ATX2_DROME - dbPTM
ATX2_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATX2_DROME
UniProt AC Q8SWR8
Protein Name Ataxin-2 homolog
Gene Name Atx2 {ECO:0000312|FlyBase:FBgn0041188}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1084
Subcellular Localization Cytoplasm .
Protein Description Regulator of actin filament formation, though it does not directly assemble with actin filaments. Required for oocyte specification and oocyte positioning in the female germline. Also required for normal eye development and bristle morphology..
Protein Sequence MNNNSKRKTRPTGGGASGGISRYNSNDNSLRPTNNKAGAGGGNGGAAVRPSAQGVYNNTFFMHSATALVGSVVEVRLRSGNIYEGVFRTFSGNFDIALELPACIKSKNLPEEGKVPKHIIFPADTVVTIVAKDFDSQYATAGAFQTDGAISDKCNGARPDEKELEPWDSGANGDIDIELDSAANGWDPNEMFRKNENTFGVTSTFDDSLASYTVPLDKGDSLEFKEAEAKAEKLAAEIENNPTCRDRLDLENGDEEALFAAVERPSTEQDQRGDRGDRERNDRDREREERDRDRDRDRGNKPRGAGDFQLRETMSSDRYITKQTRSITGPQLSHVGMSSQGSGRDRDTRGDGSMMMQSGGGSGQGGSTQSTAALMLAGGLKGVGPAPSANASADSSSKYSGGSMVKRKTVPQGGKVMRNNVPTGGSNVSVSQGGNGNSVGQNKGGYQPSMGMPSQYSYQGNSQIMHGSSQYRNQSHMGGANKLNGDSNANTNKPLPQRQMRQYQGSQSNSSLNYGGEPQSLGKPVHGSHGGHPGQNSNSPPLQTAGPQQQQQQQQQQQQQQQQQQPPQQQQHQNIQPQGQNTQPARQVRTRDNQMQELRQFGQDFQLAPSNTSPPQQQQQQQQQQQQHQVQQQQQRALQQSASPPQQQQQQQQQQQHVVLHQVPQTHLHQAALSQPHYVPQQQPQQAPLPQQQHVPHHMQQKAQQQQLVETQHQHVQKQHQSQPQVQQPPPQLLQDPSQQPLPIYHTMPPPQTSPVVVTSPVLLEQPPPQPMPVVQQQQTQQLATPKPEVSPAPPSSNTTTPTGIASTPTAGVIASAGSEKTTPAAPTPTSNSATVPTGTAATAGGATGTTPVVKKHVLNPSAKPFTPRGPSTPNPSRPHTPQTPVPMTNIYTTTGGHVPPAANQPIYVMQPQHPFPPQTHPQAGQPPRLRRSNYPPMAASQMHVSASAATGQPLITAGPIPQFIQYGHAPHQQQFQSHTYAPMQMRVYPDQPQQLQFMTQTPQSTTPSPGQPHQQFHPPPQPSPAGGGPQPAFTPPTQAATYQLMCVHPQSLLANHYFPPPTPQHPQQNQQQYQIVMQQHQPQ
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
9PhosphorylationNNNSKRKTRPTGGGA
CCCCCCCCCCCCCCC		46.0122817900
12PhosphorylationSKRKTRPTGGGASGG
CCCCCCCCCCCCCCC		45.2121082442
17PhosphorylationRPTGGGASGGISRYN
CCCCCCCCCCCCCCC		40.6121082442
21PhosphorylationGGASGGISRYNSNDN
CCCCCCCCCCCCCCC		31.8021082442
23PhosphorylationASGGISRYNSNDNSL
CCCCCCCCCCCCCCC		19.0219060867
25PhosphorylationGGISRYNSNDNSLRP
CCCCCCCCCCCCCCC		36.3019429919
202PhosphorylationNENTFGVTSTFDDSL
CCCCCCCEEECCCCC		23.5622817900
203PhosphorylationENTFGVTSTFDDSLA
CCCCCCEEECCCCCE		25.3522817900
208PhosphorylationVTSTFDDSLASYTVP
CEEECCCCCEEEEEE		27.9022817900
211PhosphorylationTFDDSLASYTVPLDK
ECCCCCEEEEEECCC		26.9918327897
221PhosphorylationVPLDKGDSLEFKEAE
EECCCCCCCCHHHHH		38.1722817900
266PhosphorylationFAAVERPSTEQDQRG
EEEEECCCCHHHCCC		51.2817018572
267PhosphorylationAAVERPSTEQDQRGD
EEEECCCCHHHCCCC		40.1122817900
326PhosphorylationYITKQTRSITGPQLS
CEEEHHCCCCCCCCC		28.0822817900
328PhosphorylationTKQTRSITGPQLSHV
EEHHCCCCCCCCCCC		44.0222817900
333PhosphorylationSITGPQLSHVGMSSQ
CCCCCCCCCCCCCCC		15.7521082442
339PhosphorylationLSHVGMSSQGSGRDR
CCCCCCCCCCCCCCC		29.6621082442
348PhosphorylationGSGRDRDTRGDGSMM
CCCCCCCCCCCCCEE		37.1321082442
403PhosphorylationSSKYSGGSMVKRKTV
CCCCCCCCCCCCEEC		24.7522817900
409PhosphorylationGSMVKRKTVPQGGKV
CCCCCCEECCCCCEE		41.2622817900
475PhosphorylationSSQYRNQSHMGGANK
CHHCCCCCCCCCCCC		20.9922817900
850PhosphorylationTAGGATGTTPVVKKH
CCCCCCCCCHHHEEE		24.4621082442
851PhosphorylationAGGATGTTPVVKKHV
CCCCCCCCHHHEEEC		18.5421082442
864AcetylationHVLNPSAKPFTPRGP
ECCCCCCCCCCCCCC		45.0321791702
867PhosphorylationNPSAKPFTPRGPSTP
CCCCCCCCCCCCCCC		22.1722817900
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 ATX2_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATX2_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 ATX2_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PER_DROMEpergenetic
23687048
PABP_DROMEpAbpgenetic
18271626
SGG_DROMEsggphysical
23687048
PER_DROMEperphysical
23687047
PER_DROMEperphysical
23687048
TIM_DROMEtimphysical
23687047
TIM_DROMEtimphysical
23687048
G3P1_DROMEGapdh1physical
23687048
PABP_DROMEpAbpphysical
23687047
FMR1_DROMEFmr1physical
24344294
CLOCK_DROMEClkphysical
23687047
CYCL_DROMEcycphysical
23687047
CRY1_DROMEcryphysical
23687048
KCC2A_DROMECaMKIIphysical
24344294
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATX2_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-208; SER-211 ANDSER-221, 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-266, AND MASSSPECTROMETRY.

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