dbPTM

SH3R1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SH3R1_HUMAN
UniProt AC	Q7Z6J0
Protein Name	E3 ubiquitin-protein ligase SH3RF1
Gene Name	SH3RF1
Organism	Homo sapiens (Human).
Sequence Length	888
Subcellular Localization	Cytoplasm, perinuclear region. Cell projection, lamellipodium. Cytoplasm. Golgi apparatus, trans-Golgi network. Colocalizes, with AKT2, in lamellipodia (By similarity). 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). May be involved in targeting of HIV-1 GAG and GAG-POL polyproteins to the plasma membrane.; 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.; Plays an essential role in the targeting of HIV-1 Gag to the plasma membrane, this function is dependent on it's RING domain, and hence it's E3 ligase activity..
Protein Sequence	MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVEELPSNILLVRLLDGIKQRPWKPGPGGGSGTNCTNALRSQSSTVANCSSKDLQSSQGGQQPRVQSWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDIIILRRQVDENWYHGEVNGIHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEGMLADKIGIFPISYVEFNSAAKQLIEWDKPPVPGVDAGECSSAAAQSSTAPKHSDTKKNTKKRHSFTSLTMANKSSQASQNRHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPSFTFPSDVPYQAALGTLNPPLPPPPLLAATVLASTPPGATAAAAAAGMGPRPMAGSTDQIAHLRPQTRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQDGWFKGTSMHTSKIGVFPGNYVAPVTRAVTNASQAKVPMSTAGQTSRGVTMVSPSTAGGPAQKLQGNGVAGSPSVVPAAVVSAAHIQTSPQAKVLLHMTGQMTVNQARNAVRTVAAHNQERPTAAVTPIQVQNAAGLSPASVGLSHHSLASPQPAPLMPGSATHTAAISISRASAPLACAAAAPLTSPSITSASLEAEPSGRIVTVLPGLPTSPDSASSACGNSSATKPDKDSKKEKKGLLKLLSGASTKRKPRVSPPASPTLEVELGSAELPLQGAVGPELPPGGGHGRAGSCPVDGDGPVTTAVAGAALAQDAFHRKASSLDSAVPIAPPPRQACSSLGPVLNESRPVVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
54	Phosphorylation	LRCPECRTLVGSGVE CCCCHHHHHCCCCCC	37.14	20068231
58	Phosphorylation	ECRTLVGSGVEELPS HHHHHCCCCCCCCCC	31.99	22210691
65	Phosphorylation	SGVEELPSNILLVRL CCCCCCCCCEEEEEC	49.48	20068231
108	Phosphorylation	SSTVANCSSKDLQSS CCCCEECCHHHHHHC	39.98	-
109	Phosphorylation	STVANCSSKDLQSSQ CCCEECCHHHHHHCC	32.18	-
114	Phosphorylation	CSSKDLQSSQGGQQP CCHHHHHHCCCCCCC	31.74	23401153
125	Phosphorylation	GQQPRVQSWSPPVRG CCCCCCCCCCCCCCC	27.02	30108239
127	Phosphorylation	QPRVQSWSPPVRGIP CCCCCCCCCCCCCCC	25.27	25159151
143	Phosphorylation	LPCAKALYNYEGKEP CCCCHHHHCCCCCCC	22.13	-
145	Phosphorylation	CAKALYNYEGKEPGD CCHHHHCCCCCCCCC	16.70	-
148	Ubiquitination	ALYNYEGKEPGDLKF HHHCCCCCCCCCCCC	49.12	29967540
210	Ubiquitination	ALYDFEVKDKEADKD EEEEEEECCHHCCCC	56.75	32142685
304	Phosphorylation	KNTKKRHSFTSLTMA CCCCCCCCCEEEEEC	33.96	29255136
306	Phosphorylation	TKKRHSFTSLTMANK CCCCCCCEEEEECCC	26.33	29255136
307	Phosphorylation	KKRHSFTSLTMANKS CCCCCCEEEEECCCC	21.60	29255136
309	Phosphorylation	RHSFTSLTMANKSSQ CCCCEEEEECCCCCH	17.63	20068231
314	Phosphorylation	SLTMANKSSQASQNR EEEECCCCCHHHCCC	27.73	23090842
315	Phosphorylation	LTMANKSSQASQNRH EEECCCCCHHHCCCC	31.23	23090842
318	Phosphorylation	ANKSSQASQNRHSME CCCCCHHHCCCCCCE	21.98	28857561
323	Phosphorylation	QASQNRHSMEISPPV HHHCCCCCCEECCCE	18.18	21712546
327	Phosphorylation	NRHSMEISPPVLISS CCCCCEECCCEEECC	15.16	30576142
333	Phosphorylation	ISPPVLISSSNPTAA ECCCEEECCCCHHHH	24.45	23090842
334	Phosphorylation	SPPVLISSSNPTAAA CCCEEECCCCHHHHH	27.43	23090842
335	Phosphorylation	PPVLISSSNPTAAAR CCEEECCCCHHHHHH	39.78	23090842
338	Phosphorylation	LISSSNPTAAARISE EECCCCHHHHHHHHH	32.93	23090842
450	Phosphorylation	PQTRPSVYVAIYPYT CCCCCCEEEEECCCC	6.62	22817900
454	Phosphorylation	PSVYVAIYPYTPRKE CCEEEEECCCCCCCH	4.77	22817900
456	Phosphorylation	VYVAIYPYTPRKEDE EEEEECCCCCCCHHC	16.65	22817900
472	Phosphorylation	ELRKGEMFLVFERCQ EECCCCEEEEEEECC	4.59	17535800
505	O-linked_Glycosylation	GNYVAPVTRAVTNAS CCCCCCHHHHHCCHH	16.32	30059200
