dbPTM

BAG6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BAG6_HUMAN
UniProt AC	P46379
Protein Name	Large proline-rich protein BAG6 {ECO:0000305}
Gene Name	BAG6 {ECO:0000312\|HGNC:HGNC:13919}
Organism	Homo sapiens (Human).
Sequence Length	1132
Subcellular Localization	Cytoplasm, cytosol . Nucleus . Secreted, exosome . Normally localized in cytosol and nucleus, it can also be released extracellularly, in exosomes, by tumor and myeloid dendritic cells (PubMed:18055229, PubMed:18852879). Cytoplasmic retention is due
Protein Description	ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. [PubMed: 21636303 Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates to their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation]
Protein Sequence	MEPNDSTSTAVEEPDSLEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVGGKVIHLVERAPPQTHLPSGASSGTGSASATHGGGSPPGTRGPGASVHDRNANSYVMVGTFNLPSDGSAVDVHINMEQAPIQSEPRVRLVMAQHMIRDIQTLLSRMETLPYLQCRGGPQPQHSQPPPQPPAVTPEPVALSSQTSEPVESEAPPREPMEAEEVEERAPAQNPELTPGPAPAGPTPAPETNAPNHPSPAEYVEVLQELQRLESRLQPFLQRYYEVLGAAATTDYNNNHEGREEDQRLINLVGESLRLLGNTFVALSDLRCNLACTPPRHLHVVRPMSHYTTPMVLQQAAIPIQINVGTTVTMTGNGTRPPPTPNAEAPPPGPGQASSVAPSSTNVESSAEGAPPPGPAPPPATSHPRVIRISHQSVEPVVMMHMNIQDSGTQPGGVPSAPTGPLGPPGHGQTLGQQVPGFPTAPTRVVIARPTPPQARPSHPGGPPVSGTLQGAGLGTNASLAQMVSGLVGQLLMQPVLVAQGTPGMAPPPAPATASASAGTTNTATTAGPAPGGPAQPPPTPQPSMADLQFSQLLGNLLGPAGPGAGGSGVASPTITVAMPGVPAFLQGMTDFLQATQTAPPPPPPPPPPPPAPEQQTMPPPGSPSGGAGSPGGLGLESLSPEFFTSVVQGVLSSLLGSLGARAGSSESIAAFIQRLSGSSNIFEPGADGALGFFGALLSLLCQNFSMVDVVMLLHGHFQPLQRLQPQLRSFFHQHYLGGQEPTPSNIRMATHTLITGLEEYVRESFSLVQVQPGVDIIRTNLEFLQEQFNSIAAHVLHCTDSGFGARLLELCNQGLFECLALNLHCLGGQQMELAAVINGRIRRMSRGVNPSLVSWLTTMMGLRLQVVLEHMPVGPDAILRYVRRVGDPPQPLPEEPMEVQGAERASPEPQRENASPAPGTTAEEAMSRGPPPAPEGGSRDEQDGASAETEPWAAAVPPEWVPIIQQDIQSQRKVKPQPPLSDAYLSGMPAKRRKTMQGEGPQLLLSEAVSRAAKAAGARPLTSPESLSRDLEAPEVQESYRQQLRSDIQKRLQEDPNYSPQRFPNAQRAFADDP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEPNDSTS -------CCCCCCCC	63.54	19413330
6	Phosphorylation	--MEPNDSTSTAVEE --CCCCCCCCCCCCC	30.78	20068231
7	Phosphorylation	-MEPNDSTSTAVEEP -CCCCCCCCCCCCCC	32.72	20068231
8	Phosphorylation	MEPNDSTSTAVEEPD CCCCCCCCCCCCCCC	20.51	20068231
9	Phosphorylation	EPNDSTSTAVEEPDS CCCCCCCCCCCCCCC	34.51	20068231
16	Phosphorylation	TAVEEPDSLEVLVKT CCCCCCCCCHHHHHH	36.83	27251275
22	Ubiquitination	DSLEVLVKTLDSQTR CCCHHHHHHCCCCCC	38.93	21890473
22	Ubiquitination	DSLEVLVKTLDSQTR CCCHHHHHHCCCCCC	38.93	21890473
22	Ubiquitination	DSLEVLVKTLDSQTR CCCHHHHHHCCCCCC	38.93	21890473
