dbPTM

CHIP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CHIP_HUMAN
UniProt AC	Q9UNE7
Protein Name	E3 ubiquitin-protein ligase CHIP {ECO:0000305}
Gene Name	STUB1 {ECO:0000312\|HGNC:HGNC:11427}
Organism	Homo sapiens (Human).
Sequence Length	303
Subcellular Localization	Cytoplasm . Nucleus . Translocates to the nucleus in response to inflammatory signals in regulatory T-cells (Treg).
Protein Description	E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation. [PubMed: 27708256 Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner]
Protein Sequence	MKGKEEKEGGARLGAGGGSPEKSPSAQELKEQGNRLFVGRKYPEAAACYGRAITRNPLVAVYYTNRALCYLKMQQHEQALADCRRALELDGQSVKAHFFLGQCQLEMESYDEAIANLQRAYSLAKEQRLNFGDDIPSALRIAKKKRWNSIEERRIHQESELHSYLSRLIAAERERELEECQRNHEGDEDDSHVRAQQACIEAKHDKYMADMDELFSQVDEKRKKRDIPDYLCGKISFELMREPCITPSGITYDRKDIEEHLQRVGHFDPVTRSPLTQEQLIPNLAMKEVIDAFISENGWVEDY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Methylation	------MKGKEEKEG ------CCCCCCCCC	77.89	-
2	Ubiquitination	------MKGKEEKEG ------CCCCCCCCC	77.89	23560854
7	Ubiquitination	-MKGKEEKEGGARLG -CCCCCCCCCCCCCC	63.85	24816145
19	Phosphorylation	RLGAGGGSPEKSPSA CCCCCCCCCCCCCCH	32.91	29255136
22	Ubiquitination	AGGGSPEKSPSAQEL CCCCCCCCCCCHHHH	71.67	33845483
23	Phosphorylation	GGGSPEKSPSAQELK CCCCCCCCCCHHHHH	23.56	29255136
25	Phosphorylation	GSPEKSPSAQELKEQ CCCCCCCCHHHHHHH	50.07	29255136
30	Sumoylation	SPSAQELKEQGNRLF CCCHHHHHHHCCCEE	47.44	-
30	Ubiquitination	SPSAQELKEQGNRLF CCCHHHHHHHCCCEE	47.44	24816145
30	Sumoylation	SPSAQELKEQGNRLF CCCHHHHHHHCCCEE	47.44	-
35	Methylation	ELKEQGNRLFVGRKY HHHHHCCCEECCCCC	36.01	-
41	Malonylation	NRLFVGRKYPEAAAC CCEECCCCCHHHHHH	60.26	30639696
41	Ubiquitination	NRLFVGRKYPEAAAC CCEECCCCCHHHHHH	60.26	-
41	Sumoylation	NRLFVGRKYPEAAAC CCEECCCCCHHHHHH	60.26	-
41	Acetylation	NRLFVGRKYPEAAAC CCEECCCCCHHHHHH	60.26	27452117
41	Sumoylation	NRLFVGRKYPEAAAC CCEECCCCCHHHHHH	60.26	-
41	Methylation	NRLFVGRKYPEAAAC CCEECCCCCHHHHHH	60.26	-
48	Glutathionylation	KYPEAAACYGRAITR CCHHHHHHHCCCCCC	2.95	22555962
49	Phosphorylation	YPEAAACYGRAITRN CHHHHHHHCCCCCCC	12.62	22817900
53	Ubiquitination	AACYGRAITRNPLVA HHHHCCCCCCCCEEE	3.42	27667366
62	Phosphorylation	RNPLVAVYYTNRALC CCCEEEEHHHHHHHH	8.54	28152594
63	Phosphorylation	NPLVAVYYTNRALCY CCEEEEHHHHHHHHH	7.31	28152594
