity)..
Protein Sequence MFGRQSGLGSSSNSSNLVEFRAGRMNMVGKMVHPDPRKGLVYMTQSDDGLMHFCWKDRTSGKVEDDLIVFPDDFEYKRVDQCKTGRVYVLKFKSSTRRMFFWMQEPKTDKDDEQCRRINELLNNPPSAHQRGGGGSNDGDLQYMLNNMSQQQLMQLFGGVGQMGGLSSLLGQMNSRTPSSRNTSSSGGGGASALQTPENVSVPRTPSAPSKSGSSRSSSNVNSQVGEGAGSSVDADAPGRSLNIDLSTALPGADAINQIIADPEHVKTLIVHLPESEDVDDDRKQQIKDNITSPQFQQALAQFSSALQSAQLGPVIKQFELSNEAVAAAFSGNLEDFVRALEKSLPPGATMGGKPSASEKKASDPETPTSVARDENTDPATEKQEEKQK
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
6Phosphorylation--MFGRQSGLGSSSN
--CCCCCCCCCCCCC
34.3319429919
183PhosphorylationRTPSSRNTSSSGGGG
CCCCCCCCCCCCCCC
28.9519429919
184PhosphorylationTPSSRNTSSSGGGGA
CCCCCCCCCCCCCCC
26.5119429919
185PhosphorylationPSSRNTSSSGGGGAS
CCCCCCCCCCCCCCC
30.8519429919
186PhosphorylationSSRNTSSSGGGGASA
CCCCCCCCCCCCCCC
41.0219429919
192PhosphorylationSSGGGGASALQTPEN
CCCCCCCCCCCCCCC
32.5519429919
196PhosphorylationGGASALQTPENVSVP
CCCCCCCCCCCCCCC
33.1619429919
201PhosphorylationLQTPENVSVPRTPSA
CCCCCCCCCCCCCCC
37.6828490779
205PhosphorylationENVSVPRTPSAPSKS
CCCCCCCCCCCCCCC
18.6128490779
207PhosphorylationVSVPRTPSAPSKSGS
CCCCCCCCCCCCCCC
52.8028490779
211AcetylationRTPSAPSKSGSSRSS
CCCCCCCCCCCCCCC
58.75-
211AcetylationRTPSAPSKSGSSRSS
CCCCCCCCCCCCCCC
58.7521791702
217PhosphorylationSKSGSSRSSSNVNSQ
CCCCCCCCCCCCCCC
39.8119060867
218PhosphorylationKSGSSRSSSNVNSQV
CCCCCCCCCCCCCCC
25.4819060867
219PhosphorylationSGSSRSSSNVNSQVG
CCCCCCCCCCCCCCC
46.1517372656
223PhosphorylationRSSSNVNSQVGEGAG
CCCCCCCCCCCCCCC
23.2029892262
252 (in isoform 2)Phosphorylation-36.6221082442
263 (in isoform 2)Phosphorylation-25.2723607784
265 (in isoform 2)Phosphorylation-31.5919429919
268 (in isoform 2)Phosphorylation-22.1919429919
363PhosphorylationSASEKKASDPETPTS
CHHHCCCCCCCCCCC
63.6822817900
367PhosphorylationKKASDPETPTSVARD
CCCCCCCCCCCHHCC
36.9419429919
369PhosphorylationASDPETPTSVARDEN
CCCCCCCCCHHCCCC
43.1619429919
370PhosphorylationSDPETPTSVARDENT
CCCCCCCCHHCCCCC
18.2522817900

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 ADRM1_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADRM1_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 ADRM1_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACT1_DROMEAct5Cphysical
14605208
BNB_DROMEbnbphysical
14605208
PSA1_DROMEProsalpha6physical
22036573
PSA4_DROMEProsalpha3physical
22036573
PSB4_DROMEProsbeta7physical
22036573
PSA2_DROMEProsalpha2physical
22036573
PSMD3_DROMERpn3physical
22036573
RS27A_DROMERpS27Aphysical
24292889

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ADRM1_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-6; THR-196; THR-205;SER-207; SER-217; SER-219 AND THR-367, 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-6; SER-185; SER-217;SER-218 AND SER-219, AND MASS SPECTROMETRY.

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