AMPH_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AMPH_MOUSE
• UniProt AC: Q7TQF7
• Protein Name: Amphiphysin
• Gene Name: Amph
• Organism: Mus musculus (Mouse).
• Sequence Length: 686
• Subcellular Localization: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton.
• Protein Description: May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton (By similarity)..
• Protein Sequence: MADIKTGIFAKNVQKRLNRAQEKVLQKLGKADETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYEPDWYGREDVKMVGEKCDVLWEDFHQKLVDGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKRKDESRISKAEEEFQKAQKVFEEFNVDLQEELPSLWSSRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTKLGDQHADKAFSIQGAPSDSGPLRIAKTPSPPEEPSPLPSPTASPNHTLAPASPAPVRPRSPSQTRKGPPVPPLPKVTPTKELKQENIINFFEDNFVPEINVTTPSQNEVLEVKKEETLLDLDFDPFKPDVAPAGSAAATHSPMSQTLPWDLWTTSTDLVQPASGGSFNDFTQAQDTSLFTMQTDQNMAETEQALPTEPQAEEPPATAAAPTAGLDLGLEMEEPKEEAVIPPATDTGETVETAVPTEGAPVEEAEAEKAALPAGEGGSPEGAKIDGESTELAISESPQPVEPEAGAPQVIPSVVIEPASNHEGEGEHQETATGTEPREAAEDVAAQGSAGEKQEVATEPTPLDSQATLPASAGAVDASLSAGDATQELPPGFLYKVETLHDFEAANSDELNLQRGDVVLVVPSDSEADQDAGWLVGVKESDWLQYRDLATYKGLFPENFTRRLE

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
34	Phosphorylation	KLGKADETKDEQFEE HHCCCCCCCHHHHHH	44.32	29899451
47	Acetylation	EEYVQNFKRQEAEGT HHHHHHHHHHHHHHH	61.80	160805
74	Phosphorylation	IKGMQEASMKLTESL HHCHHHHHHHHHHHH	18.72	25159016
78	Phosphorylation	QEASMKLTESLHEVY HHHHHHHHHHHHHHH	20.29	25159016
80	Phosphorylation	ASMKLTESLHEVYEP HHHHHHHHHHHHHCC	29.77	25159016
85	Phosphorylation	TESLHEVYEPDWYGR HHHHHHHHCCCCCCH	20.82	25159016
90	Phosphorylation	EVYEPDWYGREDVKM HHHCCCCCCHHHHHH	17.43	25159016
101	Ubiquitination	DVKMVGEKCDVLWED HHHHHHHCCCEEHHH	29.79	22790023
141	Ubiquitination	RIAKRSRKLVDYDSA HHHHHHHHHCCHHHH	54.85	-
157	Phosphorylation	HHLEALQSSKRKDES HHHHHHHHCCCCCHH	38.38	29899451
158	Phosphorylation	HLEALQSSKRKDESR HHHHHHHCCCCCHHH	24.42	29899451
215	Ubiquitination	NVSSLEAKFHKEIAV CHHHHHHHHHHHHHH	38.33	22790023
233	Ubiquitination	KLYEVMTKLGDQHAD HHHHHHHHHCHHHCC	32.17	22790023
244	Phosphorylation	QHADKAFSIQGAPSD HHCCCCEEECCCCCC	20.89	22324799
250	Phosphorylation	FSIQGAPSDSGPLRI EEECCCCCCCCCCCE	43.82	25521595
252	Phosphorylation	IQGAPSDSGPLRIAK ECCCCCCCCCCCEEE	46.80	25521595
260	Phosphorylation	GPLRIAKTPSPPEEP CCCCEEECCCCCCCC	21.70	24925903
262	Phosphorylation	LRIAKTPSPPEEPSP CCEEECCCCCCCCCC	59.32	25521595
268	Phosphorylation	PSPPEEPSPLPSPTA CCCCCCCCCCCCCCC	42.20	22324799
272	Phosphorylation	EEPSPLPSPTASPNH CCCCCCCCCCCCCCC	42.43	25521595
274	Phosphorylation	PSPLPSPTASPNHTL CCCCCCCCCCCCCCC	44.07	25521595
276	Phosphorylation	PLPSPTASPNHTLAP CCCCCCCCCCCCCCC	28.81	25521595
280	Phosphorylation	PTASPNHTLAPASPA CCCCCCCCCCCCCCC	31.12	24925903
285	Phosphorylation	NHTLAPASPAPVRPR CCCCCCCCCCCCCCC	22.12	25521595
293	Phosphorylation	PAPVRPRSPSQTRKG CCCCCCCCCCCCCCC	31.42	16733250
295	Phosphorylation	PVRPRSPSQTRKGPP CCCCCCCCCCCCCCC	45.49	17622165
297	Phosphorylation	RPRSPSQTRKGPPVP CCCCCCCCCCCCCCC	38.39	36249965
310	Phosphorylation	VPPLPKVTPTKELKQ CCCCCCCCCCHHHCH	31.22	30372032
312	Phosphorylation	PLPKVTPTKELKQEN CCCCCCCCHHHCHHC	27.99	30372032
490	Acetylation	VEEAEAEKAALPAGE HHHHHHHHHCCCCCC	46.11	156707
500	Phosphorylation	LPAGEGGSPEGAKID CCCCCCCCCCCCEEC	30.54	25521595
516	Phosphorylation	ESTELAISESPQPVE CCCEEEEECCCCCCC	26.81	29899451
518	Phosphorylation	TELAISESPQPVEPE CEEEEECCCCCCCCC	23.26	-
570	Phosphorylation	EDVAAQGSAGEKQEV HHHHHCCCCCCCCCC	22.48	29899451
629	Phosphorylation	HDFEAANSDELNLQR HHHHHCCCCCCCCCC	27.95	25521595
645	Phosphorylation	DVVLVVPSDSEADQD CEEEEEECCCHHHCC	42.00	29899451
647	Phosphorylation	VLVVPSDSEADQDAG EEEEECCCHHHCCCC	38.74	29899451
674	Ubiquitination	YRDLATYKGLFPENF HHHHHHHCCCCCCCH	44.79	22790023

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
293	S	Phosphorylation	Kinase	CDKL5	O76039	PSP
293	S	Phosphorylation	Kinase	DYRK1A	Q13627	PSP
293	S	Phosphorylation	Kinase	MAPK1	P28482	GPS

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DYN2_MOUSE	Dnm2	physical	9525921

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250 AND SER-500, ANDMASS SPECTROMETRY.
PubMed: 17114649

"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND THR-297, ANDMASS SPECTROMETRY.
PubMed: 17622165

"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, AND MASSSPECTROMETRY.
PubMed: 15345747