PUF68_DROME - dbPTM
PUF68_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PUF68_DROME
UniProt AC Q8T6B9
Protein Name Poly(U)-binding-splicing factor half pint {ECO:0000303|PubMed:11879639}
Gene Name hfp {ECO:0000303|PubMed:11879639, ECO:0000312|FlyBase:FBgn0028577}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 637
Subcellular Localization Nucleus .
Protein Description Splicing factor that regulates oogenesis and controls both mitosis and mRNA localization in the germline by regulating mRNA splicing of a subset of genes within the ovary. Probably acts by regulating the alternative splice site selection of the otu transcript. Also regulates the alternative splicing of eIF4E1 and grk, while it is not involved in the splicing of par-1, sqd and psq..
Protein Sequence MGSNDRASRSPRSDDQREISDMPATKRTRSDSGKSTDSKIPYLSQPLYDLKQTGDVKFGPGTRSALLGLLGGALPKLSSEQHDLVSKAKKYAMEQSIKMVLMKQTLAHQQQQLATQRTQVQRQQALALMCRVYVGSISFELKEDTIRVAFTPFGPIKSINMSWDPITQKHKGFAFVEYEIPEGAQLALEQMNGALMGGRNIKVGRPSNMPQAQQVIDEVQEEAKSFNRIYVASIHPDLSEEDIKSVFEAFGPILYCKLAQGTSLHTHKGYGFIEYANKQAMDEAIASMNLFDLGGQLLRVGRSITPPNALACPTTNSTMPTAAAVAAAAATAKIQALDAVASNAVLGLSQNTPVMAAGAVVTKVGAMPVVSAATSAAALHPALAQAAPALLPPGIFQAPTPVAPSLLGVPAGLQPLQAVVPTLPPPALLATPTLPMTVGGVGVGLVPTVATLAGAEASKGAAAAAALSAAANNAAVTAANLSENIKKAHEKQQEELQKKLMDEGDVQTLQQQENMSIKGQSARQLVMQRLMRPVDSRVIILRNMVGPEDVDETLQEEIQEECSKFGTVSRVIIFNEKQTENEDDDEAEIIVKIFVEFSAGAEAMRGKEALDGRFFGGRRVVAELYDQGIFDQGDLSG
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
3Phosphorylation-----MGSNDRASRS
-----CCCCCCCCCC
33.9730478224
10PhosphorylationSNDRASRSPRSDDQR
CCCCCCCCCCCCCHH
23.3625749252
13PhosphorylationRASRSPRSDDQREIS
CCCCCCCCCCHHHHC
49.2622817900
30PhosphorylationPATKRTRSDSGKSTD
CCCCCCCCCCCCCCC
35.2012537569
32PhosphorylationTKRTRSDSGKSTDSK
CCCCCCCCCCCCCCC
49.7421082442
35PhosphorylationTRSDSGKSTDSKIPY
CCCCCCCCCCCCCCC
40.7621082442

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 PUF68_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PUF68_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 PUF68_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AIMP2_DROMECG12304physical
14605208
SINAL_DROMEsinahphysical
14605208
RM39_DROMEmRpL39physical
14605208
TRXR1_DROMETrxr-1physical
14605208
CCNB_DROMECycBphysical
14605208
ACT1_DROMEAct5Cphysical
14605208
DDX6_DROMEme31Bphysical
14605208
TF2AA_DROMETfIIA-Lphysical
14605208
CLH_DROMEChcphysical
14605208
MYC_DROMEdmgenetic
26074141
OTU_DROMEotugenetic
11879639
ERCC3_DROMEhaygenetic
26074141
ERCC3_DROMEhaygenetic
20667914
TRA2_DROMEtra2physical
23880637
ERCC3_DROMEhayphysical
20667914

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PUF68_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-13 AND SER-30, AND MASSSPECTROMETRY.

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