RB27C_DROME - dbPTM
RB27C_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RB27C_DROME
UniProt AC P48809
Protein Name Heterogeneous nuclear ribonucleoprotein 27C
Gene Name Hrb27C
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 421
Subcellular Localization Nucleus. Cytoplasm. Nuclear and/or cytoplasmic.
Protein Description This protein is a component of ribonucleosomes. Could be needed to organize a concentration gradient of a dorsalizing morphogen (Dm) originating in the germinal vesicle..
Protein Sequence MEEDERGKLFVGGLSWETTQENLSRYFCRFGDIIDCVVMKNNESGRSRGFGFVTFADPTNVNHVLQNGPHTLDGRTIDPKPCNPRTLQKPKKGGGYKVFLGGLPSNVTETDLRTFFNRYGKVTEVVIMYDQEKKKSRGFGFLSFEEESSVEHVTNERYINLNGKQVEIKKAEPRDGSGGQNSNNSTVGGAYGKLGNECSHWGPHHAPINMMQGQNGQMGGPPLNMPIGAPNMMPGYQGWGTSPQQQQYGYGNSGPGSYQGWGAPPGPQGPPPQWSNYAGPQQTQGYGGYDMYNSTSTGAPSGPSGGGSWNSWNMPPNSAGPTGAPGAGAGTATDMYSRAQAWATGGPSTTGPVGGMPRTGPGNSASKSGSEYDYGGYGSGYDYDYSNYVKQEGASNYGAGPRSAYGNDSSTQPPYATSQAV
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
177PhosphorylationKAEPRDGSGGQNSNN
ECCCCCCCCCCCCCC
44.0022817900
182PhosphorylationDGSGGQNSNNSTVGG
CCCCCCCCCCCCCCC
29.5119429919
185PhosphorylationGGQNSNNSTVGGAYG
CCCCCCCCCCCCCHH
28.8119429919
186PhosphorylationGQNSNNSTVGGAYGK
CCCCCCCCCCCCHHC
25.8719429919
191PhosphorylationNSTVGGAYGKLGNEC
CCCCCCCHHCCCCCC
20.3318281928
348PhosphorylationAWATGGPSTTGPVGG
HHHCCCCCCCCCCCC
41.7121082442
359PhosphorylationPVGGMPRTGPGNSAS
CCCCCCCCCCCCCCC
41.6921082442
364PhosphorylationPRTGPGNSASKSGSE
CCCCCCCCCCCCCCC
39.5719429919
366PhosphorylationTGPGNSASKSGSEYD
CCCCCCCCCCCCCCC
27.4619429919
368PhosphorylationPGNSASKSGSEYDYG
CCCCCCCCCCCCCCC
45.0919429919
370PhosphorylationNSASKSGSEYDYGGY
CCCCCCCCCCCCCCC
39.8219429919
372PhosphorylationASKSGSEYDYGGYGS
CCCCCCCCCCCCCCC
19.0322817900
374PhosphorylationKSGSEYDYGGYGSGY
CCCCCCCCCCCCCCC
16.1420450229
377PhosphorylationSEYDYGGYGSGYDYD
CCCCCCCCCCCCCCC
12.0720450229
379PhosphorylationYDYGGYGSGYDYDYS
CCCCCCCCCCCCCHH
26.2019429919
397PhosphorylationKQEGASNYGAGPRSA
CCCCCCCCCCCCCCC
13.0725749252
403PhosphorylationNYGAGPRSAYGNDSS
CCCCCCCCCCCCCCC
29.0419429919
405PhosphorylationGAGPRSAYGNDSSTQ
CCCCCCCCCCCCCCC
20.0819429919
415PhosphorylationDSSTQPPYATSQAV-
CCCCCCCCCCCCCC-
29.2418281928

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 RB27C_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RB27C_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 RB27C_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RB97D_DROMERb97Dphysical
14605208
Y2199_DROMECG2199physical
14605208
K10_DROMEfs(1)K10physical
14605208
CTBP_DROMECtBPphysical
14605208
PROML_DROMEprominin-likephysical
14605208
FER_DROMEFERphysical
14605208
OTU_DROMEotugenetic
15056611
CUP_DROMEcupphysical
18082158
GRK_DROMEgrkphysical
15056611
PABP_DROMEpAbpphysical
18082158
OSKA_DROMEoskphysical
15056611
ROA1_DROMEHrb98DEphysical
26545814
RB87F_DROMEHrb87Fphysical
26545814

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RB27C_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-177; SER-366; SER-368;SER-370; TYR-372 AND SER-379, AND MASS SPECTROMETRY.

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