dbPTM

BAG3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BAG3_MOUSE
UniProt AC	Q9JLV1
Protein Name	BAG family molecular chaperone regulator 3
Gene Name	Bag3
Organism	Mus musculus (Mouse).
Sequence Length	577
Subcellular Localization	Nucleus . Cytoplasm . Colocalizes with HSF1 to the nucleus upon heat stress.
Protein Description	Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. Has anti-apoptotic activity. Plays a role in the HSF1 nucleocytoplasmic transport..
Protein Sequence	MSAATQSPMMQMASGNGASDRDPLPPGWEIKIDPQTGWPFFVDHNSRTTTWNDPRVPPEGPKDTASSANGPSRDGSRLLPIREGHPIYPQLRPGYIPIPVLHEGSENRQPHLFHAYSQPGVQRFRTEAAAATPQRSQSPLRGGMTEAAQTDKQCGQMPATATTAAAQPPTAHGPERSQSPAASDCSSSSSSASLPSSGRSSLGSHQLPRGYIPIPVIHEQNITRPAAQPSFHQAQKTHYPAQQGEYQPQQPVYHKIQGDDWEPRPLRAASPFRSPVRGASSREGSPARSGTPVHCPSPIRVHTVVDRPQPMTHREPPPVTQPENKPESKPGPAGPDLPPGHIPIQVIRREADSKPVSQKSPPPAEKVEVKVSSAPIPCPSPSPAPSAVPSPPKNVAAEQKAAPSPAPAEPAAPKSGEAETPPKHPGVLKVEAILEKVQGLEQAVDSFEGKKTDKKYLMIEEYLTKELLALDSVDPEGRADVRQARRDGVRKVQTILEKLEQKAIDVPGQVQVYELQPSNLEAEQPLQEIMGAVVADKDKKGPENKDPQTESQQLEAKAATPPNPSNPADSAGNLVAP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSAATQSPM ------CCCCCCCCC	26.98	-
116	Phosphorylation	QPHLFHAYSQPGVQR CCCEEEECCCCCHHH	10.16	19060867
117	Phosphorylation	PHLFHAYSQPGVQRF CCEEEECCCCCHHHH	30.59	25521595
123	Dimethylation	YSQPGVQRFRTEAAA CCCCCHHHHHHHHHH	22.17	-
126	Phosphorylation	PGVQRFRTEAAAATP CCHHHHHHHHHHCCC	27.54	23984901
132	Phosphorylation	RTEAAAATPQRSQSP HHHHHHCCCCCCCCC	18.41	24453211
136	Phosphorylation	AAATPQRSQSPLRGG HHCCCCCCCCCCCCC	29.75	25521595
138	Phosphorylation	ATPQRSQSPLRGGMT CCCCCCCCCCCCCCC	27.44	25521595
141	Methylation	QRSQSPLRGGMTEAA CCCCCCCCCCCCHHH	42.90	24129315
145	Phosphorylation	SPLRGGMTEAAQTDK CCCCCCCCHHHHHHH	26.25	25619855
150	Phosphorylation	GMTEAAQTDKQCGQM CCCHHHHHHHHCCCC	40.20	25619855
154	S-nitrosocysteine	AAQTDKQCGQMPATA HHHHHHHCCCCCCCC	5.14	-
154	S-nitrosylation	AAQTDKQCGQMPATA HHHHHHHCCCCCCCC	5.14	21278135
160	Phosphorylation	QCGQMPATATTAAAQ HCCCCCCCCCHHHCC	20.75	26160508
162	Phosphorylation	GQMPATATTAAAQPP CCCCCCCCHHHCCCC	16.77	26160508
163	O-linked_Glycosylation	QMPATATTAAAQPPT CCCCCCCHHHCCCCC	16.31	30059200
163	Phosphorylation	QMPATATTAAAQPPT CCCCCCCHHHCCCCC	16.31	26160508
170	Phosphorylation	TAAAQPPTAHGPERS HHHCCCCCCCCCCCC	37.66	25777480
177	Phosphorylation	TAHGPERSQSPAASD CCCCCCCCCCCCCCC	33.09	27087446
179	Phosphorylation	HGPERSQSPAASDCS CCCCCCCCCCCCCCC	20.11	25521595