64	Phosphorylation	PLVAVYYTNRALCYL CEEEEHHHHHHHHHH	10.67	28152594
72	2-Hydroxyisobutyrylation	NRALCYLKMQQHEQA HHHHHHHHHHHHHHH	14.27	-
72	Acetylation	NRALCYLKMQQHEQA HHHHHHHHHHHHHHH	14.27	26051181
72	Methylation	NRALCYLKMQQHEQA HHHHHHHHHHHHHHH	14.27	-
72	Ubiquitination	NRALCYLKMQQHEQA HHHHHHHHHHHHHHH	14.27	29901268
121	Phosphorylation	IANLQRAYSLAKEQR HHHHHHHHHHHHHHH	13.35	20049867
122	Phosphorylation	ANLQRAYSLAKEQRL HHHHHHHHHHHHHHC	22.36	20049867
125	Sumoylation	QRAYSLAKEQRLNFG HHHHHHHHHHHCCCC	60.72	-
125	Sumoylation	QRAYSLAKEQRLNFG HHHHHHHHHHHCCCC	60.72	-
125	Ubiquitination	QRAYSLAKEQRLNFG HHHHHHHHHHHCCCC	60.72	27667366
131	Ubiquitination	AKEQRLNFGDDIPSA HHHHHCCCCCCHHHH	15.62	29967540
137	Phosphorylation	NFGDDIPSALRIAKK CCCCCHHHHHHHHHH	40.02	25159151
149	Ubiquitination	AKKKRWNSIEERRIH HHHHCCCCHHHHHHH	25.15	32015554
149	Phosphorylation	AKKKRWNSIEERRIH HHHHCCCCHHHHHHH	25.15	24114839
183	Ubiquitination	ELEECQRNHEGDEDD HHHHHHHHCCCCCCH	16.22	24816145
191	Phosphorylation	HEGDEDDSHVRAQQA CCCCCCHHHHHHHHH	35.88	29214152
199	S-nitrosylation	HVRAQQACIEAKHDK HHHHHHHHHHHHHHH	2.22	19483679
199	S-nitrosocysteine	HVRAQQACIEAKHDK HHHHHHHHHHHHHHH	2.22	-
203	Acetylation	QQACIEAKHDKYMAD HHHHHHHHHHHHHHC	39.28	26051181
203	Sumoylation	QQACIEAKHDKYMAD HHHHHHHHHHHHHHC	39.28	-
203	Sumoylation	QQACIEAKHDKYMAD HHHHHHHHHHHHHHC	39.28	-
203	Ubiquitination	QQACIEAKHDKYMAD HHHHHHHHHHHHHHC	39.28	29967540
207	Phosphorylation	IEAKHDKYMADMDEL HHHHHHHHHHCHHHH	12.00	-
221	Ubiquitination	LFSQVDEKRKKRDIP HHHHHHHHHHHCCCC	66.12	32015554
255	2-Hydroxyisobutyrylation	SGITYDRKDIEEHLQ CCCEECHHHHHHHHH	61.22	-
255	Ubiquitination	SGITYDRKDIEEHLQ CCCEECHHHHHHHHH	61.22	24816145
255	Sumoylation	SGITYDRKDIEEHLQ CCCEECHHHHHHHHH	61.22	-
271	Phosphorylation	VGHFDPVTRSPLTQE HCCCCCCCCCCCCHH	30.71	25159151
273	Phosphorylation	HFDPVTRSPLTQEQL CCCCCCCCCCCHHHH	18.20	30266825
276	Phosphorylation	PVTRSPLTQEQLIPN CCCCCCCCHHHHCHH	33.18	17525332

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
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO2	Q9UK22	PMID:16682404
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:17241447
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
2	K	ubiquitylation		18042044
Monoubiquitinated at Lys-2 following cell stress by UBE2W, promoting the interaction with ATXN3 (By similarity).

