PAN3_DROME - dbPTM
PAN3_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAN3_DROME
UniProt AC Q95RR8
Protein Name PAN2-PAN3 deadenylation complex subunit PAN3 {ECO:0000255|HAMAP-Rule:MF_03181}
Gene Name PAN3 {ECO:0000255|HAMAP-Rule:MF_03181}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 790
Subcellular Localization Cytoplasm, P-body .
Protein Description Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and PABP, and to miRNA targets via its interaction with GW182 family proteins..
Protein Sequence MCSTYGLLSFEFSDTAAMDPIFFSPTNGIPSESKLATYMNRQNVATPSGYGLNNGFSLLNLDSPLNKKSQVTPQSPEFIPTRLGSTPNFYAPYHNAPMQLSNGLNGVNGLTAAAAAAAAAAAAAAAAVPSSTSSASSASVTISKTANGGASMLALQKTASIASVTIAQQQPQHPQKQQQHPPSVGGGAVSAASAPIAISGAPPNPAAAPFVSSMSAQTPLKGRGAMMRQESPTAAMISGAGPGEKSPPHGMTPHGASPIPSALPTSVHQENVGGTIYFYPTANAQNSQPVVNSMVVDGTHPALHGVSAVAPMSAGVPAAMMYTGHVYPGPSSNVVTMQPKTLLESAFFMPDEMRAEVLARNEISNLIMDAAEAAQHALPLEVENYHALYPLEPPAQPLHAKLTFPATTYRATHNTTGYKYCLRRIHGFRLQSTKCMTLVEMWKKLQHTNVVQLREVFTTKAFGDNSLVLVYDYHPGSQTLLAKYFTPAPETNGYTDPFQGEARPFSHKSNMQRTSNGPLLPEATIWSIIMQLTAGLKAIHHAGLACKVLDPTKIIVTGKRVRFSSCCISDITQFDPNASNPLALVNMHQQDDLTALGRLVLALACRCLQSVQRDNVQSSIDMVTRNYSTDLRNFIVYLFTTNNRRSVTDLMPMIGARFYTQLDALQSKIDMQEDELAKEMENGRLYRILVKLNSINERPDFNLDCTWSETGDRYMLKLFRDYLFHSVTEDGRPWLDHAHIVQCLNKLDAGSIERVQLMSRDEQSVLIVSYAELKNCLENAFSELMSSAAN
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
72PhosphorylationLNKKSQVTPQSPEFI
CCCCCCCCCCCCCCC
22817900
75PhosphorylationKSQVTPQSPEFIPTR
CCCCCCCCCCCCCCC
28490779
81PhosphorylationQSPEFIPTRLGSTPN
CCCCCCCCCCCCCCC
22817900
160PhosphorylationLALQKTASIASVTIA
EEEHHHHHHHEEEEH
21082442

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 PAN3_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAN3_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 PAN3_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTH2_DROMECG1307physical
14605208
MOCS3_DROMECG13090physical
14605208
DOME_DROMEdomephysical
14605208
CH36_DROMECp36physical
14605208
ER_DROMEe(r)physical
14605208
Y678_DROMECG2678physical
14605208
SIR4_DROMESirt4physical
14605208
CCNB_DROMECycBphysical
14605208
DLL_DROMEDllphysical
14605208
FD3_DROMEfd59Aphysical
14605208
BAP60_DROMEBap60physical
14605208
MS57B_DROMEMst57Dbphysical
14605208
BUN1_DROMEbunphysical
14605208
BUN2_DROMEbunphysical
14605208
GBLP_DROMERack1physical
14605208
SLCA_DROMESclAphysical
14605208

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PAN3_DROME

loading...

Related Literatures of Post-Translational Modification

TOP