dbPTM

NEDD4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NEDD4_MOUSE
UniProt AC	P46935
Protein Name	E3 ubiquitin-protein ligase NEDD4
Gene Name	Nedd4
Organism	Mus musculus (Mouse).
Sequence Length	887
Subcellular Localization	Cytoplasm. Cell membrane Peripheral membrane protein. Recruited to the plasma membrane by GRB10. Once complexed with GRB10 and IGF1R, follows IGF1R internalization, remaining associated with early endosomes. Uncouples from IGF1R-containing endosomes
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. Specifically ubiquitinates 'Lys-63' in target proteins (By similarity). Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes. Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes. Involved in ubiquitination of ERBB4 intracellular domain E4ICD1. [PubMed: 19193720 Predominantly involved in ubiquitination of membrane bound forms of ERBB4 rather than processed precursors and intermediate membrane-anchored 80 kDa fragments (m80HER4), with a lesser role in ubiquitination of ERBB4 intracellular domain E4ICD1]
Protein Sequence	MSSDMAADESEAPVLSEDEVWEFCLDKTEDGGGSPGSDVTDTCEPPCGCWELNPNSLEEEHVLFTADPYLELHNDDTRVVRVKVIAGIGLAKKDILGASDPYVRVTLYDPMSGILTSVQTKTIKKSLNPKWNEEILFRVLPQRHRILFEVFDENRLTRDDFLGQVDVPLYPLPTENPRMERPYTFKDFVLHPRSHKSRVKGYLRLKMTYLPKNGSEDENADQAEELEPGWVVLDQPDAATHLPHPPEPSPLPPGWEERQDVLGRTYYVNHESRRTQWKRPSPDDDLTDEDNDDMQLQAQRAFTTRRQISEDVDGPDNRESPENWEIVREDENTEYSGQAVQSPPSGHIDVQTHLAEEFNTRLAVCGNPATSQPVTSSNHSSRGGSLQTCIFEEQPTLPVLLPTSSGLPPGWEEKQDDRGRSYYVDHNSKTTTWSKPTMQDDPRSKIPAHLRGKTDSNDLGPLPPGWEERTHTDGRVFFINHNIKKTQWEDPRLQNVAITGPAVPYSRDYKRKYEFFRRKLKKQTDIPNKFEMKLRRANILEDSYRRIMGVKRADLLKARLWIEFDGEKGLDYGGVAREWFFLISKEMFNPYYGLFEYSATDNYTLQINPNSGLCNEDHLSYFKFIGRVAGMAVYHGKLLDGFFIRPFYKMMLQKLITLHDMESVDSEYYSSLRWILENDPTELDLRFIIDEELFGQTHQHELKTGGSEIVVTNKNKKEYIYLVIQWRFVNRIQKQMAAFKEGFFELIPQDLIKIFDENELELLMCGLGDVDVNDWREHTKYKNGYSMNHQVIHWFWKAVWMMDSEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQSFTVEQWGTPDKLPRAHTCFNRLDLPPYESFDELWDKLQMAIENTQGFDGVD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSDMAADE ------CCCCCCCCC	34.74	23984901
3	Phosphorylation	-----MSSDMAADES -----CCCCCCCCCC	30.06	23649490
10	Phosphorylation	SDMAADESEAPVLSE CCCCCCCCCCCCCCC	39.34	23649490
16	Phosphorylation	ESEAPVLSEDEVWEF CCCCCCCCCHHHHHH	43.14	30352176
34	Phosphorylation	KTEDGGGSPGSDVTD ECCCCCCCCCCCCCC	29.39	21082442
37	Phosphorylation	DGGGSPGSDVTDTCE CCCCCCCCCCCCCCC	32.09	21082442
83	Ubiquitination	DTRVVRVKVIAGIGL CCCEEEEEEEEECCC	19.84	-
92	Ubiquitination	IAGIGLAKKDILGAS EEECCCHHHHHCCCC	56.89	-
93	Ubiquitination	AGIGLAKKDILGASD EECCCHHHHHCCCCC	44.38	-
106	Phosphorylation	SDPYVRVTLYDPMSG CCCEEEEEEECCCCC	14.72	25159016
108	Phosphorylation	PYVRVTLYDPMSGIL CEEEEEEECCCCCCE	14.50	25521595
112	Phosphorylation	VTLYDPMSGILTSVQ EEEECCCCCCEEHHC	28.24	25159016
116	Phosphorylation	DPMSGILTSVQTKTI CCCCCCEEHHCCCCC	25.57	25159016
117	Phosphorylation	PMSGILTSVQTKTIK CCCCCEEHHCCCCCH	14.58	25159016
120	Phosphorylation	GILTSVQTKTIKKSL CCEEHHCCCCCHHHC	28.18	25521595
121	Ubiquitination	ILTSVQTKTIKKSLN CEEHHCCCCCHHHCC	31.03	-
124	Ubiquitination	SVQTKTIKKSLNPKW HHCCCCCHHHCCCCC	41.35	-