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 CHIP_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EM55_HUMAN	MPP1	physical	16169070
KHDR1_HUMAN	KHDRBS1	physical	16169070
HSP7C_HUMAN	HSPA8	physical	10330192
HSP74_HUMAN	HSPA4	physical	10330192
DNJB1_HUMAN	DNAJB1	physical	10330192
CP3A4_HUMAN	CYP3A4	physical	19103148
RUNX2_HUMAN	RUNX2	physical	18541707
CHIP_HUMAN	STUB1	physical	18485199
UB2D1_HUMAN	UBE2D1	physical	18485199
UB2E2_HUMAN	UBE2E2	physical	18485199
GCYA2_HUMAN	GUCY1A2	physical	17873020
UB2D1_HUMAN	UBE2D1	physical	17873020
M3K5_HUMAN	MAP3K5	physical	17595347
HS90A_HUMAN	HSP90AA1	physical	17324930
AHR_HUMAN	AHR	physical	17209571
ATX1_HUMAN	ATXN1	physical	16831871
RON_HUMAN	MST1R	physical	16740632
TERA_HUMAN	VCP	physical	16621797
CHIP_HUMAN	STUB1	physical	16714300
BAG2_HUMAN	BAG2	physical	16169850
HSP74_HUMAN	HSPA4	physical	16169850
M3K5_HUMAN	MAP3K5	physical	16038411
CFTR_HUMAN	CFTR	physical	15611333
HSP7C_HUMAN	HSPA8	physical	15538384
ESR1_HUMAN	ESR1	physical	15538384
DJC13_HUMAN	DNAJC13	physical	15538384
HS90A_HUMAN	HSP90AA1	physical	15538384
HSP74_HUMAN	HSPA4	physical	15538384
BAG1_HUMAN	BAG1	physical	15538384
CHIP_HUMAN	STUB1	physical	15538384
NOS1_HUMAN	NOS1	physical	15466472
TAU_HUMAN	MAPT	physical	15447663
UB2D3_HUMAN	UBE2D3	physical	11743028
CHIP_HUMAN	STUB1	physical	11743028
UB2D1_HUMAN	UBE2D1	physical	11557750
HSP7C_HUMAN	HSPA8	physical	11557750
GCR_HUMAN	NR3C1	physical	11146632
HS90A_HUMAN	HSP90AA1	physical	11146632
UBC_HUMAN	UBC	physical	11146632
RUNX1_HUMAN	RUNX1	physical	19524548
LRRK2_HUMAN	LRRK2	physical	19196961
HS90A_HUMAN	HSP90AA1	physical	19196961
HSP74_HUMAN	HSPA4	physical	19196961
FOXO1_HUMAN	FOXO1	physical	19483080
GCYB1_HUMAN	GUCY1B3	physical	19478201
GCYA3_HUMAN	GUCY1A3	physical	19478201
DAXX_HUMAN	DAXX	physical	19465479
HSP74_HUMAN	HSPA4	physical	19648119
SODC_HUMAN	SOD1	physical	17157513
A4_HUMAN	APP	physical	17317785
CH60_HUMAN	HSPD1	physical	17317785
HSP74_HUMAN	HSPA4	physical	17317785
HS90A_HUMAN	HSP90AA1	physical	17317785
HSP74_HUMAN	HSPA4	physical	21454478
HSP7C_HUMAN	HSPA8	physical	21454478
AKT1_HUMAN	AKT1	physical	21767636
NQO1_HUMAN	NQO1	physical	21220432
IRF1_HUMAN	IRF1	physical	20947504
SMAD1_HUMAN	SMAD1	physical	21454478
HSP7C_HUMAN	HSPA8	physical	20618441
HS90A_HUMAN	HSP90AA1	physical	20618441
P53_HUMAN	TP53	physical	20618441
CHIP_HUMAN	STUB1	physical	20146531
HSP74_HUMAN	HSPA4	physical	20146531
HS90A_HUMAN	HSP90AA1	physical	20146531
UB2D1_HUMAN	UBE2D1	physical	20146531
UBE2N_HUMAN	UBE2N	physical	20146531
SENP3_HUMAN	SENP3	physical	20924358
HSP74_HUMAN	HSPA4	physical	19913553
HS90A_HUMAN	HSP90AA1	physical	19913553
HSP7C_HUMAN	HSPA8	physical	21911421
TRAF6_HUMAN	TRAF6	physical	21911421
KPCZ_HUMAN	PRKCZ	physical	21911421
SRC_HUMAN	SRC	physical	21911421
HSP74_HUMAN	HSPA4	physical	21549100
MYCD_HUMAN	MYOCD	physical	19237536
HSP74_HUMAN	HSPA4	physical	20704274
HS90A_HUMAN	HSP90AA1	physical	20704274
UBC_HUMAN	UBC	physical	18042044
DPOLB_HUMAN	POLB	physical	19713937
HS90A_HUMAN	HSP90AA1	physical	18784277
HSP74_HUMAN	HSPA4	physical	18784277
PSMD4_HUMAN	PSMD4	physical	19240029
HSP74_HUMAN	HSPA4	physical	19940151
HIF1A_HUMAN	HIF1A	physical	19940151
LRRK2_HUMAN	LRRK2	physical	19536328
SMAD1_HUMAN	SMAD1	physical	14701756
TAU_HUMAN	MAPT	physical	20466727
BAG1_HUMAN	BAG1	physical	20675402
ATX3_HUMAN	ATXN3	physical	20943656
NOS1_HUMAN	NOS1	physical	20729196
CP2E1_HUMAN	CYP2E1	physical	21209460
UB2D1_HUMAN	UBE2D1	physical	21518764
UB2D2_HUMAN	UBE2D2	physical	21518764
UB2D3_HUMAN	UBE2D3	physical	21518764
UB2E1_HUMAN	UBE2E1	physical	21518764
UB2E2_HUMAN	UBE2E2	physical	21518764
UB2E3_HUMAN	UBE2E3	physical	21518764
UBE2N_HUMAN	UBE2N	physical	21518764
UBE2W_HUMAN	UBE2W	physical	21518764
CHIP_HUMAN	STUB1	physical	21518764
HSP74_HUMAN	HSPA4	physical	21518764
TAU_HUMAN	MAPT	physical	14612456
SGK1_HUMAN	SGK1	physical	20947508
CHIP_HUMAN	STUB1	physical	12574167
ERBB2_HUMAN	ERBB2	physical	12574167
HSP74_HUMAN	HSPA4	physical	12574167
HS90A_HUMAN	HSP90AA1	physical	12574167
M3K2_HUMAN	MAP3K2	physical	20588253
CHIP_HUMAN	STUB1	physical	21358815
HSP74_HUMAN	HSPA4	physical	21358815
SYUA_HUMAN	SNCA	physical	21358815
M3K5_HUMAN	MAP3K5	physical	20349136
HSP74_HUMAN	HSPA4	physical	20349136
ANDR_HUMAN	AR	physical	21157430
CFTR_HUMAN	CFTR	physical	19056735
CFTR_HUMAN	CFTR	physical	21898230
ERBB2_HUMAN	ERBB2	physical	17875712
HSP7C_HUMAN	HSPA8	physical	15198682
MYC_HUMAN	MYC	physical	22543587
TF65_HUMAN	RELA	physical	22535373
PTEN_HUMAN	PTEN	physical	22427670
HS90A_HUMAN	HSP90AA1	physical	16275660
HSP7C_HUMAN	HSPA8	physical	16275660
HSP74_HUMAN	HSPA4	physical	16275660
UB2Q1_HUMAN	UBE2Q1	physical	16275660
ATCAY_HUMAN	ATCAY	physical	16275660
TRAF2_HUMAN	TRAF2	physical	21793045
DNJA3_HUMAN	DNAJA3	physical	21710689
UBC_RAT	Ubc	physical	20724525
NHLC1_HUMAN	NHLRC1	physical	19892702
HSP74_HUMAN	HSPA4	physical	19892702
HSP74_HUMAN	HSPA4	physical	18436529
SYUA_HUMAN	SNCA	physical	18436529
P53_HUMAN	TP53	physical	17666403
ATX1_HUMAN	ATXN1	physical	17127076
ANDR_HUMAN	AR	physical	16725394
HSF1_HUMAN	HSF1	physical	16293251
HSP74_HUMAN	HSPA4	physical	16293251
HSP7C_HUMAN	HSPA8	physical	16293251
HS90A_HUMAN	HSP90AA1	physical	16293251
CHIP_HUMAN	STUB1	physical	16207813
HSP7C_HUMAN	HSPA8	physical	16207813
HS90A_HUMAN	HSP90AA1	physical	16207813
HPBP1_HUMAN	HSPBP1	physical	16207813