22	Ubiquitination	DSLEVLVKTLDSQTR CCCHHHHHHCCCCCC	38.93	21890473
22 (in isoform 1)	Ubiquitination	-	38.93	21890473
22 (in isoform 2)	Ubiquitination	-	38.93	21890473
22 (in isoform 3)	Ubiquitination	-	38.93	21890473
26	Phosphorylation	VLVKTLDSQTRTFIV HHHHHCCCCCCEEEE	36.24	17478428
30	Phosphorylation	TLDSQTRTFIVGAQM HCCCCCCEEEEEEEE	22.54	25690035
40	Ubiquitination	VGAQMNVKEFKEHIA EEEEECHHHHHHHHH	53.05	21890473
40	Ubiquitination	VGAQMNVKEFKEHIA EEEEECHHHHHHHHH	53.05	21890473
40	Ubiquitination	VGAQMNVKEFKEHIA EEEEECHHHHHHHHH	53.05	21890473
40	Ubiquitination	VGAQMNVKEFKEHIA EEEEECHHHHHHHHH	53.05	21890473
40 (in isoform 1)	Ubiquitination	-	53.05	21890473
40 (in isoform 2)	Ubiquitination	-	53.05	21890473
40 (in isoform 3)	Ubiquitination	-	53.05	21890473
56	Ubiquitination	SVSIPSEKQRLIYQG HCCCCHHHHHHHEEC	45.09	21890473
56	Ubiquitination	SVSIPSEKQRLIYQG HCCCCHHHHHHHEEC	45.09	21890473
56	Ubiquitination	SVSIPSEKQRLIYQG HCCCCHHHHHHHEEC	45.09	21890473
56	Acetylation	SVSIPSEKQRLIYQG HCCCCHHHHHHHEEC	45.09	20167786
56	Ubiquitination	SVSIPSEKQRLIYQG HCCCCHHHHHHHEEC	45.09	21890473
56 (in isoform 1)	Ubiquitination	-	45.09	21890473
56 (in isoform 2)	Ubiquitination	-	45.09	21890473
56 (in isoform 3)	Ubiquitination	-	45.09	21890473
70	2-Hydroxyisobutyrylation	GRVLQDDKKLQEYNV CEECCCCHHHEEEEC	64.77	-
70	Acetylation	GRVLQDDKKLQEYNV CEECCCCHHHEEEEC	64.77	25953088
70	Ubiquitination	GRVLQDDKKLQEYNV CEECCCCHHHEEEEC	64.77	-
71	Ubiquitination	RVLQDDKKLQEYNVG EECCCCHHHEEEECC	63.50	-
75	Phosphorylation	DDKKLQEYNVGGKVI CCHHHEEEECCCEEE	11.37	28152594
80	Ubiquitination	QEYNVGGKVIHLVER EEEECCCEEEEEEEC	31.89	21890473
80	Ubiquitination	QEYNVGGKVIHLVER EEEECCCEEEEEEEC	31.89	21890473
80	Ubiquitination	QEYNVGGKVIHLVER EEEECCCEEEEEEEC	31.89	21890473
80	Ubiquitination	QEYNVGGKVIHLVER EEEECCCEEEEEEEC	31.89	21890473
80 (in isoform 1)	Ubiquitination	-	31.89	21890473
80 (in isoform 2)	Ubiquitination	-	31.89	21890473
80 (in isoform 3)	Ubiquitination	-	31.89	21890473
92	Phosphorylation	VERAPPQTHLPSGAS EECCCCCCCCCCCCC	31.02	23927012
96	Phosphorylation	PPQTHLPSGASSGTG CCCCCCCCCCCCCCC	54.04	22167270
99	Phosphorylation	THLPSGASSGTGSAS CCCCCCCCCCCCCCC	32.59	30266825
100	Phosphorylation	HLPSGASSGTGSASA CCCCCCCCCCCCCCC	39.58	30266825
102	Phosphorylation	PSGASSGTGSASATH CCCCCCCCCCCCCCC	29.88	30266825
104	Phosphorylation	GASSGTGSASATHGG CCCCCCCCCCCCCCC	20.91	22167270
106	Phosphorylation	SSGTGSASATHGGGS CCCCCCCCCCCCCCC	35.08	29255136
108	Phosphorylation	GTGSASATHGGGSPP CCCCCCCCCCCCCCC	20.68	22167270
113	Phosphorylation	SATHGGGSPPGTRGP CCCCCCCCCCCCCCC	31.06	29255136
117	Phosphorylation	GGGSPPGTRGPGASV CCCCCCCCCCCCCCC	37.92	22167270
123	Phosphorylation	GTRGPGASVHDRNAN CCCCCCCCCCCCCCC	26.37	23401153
178	Phosphorylation	HMIRDIQTLLSRMET HHHHHHHHHHHHHHH	29.96	21406692
181	Phosphorylation	RDIQTLLSRMETLPY HHHHHHHHHHHHCCC	32.47	21406692
181 (in isoform 2)	Phosphorylation	-	32.47	22817900
181 (in isoform 3)	Phosphorylation	-	32.47	22817900
181 (in isoform 4)	Phosphorylation	-	32.47	22817900
181 (in isoform 5)	Phosphorylation	-	32.47	22817900
185	Phosphorylation	TLLSRMETLPYLQCR HHHHHHHHCCCCCCC	24.56	22210691
200	Phosphorylation	GGPQPQHSQPPPQPP CCCCCCCCCCCCCCC	38.85	25850435
210	Phosphorylation	PPQPPAVTPEPVALS CCCCCCCCCCCEECC	24.84	25850435
217	Phosphorylation	TPEPVALSSQTSEPV CCCCEECCCCCCCCC	15.63	25850435
218	Phosphorylation	PEPVALSSQTSEPVE CCCEECCCCCCCCCC	38.02	17478428
220	Phosphorylation	PVALSSQTSEPVESE CEECCCCCCCCCCCC	36.68	25850435
221	Phosphorylation	VALSSQTSEPVESEA EECCCCCCCCCCCCC	32.06	25850435
251	Phosphorylation	PAQNPELTPGPAPAG CCCCCCCCCCCCCCC	25.25	29496963
260	O-linked_Glycosylation	GPAPAGPTPAPETNA CCCCCCCCCCCCCCC	31.03	OGP
260	Phosphorylation	GPAPAGPTPAPETNA CCCCCCCCCCCCCCC	31.03	25332170
265	Phosphorylation	GPTPAPETNAPNHPS CCCCCCCCCCCCCCC	35.30	25332170
329	Phosphorylation	LINLVGESLRLLGNT HHHHHHHHHHHHCCC	16.92	21601212
341	Phosphorylation	GNTFVALSDLRCNLA CCCEEEHHHCCCCCC	25.51	24719451
344	Methylation	FVALSDLRCNLACTP EEEHHHCCCCCCCCC	16.56	-
350	Phosphorylation	LRCNLACTPPRHLHV CCCCCCCCCCCEEEE	30.62	22617229
508	Phosphorylation	RVVIARPTPPQARPS EEEEECCCCCCCCCC	41.89	26270265
697	Phosphorylation	GLGLESLSPEFFTSV CCCHHHCCHHHHHHH	31.49	-
722	Phosphorylation	SLGARAGSSESIAAF HHHHCCCCHHHHHHH	29.92	25693802
723	Phosphorylation	LGARAGSSESIAAFI HHHCCCCHHHHHHHH	34.15	25693802
725	Phosphorylation	ARAGSSESIAAFIQR HCCCCHHHHHHHHHH	21.34	25693802
806	Sulfoxidation	PTPSNIRMATHTLIT CCHHHHHHHHHHHHH	4.46	28183972
818	Phosphorylation	LITGLEEYVRESFSL HHHCHHHHHHHHCCE	8.74	22817900
832 (in isoform 4)	Phosphorylation	-	6.42	23663014
915	Phosphorylation	PSLVSWLTTMMGLRL HHHHHHHHHHHHHHH	13.34	-
955	Sulfoxidation	QPLPEEPMEVQGAER CCCCCCCCCCCCCCC	9.97	30846556
964	Phosphorylation	VQGAERASPEPQREN CCCCCCCCCCCCCCC	35.70	29255136
973	Phosphorylation	EPQRENASPAPGTTA CCCCCCCCCCCCCCH	32.93	19664994
978	Phosphorylation	NASPAPGTTAEEAMS CCCCCCCCCHHHHHH	23.05	22167270
979	Phosphorylation	ASPAPGTTAEEAMSR CCCCCCCCHHHHHHC	37.68	22167270
984	Sulfoxidation	GTTAEEAMSRGPPPA CCCHHHHHHCCCCCC	2.95	21406390
985	Phosphorylation	TTAEEAMSRGPPPAP CCHHHHHHCCCCCCC	40.93	30278072
996	Phosphorylation	PPAPEGGSRDEQDGA CCCCCCCCCCCCCCC	47.63	28176443
1027 (in isoform 2)	Ubiquitination	-	41.63	21890473
1033	Acetylation	IQSQRKVKPQPPLSD HHHCCCCCCCCCCCH	40.76	26051181
1033	Ubiquitination	IQSQRKVKPQPPLSD HHHCCCCCCCCCCCH	40.76	21906983
1033 (in isoform 1)	Ubiquitination	-	40.76	21890473
1039	Phosphorylation	VKPQPPLSDAYLSGM CCCCCCCCHHHHCCC	26.43	19060867
1042	Phosphorylation	QPPLSDAYLSGMPAK CCCCCHHHHCCCCCC	13.34	19060867
1043	Ubiquitination	PPLSDAYLSGMPAKR CCCCHHHHCCCCCCC	3.70	21890473
1043 (in isoform 2)	Ubiquitination	-	3.70	21890473
1044	Phosphorylation	PLSDAYLSGMPAKRR CCCHHHHCCCCCCCC	21.99	28555341
1046	Ubiquitination	SDAYLSGMPAKRRKT CHHHHCCCCCCCCCC	2.34	21890473
1046 (in isoform 2)	Ubiquitination	-	2.34	21890473
1049	Ubiquitination	YLSGMPAKRRKTMQG HHCCCCCCCCCCCCC	47.03	21890473
1049	Acetylation	YLSGMPAKRRKTMQG HHCCCCCCCCCCCCC	47.03	25953088
1049	Ubiquitination	YLSGMPAKRRKTMQG HHCCCCCCCCCCCCC	47.03	21890473
1049 (in isoform 1)	Ubiquitination	-	47.03	21890473
1049 (in isoform 5)	Phosphorylation	-	47.03	27251275
1052	Ubiquitination	GMPAKRRKTMQGEGP CCCCCCCCCCCCCCH	53.00	21890473
1052	Ubiquitination	GMPAKRRKTMQGEGP CCCCCCCCCCCCCCH	53.00	21890473
1052 (in isoform 1)	Ubiquitination	-	53.00	21890473
1053	Phosphorylation	MPAKRRKTMQGEGPQ CCCCCCCCCCCCCHH	16.96	25159151
1063 (in isoform 3)	Ubiquitination	-	6.22	21890473
1064	Phosphorylation	EGPQLLLSEAVSRAA CCHHHHHHHHHHHHH	24.39	-
1072	Ubiquitination	EAVSRAAKAAGARPL HHHHHHHHHCCCCCC	37.47	-
1079 (in isoform 3)	Ubiquitination	-	6.54	21890473
1080	Phosphorylation	AAGARPLTSPESLSR HCCCCCCCCHHHHHH	44.94	23401153
1081	Phosphorylation	AGARPLTSPESLSRD CCCCCCCCHHHHHHC	34.06	19664994
1082 (in isoform 3)	Ubiquitination	-	29.93	21890473
1084	Phosphorylation	RPLTSPESLSRDLEA CCCCCHHHHHHCCCC	34.72	23927012
1086	Phosphorylation	LTSPESLSRDLEAPE CCCHHHHHHCCCCHH	32.78	23927012
1104	Phosphorylation	SYRQQLRSDIQKRLQ HHHHHHHHHHHHHHH	47.89	27251275
1116	Phosphorylation	RLQEDPNYSPQRFPN HHHHCCCCCCCCCCC	27.41	21945579
1117	Phosphorylation	LQEDPNYSPQRFPNA HHHCCCCCCCCCCCH	22.61	19664994
1146 (in isoform 3)	Phosphorylation	-		27642862

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
26	S	Phosphorylation	Kinase	ATM	Q13315	PSP
218	S	Phosphorylation	Kinase	ATM	Q13315	PSP
1080	T	Phosphorylation	Kinase	ICK	Q9UPZ9	PSP
1080	T	Phosphorylation	Kinase	MLTK	Q9NYL2	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BAG6_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 BAG6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FBLN4_HUMAN	EFEMP2	physical	16189514
KLH12_HUMAN	KLHL12	physical	16189514
RCN2_HUMAN	RCN2	physical	16169070
MIC60_HUMAN	IMMT	physical	16169070
ELP1_HUMAN	IKBKAP	physical	16169070
SETB1_HUMAN	SETDB1	physical	16169070
NBL1_HUMAN	NBL1	physical	10390159
CTCFL_HUMAN	CTCFL	physical	18765639
PCKGC_HUMAN	PCK1	physical	21726808
APLP2_HUMAN	APLP2	physical	22641691
DOT1L_HUMAN	DOT1L	physical	22373577
H32_HUMAN	HIST2H3C	physical	22373577
AMFR_HUMAN	AMFR	physical	21636303
TERA_HUMAN	VCP	physical	21636303
UBL4A_HUMAN	UBL4A	physical	21636303
UBL4A_HUMAN	UBL4A	physical	20676083
S61A1_HUMAN	SEC61A1	physical	20676083
VAMP2_HUMAN	VAMP2	physical	20676083
STX5_HUMAN	STX5	physical	20676083
AIFM1_HUMAN	AIFM1	physical	18056262
AMFR_HUMAN	AMFR	physical	23246001
FAF2_HUMAN	FAF2	physical	23246001
HAVR2_HUMAN	HAVCR2	physical	22863785
SGTA_HUMAN	SGTA	physical	23246001
UBL4A_HUMAN	UBL4A	physical	23246001
SGTA_HUMAN	SGTA	physical	23533635
FAF2_HUMAN	FAF2	physical	23665563
GET4_HUMAN	GET4	physical	23665563
TERA_HUMAN	VCP	physical	23665563
BAG6_HUMAN	BAG6	physical	23665563
TNR6_HUMAN	FAS	physical	21988832
OSTP_HUMAN	SPP1	physical	21988832
CLUS_HUMAN	CLU	physical	21988832
IC1_HUMAN	SERPING1	physical	21988832
C1QA_HUMAN	C1QA	physical	21988832
CDN1A_HUMAN	CDKN1A	physical	21988832
IL8_HUMAN	CXCL8	physical	21988832
LBP_HUMAN	LBP	physical	21988832
NPY_HUMAN	NPY	physical	21988832
RPB11_HUMAN	POLR2J	physical	21988832
PTN_HUMAN	PTN	physical	21988832
SDC2_HUMAN	SDC2	physical	21988832
HSP13_HUMAN	HSPA13	physical	21988832
P63_HUMAN	TP63	physical	21988832
C1QR1_HUMAN	CD93	physical	21988832
ANM2_HUMAN	PRMT2	physical	23455924
ASNA_HUMAN	ASNA1	physical	22863883
EF1D_HUMAN	EEF1D	physical	22863883
PP4C_HUMAN	PPP4C	physical	22863883
WDHD1_HUMAN	WDHD1	physical	22863883
1A02_HUMAN	HLA-A	physical	21636303
1A03_HUMAN	HLA-A	physical	21636303
1A01_HUMAN	HLA-A	physical	21636303
1A26_HUMAN	HLA-A	physical	21636303
OPSD_BOVIN	RHO	physical	24806960
LCK_HUMAN	LCK	physical	22863785
BAG6_HUMAN	BAG6	physical	24133212
NCTR3_HUMAN	NCR3	physical	24133212
SED5_YEAST	SED5	physical	20516149
RN126_HUMAN	RNF126	physical	25416956
KLH12_HUMAN	KLHL12	physical	25416956
FAM9B_HUMAN	FAM9B	physical	25416956
SGTA_HUMAN	SGTA	physical	25415308
UBP13_HUMAN	USP13	physical	24424410
UBL4A_HUMAN	UBL4A	physical	25713138
UBL4A_HUMAN	UBL4A	physical	24581120
RPN1_HUMAN	RPN1	physical	24594942
BLMH_HUMAN	BLMH	physical	26496610
CALU_HUMAN	CALU	physical	26496610
ICAL_HUMAN	CAST	physical	26496610
CDN2A_HUMAN	CDKN2A	physical	26496610
ARF_HUMAN	CDKN2A	physical	26496610
CRY1_HUMAN	CRY1	physical	26496610
ECHM_HUMAN	ECHS1	physical	26496610
ERF1_HUMAN	ETF1	physical	26496610
FACD2_HUMAN	FANCD2	physical	26496610
MTOR_HUMAN	MTOR	physical	26496610
GOGA1_HUMAN	GOLGA1	physical	26496610
T2FB_HUMAN	GTF2F2	physical	26496610
HEXA_HUMAN	HEXA	physical	26496610
ITB4_HUMAN	ITGB4	physical	26496610
TAU_HUMAN	MAPT	physical	26496610
M3K4_HUMAN	MAP3K4	physical	26496610
NHS_HUMAN	NHS	physical	26496610
NOP2_HUMAN	NOP2	physical	26496610
YBOX1_HUMAN	YBX1	physical	26496610
FURIN_HUMAN	FURIN	physical	26496610
PHLP_HUMAN	PDCL	physical	26496610
KPB2_HUMAN	PHKA2	physical	26496610
PRI2_HUMAN	PRIM2	physical	26496610
PTMA_HUMAN	PTMA	physical	26496610
PWP2_HUMAN	PWP2	physical	26496610
RET_HUMAN	RET	physical	26496610
SRSF2_HUMAN	SRSF2	physical	26496610
UAP1_HUMAN	UAP1	physical	26496610
TARB1_HUMAN	TARBP1	physical	26496610
TCOF_HUMAN	TCOF1	physical	26496610
ICAM5_HUMAN	ICAM5	physical	26496610
TLN1_HUMAN	TLN1	physical	26496610
UBP1_HUMAN	USP1	physical	26496610
UBL4A_HUMAN	UBL4A	physical	26496610
RAD54_HUMAN	RAD54L	physical	26496610
KCAB2_HUMAN	KCNAB2	physical	26496610
EIF3H_HUMAN	EIF3H	physical	26496610
MTA1_HUMAN	MTA1	physical	26496610
PTTG1_HUMAN	PTTG1	physical	26496610
CIP4_HUMAN	TRIP10	physical	26496610
GT2D1_HUMAN	GTF2IRD1	physical	26496610
C2CD5_HUMAN	C2CD5	physical	26496610
NPA1P_HUMAN	URB1	physical	26496610
OSBL2_HUMAN	OSBPL2	physical	26496610
OXSR1_HUMAN	OXSR1	physical	26496610
UBP15_HUMAN	USP15	physical	26496610
CEBPZ_HUMAN	CEBPZ	physical	26496610
VPP3_HUMAN	TCIRG1	physical	26496610
TBB3_HUMAN	TUBB3	physical	26496610
LTOR5_HUMAN	LAMTOR5	physical	26496610
RPC6_HUMAN	POLR3F	physical	26496610
CNTRL_HUMAN	CNTRL	physical	26496610
TARA_HUMAN	TRIOBP	physical	26496610
FND3A_HUMAN	FNDC3A	physical	26496610
RRP5_HUMAN	PDCD11	physical	26496610
WDFY3_HUMAN	WDFY3	physical	26496610
CNOT1_HUMAN	CNOT1	physical	26496610
RRP1B_HUMAN	RRP1B	physical	26496610
SIR5_HUMAN	SIRT5	physical	26496610
MACF1_HUMAN	MACF1	physical	26496610
MYOF_HUMAN	MYOF	physical	26496610
WDR91_HUMAN	WDR91	physical	26496610
PLPL8_HUMAN	PNPLA8	physical	26496610
CHMP5_HUMAN	CHMP5	physical	26496610
SIR6_HUMAN	SIRT6	physical	26496610
GET4_HUMAN	GET4	physical	26496610
PPIL3_HUMAN	PPIL3	physical	26496610
XRN1_HUMAN	XRN1	physical	26496610
PALMD_HUMAN	PALMD	physical	26496610
URFB1_HUMAN	UHRF1BP1	physical	26496610
UACA_HUMAN	UACA	physical	26496610