183	Phosphorylation	RSQSPAASDCSSSSS CCCCCCCCCCCCCCC	41.05	25521595
185	S-nitrosocysteine	QSPAASDCSSSSSSA CCCCCCCCCCCCCCC	3.83	-
185	S-nitrosylation	QSPAASDCSSSSSSA CCCCCCCCCCCCCCC	3.83	21278135
186	Phosphorylation	SPAASDCSSSSSSAS CCCCCCCCCCCCCCC	37.94	27742792
187	Phosphorylation	PAASDCSSSSSSASL CCCCCCCCCCCCCCC	40.34	25619855
188	Phosphorylation	AASDCSSSSSSASLP CCCCCCCCCCCCCCC	20.25	25619855
189	O-linked_Glycosylation	ASDCSSSSSSASLPS CCCCCCCCCCCCCCC	30.20	30059200
189	Phosphorylation	ASDCSSSSSSASLPS CCCCCCCCCCCCCCC	30.20	25619855
190	Phosphorylation	SDCSSSSSSASLPSS CCCCCCCCCCCCCCC	31.69	25619855
191	Phosphorylation	DCSSSSSSASLPSSG CCCCCCCCCCCCCCC	24.67	25619855
193	Phosphorylation	SSSSSSASLPSSGRS CCCCCCCCCCCCCCC	42.64	25619855
196	Phosphorylation	SSSASLPSSGRSSLG CCCCCCCCCCCCCCC	51.20	25619855
197	Phosphorylation	SSASLPSSGRSSLGS CCCCCCCCCCCCCCC	35.96	25619855
200	Phosphorylation	SLPSSGRSSLGSHQL CCCCCCCCCCCCCCC	33.18	27742792
201	Phosphorylation	LPSSGRSSLGSHQLP CCCCCCCCCCCCCCC	35.07	26824392
204	Phosphorylation	SGRSSLGSHQLPRGY CCCCCCCCCCCCCCE	17.22	24453211
211	Phosphorylation	SHQLPRGYIPIPVIH CCCCCCCEECCCEEE	12.56	29514104
230	Phosphorylation	TRPAAQPSFHQAQKT CCCCCCCCHHHHHHH	24.23	29514104
246	Phosphorylation	YPAQQGEYQPQQPVY CCCCCCCCCCCCCCE	32.11	22817900
253	Phosphorylation	YQPQQPVYHKIQGDD CCCCCCCEEECCCCC	12.22	20116462
255	Ubiquitination	PQQPVYHKIQGDDWE CCCCCEEECCCCCCC	21.02	-
264	Dimethylation	QGDDWEPRPLRAASP CCCCCCCCCCCCCCC	31.22	-
267	Methylation	DWEPRPLRAASPFRS CCCCCCCCCCCCCCC	30.69	24129315
270	Phosphorylation	PRPLRAASPFRSPVR CCCCCCCCCCCCCCC	24.48	27087446
274	Phosphorylation	RAASPFRSPVRGASS CCCCCCCCCCCCCCC	28.29	27087446
277	Methylation	SPFRSPVRGASSREG CCCCCCCCCCCCCCC	38.04	-
280	Phosphorylation	RSPVRGASSREGSPA CCCCCCCCCCCCCCC	32.52	23684622
281	Phosphorylation	SPVRGASSREGSPAR CCCCCCCCCCCCCCC	33.54	27087446
285	Phosphorylation	GASSREGSPARSGTP CCCCCCCCCCCCCCC	15.61	27087446
289	Phosphorylation	REGSPARSGTPVHCP CCCCCCCCCCCCCCC	49.47	27742792
291	Phosphorylation	GSPARSGTPVHCPSP CCCCCCCCCCCCCCC	24.31	25521595
295	Glutathionylation	RSGTPVHCPSPIRVH CCCCCCCCCCCCEEE	3.48	24333276
295	S-palmitoylation	RSGTPVHCPSPIRVH CCCCCCCCCCCCEEE	3.48	26165157
297	Phosphorylation	GTPVHCPSPIRVHTV CCCCCCCCCCEEEEE	38.05	25521595
312	Phosphorylation	VDRPQPMTHREPPPV CCCCCCCCCCCCCCC	25.19	-
320	Phosphorylation	HREPPPVTQPENKPE CCCCCCCCCCCCCCC	44.15	-
