dbPTM

PFD5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PFD5_HUMAN
UniProt AC	Q99471
Protein Name	Prefoldin subunit 5
Gene Name	PFDN5
Organism	Homo sapiens (Human).
Sequence Length	154
Subcellular Localization	Isoform 1: Nucleus. Isoform 2: Cytoplasm. Isoform 3: 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. Represses the transcriptional activity of MYC..
Protein Sequence	MAQSINITELNLPQLEMLKNQLDQEVEFLSTSIAQLKVVQTKYVEAKDCLNVLNKSNEGKELLVPLTSSMYVPGKLHDVEHVLIDVGTGYYVEKTAEDAKDFFKRKIDFLTKQMEKIQPALQEKHAMKQAVMEMMSQKIQQLTALGAAQATAKA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAQSINITE ------CCCCCCCCC	16.30	22223895
4	Phosphorylation	----MAQSINITELN ----CCCCCCCCCCC	14.20	24043423
4 (in isoform 3)	Phosphorylation	-	14.20	24043423
8 (in isoform 3)	Phosphorylation	-	29.90	24043423
8	Phosphorylation	MAQSINITELNLPQL CCCCCCCCCCCHHHH	29.90	24043423
26 (in isoform 3)	Phosphorylation	-	5.39	24043423
42	Acetylation	QLKVVQTKYVEAKDC HHHHEEEEEECHHHH	30.15	19608861
42	2-Hydroxyisobutyrylation	QLKVVQTKYVEAKDC HHHHEEEEEECHHHH	30.15	-
42	Ubiquitination	QLKVVQTKYVEAKDC HHHHEEEEEECHHHH	30.15	27667366
47	Acetylation	QTKYVEAKDCLNVLN EEEEECHHHHHHHHC	35.15	23749302
47	Malonylation	QTKYVEAKDCLNVLN EEEEECHHHHHHHHC	35.15	26320211
47	Ubiquitination	QTKYVEAKDCLNVLN EEEEECHHHHHHHHC	35.15	29967540
49	Ubiquitination	KYVEAKDCLNVLNKS EEECHHHHHHHHCCC	2.69	21963094
55	Acetylation	DCLNVLNKSNEGKEL HHHHHHCCCCCCCCC	50.96	-
55	Ubiquitination	DCLNVLNKSNEGKEL HHHHHHCCCCCCCCC	50.96	27667366
56	Phosphorylation	CLNVLNKSNEGKELL HHHHHCCCCCCCCCE	38.75	29255136
60	Ubiquitination	LNKSNEGKELLVPLT HCCCCCCCCCEEECC	38.72	29967540
67	Ubiquitination	KELLVPLTSSMYVPG CCCEEECCCCEECCC	16.82	21890473
67	Acetylation	KELLVPLTSSMYVPG CCCEEECCCCEECCC	16.82	19608861
67	Ubiquitination	KELLVPLTSSMYVPG CCCEEECCCCEECCC	16.82	22817900
67	Phosphorylation	KELLVPLTSSMYVPG CCCEEECCCCEECCC	16.82	29083192
68	Phosphorylation	ELLVPLTSSMYVPGK CCEEECCCCEECCCC	22.31	29083192
69	Phosphorylation	LLVPLTSSMYVPGKL CEEECCCCEECCCCC	14.64	29083192
71	Phosphorylation	VPLTSSMYVPGKLHD EECCCCEECCCCCCC	12.87	29083192
71	Ubiquitination	VPLTSSMYVPGKLHD EECCCCEECCCCCCC	12.87	22817900
79	Ubiquitination	VPGKLHDVEHVLIDV CCCCCCCCEEEEEEC	3.69	29967540
90	Phosphorylation	LIDVGTGYYVEKTAE EEECCCCEEEEECHH	12.27	22817900
91	Phosphorylation	IDVGTGYYVEKTAED EECCCCEEEEECHHH	11.95	27642862
94	Ubiquitination	GTGYYVEKTAEDAKD CCCEEEEECHHHHHH	42.88	21906983
100	Acetylation	EKTAEDAKDFFKRKI EECHHHHHHHHHHHH	68.35	27452117
100	Ubiquitination	EKTAEDAKDFFKRKI EECHHHHHHHHHHHH	68.35	29967540
104	Ubiquitination	EDAKDFFKRKIDFLT HHHHHHHHHHHHHHH	53.42	-
106	2-Hydroxyisobutyrylation	AKDFFKRKIDFLTKQ HHHHHHHHHHHHHHH	47.41	-
108	Ubiquitination	DFFKRKIDFLTKQME HHHHHHHHHHHHHHH	35.22	21963094
112	Ubiquitination	RKIDFLTKQMEKIQP HHHHHHHHHHHHHHH	50.20	22817900
112	Acetylation	RKIDFLTKQMEKIQP HHHHHHHHHHHHHHH	50.20	19608861
116	Ubiquitination	FLTKQMEKIQPALQE HHHHHHHHHHHHHHH	41.10	22817900
116	Acetylation	FLTKQMEKIQPALQE HHHHHHHHHHHHHHH	41.10	23236377
124	Ubiquitination	IQPALQEKHAMKQAV HHHHHHHHHHHHHHH	24.57	29967540
124	2-Hydroxyisobutyrylation	IQPALQEKHAMKQAV HHHHHHHHHHHHHHH	24.57	-
124	Acetylation	IQPALQEKHAMKQAV HHHHHHHHHHHHHHH	24.57	26822725
128	Acetylation	LQEKHAMKQAVMEMM HHHHHHHHHHHHHHH	35.57	25953088
153	Ubiquitination	GAAQATAKA------ HHHHHHHCC------	50.72	21906983

