POLO_DROME - dbPTM
POLO_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID POLO_DROME
UniProt AC P52304
Protein Name Serine/threonine-protein kinase polo
Gene Name polo
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 576
Subcellular Localization Cytoplasm .
Protein Description May play a role in regulating both nuclear and cytoplasmic aspects of the mitotic cycle. [PubMed: 1660828 Regulates localization of the augmin complex during mitosis by ensuring its location on mitotic spindles]
Protein Sequence MAAKPEDKSTDIPDRLVDINQRKTYKRMRFFGKGGFAKCYEIIDVETDDVFAGKIVSKKLMIKHNQKEKTAQEITIHRSLNHPNIVKFHNYFEDSQNIYIVLELCKKRSMMELHKRRKSITEFECRYYIYQIIQGVKYLHDNRIIHRDLKLGNLFLNDLLHVKIGDFGLATRIEYEGERKKTLCGTPNYIAPEILTKKGHSFEVDIWSIGCVMYTLLVGQPPFETKTLKDTYSKIKKCEYRVPSYLRKPAADMVIAMLQPNPESRPAIGQLLNFEFLKGSKVPMFLPSSCLTMAPRIGSNDTIEDSMHRKPLMEMNGIRPDDTRLESTFLKANLHDAITASAQVCRHSEDYRSDIESLYQQLTNLINGKPRILQGNLGDENTDPAAQPLFWISKWVDYSDKYGFGYQLCDEGIGVMFNDTTKLILLPNQINVHFIDKDGKETYMTTTDYCKSLDKKMKLLSYFKRYMIEHLVKAGANNVNIESDQISRMPHLHSWFRTTCAVVMHLTNGSVQLNFSDHMKLILCPRMSAITYMDQEKNFRTYRFSTIVENGVSKDLYQKIRYAQEKLRKMLEKMFT
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
33AcetylationKRMRFFGKGGFAKCY
HHHHHCCCCCCCCEE		51.1821791702
182PhosphorylationYEGERKKTLCGTPNY
EECCCCCCCCCCCCC		30.2522817900
186PhosphorylationRKKTLCGTPNYIAPE
CCCCCCCCCCCCCHH		13.8322817900
299PhosphorylationTMAPRIGSNDTIEDS
CCCCCCCCCCCHHHH		29.2119429919
302PhosphorylationPRIGSNDTIEDSMHR
CCCCCCCCHHHHHCC		30.4322817900
306PhosphorylationSNDTIEDSMHRKPLM
CCCCHHHHHCCCCCH		12.0522817900
323PhosphorylationNGIRPDDTRLESTFL
CCCCCCCCHHHHHCH		44.5322817900
327PhosphorylationPDDTRLESTFLKANL
CCCCHHHHHCHHHHH		29.1122817900
328PhosphorylationDDTRLESTFLKANLH
CCCHHHHHCHHHHHH		24.5022817900
566AcetylationKIRYAQEKLRKMLEK
HHHHHHHHHHHHHHH		41.3221791702
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 POLO_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of POLO_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 POLO_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
JRA_DROMEJraphysical
14605208
Y5057_DROMECG45057physical
14605208
PSA2_DROMEProsalpha2physical
14605208
MBL_DROMEmblphysical
14605208
DFD_DROMEDfdphysical
15575970
MTRM_DROMEmtrmphysical
15710747
MARS_DROMEmarsphysical
15710747
PDM2A_DROMEpdm2physical
15710747
PDM2B_DROMEpdm2physical
15710747
TAP_DROMEtapphysical
15710747
DDB1_DROMEpicphysical
15710747
SPEN_DROMEspenphysical
15710747
OMB_DROMEbiphysical
15710747
Y3380_DROMECG13380physical
15710747
DCA10_DROMECG1523physical
15710747
RS8_DROMERpS8physical
15710747
DALMA_DROMEdmtphysical
15710747
MYOD_DROMEnauphysical
15710747
NOTCH_DROMENphysical
22036573
NUMB_DROMEnumbgenetic
17805297
NUMB_DROMEnumbgenetic
21558368
SIR2_DROMESir2genetic
23136393
MAEL_DROMEmaelgenetic
23136393
MA205_DROMEMap205genetic
18832073
PP2A_DROMEmtsgenetic
21852958
2ABA_DROMEtwsgenetic
21852958
KI10A_DROMEKlp10Aphysical
27799364
CNN_DROMEcnnphysical
26447129
CNN_DROMEcnnphysical
27096551
MTRM_DROMEmtrmphysical
23479640
POLO_DROMEpolophysical
23857770
CLASP_DROMEchbphysical
27799364
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of POLO_DROME

loading...

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 THR-182; THR-186; SER-299;THR-302; SER-306; THR-323; SER-327 AND THR-328, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory