dbPTM

BAG2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BAG2_HUMAN
UniProt AC	O95816
Protein Name	BAG family molecular chaperone regulator 2
Gene Name	BAG2
Organism	Homo sapiens (Human).
Sequence Length	211
Subcellular Localization
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. [PubMed: 24318877]
Protein Sequence	MAQAKINAKANEGRFCRSSSMADRSSRLLESLDQLELRVEALREAATAVEQEKEILLEMIHSIQNSQDMRQISDGEREELNLTANRLMGRTLTVEVSVETIRNPQQQESLKHATRIIDEVVNKFLDDLGNAKSHLMSLYSACSSEVPHGPVDQKFQSIVIGCALEDQKKIKRRLETLLRNIENSDKAIKLLEHSKGAGSKTLQQNAESRFN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAQAKINAK ------CCCCHHCCC	20.31	22814378
5	Ubiquitination	---MAQAKINAKANE ---CCCCHHCCCCCC	25.14	22817900
5	Acetylation	---MAQAKINAKANE ---CCCCHHCCCCCC	25.14	25953088
9	2-Hydroxyisobutyrylation	AQAKINAKANEGRFC CCCHHCCCCCCCCCC	47.45	-
9	Ubiquitination	AQAKINAKANEGRFC CCCHHCCCCCCCCCC	47.45	27667366
9	Acetylation	AQAKINAKANEGRFC CCCHHCCCCCCCCCC	47.45	25953088
9	Succinylation	AQAKINAKANEGRFC CCCHHCCCCCCCCCC	47.45	23954790
18	Phosphorylation	NEGRFCRSSSMADRS CCCCCCCCHHHHHHH	28.13	30576142
19	Phosphorylation	EGRFCRSSSMADRSS CCCCCCCHHHHHHHH	12.55	23403867
20	Phosphorylation	GRFCRSSSMADRSSR CCCCCCHHHHHHHHH	21.16	26329039
25	Phosphorylation	SSSMADRSSRLLESL CHHHHHHHHHHHHHH	21.98	27050516
26	Phosphorylation	SSMADRSSRLLESLD HHHHHHHHHHHHHHH	28.04	21406692
31	Phosphorylation	RSSRLLESLDQLELR HHHHHHHHHHHHHHH	36.90	29214152
53	Acetylation	ATAVEQEKEILLEMI HHHHHHHHHHHHHHH	50.15	26051181
59	Sulfoxidation	EKEILLEMIHSIQNS HHHHHHHHHHHHHCC	3.18	30846556
69	Sulfoxidation	SIQNSQDMRQISDGE HHHCCHHHHHCCCCC	2.35	30846556
73	Phosphorylation	SQDMRQISDGEREEL CHHHHHCCCCCHHHH	31.09	23401153
78	Ubiquitination	QISDGEREELNLTAN HCCCCCHHHHHHCHH	63.63	27667366
83	Phosphorylation	EREELNLTANRLMGR CHHHHHHCHHHHCCC	22.32	23403867
90	Ubiquitination	TANRLMGRTLTVEVS CHHHHCCCCEEEEEE	16.76	22817900
111	Acetylation	PQQQESLKHATRIID HHHHHHHHHHHHHHH	40.24	19608861
111	Ubiquitination	PQQQESLKHATRIID HHHHHHHHHHHHHHH	40.24	27667366
121	Ubiquitination	TRIIDEVVNKFLDDL HHHHHHHHHHHHHHH	6.41	-
121	Ubiquitination	TRIIDEVVNKFLDDL HHHHHHHHHHHHHHH	6.41	21963094
123	Acetylation	IIDEVVNKFLDDLGN HHHHHHHHHHHHHCC	35.38	26051181
123	Ubiquitination	IIDEVVNKFLDDLGN HHHHHHHHHHHHHCC	35.38	21906983
132	Acetylation	LDDLGNAKSHLMSLY HHHHCCHHHHHHHHH	42.27	26051181
133	Phosphorylation	DDLGNAKSHLMSLYS HHHCCHHHHHHHHHH	21.31	20068231
136	Ubiquitination	GNAKSHLMSLYSACS CCHHHHHHHHHHHHC	1.86	-
136	Sulfoxidation	GNAKSHLMSLYSACS CCHHHHHHHHHHHHC	1.86	30846556
137	Phosphorylation	NAKSHLMSLYSACSS CHHHHHHHHHHHHCC	30.43	20068231
139	Phosphorylation	KSHLMSLYSACSSEV HHHHHHHHHHHCCCC	6.21	20068231
140	Phosphorylation	SHLMSLYSACSSEVP HHHHHHHHHHCCCCC	28.26	20068231
143	Phosphorylation	MSLYSACSSEVPHGP HHHHHHHCCCCCCCC	29.29	20068231
144	Phosphorylation	SLYSACSSEVPHGPV HHHHHHCCCCCCCCC	42.36	20068231
153	Ubiquitination	VPHGPVDQKFQSIVI CCCCCCCHHHHHHHH	49.01	-
153	Ubiquitination	VPHGPVDQKFQSIVI CCCCCCCHHHHHHHH	49.01	23000965
153	Acetylation	VPHGPVDQKFQSIVI CCCCCCCHHHHHHHH	49.01	-
154	Ubiquitination	PHGPVDQKFQSIVIG CCCCCCHHHHHHHHH	40.69	21963094
156	Ubiquitination	GPVDQKFQSIVIGCA CCCCHHHHHHHHHHC	39.00	-
156	Ubiquitination	GPVDQKFQSIVIGCA CCCCHHHHHHHHHHC	39.00	23000965
162	Ubiquitination	FQSIVIGCALEDQKK HHHHHHHHCCCCHHH	2.41	23000965
162	S-nitrosocysteine	FQSIVIGCALEDQKK HHHHHHHHCCCCHHH	2.41	-
162	Ubiquitination	FQSIVIGCALEDQKK HHHHHHHHCCCCHHH	2.41	-
162	S-nitrosylation	FQSIVIGCALEDQKK HHHHHHHHCCCCHHH	2.41	19483679
167	Ubiquitination	IGCALEDQKKIKRRL HHHCCCCHHHHHHHH	39.30	23000965
167	Ubiquitination	IGCALEDQKKIKRRL HHHCCCCHHHHHHHH	39.30	-
168	Acetylation	GCALEDQKKIKRRLE HHCCCCHHHHHHHHH	69.64	26051181
168	Ubiquitination	GCALEDQKKIKRRLE HHCCCCHHHHHHHHH	69.64	32015554
169	Acetylation	CALEDQKKIKRRLET HCCCCHHHHHHHHHH	48.07	7493289
169	Ubiquitination	CALEDQKKIKRRLET HCCCCHHHHHHHHHH	48.07	-
176	Phosphorylation	KIKRRLETLLRNIEN HHHHHHHHHHHHHCC	35.37	23312004
186	Acetylation	RNIENSDKAIKLLEH HHHCCCHHHHHHHHH	52.40	23749302
186	Ubiquitination	RNIENSDKAIKLLEH HHHCCCHHHHHHHHH	52.40	23000965
189	Ubiquitination	ENSDKAIKLLEHSKG CCCHHHHHHHHHCCC	52.45	23000965
189	Acetylation	ENSDKAIKLLEHSKG CCCHHHHHHHHHCCC	52.45	25953088
195	Ubiquitination	IKLLEHSKGAGSKTL HHHHHHCCCCCCHHH	55.47	23000965
195	Acetylation	IKLLEHSKGAGSKTL HHHHHHCCCCCCHHH	55.47	26210075
199	Phosphorylation	EHSKGAGSKTLQQNA HHCCCCCCHHHHHHH	23.18	25262027
200	2-Hydroxyisobutyrylation	HSKGAGSKTLQQNAE HCCCCCCHHHHHHHH	52.95	-
200	Ubiquitination	HSKGAGSKTLQQNAE HCCCCCCHHHHHHHH	52.95	23000965
201	Phosphorylation	SKGAGSKTLQQNAES CCCCCCHHHHHHHHH	31.34	25262027

