dbPTM

BIN1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BIN1_MOUSE
UniProt AC	O08539
Protein Name	Myc box-dependent-interacting protein 1
Gene Name	Bin1
Organism	Mus musculus (Mouse).
Sequence Length	588
Subcellular Localization	Cytoplasm. Nucleus.
Protein Description	May be involved in regulation of synaptic vesicle endocytosis. May act as a tumor suppressor and inhibits malignant cell transformation..
Protein Sequence	MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLSECLQEVYEPEWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEKAAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVSLEKQHGSNTFTVKAQPSDNAPEKGNKSPSPPPDGSPAATPEIRVNHEPEPASGASPGATIPKSPSQLRKGPPVPPPPKHTPSKEMKQEQILSLFDDAFVPEISVTTPSQFEAPGPFSEQASLLDLDFEPLPPVASPVKAPTPSGQSIPWDLWEPTESQAGILPSGEPSSAEGSFAVAWPSQTAEPGPAQPAEASEVVGGAQEPGETAASEATSSSLPAVVVETFSATVNGAVEGSAGTGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERVQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEMGSKGV ------CCCCCCCCC	18.58	-
6	Phosphorylation	--MAEMGSKGVTAGK --CCCCCCCCCCHHH	25.56	27149854
35	Ubiquitination	KVLQKLGKADETKDE HHHHHHCCCCCCCHH	64.20	22790023
47	Glutathionylation	KDEQFEQCVQNFNKQ CHHHHHHHHHHHHHH	2.40	24333276
53	Ubiquitination	QCVQNFNKQLTEGTR HHHHHHHHHCCCCCH	42.41	22790023
73	Ubiquitination	RTYLASVKAMHEASK HHHHHHHHHHHHHHH	37.18	22790023
146	Acetylation	RIAKRGRKLVDYDSA HHHHHCCCCCCHHHH	56.54	22826441
146	Ubiquitination	RIAKRGRKLVDYDSA HHHHHCCCCCCHHHH	56.54	22790023
157	Phosphorylation	YDSARHHYESLQTAK HHHHHHHHHHHHHHC	10.90	29514104
159	Phosphorylation	SARHHYESLQTAKKK HHHHHHHHHHHHCHH	20.72	29899451
173 (in isoform 2)	Ubiquitination	-	49.80	-
211	Ubiquitination	QAEEELIKAQKVFEE HHHHHHHHHHHHHHH	58.34	-
258	Ubiquitination	NFHKEMSKLNQNLND HHHHHHHHHHHHHHH	50.58	22790023
272	Ubiquitination	DVLVSLEKQHGSNTF HHHHHHHHHCCCCEE	53.54	22790023
276	Phosphorylation	SLEKQHGSNTFTVKA HHHHHCCCCEEEEEE	30.49	29899451
278	Phosphorylation	EKQHGSNTFTVKAQP HHHCCCCEEEEEEEC	23.52	29899451
280	Phosphorylation	QHGSNTFTVKAQPSD HCCCCEEEEEEECCC	21.04	29899451
282	Ubiquitination	GSNTFTVKAQPSDNA CCCEEEEEEECCCCC	37.94	22790023
286	Phosphorylation	FTVKAQPSDNAPEKG EEEEEECCCCCCCCC	31.27	22942356
296	Phosphorylation	APEKGNKSPSPPPDG CCCCCCCCCCCCCCC	34.31	24925903
298	Phosphorylation	EKGNKSPSPPPDGSP CCCCCCCCCCCCCCC	58.07	24925903
303 (in isoform 2)	Phosphorylation	-	41.10	29899451
304	Phosphorylation	PSPPPDGSPAATPEI CCCCCCCCCCCCCCE	20.81	24925903
308	Phosphorylation	PDGSPAATPEIRVNH CCCCCCCCCCEEECC	24.46	25521595
321	Phosphorylation	NHEPEPASGASPGAT CCCCCCCCCCCCCCC	45.68	24925903
324	Phosphorylation	PEPASGASPGATIPK CCCCCCCCCCCCCCC	27.65	24925903
328	Phosphorylation	SGASPGATIPKSPSQ CCCCCCCCCCCCHHH	43.67	25521595
332	Phosphorylation	PGATIPKSPSQLRKG CCCCCCCCHHHHCCC	25.16	26824392
334	Phosphorylation	ATIPKSPSQLRKGPP CCCCCCHHHHCCCCC	49.27	26824392
349	Phosphorylation	VPPPPKHTPSKEMKQ CCCCCCCCCCHHHCH	35.07	26824392
351	Phosphorylation	PPPKHTPSKEMKQEQ CCCCCCCCHHHCHHH	42.26	26643407
404	Phosphorylation	EPLPPVASPVKAPTP CCCCCCCCCCCCCCC	30.38	27149854

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
Oops, there are no upstream regulatory protein records of BIN1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BIN1_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 BIN1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
WASL_MOUSE	Wasl	physical	25262827
E2F1_MOUSE	E2f1	physical	25257171

Drug and Disease Associations

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

Regulatory Network of BIN1_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 SER-332, AND MASSSPECTROMETRY.	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 SER-296; SER-298 ANDSER-324, AND MASS SPECTROMETRY.	19367708 [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 SER-296; SER-298; SER-304AND THR-308, AND MASS SPECTROMETRY.	17242355 [Abstract]
"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-296; SER-298 ANDSER-304, AND MASS SPECTROMETRY.	17114649 [Abstract]