125	Ubiquitination	VQTKTIKKSLNPKWN HCCCCCHHHCCCCCC	57.22	-
130	Acetylation	IKKSLNPKWNEEILF CHHHCCCCCCHHHHH	62.67	23806337
130	Ubiquitination	IKKSLNPKWNEEILF CHHHCCCCCCHHHHH	62.67	-
183	Phosphorylation	NPRMERPYTFKDFVL CCCCCCCEEECCEEE	30.91	29514104
186	Ubiquitination	MERPYTFKDFVLHPR CCCCEEECCEEECCC	42.32	-
206	Ubiquitination	VKGYLRLKMTYLPKN HCEEEEEEEEECCCC	23.82	-
215	Phosphorylation	TYLPKNGSEDENADQ EECCCCCCCCCCHHH	51.79	24453211
249	Phosphorylation	LPHPPEPSPLPPGWE CCCCCCCCCCCCCHH	37.09	25338131
267	Phosphorylation	DVLGRTYYVNHESRR CCCCCEEECCCHHCC	8.31	29514104
275	Phosphorylation	VNHESRRTQWKRPSP CCCHHCCCCCCCCCC	37.36	26745281
278	Ubiquitination	ESRRTQWKRPSPDDD HHCCCCCCCCCCCCC	44.61	-
281	Phosphorylation	RTQWKRPSPDDDLTD CCCCCCCCCCCCCCC	45.02	27742792
287	Phosphorylation	PSPDDDLTDEDNDDM CCCCCCCCCCCCHHH	44.32	27087446
309	Phosphorylation	FTTRRQISEDVDGPD HHHHHHHHCCCCCCC	21.29	27087446
320	Phosphorylation	DGPDNRESPENWEIV CCCCCCCCCCCCEEE	33.99	25521595
333	Phosphorylation	IVREDENTEYSGQAV EEECCCCCCCCCEEC	33.96	23649490
370	Phosphorylation	AVCGNPATSQPVTSS EECCCCCCCCCCCCC	29.20	25619855
371	Phosphorylation	VCGNPATSQPVTSSN ECCCCCCCCCCCCCC	34.29	25619855
375	Phosphorylation	PATSQPVTSSNHSSR CCCCCCCCCCCCCCC	32.87	25619855
375	O-linked_Glycosylation	PATSQPVTSSNHSSR CCCCCCCCCCCCCCC	32.87	21540332
376	Phosphorylation	ATSQPVTSSNHSSRG CCCCCCCCCCCCCCC	29.40	25619855
377	Phosphorylation	TSQPVTSSNHSSRGG CCCCCCCCCCCCCCC	29.24	25619855
380	Phosphorylation	PVTSSNHSSRGGSLQ CCCCCCCCCCCCCCE	26.44	25619855
381	Phosphorylation	VTSSNHSSRGGSLQT CCCCCCCCCCCCCEE	27.65	25619855
385	Phosphorylation	NHSSRGGSLQTCIFE CCCCCCCCCEEEEEC	21.81	30352176
421	Phosphorylation	KQDDRGRSYYVDHNS CCCCCCCEEEEECCC	24.52	27149854
422	Phosphorylation	QDDRGRSYYVDHNSK CCCCCCEEEEECCCC	13.22	27149854
423	Phosphorylation	DDRGRSYYVDHNSKT CCCCCEEEEECCCCC	10.72	27149854
428	Phosphorylation	SYYVDHNSKTTTWSK EEEEECCCCCCCCCC	28.14	27149854
429	Ubiquitination	YYVDHNSKTTTWSKP EEEECCCCCCCCCCC	56.03	-
432	Phosphorylation	DHNSKTTTWSKPTMQ ECCCCCCCCCCCCCC	32.73	29514104
453	Ubiquitination	IPAHLRGKTDSNDLG CCHHHCCCCCCCCCC	42.60	-
454	Phosphorylation	PAHLRGKTDSNDLGP CHHHCCCCCCCCCCC	47.70	22871156
456	Phosphorylation	HLRGKTDSNDLGPLP HHCCCCCCCCCCCCC	37.16	27149854
470	Phosphorylation	PPGWEERTHTDGRVF CCCCCEECCCCCEEE	32.19	17544362
472	Phosphorylation	GWEERTHTDGRVFFI CCCEECCCCCEEEEE	39.26	22871156
484	Ubiquitination	FFINHNIKKTQWEDP EEEECCCCCCCCCCC	55.90	-
529	Acetylation	KQTDIPNKFEMKLRR CCCCCCCHHHHHHHH	37.03	22826441
543	Phosphorylation	RANILEDSYRRIMGV HHHHCHHHHHHHHCC	15.91	29514104
557	Ubiquitination	VKRADLLKARLWIEF CCHHHHHHEEEEEEE	38.46	-
568	Ubiquitination	WIEFDGEKGLDYGGV EEEECCCCCCCCCCH	71.01	-
572	Phosphorylation	DGEKGLDYGGVAREW CCCCCCCCCCHHHHH	22.33	29514104
591	Phosphorylation	SKEMFNPYYGLFEYS CHHHHCCCCCEEEEE	15.98	-
592	Phosphorylation	KEMFNPYYGLFEYSA HHHHCCCCCEEEEEC	14.49	-
663	Phosphorylation	ITLHDMESVDSEYYS HHHHCHHCCCHHHHH	25.29	-
734	Acetylation	RFVNRIQKQMAAFKE HHHHHHHHHHHHHHH	39.40	22826441
844	Phosphorylation	FTVEQWGTPDKLPRA EEEEECCCCCCCCCC	25.92	27180971