BAG1_HUMAN	BAG1	physical	16207813
PSMD1_HUMAN	PSMD1	physical	16207813
PSA3_HUMAN	PSMA3	physical	16207813
BAG2_HUMAN	BAG2	physical	16207813
P53_HUMAN	TP53	physical	15911628
NHLC1_HUMAN	NHLRC1	physical	21652633
EPM2A_HUMAN	EPM2A	physical	21652633
ATX3_HUMAN	ATXN3	physical	21625540
CHIP_HUMAN	STUB1	physical	22842904
HSP7C_HUMAN	HSPA8	physical	15215316
HPBP1_HUMAN	HSPBP1	physical	15215316
RAF1_HUMAN	RAF1	physical	15215316
MIF_HUMAN	MIF	physical	22271573
RAF1_HUMAN	RAF1	physical	15936278
TERT_HUMAN	TERT	physical	20959453
P53_HUMAN	TP53	physical	22254155
HSP74_HUMAN	HSPA4	physical	21775628
P53_HUMAN	TP53	physical	15001357
HS90A_HUMAN	HSP90AA1	physical	15001357
PSMD4_HUMAN	PSMD4	physical	22350919
CFTR_HUMAN	CFTR	physical	11146634
PSA3_HUMAN	PSMA3	physical	11146634
HSP7C_HUMAN	HSPA8	physical	11146634
DNJC5_HUMAN	DNAJC5	physical	19098309
MET_HUMAN	MET	physical	21325980
HSP74_HUMAN	HSPA4	physical	21325980
HS90A_HUMAN	HSP90AA1	physical	21325980
SMG5_HUMAN	SMG5	physical	16809764
UB2D1_HUMAN	UBE2D1	physical	19103148
UB2D2_HUMAN	UBE2D2	physical	15911628
UB2D3_HUMAN	UBE2D3	physical	19713937
UB2E1_HUMAN	UBE2E1	physical	19713937
UB2D1_HUMAN	UBE2D1	physical	21209460
UB2D1_HUMAN	UBE2D1	physical	19056735
UB2D2_HUMAN	UBE2D2	physical	21358815
UB2D1_HUMAN	UBE2D1	physical	20729196
UB2D2_HUMAN	UBE2D2	physical	19237536
UB2D3_HUMAN	UBE2D3	physical	20618441
UB2D1_HUMAN	UBE2D1	physical	21454478
UB2D1_HUMAN	UBE2D1	physical	21898230
UB2D1_HUMAN	UBE2D1	physical	15198682
UB2D2_HUMAN	UBE2D2	physical	16275660
UB2D3_HUMAN	UBE2D3	physical	21625540
UB2D1_HUMAN	UBE2D1	physical	22842904
UB2D1_HUMAN	UBE2D1	physical	16831871
UB2D1_HUMAN	UBE2D1	physical	16740632
UB2D1_HUMAN	UBE2D1	physical	15215316
UB2L3_HUMAN	UBE2L3	physical	16714300
UB2D2_HUMAN	UBE2D2	physical	15936278
UB2D1_HUMAN	UBE2D1	physical	15466472
UB2D2_HUMAN	UBE2D2	physical	15447663
UB2D1_HUMAN	UBE2D1	physical	19648119
UB2D3_HUMAN	UBE2D3	physical	19913553
UB2V1_HUMAN	UBE2V1	physical	21911421
UB2D1_HUMAN	UBE2D1	physical	21911421
UB2D1_HUMAN	UBE2D1	physical	16809764
UB2D3_HUMAN	UBE2D3	physical	20704274
UB2V1_HUMAN	UBE2V1	physical	18042044
UB2D1_HUMAN	UBE2D1	physical	18042044
UB2D2_HUMAN	UBE2D2	physical	20466727
UB2D2_HUMAN	UBE2D2	physical	20675402
UB2D1_HUMAN	UBE2D1	physical	20675402
UB2D3_HUMAN	UBE2D3	physical	20675402
UB2D3_HUMAN	UBE2D3	physical	20943656
UB2D1_HUMAN	UBE2D1	physical	12574167
UB2D1_HUMAN	UBE2D1	physical	21157430
UB2V1_HUMAN	UBE2V1	physical	22939629
UB2V2_HUMAN	UBE2V2	physical	22939629
CFLAR_HUMAN	CFLAR	physical	23256568
HS90A_HUMAN	HSP90AA1	physical	23256568
NOS1_HUMAN	NOS1	physical	23109339
IRF1_HUMAN	IRF1	physical	23134341
P53_HUMAN	TP53	physical	23134341
S10A2_HUMAN	S100A2	physical	23344957
