GROU_DROME - dbPTM
GROU_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GROU_DROME
UniProt AC P16371
Protein Name Protein groucho
Gene Name gro
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 730
Subcellular Localization Nucleus.
Protein Description Transcriptional corepressor that regulates transcription when recruited to specific target DNA by hairy-related bHLH proteins. Maternally required for neurogenesis; in the segregation of the neuroectoderm. Directly or indirectly interacts with Notch and Delta..
Protein Sequence MYPSPVRHPAAGGPPPQGPIKFTIADTLERIKEEFNFLQAQYHSIKLECEKLSNEKTEMQRHYVMYYEMSYGLNVEMHKQTEIAKRLNTLINQLLPFLQADHQQQVLQAVERAKQVTMQELNLIIGHQQQHGIQQLLQQIHAQQVPGGPPQPMGALNPFGALGATMGLPHGPQGLLNKPPEHHRPDIKPTGLEGPAAAEERLRNSVSPADREKYRTRSPLDIENDSKRRKDEKLQEDEGEKSDQDLVVDVANEMESHSPRPNGEHVSMEVRDRESLNGERLEKPSSSGIKQERPPSRSGSSSSRSTPSLKTKDMEKPGTPGAKARTPTPNAAAPAPGVNPKQMMPQGPPPAGYPGAPYQRPADPYQRPPSDPAYGRPPPMPYDPHAHVRTNGIPHPSALTGGKPAYSFHMNGEGSLQPVPFPPDALVGVGIPRHARQINTLSHGEVVCAVTISNPTKYVYTGGKGCVKVWDISQPGNKNPVSQLDCLQRDNYIRSVKLLPDGRTLIVGGEASNLSIWDLASPTPRIKAELTSAAPACYALAISPDSKVCFSCCSDGNIAVWDLHNEILVRQFQGHTDGASCIDISPDGSRLWTGGLDNTVRSWDLREGRQLQQHDFSSQIFSLGYCPTGDWLAVGMENSHVEVLHASKPDKYQLHLHESCVLSLRFAACGKWFVSTGKDNLLNAWRTPYGASIFQSKETSSVLSCDISTDDKYIVTGSGDKKATVYEVIY
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
167 (in isoform 2)Sumoylation-31.53-
177 (in isoform 2)Sumoylation-60.89-
205PhosphorylationAEERLRNSVSPADRE
HHHHHHHCCCHHHHH		19.9619429919
207PhosphorylationERLRNSVSPADREKY
HHHHHCCCHHHHHHH		17.7521082442
216PhosphorylationADREKYRTRSPLDIE
HHHHHHHCCCCCCCC		32.2019429919
218PhosphorylationREKYRTRSPLDIEND
HHHHHCCCCCCCCCC		29.2421082442
226PhosphorylationPLDIENDSKRRKDEK
CCCCCCCHHHHHHHH		39.3822817900
233AcetylationSKRRKDEKLQEDEGE
HHHHHHHHHCCCCCC		66.6521791702
242PhosphorylationQEDEGEKSDQDLVVD
CCCCCCCCHHHEHHH		35.8819429919
256PhosphorylationDVANEMESHSPRPNG
HHHHHHHHCCCCCCC		28.1419429919
258PhosphorylationANEMESHSPRPNGEH
HHHHHHCCCCCCCCC		31.7019429919
267PhosphorylationRPNGEHVSMEVRDRE
CCCCCCCEEEEECHH		15.9019429919
272 (in isoform 2)Sumoylation-64.97-
275PhosphorylationMEVRDRESLNGERLE
EEEECHHHHCCCCCC		28.2019429919
279 (in isoform 2)Sumoylation-53.68-
296PhosphorylationIKQERPPSRSGSSSS
CCCCCCCCCCCCCCC		41.5828490779
300PhosphorylationRPPSRSGSSSSRSTP
CCCCCCCCCCCCCCC		28.4425749252
319PhosphorylationKDMEKPGTPGAKART
CCCCCCCCCCCCCCC		27.3825749252
326PhosphorylationTPGAKARTPTPNAAA
CCCCCCCCCCCCCCC		36.0521082442
328PhosphorylationGAKARTPTPNAAAPA
CCCCCCCCCCCCCCC		28.6721082442
543PhosphorylationACYALAISPDSKVCF
HHHHEEECCCCCEEE		19.6322817900
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
242SPhosphorylationKinaseCK2-Uniprot
258SPhosphorylationKinaseCDC2P23572
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GROU_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 GROU_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPN_DROMEdpnphysical
14605208
PANG1_DROMEpanphysical
17113388
PANG2_DROMEpanphysical
17113388
MYC_DROMEdmphysical
17898168
PANG1_DROMEpanphysical
19460168
PANG2_DROMEpanphysical
19460168
NOTCH_DROMENgenetic
11719214
WNTG_DROMEwggenetic
11128568
EGFR_DROMEEgfrgenetic
9383058
KNIR_DROMEknigenetic
19805071
ESMB_DROMEE(spl)mbeta-HLHgenetic
15592470
ERKA_DROMErlgenetic
9383058
RUNT_DROMErunphysical
9371806
DORS_DROMEdlphysical
9367978
HMEN_DROMEenphysical
25242320
HDAC1_DROMERpd3physical
10485845
HDAC1_DROMERpd3physical
15802274
HAIR_DROMEhphysical
21343912
HAIR_DROMEhphysical
9524128
HAIR_DROMEhphysical
9892668
CTBP_DROMECtBPphysical
16287856
RU1C_DROMEsnRNP-U1-Cphysical
26483546
HLES_DROMEHphysical
16287856
ESMD_DROMEE(spl)mdelta-HLHphysical
9371806
ESMC_DROMEE(spl)mgamma-HLHphysical
9371806
ESMB_DROMEE(spl)mbeta-HLHphysical
9371806
ESM3_DROMEE(spl)m3-HLHphysical
9371806
ESM5_DROMEE(spl)m5-HLHphysical
9371806
ESM8_DROMEE(spl)m8-HLHphysical
9371806
GROU_DROMEgrophysical
18034187
GROU_DROMEgrophysical
19036929
PANG1_DROMEpanphysical
19036929
PANG2_DROMEpanphysical
19036929
PANG1_DROMEpanphysical
9751710
PANG2_DROMEpanphysical
9751710
PAX6_DROMEeyphysical
15802274
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GROU_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-205; SER-207; SER-218;SER-242; SER-258; SER-267; THR-326 AND THR-328, AND MASS SPECTROMETRY.

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