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
470	T	Phosphorylation	Kinase	GRK2	P21146	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	Nedd4	P46935	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NEDD4_MOUSE !!

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 NEDD4_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
N4BP3_HUMAN	N4BP3	physical	11717310
GRB10_MOUSE	Grb10	physical	20980250
TNIK_MOUSE	Tnik	physical	20159449
RAP2A_MOUSE	Rap2a	physical	20159449
SCNNA_MOUSE	Scnn1a	physical	18687683
1433B_MOUSE	Ywhab	physical	18687683
1433E_MOUSE	Ywhae	physical	18687683
CBL_MOUSE	Cbl	physical	18931680
1433B_MOUSE	Ywhab	physical	16099816
VIF_HV1B1	vif	physical	15013426
VIF_HV1BR	vif	physical	15013426
VIF_HV1H2	vif	physical	15013426
BEAN1_MOUSE	Bean1	physical	11042109
WBP1_MOUSE	Wbp1	physical	11042109
WBP2_MOUSE	Wbp2	physical	11042109
TMG2_MOUSE	Prrg2	physical	11042109
RNF11_MOUSE	Rnf11	physical	11042109
LITAF_MOUSE	Litaf	physical	11042109
NFIP1_MOUSE	Ndfip1	physical	11042109
ARBK1_MOUSE	Adrbk1	physical	17544362
SCNNA_MOUSE	Scnn1a	physical	10212229
SCNNB_MOUSE	Scnn1b	physical	10212229
SCNNG_MOUSE	Scnn1g	physical	10212229
DLG3_MOUSE	Dlg3	physical	21920314
HUNK_MOUSE	Hunk	physical	22745772
SCN5A_MOUSE	Scn5a	physical	15123669
SCN8A_MOUSE	Scn8a	physical	15123669
SCN9A_MOUSE	Scn9a	physical	15123669
SCNAA_MOUSE	Scn10a	physical	15123669
NMDE4_RAT	Grin2d	physical	23639431
NMDE1_HUMAN	GRIN2A	physical	23639431
EI2BE_RAT	Eif2b5	physical	23707720
TNR5_MOUSE	Cd40	physical	25072696
TRAF3_MOUSE	Traf3	physical	25072696
TRAF2_MOUSE	Traf2	physical	25072696
NEDD4_MOUSE	Nedd4	physical	11435423
UB2D3_HUMAN	UBE2D3	physical	11435423
N4BP1_MOUSE	N4bp1	physical	16337426
UB2D2_HUMAN	UBE2D2	physical	16337426
UB2D1_HUMAN	UBE2D1	physical	16337426
UB2L3_HUMAN	UBE2L3	physical	16337426

Drug and Disease Associations

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

Regulatory Network of NEDD4_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287 AND SER-309, ANDMASS SPECTROMETRY.	19131326 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287 AND SER-309, ANDMASS SPECTROMETRY.	19367708 [Abstract]
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND MASSSPECTROMETRY.	16452087 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, AND MASSSPECTROMETRY.	17242355 [Abstract]