S10A6_HUMAN	S100A6	physical	23344957
S100P_HUMAN	S100P	physical	23344957
HSP74_HUMAN	HSPA4	physical	23344957
HS90A_HUMAN	HSP90AA1	physical	23344957
SMAD1_HUMAN	SMAD1	physical	23344957
HSF1_HUMAN	HSF1	physical	23344957
UB2D1_HUMAN	UBE2D1	physical	23344957
KCNQ4_HUMAN	KCNQ4	physical	23431407
ATX3_HUMAN	ATXN3	physical	19153604
CHIP_HUMAN	STUB1	physical	23560854
UBE2W_HUMAN	UBE2W	physical	23560854
LIMS1_HUMAN	LIMS1	physical	23554879
UFO_HUMAN	AXL	physical	23629654
S12A3_HUMAN	SLC12A3	physical	23482560
HSP7C_HUMAN	HSPA8	physical	23865999
UB2D3_HUMAN	UBE2D3	physical	23865999
CHIP_HUMAN	STUB1	physical	23990462
HSP7C_HUMAN	HSPA8	physical	23990462
FOXP3_HUMAN	FOXP3	physical	23973223
UB2D2_HUMAN	UBE2D2	physical	23973223
SIR6_HUMAN	SIRT6	physical	24043303
UB2D3_HUMAN	UBE2D3	physical	24043303
KTNA1_HUMAN	KATNA1	physical	23904609
HS90A_HUMAN	HSP90AA1	physical	23904609
M3K7_HUMAN	MAP3K7	physical	23322406
IKKA_HUMAN	CHUK	physical	23322406
MALT1_HUMAN	MALT1	physical	23322406
TRAF6_HUMAN	TRAF6	physical	23322406
RAF1_HUMAN	RAF1	physical	22350907
UB2D2_HUMAN	UBE2D2	physical	22350907
IF5A1_HUMAN	EIF5A	physical	24509416
TERA_HUMAN	VCP	physical	24100225
CIP2A_HUMAN	KIAA1524	physical	24293411
JOS1_HUMAN	JOSD1	physical	23625928
JOS2_HUMAN	JOSD2	physical	23625928
UB2D3_HUMAN	UBE2D3	physical	23625928
CHIP_HUMAN	STUB1	physical	18988734
HSP7C_HUMAN	HSPA8	physical	18988734
UB2D1_HUMAN	UBE2D1	physical	18988734
TRAF6_HUMAN	TRAF6	physical	24578159
PA2G4_HUMAN	PA2G4	physical	24651434
EGFR_HUMAN	EGFR	physical	24722501
MLF2_HUMAN	MLF2	physical	25036637
HSP72_HUMAN	HSPA2	physical	25036637
DNJB6_HUMAN	DNAJB6	physical	25036637
BAG2_HUMAN	BAG2	physical	25036637
NADE_HUMAN	NADSYN1	physical	25036637
UBE2N_HUMAN	UBE2N	physical	25036637
HS71L_HUMAN	HSPA1L	physical	25036637
HS74L_HUMAN	HSPA4L	physical	25036637
TXLNG_HUMAN	TXLNG	physical	25036637
NUCG_HUMAN	ENDOG	physical	23764847
HSP74_HUMAN	HSPA4	physical	23764847
M3K11_HUMAN	MAP3K11	physical	24912674
SNAI2_HUMAN	SNAI2	physical	23851495
ERN1_HUMAN	ERN1	physical	25225294
UBE2N_HUMAN	UBE2N	physical	25225294
HSP7C_HUMAN	HSPA8	physical	25258038
CHIP_HUMAN	STUB1	physical	25258038
UB2D3_HUMAN	UBE2D3	physical	25258038
P53_HUMAN	TP53	physical	25144556
TAU_HUMAN	MAPT	physical	16275660
UBC_HUMAN	UBC	physical	16307917
UBE2N_HUMAN	UBE2N	physical	16307917
UB2V1_HUMAN	UBE2V1	physical	16307917
UB2D1_HUMAN	UBE2D1	physical	16307917
FMR1_HUMAN	FMR1	physical	25268320
UB2D1_HUMAN	UBE2D1	physical	19240029
CP3A4_HUMAN	CYP3A4	physical	22101235
UB2D1_HUMAN	UBE2D1	physical	22101235
ABL1_HUMAN	ABL1	physical	20675402
BCR_HUMAN	BCR	physical	20675402
RUSC1_HUMAN	RUSC1	physical	25416956
THIOM_HUMAN	TXN2	physical	25416956