509	Phosphorylation	APVTRAVTNASQAKV CCHHHHHCCHHHCCC	24.88	30619164
512	Phosphorylation	TRAVTNASQAKVPMS HHHHCCHHHCCCCCC	32.51	30619164
515 (in isoform 1)	Ubiquitination	-	38.95	21906983
515	Ubiquitination	VTNASQAKVPMSTAG HCCHHHCCCCCCCCC	38.95	27667366
519	O-linked_Glycosylation	SQAKVPMSTAGQTSR HHCCCCCCCCCCCCC	14.72	30059200
519	Phosphorylation	SQAKVPMSTAGQTSR HHCCCCCCCCCCCCC	14.72	30619164
520	O-linked_Glycosylation	QAKVPMSTAGQTSRG HCCCCCCCCCCCCCC	28.67	30059200
520	Phosphorylation	QAKVPMSTAGQTSRG HCCCCCCCCCCCCCC	28.67	30619164
524	Phosphorylation	PMSTAGQTSRGVTMV CCCCCCCCCCCEEEE	21.34	30619164
525	O-linked_Glycosylation	MSTAGQTSRGVTMVS CCCCCCCCCCEEEEC	21.10	30059200
525	Phosphorylation	MSTAGQTSRGVTMVS CCCCCCCCCCEEEEC	21.10	30619164
529	Phosphorylation	GQTSRGVTMVSPSTA CCCCCCEEEECCCCC	18.06	22199227
532	Phosphorylation	SRGVTMVSPSTAGGP CCCEEEECCCCCCCC	11.43	25159151
534	Phosphorylation	GVTMVSPSTAGGPAQ CEEEECCCCCCCCCH	24.31	28985074
535	Phosphorylation	VTMVSPSTAGGPAQK EEEECCCCCCCCCHH	32.48	22199227
551	Phosphorylation	QGNGVAGSPSVVPAA CCCCCCCCCCHHCCE	12.31	22199227
551	O-linked_Glycosylation	QGNGVAGSPSVVPAA CCCCCCCCCCHHCCE	12.31	30059200
553	Phosphorylation	NGVAGSPSVVPAAVV CCCCCCCCHHCCEEE	37.13	22199227
561	Phosphorylation	VVPAAVVSAAHIQTS HHCCEEEEHHHCCCC	17.09	22199227
561	O-linked_Glycosylation	VVPAAVVSAAHIQTS HHCCEEEEHHHCCCC	17.09	30059200
567	Phosphorylation	VSAAHIQTSPQAKVL EEHHHCCCCCCHHHH	41.60	22199227
568	Phosphorylation	SAAHIQTSPQAKVLL EHHHCCCCCCHHHHH	9.91	22199227
578	Phosphorylation	AKVLLHMTGQMTVNQ HHHHHHHHCCCHHHH	17.32	-
653	Phosphorylation	AISISRASAPLACAA EEEEECCCCCHHHHH	29.34	22199227
665	Phosphorylation	CAAAAPLTSPSITSA HHHCCCCCCCCCCCC	37.22	22199227
666	Phosphorylation	AAAAPLTSPSITSAS HHCCCCCCCCCCCCE	25.08	25850435
668	Phosphorylation	AAPLTSPSITSASLE CCCCCCCCCCCCEEE	37.96	22199227
670	Phosphorylation	PLTSPSITSASLEAE CCCCCCCCCCEEEEC	23.68	22199227
671	Phosphorylation	LTSPSITSASLEAEP CCCCCCCCCEEEECC	17.75	25850435
673	Phosphorylation	SPSITSASLEAEPSG CCCCCCCEEEECCCC	26.89	25850435
684	Phosphorylation	EPSGRIVTVLPGLPT CCCCCEEEEECCCCC	17.60	-
691	Phosphorylation	TVLPGLPTSPDSASS EEECCCCCCCCCHHH	58.91	22199227
692	Phosphorylation	VLPGLPTSPDSASSA EECCCCCCCCCHHHH	25.44	22199227
695	Phosphorylation	GLPTSPDSASSACGN CCCCCCCCHHHHCCC	33.17	22199227
697	Phosphorylation	PTSPDSASSACGNSS CCCCCCHHHHCCCCC	23.55	22199227
698	Phosphorylation	TSPDSASSACGNSSA CCCCCHHHHCCCCCC	27.56	22199227
703	Phosphorylation	ASSACGNSSATKPDK HHHHCCCCCCCCCCC	13.46	22199227
704	Phosphorylation	SSACGNSSATKPDKD HHHCCCCCCCCCCCC	43.91	22199227
706	Phosphorylation	ACGNSSATKPDKDSK HCCCCCCCCCCCCCH	45.09	22199227
724	Phosphorylation	KGLLKLLSGASTKRK HHHHHHHHCCCCCCC	42.63	29514088
727	Phosphorylation	LKLLSGASTKRKPRV HHHHHCCCCCCCCCC	37.68	29514088
728	Phosphorylation	KLLSGASTKRKPRVS HHHHCCCCCCCCCCC	34.04	29514088
735	Phosphorylation	TKRKPRVSPPASPTL CCCCCCCCCCCCCCE	26.84	30278072
739	Phosphorylation	PRVSPPASPTLEVEL CCCCCCCCCCEEEEE	24.96	30278072
741	Phosphorylation	VSPPASPTLEVELGS CCCCCCCCEEEEECC	32.81	26055452
748	Phosphorylation	TLEVELGSAELPLQG CEEEEECCCCCCCCC	31.06	27732954
772	Phosphorylation	GGHGRAGSCPVDGDG CCCCCCCCCCCCCCC	17.79	21945579
782	Phosphorylation	VDGDGPVTTAVAGAA CCCCCCCHHHHHHHH	16.51	21945579
783	Phosphorylation	DGDGPVTTAVAGAAL CCCCCCHHHHHHHHH	21.26	21945579
800	Phosphorylation	DAFHRKASSLDSAVP HHHHHHHHCCCCCCC	34.17	30266825
801	Phosphorylation	AFHRKASSLDSAVPI HHHHHHHCCCCCCCC	40.84	30266825
804	Phosphorylation	RKASSLDSAVPIAPP HHHHCCCCCCCCCCC	36.14	30266825
817	Phosphorylation	PPPRQACSSLGPVLN CCCCHHHHHHHHHCC	31.45	28555341
818	Phosphorylation	PPRQACSSLGPVLNE CCCHHHHHHHHHCCC	36.91	28555341
860	Ubiquitination	GDIVFVHKKREDGWF CCEEEEEEECCCCCE	48.50	27667366

