FMR1_DROME - dbPTM
FMR1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FMR1_DROME
UniProt AC Q9NFU0
Protein Name Synaptic functional regulator FMR1 {ECO:0000305}
Gene Name Fmr1 {ECO:0000312|EMBL:AAF14639.1}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 684
Subcellular Localization Cytoplasm . Perikaryon . Cell projection . Cell junction, synapse . Cytoplasm, Stress granule . Cytoplasm, Cytoplasmic ribonucleoprotein granule . Localizes in the neuronal soma and cell processes, and in pre- and postsynaptic neurons, as well as in
Protein Description Polyribosome-associated RNA-binding protein that plays a role in neuronal development and synaptic plasticity through the regulation of protein synthesis of mRNAs. [PubMed: 11046149]
Protein Sequence MEDLLVEVRLDNGAYYKGQVTAVADDGIFVDVDGVPESMKYPFVNVRLPPEETVEVAAPIFEEGMEVEVFTRTNDRETCGWWVGIIKMRKAEIYAVAYIGFETSYTEICELGRLRAKNSNPPITAKTFYQFTLPVPEELREEAQKDGIHKEFQRTIDAGVCNYSRDLDALIVISKFEHTQKRASMLKDMHFRNLSQKVMLLKRTEEAARQLETTKLMSRGNYVEEFRVRDDLMGLAIGSHGSNIQAARTVDGVTNIELEEKSCTFKISGETEESVQRARAMLEYAEEFFQVPRELVGKVIGKNGRIIQEIVDKSGVFRIKVSAIAGDDEQDQNIPRELAHVPFVFIGTVESIANAKVLLEYHLSHLKEVEQLRQEKMEIDQQLRAIQESSMGSTQSFPVTRRSERGYSSDIESVRSMRGGGGGQRGRVRGRGGGGPGGGNGLNQRYHNNRRDEDDYNSRGDHQRDQQRGYNDRGGGDNTGSYRGGGGGAGGPGNNRRGGINRRPPRNDQQNGRDYQHHNHTTEEVRETREMSSVERADSNSSYEGSSRRRRRQKNNNGPSNTNGAVANNNNKPQSAQQPQQQQPPAPGNKAALNAGDASKQNSGNANAAGGASKPKDASRNGDKQQAGTQQQQPSQVQQQQAAQQQQPKPRRNKNRSNNHTDQPSGQQQLAENVKKEGLVNGTS
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
393PhosphorylationIQESSMGSTQSFPVT
HHHHCCCCCCCCCCC		18.0325749252
394PhosphorylationQESSMGSTQSFPVTR
HHHCCCCCCCCCCCC		23.6221082442
396PhosphorylationSSMGSTQSFPVTRRS
HCCCCCCCCCCCCCC		31.4422817900
403PhosphorylationSFPVTRRSERGYSSD
CCCCCCCCCCCCCCC		28.4922817900
407PhosphorylationTRRSERGYSSDIESV
CCCCCCCCCCCHHHH		15.9529892262
408PhosphorylationRRSERGYSSDIESVR
CCCCCCCCCCHHHHH		25.1021082442
409PhosphorylationRSERGYSSDIESVRS
CCCCCCCCCHHHHHC		33.8421082442
413PhosphorylationGYSSDIESVRSMRGG
CCCCCHHHHHCCCCC		24.1419429919
458PhosphorylationRDEDDYNSRGDHQRD
CCCCCCCCCCCHHHH		31.2622817900
521PhosphorylationDYQHHNHTTEEVRET
CCCCCCCCHHHHHHH		41.0222817900
532PhosphorylationVRETREMSSVERADS
HHHHHHHHCCCCCCC		26.8619429919
533PhosphorylationRETREMSSVERADSN
HHHHHHHCCCCCCCC		27.0419429919
539PhosphorylationSSVERADSNSSYEGS
HCCCCCCCCCCCCCH		37.3119429919
541PhosphorylationVERADSNSSYEGSSR
CCCCCCCCCCCCHHH		37.9419429919
542PhosphorylationERADSNSSYEGSSRR
CCCCCCCCCCCHHHH		31.3019429919
543PhosphorylationRADSNSSYEGSSRRR
CCCCCCCCCCHHHHH		24.9119429919
546PhosphorylationSNSSYEGSSRRRRRQ
CCCCCCCHHHHHHHH		14.5619429919