CCL28_HUMAN	CCL28	physical	25416956
NOE3_HUMAN	OLFM3	physical	25416956
SQSTM_HUMAN	SQSTM1	physical	23686137
ERBB2_HUMAN	ERBB2	physical	12239347
PSMD4_HUMAN	PSMD4	physical	11146632
CFTR_HUMAN	CFTR	physical	15215316
UB2D3_HUMAN	UBE2D3	physical	19153604
HSP7C_HUMAN	HSPA8	physical	17178836
MCF2_HUMAN	MCF2	physical	17178836
CP3A4_HUMAN	CYP3A4	physical	25451919
UB2D1_HUMAN	UBE2D1	physical	25451919
DAAF4_HUMAN	DYX1C1	physical	19423554
TCPE_HUMAN	CCT5	physical	26344197
TCPH_HUMAN	CCT7	physical	26344197
PSMD4_HUMAN	PSMD4	physical	26344197
UBP5_HUMAN	USP5	physical	26344197
P53_HUMAN	TP53	physical	25543083
PTEN_HUMAN	PTEN	physical	26280536
UB2D3_HUMAN	UBE2D3	physical	26280536
BACE1_HUMAN	BACE1	physical	25773675
HSP7C_HUMAN	HSPA8	physical	25684577
CHIP_HUMAN	STUB1	physical	25684577
UB2D2_HUMAN	UBE2D2	physical	25684577
ANM5_HUMAN	PRMT5	physical	26658161
KCNA5_HUMAN	KCNA5	physical	26232501
HSP7C_HUMAN	HSPA8	physical	26232501
IRF1_HUMAN	IRF1	physical	26330542
P53_HUMAN	TP53	physical	26330542
CHIP_HUMAN	STUB1	physical	26330542
BAG1_HUMAN	BAG1	physical	26330542
HS90A_HUMAN	HSP90AA1	physical	26330542
UB2D1_HUMAN	UBE2D1	physical	26330542
UB2D1_HUMAN	UBE2D1	physical	23109339
CHIP_HUMAN	STUB1	physical	17426036
UBE2N_HUMAN	UBE2N	physical	17426036
UB2D1_HUMAN	UBE2D1	physical	17426036
PARP1_HUMAN	PARP1	physical	27787517
HIPK2_HUMAN	HIPK2	physical	27787517
PPARG_HUMAN	PPARG	physical	28059128
UB2D3_HUMAN	UBE2D3	physical	28059128
ANDR_HUMAN	AR	physical	27903893
UB2D1_HUMAN	UBE2D1	physical	27903893
RFX1_HUMAN	RFX1	physical	27283392
HSP7C_HUMAN	HSPA8	physical	27283392
P53_HUMAN	TP53	physical	27775703
CHIP_HUMAN	STUB1	physical	28134249
UB2D2_HUMAN	UBE2D2	physical	28134249
DDIAS_HUMAN	DDIAS	physical	28079882
EGFR_HUMAN	EGFR	physical	27475501
HSP7C_HUMAN	HSPA8	physical	27709416
RHDF2_HUMAN	RHBDF2	physical	29069608
CDN1A_HUMAN	CDKN1A	physical	28232384
M3K21_HUMAN	KIAA1804	physical	28757353
CHIP_HUMAN	STUB1	physical	28757353
UB2D1_HUMAN	UBE2D1	physical	28757353
UB2D2_HUMAN	UBE2D2	physical	28757353
UB2D3_HUMAN	UBE2D3	physical	28757353
UB2D4_HUMAN	UBE2D4	physical	28757353
UBE2N_HUMAN	UBE2N	physical	28757353
UBE2W_HUMAN	UBE2W	physical	28757353
CP2E1_RABIT	LOC100342572	physical	16331994
IRF1_HUMAN	IRF1	physical	28362432
UB2D1_HUMAN	UBE2D1	physical	28362432
TPD52_HUMAN	TPD52	physical	27835608
ANDR_HUMAN	AR	physical	27835608
HSP7C_MOUSE	Hspa8	physical	29091030
CHIP_HUMAN	STUB1	physical	29091030
NQO1_HUMAN	NQO1	physical	29091030
UB2D1_HUMAN	UBE2D1	physical	29091030
RHG17_MOUSE	Arhgap17	physical	29091030
BIN1_MOUSE	Bin1	physical	29091030
CDK6_MOUSE	Cdk6	physical	29091030
GPSM2_MOUSE	Gpsm2	physical	29091030
RFA1_MOUSE	Rpa1	physical	29091030