328	Phosphorylation	QPENKPESKPGPAGP CCCCCCCCCCCCCCC	53.32	-
353	Phosphorylation	VIRREADSKPVSQKS EEECHHCCCCCCCCC	46.00	26824392
357	Phosphorylation	EADSKPVSQKSPPPA HHCCCCCCCCCCCCH	40.18	26824392
360	Phosphorylation	SKPVSQKSPPPAEKV CCCCCCCCCCCHHHE	34.69	26824392
366	Acetylation	KSPPPAEKVEVKVSS CCCCCHHHEEEEEEC	45.89	23806337
372	Phosphorylation	EKVEVKVSSAPIPCP HHEEEEEECCCCCCC	18.31	25619855
372	O-linked_Glycosylation	EKVEVKVSSAPIPCP HHEEEEEECCCCCCC	18.31	30059200
373	Phosphorylation	KVEVKVSSAPIPCPS HEEEEEECCCCCCCC	40.84	25619855
373	O-linked_Glycosylation	KVEVKVSSAPIPCPS HEEEEEECCCCCCCC	40.84	30059200
378	S-nitrosylation	VSSAPIPCPSPSPAP EECCCCCCCCCCCCC	5.58	21278135
378	S-nitrosocysteine	VSSAPIPCPSPSPAP EECCCCCCCCCCCCC	5.58	-
380	Phosphorylation	SAPIPCPSPSPAPSA CCCCCCCCCCCCCCC	44.73	26824392
382	Phosphorylation	PIPCPSPSPAPSAVP CCCCCCCCCCCCCCC	37.72	25521595
386	Phosphorylation	PSPSPAPSAVPSPPK CCCCCCCCCCCCCCC	43.96	27742792
390	Phosphorylation	PAPSAVPSPPKNVAA CCCCCCCCCCCCCCH	47.43	26824392
404	Phosphorylation	AEQKAAPSPAPAEPA HHHCCCCCCCCCCCC	29.03	25521595
415	Phosphorylation	AEPAAPKSGEAETPP CCCCCCCCCCCCCCC	40.58	23684622
420	Phosphorylation	PKSGEAETPPKHPGV CCCCCCCCCCCCCCC	52.52	26824392
450	Ubiquitination	AVDSFEGKKTDKKYL HHHHCCCCCCCCCEE	45.35	27667366
455	Ubiquitination	EGKKTDKKYLMIEEY CCCCCCCCEEHHHHH	46.56	-
456	Phosphorylation	GKKTDKKYLMIEEYL CCCCCCCEEHHHHHH	13.77	18779572
462	Phosphorylation	KYLMIEEYLTKELLA CEEHHHHHHHHHHHH	13.59	18779572
551	Phosphorylation	NKDPQTESQQLEAKA CCCCCHHHHHHHHHH	26.98	27841257
560	Phosphorylation	QLEAKAATPPNPSNP HHHHHHCCCCCCCCC	44.10	25521595
565	Phosphorylation	AATPPNPSNPADSAG HCCCCCCCCCCCCCC	63.18	26824392
570	Phosphorylation	NPSNPADSAGNLVAP CCCCCCCCCCCCCCC	39.93	25619855

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 BAG3_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BAG3_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 BAG3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HS71B_MOUSE	Hspa1b	physical	11527400
HSP7C_MOUSE	Hspa8	physical	20884878
CAZA1_MOUSE	Capza1	physical	20884878
CAPZB_MOUSE	Capzb	physical	20884878

Drug and Disease Associations

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

Regulatory Network of BAG3_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-390, AND MASSSPECTROMETRY.	19131326 [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-297, AND MASSSPECTROMETRY.	17242355 [Abstract]