547PhosphorylationNSSYEGSSRRRRRQK
CCCCCCHHHHHHHHC		40.4319429919
657PhosphorylationPRRNKNRSNNHTDQP
CCCCCCCCCCCCCCC		51.9119429919
661PhosphorylationKNRSNNHTDQPSGQQ
CCCCCCCCCCCHHHH		38.1519429919
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
409SPhosphorylationKinaseCK2-FAMILY-GPS
409SPhosphorylationKinaseCKII_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FMR1_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 FMR1_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AGO2_DROMEAGO2physical
15231716
AGO2_DROMEAGO2physical
12368260
AGO2_DROMEAGO2physical
12368261
DCR1_DROMEDcr-1physical
12368261
DDX17_DROMERm62physical
12368261
RL11_DROMERpL11physical
12368261
RL5_DROMERpL5physical
12368261
FUTSC_DROMEfutschgenetic
11733059
FUTSC_DROMEfutschgenetic
12086644
FUTSC_DROMEfutschphysical
11733059
ADAR_DROMEAdargenetic
22037499
PDE4B_DROMEdncgenetic
22993428
PDE4E_DROMEdncgenetic
22993428
PDE4C_DROMEdncgenetic
22993428
PDE4A_DROMEdncgenetic
22993428
PDE4B_DROMEdncgenetic
25568131
PDE4E_DROMEdncgenetic
25568131
PDE4C_DROMEdncgenetic
25568131
PDE4A_DROMEdncgenetic
25568131
TOP3B_DROMETop3betagenetic
23912945
L2GL_DROMEl(2)glgenetic
15621528
PROF_DROMEchicgenetic
15964283
CEG1A_DROMECenG1Agenetic
25921541
RBP9X_DROMERanBPMgenetic
20498842
SMD3_DROMESmD3genetic
19487564
OAZ_DROMEOdagenetic
19487564
STAU_DROMEstaugenetic
18776892
PABP_DROMEpAbpgenetic
19487564
RAC1_DROMERac1genetic
12818175
RAC1_DROMERac1genetic
15964283
RAC1_DROMERac1genetic
14530299
RAC1_DROMERac1genetic
27335463
ORB2_DROMEorb2genetic
19487564
DIAP1_DROMEthgenetic
11046149
HEM_DROMEHemgenetic
15385157
DDX17_DROMERm62genetic
19487564
TIMP_DROMETimpgenetic
21669931
CYFIP_DROMESra-1genetic
12818175
CYFIP_DROMESra-1genetic
15385157
DCO_DROMEdcogenetic
19487564
GRM_DROMEmGluRgenetic
18280750
GRM_DROMEmGluRgenetic
19036865
GRM_DROMEmGluRgenetic
22993428
ABL_DROMEAblgenetic
25988807
APKC_DROMEaPKCgenetic
15621528
ADAR_DROMEAdarphysical
22037499
TORS_DROMETorsinphysical
27313903
TOP3B_DROMETop3betaphysical
23912945
PIWI_DROMEpiwiphysical
26842990
AUB_DROMEaubphysical
25908854
LIG_DROMEligphysical
26117838
FMR1_DROMEFmr1physical
11733059
FMR1_DROMEFmr1physical
23666178
FMR1_DROMEFmr1physical
12460546
CYFIP_DROMESra-1physical
12818175
CYFIP_DROMESra-1physical
25908854
KCC2A_DROMECaMKIIphysical
24344294
FUTSC_DROMEfutschphysical
23666178
CAPR1_DROMECaprphysical
21068064
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FMR1_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-403; SER-408; SER-409;SER-413; SER-532; SER-533; SER-539 AND SER-541, AND MASS SPECTROMETRY.

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