RFA3_MOUSE	Rpa3	physical	29091030
STAU1_MOUSE	Stau1	physical	29091030
ITF2_MOUSE	Tcf4	physical	29091030
TNR6B_MOUSE	Tnrc6b	physical	29091030
VPS4A_MOUSE	Vps4a	physical	29091030
AAAS_MOUSE	Aaas	physical	29091030
AKAP9_MOUSE	Akap9	physical	29091030
RHG33_MOUSE	Arhgap33	physical	29091030
BAIP2_MOUSE	Baiap2	physical	29091030
CNBP_MOUSE	Cnbp	physical	29091030
DNJB6_MOUSE	Dnajb6	physical	29091030
DJC25_MOUSE	Dnajc25	physical	29091030
DNJC9_MOUSE	Dnajc9	physical	29091030
IF6_MOUSE	Eif6	physical	29091030
FBW1B_MOUSE	Fbxw11	physical	29091030
GGYF1_MOUSE	Gigyf1	physical	29091030
ILVBL_MOUSE	Ilvbl	physical	29091030
KIFC3_MOUSE	Kifc3	physical	29091030
KIFC1_MOUSE	Kifc5b	physical	29091030
PRC2B_MOUSE	Prrc2b	physical	29091030
RL26_MOUSE	Rpl26	physical	29091030
RL31_MOUSE	Rpl31	physical	29091030
RL35_MOUSE	Rpl35	physical	29091030
RS24_MOUSE	Rps24	physical	29091030
RTF2_MOUSE	Rtfdc1	physical	29091030
SDF2L_MOUSE	Sdf2l1	physical	29091030
SP1_MOUSE	Sp1	physical	29091030
TAF6_MOUSE	Taf6	physical	29091030
TOPB1_MOUSE	Topbp1	physical	29091030
UBP2L_MOUSE	Ubap2l	physical	29091030
VKOR1_MOUSE	Vkorc1	physical	29091030
YIF1B_MOUSE	Yif1b	physical	29091030

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615768	Spinocerebellar ataxia, autosomal recessive, 16 (SCAR16)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CHIP_HUMAN

Related Literatures of Post-Translational Modification

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-19 AND SER-23, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.	19369195 [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, AND MASSSPECTROMETRY.	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-19; SER-23 AND SER-273,AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-19 AND SER-23, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-23, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.	17287340 [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-19 AND SER-23, 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-19 AND SER-23, AND MASSSPECTROMETRY.	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-19 AND SER-23, AND MASSSPECTROMETRY.	15302935 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-276, AND MASSSPECTROMETRY.	17525332 [Abstract]
Ubiquitylation
Reference	PubMed
"Two different classes of E2 ubiquitin-conjugating enzymes arerequired for the mono-ubiquitination of proteins and elongation bypolyubiquitin chains with a specific topology."; Windheim M., Peggie M., Cohen P.; Biochem. J. 409:723-729(2008). Cited for: POLYUBIQUITINATION AT LYS-22; LYS-221 AND LYS-255, AND DOMAIN TPR.	18042044 [Abstract]

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