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 PFD5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PFD5_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 PFD5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PFD6_HUMAN	PFDN6	physical	14634002
MYC_HUMAN	MYC	physical	9792694
TIF1B_HUMAN	TRIM28	physical	11585818
HDAC1_HUMAN	HDAC1	physical	11585818
SIN3A_HUMAN	SIN3A	physical	11585818
MYC_HUMAN	MYC	physical	11585818
EGR1_HUMAN	EGR1	physical	18281035
SP1_HUMAN	SP1	physical	18281035
VIRF3_HHV8P	vIRF-3	physical	17728244
MYC_HUMAN	MYC	physical	17728244
PRS6B_HUMAN	PSMC4	physical	17786314
SKP2_HUMAN	SKP2	physical	17786314
PFD6_HUMAN	PFDN6	physical	22939629
TCPQ_HUMAN	CCT8	physical	22939629
SYDC_HUMAN	DARS	physical	22939629
SYIC_HUMAN	IARS	physical	22939629
PFD1_HUMAN	PFDN1	physical	22844532
PFD2_HUMAN	PFDN2	physical	22844532
PFD3_HUMAN	VBP1	physical	22844532
RN115_HUMAN	RNF115	physical	22844532
MYC_HUMAN	MYC	physical	22844532
P73_HUMAN	TP73	physical	11844794
MYC_HUMAN	MYC	physical	11844794
AASD1_HUMAN	AARSD1	physical	22863883
ARPC2_HUMAN	ARPC2	physical	22863883
GPC1_HUMAN	GPC1	physical	22863883
IPO7_HUMAN	IPO7	physical	22863883
NIF3L_HUMAN	NIF3L1	physical	22863883
NRDC_HUMAN	NRD1	physical	22863883
NSUN2_HUMAN	NSUN2	physical	22863883
PDIA6_HUMAN	PDIA6	physical	22863883
PFD2_HUMAN	PFDN2	physical	22863883
KAP0_HUMAN	PRKAR1A	physical	22863883
RFA1_HUMAN	RPA1	physical	22863883
SH3G1_HUMAN	SH3GL1	physical	22863883
PSME3_HUMAN	PSME3	physical	25416956
CACO2_HUMAN	CALCOCO2	physical	25416956
GLRX3_HUMAN	GLRX3	physical	25416956
IKZF3_HUMAN	IKZF3	physical	25416956
FLNA_HUMAN	FLNA	physical	26344197
GFPT1_HUMAN	GFPT1	physical	26344197
PFD3_HUMAN	VBP1	physical	26344197

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 PFD5_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 ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-42 AND LYS-112, AND MASSSPECTROMETRY.	19608861 [Abstract]