dbPTM

PFD3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PFD3_HUMAN
UniProt AC	P61758
Protein Name	Prefoldin subunit 3
Gene Name	VBP1
Organism	Homo sapiens (Human).
Sequence Length	197
Subcellular Localization	Cytoplasm. Nucleus. In complex with VHL can translocate to the nucleus.
Protein Description	Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins..
Protein Sequence	MAAVKDSCGKGEMATGNGRRLHLGIPEAVFVEDVDSFMKQPGNETADTVLKKLDEQYQKYKFMELNLAQKKRRLKGQIPEIKQTLEILKYMQKKKESTNSMETRFLLADNLYCKASVPPTDKMCLWLGANVMLEYDIDEAQALLEKNLSTATKNLDSLEEDLDFLRDQFTTTEVNMARVYNWDVKRRNKDDSTKNKA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAVKDSCG ------CCCCCCCCC	22.44	22814378
5	Acetylation	---MAAVKDSCGKGE ---CCCCCCCCCCCC	38.92	23749302
5	Ubiquitination	---MAAVKDSCGKGE ---CCCCCCCCCCCC	38.92	-
7	Phosphorylation	-MAAVKDSCGKGEMA -CCCCCCCCCCCCCC	21.03	25159151
10	Ubiquitination	AVKDSCGKGEMATGN CCCCCCCCCCCCCCC	56.90	-
10	Acetylation	AVKDSCGKGEMATGN CCCCCCCCCCCCCCC	56.90	26051181
39	Ubiquitination	EDVDSFMKQPGNETA ECHHHHHCCCCCCCH	51.86	-
51	Ubiquitination	ETADTVLKKLDEQYQ CCHHHHHHHHHHHHH	47.13	-
51	Acetylation	ETADTVLKKLDEQYQ CCHHHHHHHHHHHHH	47.13	25953088
52	Ubiquitination	TADTVLKKLDEQYQK CHHHHHHHHHHHHHH	57.94	-
54	Ubiquitination	DTVLKKLDEQYQKYK HHHHHHHHHHHHHHH	50.24	-
54	Acetylation	DTVLKKLDEQYQKYK HHHHHHHHHHHHHHH	50.24	-
56	Ubiquitination	VLKKLDEQYQKYKFM HHHHHHHHHHHHHHH	45.70	-
59	Ubiquitination	KLDEQYQKYKFMELN HHHHHHHHHHHHHHH	45.53	21890473
59	Acetylation	KLDEQYQKYKFMELN HHHHHHHHHHHHHHH	45.53	19608861
60	Phosphorylation	LDEQYQKYKFMELNL HHHHHHHHHHHHHHH	8.24	-
61	Ubiquitination	DEQYQKYKFMELNLA HHHHHHHHHHHHHHH	45.32	21890473
61	Acetylation	DEQYQKYKFMELNLA HHHHHHHHHHHHHHH	45.32	27452117
63	Sulfoxidation	QYQKYKFMELNLAQK HHHHHHHHHHHHHHH	5.11	21406390
65	Ubiquitination	QKYKFMELNLAQKKR HHHHHHHHHHHHHHH	4.23	-
66	Ubiquitination	KYKFMELNLAQKKRR HHHHHHHHHHHHHHH	21.74	-
70	Acetylation	MELNLAQKKRRLKGQ HHHHHHHHHHHHCCC	42.51	25953088
70	Ubiquitination	MELNLAQKKRRLKGQ HHHHHHHHHHHHCCC	42.51	21890473
71	Ubiquitination	ELNLAQKKRRLKGQI HHHHHHHHHHHCCCC	30.58	-
75	Ubiquitination	AQKKRRLKGQIPEIK HHHHHHHCCCCHHHH	47.13	-
77	Ubiquitination	KKRRLKGQIPEIKQT HHHHHCCCCHHHHHH	46.61	-
82	Ubiquitination	KGQIPEIKQTLEILK CCCCHHHHHHHHHHH	35.25	21890473
84	Ubiquitination	QIPEIKQTLEILKYM CCHHHHHHHHHHHHH	22.74	-
89	Ubiquitination	KQTLEILKYMQKKKE HHHHHHHHHHHHHCC	44.32	21890473
95	Ubiquitination	LKYMQKKKESTNSME HHHHHHHCCCCCCHH	65.02	21890473
97	Ubiquitination	YMQKKKESTNSMETR HHHHHCCCCCCHHHH	41.59	21890473
97	Phosphorylation	YMQKKKESTNSMETR HHHHHCCCCCCHHHH	41.59	20068231
98	Phosphorylation	MQKKKESTNSMETRF HHHHCCCCCCHHHHH	32.19	20068231
100	Phosphorylation	KKKESTNSMETRFLL HHCCCCCCHHHHHHH	20.34	25954137
103	Phosphorylation	ESTNSMETRFLLADN CCCCCHHHHHHHCCC	20.34	20068231
106	Ubiquitination	NSMETRFLLADNLYC CCHHHHHHHCCCEEE	3.29	21890473
112	Phosphorylation	FLLADNLYCKASVPP HHHCCCEEECCCCCC	9.73	28796482
113	Glutathionylation	LLADNLYCKASVPPT HHCCCEEECCCCCCC	3.15	22555962
113	S-nitrosylation	LLADNLYCKASVPPT HHCCCEEECCCCCCC	3.15	19483679
113	S-nitrosocysteine	LLADNLYCKASVPPT HHCCCEEECCCCCCC	3.15	-
114	Ubiquitination	LADNLYCKASVPPTD HCCCEEECCCCCCCC	30.09	-
118	Ubiquitination	LYCKASVPPTDKMCL EEECCCCCCCCCCEE	24.47	21890473
125	Ubiquitination	PPTDKMCLWLGANVM CCCCCCEEEECCCEE	3.65	21890473
148	Ubiquitination	QALLEKNLSTATKNL HHHHHHCHHHHHHCH	7.73	-
153	Ubiquitination	KNLSTATKNLDSLEE HCHHHHHHCHHHHHH	53.72	21906983
157	Phosphorylation	TATKNLDSLEEDLDF HHHHCHHHHHHHHHH	40.63	20873877
170	Phosphorylation	DFLRDQFTTTEVNMA HHHHHHCCCCHHHHH	27.46	25022875
176	Sulfoxidation	FTTTEVNMARVYNWD CCCCHHHHHHHCCCC	2.81	21406390
180	Ubiquitination	EVNMARVYNWDVKRR HHHHHHHCCCCCCCC	12.65	-
185	Ubiquitination	RVYNWDVKRRNKDDS HHCCCCCCCCCCCCC	43.07	21890473
185	Acetylation	RVYNWDVKRRNKDDS HHCCCCCCCCCCCCC	43.07	25953088
189	Ubiquitination	WDVKRRNKDDSTKNK CCCCCCCCCCCCCCC	62.19	21890473
221	Ubiquitination	------------------------------- -------------------------------		21890473

