SH3R1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SH3R1_MOUSE
• UniProt AC: Q69ZI1
• Protein Name: E3 ubiquitin-protein ligase SH3RF1
• Gene Name: Sh3rf1
• Organism: Mus musculus (Mouse).
• Sequence Length: 892
• Subcellular Localization: Cytoplasm, perinuclear region. Cell projection, lamellipodium . Golgi apparatus, trans-Golgi network . Colocalizes, with AKT2, in lamellipodia. Colocalizes, with HERP1, in trans-Golgi network..
• Protein Description: Acts as a scaffold protein, contributes to Rac-induced signal transduction such as JNKs (MAPK8 and MAPK9) activation and induces apoptosis. Within a signaling complex, it probably recruits protein kinases such as MAP3K10 or MAP3K11 which are in turn activated leading to the sequential activation of MAP2K4, MAP2K7 and JNKs (MAPK8 and MAPK9) (By similarity). In fibroblasts, induces apoptosis.; Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes such as UBE2D1 or UBE2N and then transfers it to substrates. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-dependent and clathrin-independent endocytosis..
• Protein Sequence: MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVDELPSNILLVRLLDGIKQRPWKPGPGGGGGTTCTNTLRAQGSTVVNCGSKDLQSSQCGQQPRVQAWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDIIILRRQVDENWYHGEVSGVHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEGMLADKIGIFPISYVEFNSAAKQLIEWDKPPVPGVDTAECPSATAQSTSASKHPDTKKNTRKRHSFTSLTMANKSSQGSQNRHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPAFTFPSDVPYQAALGSMNPPLPPPPLLAATVLASTPSGATAAVAAAAAAAAAAGMGPRPVMGSSEQIAHLRPQTRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQDGWYKGTSMHTSKIGVFPGNYVAPVTRAVTNASQAKVSMSTAGQASRGVTMVSPSTAGGPTQKPQGNGVAGNPSVVPTAVVSAAHIQTSPQAKVLLHMSGQMTVNQARNAVRTVAAHSQERPTAAVTPIQVQNAACLGPASVGLPHHSLASQPLPPMAGPAAHGAAVSISRTNAPMACAAGASLASPNMTSAMLETEPSGRTVTILPGLPTSPESAASACGNSSAGKPDKDSKKEKKGLLKLLSGASTKRKPRVSPPASPTLDVELGAGEAPLQGAVGPELPLGGSHGRVGSCPTDGDGPVAAGTAALAQDAFHRKTSSLDSAVPIAPPPRQACSSLGPVMNEARPVVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI

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
127	Phosphorylation	QPRVQAWSPPVRGIP CCCCCCCCCCCCCCC	23.49	25338131
299	Phosphorylation	HPDTKKNTRKRHSFT CCCCCCCCCCCCCEE	46.58	19854140
304	Phosphorylation	KNTRKRHSFTSLTMA CCCCCCCCEEEEEEC	33.96	26824392
306	Phosphorylation	TRKRHSFTSLTMANK CCCCCCEEEEEECCC	26.33	25266776
307	Phosphorylation	RKRHSFTSLTMANKS CCCCCEEEEEECCCC	21.60	25168779
314	Phosphorylation	SLTMANKSSQGSQNR EEEECCCCCCCCCCC	27.92	26643407
315	Phosphorylation	LTMANKSSQGSQNRH EEECCCCCCCCCCCC	39.92	26643407
318	Phosphorylation	ANKSSQGSQNRHSME CCCCCCCCCCCCCCE	19.35	18846507
323	Phosphorylation	QGSQNRHSMEISPPV CCCCCCCCCEECCCE	18.18	18846507
327	Phosphorylation	NRHSMEISPPVLISS CCCCCEECCCEEECC	15.16	18846507
512	O-linked_Glycosylation	GNYVAPVTRAVTNAS CCCEECHHHHHCCHH	16.32	55413703
527	O-linked_Glycosylation	QAKVSMSTAGQASRG HCEECHHCCCCCCCC	26.60	22517741
539	Phosphorylation	SRGVTMVSPSTAGGP CCCEEEECCCCCCCC	11.43	-
547	Phosphorylation	PSTAGGPTQKPQGNG CCCCCCCCCCCCCCC	53.12	28576409
701	Phosphorylation	GLPTSPESAASACGN CCCCCHHHHHHHCCC	32.30	21183079
704	Phosphorylation	TSPESAASACGNSSA CCHHHHHHHCCCCCC	24.65	21183079
730	Phosphorylation	KGLLKLLSGASTKRK HHHHHHHHCCCCCCC	42.63	28833060
733	Phosphorylation	LKLLSGASTKRKPRV HHHHHCCCCCCCCCC	37.68	28833060
734	Phosphorylation	KLLSGASTKRKPRVS HHHHCCCCCCCCCCC	34.04	23984901
741	Phosphorylation	TKRKPRVSPPASPTL CCCCCCCCCCCCCCE	26.84	27087446
745	Phosphorylation	PRVSPPASPTLDVEL CCCCCCCCCCEEEEE	24.96	27087446
747	Phosphorylation	VSPPASPTLDVELGA CCCCCCCCEEEEECC	32.85	27087446
772	Phosphorylation	PELPLGGSHGRVGSC CCCCCCCCCCCCCCC	22.44	25619855
803	Phosphorylation	QDAFHRKTSSLDSAV HHHHHHCCCCCCCCC	24.41	26643407
804	Phosphorylation	DAFHRKTSSLDSAVP HHHHHCCCCCCCCCC	31.75	26643407
805	Phosphorylation	AFHRKTSSLDSAVPI HHHHCCCCCCCCCCC	41.23	25521595
808	Phosphorylation	RKTSSLDSAVPIAPP HCCCCCCCCCCCCCC	36.14	26643407

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
304	S	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
304	S	Phosphorylation	Phosphorylated at Ser-304 by AKT1 and AKT2.	21183079

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SH3R1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SHRM3_MOUSE	Shroom3	physical	18829867

Drug and Disease Associations

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