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
125	S	Phosphorylation	Kinase	AKT1	P31749	GPS
125	S	Phosphorylation	Kinase	AKT2	P31751	GPS
304	S	Phosphorylation	Kinase	AKT1	P31749	PSP
304	S	Phosphorylation	Kinase	AKT2	P31751	PSP
800	S	Phosphorylation	Kinase	AKT1	P31749	GPS
800	S	Phosphorylation	Kinase	AKT2	P31751	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
304	S	Phosphorylation		17535800
Phosphorylated at Ser-304 by AKT1 and AKT2.

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 SH3R1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AKT2_HUMAN	AKT2	physical	14504284
M3K11_HUMAN	MAP3K11	physical	14504284
PDC6I_HUMAN	PDCD6IP	physical	19393081
KCNJ1_HUMAN	KCNJ1	physical	19710010
SEM6A_HUMAN	SEMA6A	physical	12421765
SH3R2_HUMAN	SH3RF2	physical	22128169
SIAH1_HUMAN	SIAH1	physical	16230351
SIAH2_HUMAN	SIAH2	physical	21586138
UBE2N_HUMAN	UBE2N	physical	19393081
UB2D3_HUMAN	UBE2D3	physical	19393081
UB2D1_HUMAN	UBE2D1	physical	19710010
HERP1_HUMAN	HERPUD1	physical	17420289
SH3R1_HUMAN	SH3RF1	physical	17420289
UBE2N_HUMAN	UBE2N	physical	17420289
UB2D3_HUMAN	UBE2D3	physical	17420289
FAT1_HUMAN	FAT1	physical	28129444

Drug and Disease Associations

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

Regulatory Network of SH3R1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Regulation of the pro-apoptotic scaffolding protein POSH by Akt."; Lyons T.R., Thorburn J., Ryan P.W., Thorburn A., Anderson S.M.,Kassenbrock C.K.; J. Biol. Chem. 282:21987-21997(2007). Cited for: INTERACTION WITH AKT1 AND AKT2, PHOSPHORYLATION AT SER-304,MUTAGENESIS OF SER-304, AND MASS SPECTROMETRY.	17535800 [Abstract]

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