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
20	S	Phosphorylation	Kinase	MAPK2	P49137	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BAG2_HUMAN !!

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 BAG2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HSP7C_HUMAN	HSPA8	physical	9873016
CHIP_HUMAN	STUB1	physical	16169850
HSP74_HUMAN	HSPA4	physical	16169850
HSP7C_HUMAN	HSPA8	physical	16207813
CHIP_HUMAN	STUB1	physical	16207813
BAG2_HUMAN	BAG2	physical	16207813
PPIH_HUMAN	PPIH	physical	22365833
HSP7C_HUMAN	HSPA8	physical	22365833
SLU7_HUMAN	SLU7	physical	22365833
WDR83_HUMAN	WDR83	physical	22365833
CCAR2_HUMAN	CCAR2	physical	22365833
MEP50_HUMAN	WDR77	physical	22365833
AUXI_HUMAN	DNAJC6	physical	22365833
BAG2_HUMAN	BAG2	physical	22365833
AHNK_HUMAN	AHNAK	physical	22863883
PINK1_HUMAN	PINK1	physical	24383081
PINK1_HUMAN	PINK1	physical	24513209
MLF2_HUMAN	MLF2	physical	25036637
CHIP_HUMAN	STUB1	physical	25036637
STXB2_HUMAN	STXBP2	physical	25036637
DNJB6_HUMAN	DNAJB6	physical	25036637
DNJB1_HUMAN	DNAJB1	physical	25036637
TAB1_HUMAN	TAB1	physical	25036637
BAG2_HUMAN	BAG2	physical	25416956

Drug and Disease Associations

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

Regulatory Network of BAG2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-111, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASSSPECTROMETRY.	18691976 [Abstract]