SMUF1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SMUF1_DROME
• UniProt AC: Q9V853
• Protein Name: E3 ubiquitin-protein ligase Smurf1
• Gene Name: Smurf {ECO:0000303|PubMed:11703946}
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 1061
• Protein Description: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Down-regulates Dpp signaling after gastrulation by promoting MAD ubiquitination and subsequent degradation..
• Protein Sequence: MNKLDYPRRNGTHKVRITILCARNLARKDLFRLPDPFAKVQVDGTGQVYSTEISKSSLDPKWNAHYDLFLGIGDAITITVWNQRKIHKGSGFLGCVRIPAFNIQSLKGAGFQRLDLGKLSPDDDELVRGQIIISLLSKDGPSSGNPLAIVGPSGDVRGPSEDDSSEDSLPEGWEERRTDNGRVYYVNHATKSTQWDRPRQPGVVGSSHATSPQQRHNTHNGNSGDRQAPAGPTRSTTCTNLMNNGHRSRDLSVTASDERRHSTEILSSVGKENTSPTTPVSATTTPGKKTSSSNSSSAGGRTLEQRPTNEPATPTSSTTSASVRLHSNDNHVKTPKHQTNGHAPPESTPTSPTGQQNYVNGNAQNGSTSGNGSGQAAQPQSASNGWTQEDAATTTSPSTTTSPPRHSQSPPTPNISPPASVTPSANGNVHSPNANSTPAGSGGGSRSYTAATPGQRSQRRSSRQQGEESSTRRRSSRGTRNGGTSGGGGGGGSGQRYASAAIAAANQAARPFLDLPPGYEMRTTQQGQVYFYHIPTGVSTWHDPRIPRDFDTQHLTLDAIGPLPSGWEQRKTASGRVYFVDHNNRTTQFTDPRLSGSILQMIRRGTVPPTSAANAGTPAPPSATPATPSAAAAVPPQATPASNATPTTLTTTTNPPHRIVPDLPQGLLEGADLLPKYRRDLVGKLRALRTELQTMQPQSGHCRLEVSRNEIFEESYRLIMKMRAKDMRKRLMVKFKGEEGLDYGGVAREWLHLLSREMLNPQYGLFQYSRDDHYTLQINPDSGVNPDHLSYFHFVGRTLGIAVFHGHCLDGGFTTPFYKQLLNKPITLGDIEGVDPDLHRSLTWMLESNISGIIESTFSVENNSFGALVVHELKPGGASIPVTEENKREYVKLYVNYRFMRGIEQQFLALQKGFCELIPSHLLRPFDERELELVIGGISSIDVNDWRNNTRLKHCTNETTQVLWFWQVVESYSSEMRARLLQFVTGSSRVPLQGFRALQGSTGAVGPRLFTIHLTADVPTQNLPKAHTCFNRIDLPPYETYQLLCDKLTQAVEETCGFAVE

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
252	Phosphorylation	GHRSRDLSVTASDER CCCCCCCCEECCHHH	23.01	22817900
262	Phosphorylation	ASDERRHSTEILSSV CCHHHHHHHHHHHHC	26.39	19429919
263	Phosphorylation	SDERRHSTEILSSVG CHHHHHHHHHHHHCC	22.41	19429919
313	Phosphorylation	RPTNEPATPTSSTTS CCCCCCCCCCCCCCC	37.50	21082442
327	Phosphorylation	SASVRLHSNDNHVKT CEEEEEECCCCCCCC	50.93	19429919
409	Phosphorylation	SPPRHSQSPPTPNIS CCCCCCCCCCCCCCC	35.54	22817900
412	Phosphorylation	RHSQSPPTPNISPPA CCCCCCCCCCCCCCC	32.14	22817900
416	Phosphorylation	SPPTPNISPPASVTP CCCCCCCCCCCCCCC	31.32	22817900
461	Phosphorylation	GQRSQRRSSRQQGEE CCCHHHHHHHHCCCC	31.87	22817900
462	Phosphorylation	QRSQRRSSRQQGEES CCHHHHHHHHCCCCC	32.09	22817900
595	Phosphorylation	QFTDPRLSGSILQMI EECCCCCCHHHHHHH	31.60	22817900
597	Phosphorylation	TDPRLSGSILQMIRR CCCCCCHHHHHHHHC	19.42	22817900

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SMUF1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SMUF1_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SMUF1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DECA_DROME	dpp	genetic	11703946
FUSED_DROME	fu	physical	21145463
SMO_DROME	smo	physical	24302888
PTC_DROME	ptc	physical	24302888
WARTS_DROME	wts	physical	25450375
WARTS_DROME	wts	physical	27856247

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-262; THR-412 ANDSER-416, AND MASS SPECTROMETRY.
PubMed: 18327897