CEP55_HUMAN	CEP55	physical	26496610
DNJA4_HUMAN	DNAJA4	physical	26496610
PLXA3_HUMAN	PLXNA3	physical	26496610
RN126_HUMAN	RNF126	physical	26496610
BI2L1_HUMAN	BAIAP2L1	physical	26496610
P4R3B_HUMAN	SMEK2	physical	26496610
Z286A_HUMAN	ZNF286A	physical	26496610
UVSSA_HUMAN	UVSSA	physical	26496610
ENOPH_HUMAN	ENOPH1	physical	26496610
RM17_HUMAN	MRPL17	physical	26496610
DEFM_HUMAN	PDF	physical	26496610
IPO4_HUMAN	IPO4	physical	26496610
SEN2_HUMAN	TSEN2	physical	26496610
MTMRD_HUMAN	SBF2	physical	26496610
ASCC2_HUMAN	ASCC2	physical	26496610
WDR83_HUMAN	WDR83	physical	26496610
MYPN_HUMAN	MYPN	physical	26496610
UBP32_HUMAN	USP32	physical	26496610
ARP8_HUMAN	ACTR8	physical	26496610
RAVR1_HUMAN	RAVER1	physical	26496610
RM55_HUMAN	MRPL55	physical	26496610
PDE12_HUMAN	PDE12	physical	26496610
REEP3_HUMAN	REEP3	physical	26496610
UBXN1_HUMAN	UBXN1	physical	26389662
GET4_HUMAN	GET4	physical	24981174
UBL4A_HUMAN	UBL4A	physical	24981174
ASNA_HUMAN	ASNA1	physical	24981174
HUWE1_HUMAN	HUWE1	physical	24981174
UBR5_HUMAN	UBR5	physical	24981174
UBR3_HUMAN	UBR3	physical	24981174
UBR2_HUMAN	UBR2	physical	24981174
RN123_HUMAN	RNF123	physical	24981174
WWP2_HUMAN	WWP2	physical	24981174
HECD3_HUMAN	HECTD3	physical	24981174
RNF12_HUMAN	RLIM	physical	24981174
TRAD1_HUMAN	TRAFD1	physical	24981174
TRI27_HUMAN	TRIM27	physical	24981174
RO52_HUMAN	TRIM21	physical	24981174
TRI11_HUMAN	TRIM11	physical	24981174
FANCL_HUMAN	FANCL	physical	24981174
RN126_HUMAN	RNF126	physical	24981174
CHIP_HUMAN	STUB1	physical	24981174
CIP1_HUMAN	CCNB1IP1	physical	24981174
RNF5_HUMAN	RNF5	physical	24981174
RN115_HUMAN	RNF115	physical	24981174
HSP72_HUMAN	HSPA2	physical	26153132
RN126_HUMAN	RNF126	physical	27193484
SGTA_HUMAN	SGTA	physical	27193484

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 BAG6_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-108; SER-113; THR-350; SER-973 AND SER-1117,AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964 AND SER-973, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-108; SER-113; THR-350; SER-973 AND SER-1117,AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; THR-350; SER-964;SER-973; SER-1081 AND SER-1117, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASSSPECTROMETRY.	17924679 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1117, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964; SER-1039 ANDTYR-1042, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964; SER-973 ANDSER-1117, AND MASS SPECTROMETRY.	15302935 [Abstract]