dbPTM

SNTB2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SNTB2_MOUSE
UniProt AC	Q61235
Protein Name	Beta-2-syntrophin
Gene Name	Sntb2
Organism	Mus musculus (Mouse).
Sequence Length	520
Subcellular Localization	Membrane . Cytoplasmic vesicle, secretory vesicle membrane Peripheral membrane protein . Cell junction. Cytoplasm, cytoskeleton . Membrane-associated. In insulinoma cell line, it is enriched in secretory granules (By similarity). In muscle, it is e
Protein Description	Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex. May play a role in the regulation of secretory granules via its interaction with PTPRN (By similarity)..
Protein Sequence	MAVWTRATKAGLVELLLRERWVRVVAELSGESLSLTGDAAAVEPEPPAAAFNGLPNGGGGESLPGSPNRGLGPPSPPAPPRGPAGEASASPPVRRVRVVKQEAGGLGISIKGGRENRMPILISKIFPGLAADQSRALRLGDAILSVNGTDLRQATHDQAVQALKRAGKEVLLEVKFIREVTPYIKKPSLVSDLPWEGASPQSPSFSGSEDSGSPKHQNTTKDRKVIPLKMCFAARNLSMPDLENRLIELHSPDSRNTLILRCKDTATAHSWFVAIHTNIMALLPQVLAELNAMLGATSTAGGSKEVKHIAWLAEQAKLDGGRQQWRPVLMAVTEKDLLLYDCMPWTRDAWASPCHSYPLVATRLVHSGSGCRSPSLGSDLTFATRTGSRQGIEMHLFRVETHRDLSTWTRILVQGCHAAAELIKEVSLGCTLSGQEVRFTVHYEHGFTITRDNGGASSILYRYPFERLKMSADDGIRNLYLDFGGPEGELTMDLHSCPKPIVFVLHTFLSAKVTRMGLLV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
32	Phosphorylation	VAELSGESLSLTGDA HHHHHCCEEEEECCC	27.12	23649490
62	Phosphorylation	PNGGGGESLPGSPNR CCCCCCCCCCCCCCC	43.04	25338131
66	Phosphorylation	GGESLPGSPNRGLGP CCCCCCCCCCCCCCC	19.64	23649490
75	Phosphorylation	NRGLGPPSPPAPPRG CCCCCCCCCCCCCCC	46.80	27087446
88	Phosphorylation	RGPAGEASASPPVRR CCCCCCCCCCCCEEE	25.61	26824392
90	Phosphorylation	PAGEASASPPVRRVR CCCCCCCCCCEEEEE	27.52	27087446
109	Phosphorylation	EAGGLGISIKGGREN CCCCCCEEEECCCCC	19.22	24453211
111	Ubiquitination	GGLGISIKGGRENRM CCCCEEEECCCCCCC	48.82	-
168	Ubiquitination	QALKRAGKEVLLEVK HHHHHCCCCEEEEEE	43.60	-
181	Phosphorylation	VKFIREVTPYIKKPS EEEHHECCCCCCCCC	12.96	26160508
183	Phosphorylation	FIREVTPYIKKPSLV EHHECCCCCCCCCCC	18.92	26160508
188	Phosphorylation	TPYIKKPSLVSDLPW CCCCCCCCCCCCCCC	50.73	21082442
191	Phosphorylation	IKKPSLVSDLPWEGA CCCCCCCCCCCCCCC	38.43	25619855
199	Phosphorylation	DLPWEGASPQSPSFS CCCCCCCCCCCCCCC	34.04	25619855
202	Phosphorylation	WEGASPQSPSFSGSE CCCCCCCCCCCCCCC	26.37	26824392
204	Phosphorylation	GASPQSPSFSGSEDS CCCCCCCCCCCCCCC	36.97	22942356
206	Phosphorylation	SPQSPSFSGSEDSGS CCCCCCCCCCCCCCC	45.83	25168779
208	Phosphorylation	QSPSFSGSEDSGSPK CCCCCCCCCCCCCCC	36.71	21082442
211	Phosphorylation	SFSGSEDSGSPKHQN CCCCCCCCCCCCCCC	36.80	21082442
213	Phosphorylation	SGSEDSGSPKHQNTT CCCCCCCCCCCCCCC	34.43	27087446
238	Phosphorylation	CFAARNLSMPDLENR HHHHCCCCCCHHHHH	31.64	27180971
317	Ubiquitination	AWLAEQAKLDGGRQQ HHHHHHHCCCCCHHC	46.97	-
367	Phosphorylation	VATRLVHSGSGCRSP EEEEEEECCCCCCCC	27.46	21659605
369	Phosphorylation	TRLVHSGSGCRSPSL EEEEECCCCCCCCCC	37.42	26643407
373	Phosphorylation	HSGSGCRSPSLGSDL ECCCCCCCCCCCCCC	23.94	26824392
375	Phosphorylation	GSGCRSPSLGSDLTF CCCCCCCCCCCCCEE	46.76	26824392
378	Phosphorylation	CRSPSLGSDLTFATR CCCCCCCCCCEEEEC	34.44	24068923
381	Phosphorylation	PSLGSDLTFATRTGS CCCCCCCEEEECCCC	19.06	27149854
384	Phosphorylation	GSDLTFATRTGSRQG CCCCEEEECCCCCCC	25.27	20415495

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
75	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
75	S	Phosphorylation	Kinase	CDK5	P49615	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SNTB2_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 SNTB2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SNTB2_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of SNTB2_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-90, AND MASSSPECTROMETRY.	19131326 [Abstract]
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASSSPECTROMETRY.	19144319 [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-90, AND MASSSPECTROMETRY.	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-75 AND SER-90, AND MASSSPECTROMETRY.	17114649 [Abstract]