SMUF1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SMUF1_MOUSE
• UniProt AC: Q9CUN6
• Protein Name: E3 ubiquitin-protein ligase SMURF1
• Gene Name: Smurf1
• Organism: Mus musculus (Mouse).
• Sequence Length: 731
• Subcellular Localization: Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
• Protein Description: E3 ubiquitin-protein ligase that acts as a negative regulator of BMP signaling pathway (By similarity). Mediates ubiquitination and degradation of SMAD1 and SMAD5, 2 receptor-regulated SMADs specific for the BMP pathway (By similarity). Promotes ubiquitination and subsequent proteasomal degradation of TRAF family members and RHOA (By similarity). Promotes ubiquitination and subsequent proteasomal degradation of MAVS. [PubMed: 23087404 Plays a role in dendrite formation by melanocytes (By similarity]
• Protein Sequence: MSNPGTRRNGSSIKIRLTVLCAKNLAKKDFFRLPDPFAKIVVDGSGQCHSTDTVKNTLDPKWNQHYDLYVGKTDSITISVWNHKKIHKKQGAGFLGCVRLLSNAISRLKDTGYQRLDLCKLNPSDTDAVRGQIVVSLQTRDRIGGGGSVVDCRGLLENEGTVYEDSGPGRPLSCLMEEPAPYTDGTGAAAGGGNCRFVESPSQDQRLLVQRLRNPEVRGPLQTPQNRPHGHQSPELPEGYEQRTTVQGQVYFLHTQTGVSTWHDPRIPRDLNSVNCDELGPLPPGWEVRSTVSGRIYFVDHNNRTTQFTDPRLHHIMNHQCQLKEPSQPLQLPSEGSVEDEELPAQRYERDLVQKLKVLRHELSLQQPQAGHCRIEVSREEIFEESYRQIMKMRPKDLKKRLMVKFRGEEGLDYGGVAREWLYLLCHEMLNPYYGLFQYSTDNIYTLQINPDSSINPDHLSYFHFVGRIMGLAVFHGHYINGGFTVPFYKQLLGKPIQLSDLESVDPELHKSLVWILENDITPVLDHTFCVEHNAFGRILQHELKPNGRNVPVTEENKKEYVRLYVNWRFMRGIEAQFLALQKGFNELIPQHLLKPFDQKELELIIGGLDKIDLNDWKSNTRLKHCVADSNIVRWFWQAVETFDEERRARLLQFVTGSTRVPLQGFKALQGSTGAAGPRLFTIHLIDANTDNLPKAHTCFNRIDIPPYESYEKLYEKLLTAVEETCGFAVE

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
11	Phosphorylation	PGTRRNGSSIKIRLT CCCCCCCCCCCHHHH	32.22	-
12	Phosphorylation	GTRRNGSSIKIRLTV CCCCCCCCCCHHHHH	29.33	-
148	Phosphorylation	DRIGGGGSVVDCRGL CCCCCCCCEEECCHH	23.42	-
200	Phosphorylation	GNCRFVESPSQDQRL CCCEECCCCCHHHHH	25.26	23527152
202	Phosphorylation	CRFVESPSQDQRLLV CEECCCCCHHHHHHH	56.52	28066266
233	Phosphorylation	NRPHGHQSPELPEGY CCCCCCCCCCCCCCC	18.05	29899451
290	Phosphorylation	PPGWEVRSTVSGRIY CCCCEEEEEEECEEE	38.03	28285833
291	Phosphorylation	PGWEVRSTVSGRIYF CCCEEEEEEECEEEE	14.23	28285833
293	Phosphorylation	WEVRSTVSGRIYFVD CEEEEEEECEEEEEE	23.57	28285833
297	Phosphorylation	STVSGRIYFVDHNNR EEEECEEEEEECCCC	9.01	28285833
306	Phosphorylation	VDHNNRTTQFTDPRL EECCCCEEEECCHHH	20.60	21262463
386	Phosphorylation	REEIFEESYRQIMKM HHHHHHHHHHHHHHC	20.58	28059163
387	Phosphorylation	EEIFEESYRQIMKMR HHHHHHHHHHHHHCC	15.15	28059163
392	Ubiquitination	ESYRQIMKMRPKDLK HHHHHHHHCCHHHHH	33.13	-
434	Phosphorylation	HEMLNPYYGLFQYST HHHHCCCCCCEEEEC	14.49	-

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
148	S	Phosphorylation	Kinase	AMPKA1	Q5EG47	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
355	K	ubiquitylation	Ubiquitinated by the SCF(FBXL15) complex at Lys-355 and Lys-357, leading to its degradation by the proteasome.	-
357	K	ubiquitylation	Lys-357 is the primary ubiquitination site.	-
357	K	ubiquitylation	Ubiquitinated by the SCF(FBXL15) complex at Lys-355 and Lys-357, leading to its degradation by the proteasome.	-

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WFS1_MOUSE	Wfs1	physical	21454619
PAR6A_MOUSE	Pard6a	physical	19379695
DVL2_MOUSE	Dvl2	physical	19379695
SMUF2_MOUSE	Smurf2	genetic	19379695
UB2D3_HUMAN	UBE2D3	physical	15820682

Drug and Disease Associations

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