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 PFD3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PFD3_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 PFD3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MSH4_HUMAN	MSH4	physical	12591739
POL_HV1H2	gag-pol	physical	17698809
PFD4_HUMAN	PFDN4	physical	22939629
PFD5_HUMAN	PFDN5	physical	22939629
PFD6_HUMAN	PFDN6	physical	22939629
SYK_HUMAN	KARS	physical	22939629
SYEP_HUMAN	EPRS	physical	22939629
GARS_HUMAN	GARS	physical	22939629
SYIC_HUMAN	IARS	physical	22939629
SYDC_HUMAN	DARS	physical	22939629
SYQ_HUMAN	QARS	physical	22939629
TRM1_HUMAN	TRMT1	physical	22939629
PRS7_HUMAN	PSMC2	physical	22939629
TERA_HUMAN	VCP	physical	23964080
VHL_HUMAN	VHL	physical	23964080
MSH4_HUMAN	MSH4	physical	23964080
PFD2_HUMAN	PFDN2	physical	22863883
PFD4_HUMAN	PFDN4	physical	22863883
PFD5_HUMAN	PFDN5	physical	22863883
PFD6_HUMAN	PFDN6	physical	22863883
LA_HUMAN	SSB	physical	22863883
TNPO1_HUMAN	TNPO1	physical	22863883
UBQL2_HUMAN	UBQLN2	physical	22863883
PNMA1_HUMAN	PNMA1	physical	25416956
UBL7_HUMAN	UBL7	physical	25416956
CBS_HUMAN	CBS	physical	26344197
FLNA_HUMAN	FLNA	physical	26344197
TXD12_HUMAN	TXNDC12	physical	26344197
UBL7_HUMAN	UBL7	physical	28514442
KPBB_HUMAN	PHKB	physical	28514442
COPRS_HUMAN	COPRS	physical	28514442
SGF29_HUMAN	CCDC101	physical	28514442
PFD5_HUMAN	PFDN5	physical	28514442
SPT6H_HUMAN	SUPT6H	physical	28514442
PFD6_HUMAN	PFDN6	physical	28514442
PFD1_HUMAN	PFDN1	physical	28514442
PDRG1_HUMAN	PDRG1	physical	28514442
STK26_HUMAN	STK26	physical	28514442
ERF3A_HUMAN	GSPT1	physical	28514442

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 PFD3_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-59, AND MASS SPECTROMETRY.	19608861 [Abstract]