PFD1_HUMAN - dbPTM
PFD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PFD1_HUMAN
UniProt AC O60925
Protein Name Prefoldin subunit 1
Gene Name PFDN1
Organism Homo sapiens (Human).
Sequence Length 122
Subcellular Localization
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 MAAPVDLELKKAFTELQAKVIDTQQKVKLADIQIEQLNRTKKHAHLTDTEIMTLVDETNMYEGVGRMFILQSKEAIHSQLLEKQKIAEEKIKELEQKKSYLERSVKEAEDNIREMLMARRAQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAAPVDLEL
------CCCCCCHHH
22.0719413330
10AcetylationAPVDLELKKAFTELQ
CCCCHHHHHHHHHHH
32.4525953088
10UbiquitinationAPVDLELKKAFTELQ
CCCCHHHHHHHHHHH
32.4529901268
11UbiquitinationPVDLELKKAFTELQA
CCCHHHHHHHHHHHH
62.4527667366
19UbiquitinationAFTELQAKVIDTQQK
HHHHHHHHHCCCHHH
27.1123000965
26AcetylationKVIDTQQKVKLADIQ
HHCCCHHHHHHHHHH
31.3625953088
28MethylationIDTQQKVKLADIQIE
CCCHHHHHHHHHHHH
45.0223644510
28UbiquitinationIDTQQKVKLADIQIE
CCCHHHHHHHHHHHH
45.0233845483
28MalonylationIDTQQKVKLADIQIE
CCCHHHHHHHHHHHH
45.0226320211
28AcetylationIDTQQKVKLADIQIE
CCCHHHHHHHHHHHH
45.0225953088
61PhosphorylationLVDETNMYEGVGRMF
HHCCCCCCCCCCHHH
16.1727642862
72PhosphorylationGRMFILQSKEAIHSQ
CHHHHHHCHHHHHHH
29.0821712546
83UbiquitinationIHSQLLEKQKIAEEK
HHHHHHHHHHHHHHH
57.7829967540
97AcetylationKIKELEQKKSYLERS
HHHHHHHHHHHHHHH
34.0225953088
99PhosphorylationKELEQKKSYLERSVK
HHHHHHHHHHHHHHH
41.82-
106UbiquitinationSYLERSVKEAEDNIR
HHHHHHHHHHHHHHH
53.0727667366

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 PFD1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PFD1_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 PFD1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTS_HUMANACTA1physical
14634002
TBA1A_HUMANTUBA1Aphysical
14634002
GASP1_HUMANGPRASP1physical
16169070
HIP1_HUMANHIP1physical
16169070
MIC60_HUMANIMMTphysical
16169070
PSME1_HUMANPSME1physical
16169070
MED31_HUMANMED31physical
16169070
GIT1_HUMANGIT1physical
16169070
HAP1_HUMANHAP1physical
16169070
CE126_HUMANKIAA1377physical
16169070
LRIF1_HUMANLRIF1physical
16169070
RLA1_HUMANRPLP1physical
16169070
MIC60_HUMANIMMTphysical
21900206
EIF3C_HUMANEIF3Cphysical
21900206
HMGX3_HUMANHMGXB3physical
21900206
NDC80_HUMANNDC80physical
21900206
GIT1_HUMANGIT1physical
21900206
EDRF1_HUMANEDRF1physical
21900206
EXT2_HUMANEXT2physical
21900206
RMI1_HUMANRMI1physical
21900206
CMGA_HUMANCHGAphysical
21900206
EZH2_HUMANEZH2physical
21900206
INP5K_HUMANINPP5Kphysical
21900206
RS28_HUMANRPS28physical
21900206
BRK1_HUMANBRK1physical
21900206
EOMES_HUMANEOMESphysical
21900206
FA20C_HUMANFAM20Cphysical
21900206
K0408_HUMANKIAA0408physical
21900206
DCTN1_HUMANDCTN1physical
21900206
MYOME_HUMANPDE4DIPphysical
21900206
IF4A2_HUMANEIF4A2physical
21900206
SUMO3_HUMANSUMO3physical
21900206
CC85A_HUMANCCDC85Aphysical
21900206
DGC14_HUMANDGCR14physical
21900206
PLXB2_HUMANPLXNB2physical
21900206
SPTN4_HUMANSPTBN4physical
21900206
ODPB_HUMANPDHBphysical
21900206
COT1_HUMANNR2F1physical
21900206
SC31A_HUMANSEC31Aphysical
21900206
JADE1_HUMANJADE1physical
21900206
TTC38_HUMANTTC38physical
21900206
ALBU_HUMANALBphysical
21900206
IF140_HUMANIFT140physical
21900206
KPCD2_HUMANPRKD2physical
21900206
ASNA_HUMANASNA1physical
21900206
HXD8_HUMANHOXD8physical
21900206
PTN_HUMANPTNphysical
21900206
SNX5_HUMANSNX5physical
21900206
ZN235_HUMANZNF235physical
21900206
PFD2_HUMANPFDN2physical
22939629
PFD6_HUMANPFDN6physical
22939629
PFD5_HUMANPFDN5physical
22939629
PFD4_HUMANPFDN4physical
22939629
AASD1_HUMANAARSD1physical
22863883
DPP8_HUMANDPP8physical
22863883
FEN1_HUMANFEN1physical
22863883
PFD5_HUMANPFDN5physical
22863883
PP2AA_HUMANPPP2CAphysical
22863883
KAPCB_HUMANPRKACBphysical
22863883
PRPS1_HUMANPRPS1physical
22863883
SH3G1_HUMANSH3GL1physical
22863883
TSN_HUMANTSNphysical
22863883
UGGG1_HUMANUGGT1physical
22863883
PFD2_HUMANPFDN2physical
26344197
PFD5_HUMANPFDN5physical
26344197
PFD6_HUMANPFDN6physical
26344197
PFD3_HUMANVBP1physical
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 PFD1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.

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