PFD4_HUMAN - dbPTM
PFD4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PFD4_HUMAN
UniProt AC Q9NQP4
Protein Name Prefoldin subunit 4
Gene Name PFDN4
Organism Homo sapiens (Human).
Sequence Length 134
Subcellular Localization Nucleus . Cytoplasm . Mitochondrion .
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 MAATMKKAAAEDVNVTFEDQQKINKFARNTSRITELKEEIEVKKKQLQNLEDACDDIMLADDDCLMIPYQIGDVFISHSQEETQEMLEEAKKNLQEEIDALESRVESIQRVLADLKVQLYAKFGSNINLEADES
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------MAATMKKAA
------CCCHHHHHH
16.1922814378
4Phosphorylation----MAATMKKAAAE
----CCCHHHHHHHH
21.71-
6Ubiquitination--MAATMKKAAAEDV
--CCCHHHHHHHHHC
34.6022817900
7Ubiquitination-MAATMKKAAAEDVN
-CCCHHHHHHHHHCC
32.2222817900
31PhosphorylationNKFARNTSRITELKE
HHHHHCCHHHHHHHH
25.8225159151
37UbiquitinationTSRITELKEEIEVKK
CHHHHHHHHHHHHHH
47.2533845483
432-HydroxyisobutyrylationLKEEIEVKKKQLQNL
HHHHHHHHHHHHCCH
41.27-
92UbiquitinationEMLEEAKKNLQEEID
HHHHHHHHHHHHHHH
70.6829967540
103PhosphorylationEEIDALESRVESIQR
HHHHHHHHHHHHHHH
42.3421712546
125PhosphorylationQLYAKFGSNINLEAD
HHHHHCCCCCCCCCC
37.3626846344
134PhosphorylationINLEADES-------
CCCCCCCC-------
46.1723927012

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 PFD4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PFD4_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 PFD4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PFD5_HUMANPFDN5physical
22939629
PFD6_HUMANPFDN6physical
22939629
PFD3_HUMANVBP1physical
25416956
IF6_HUMANEIF6physical
26344197
FLNA_HUMANFLNAphysical
26344197
GFPT1_HUMANGFPT1physical
26344197
MSH2_HUMANMSH2physical
26344197
PFD1_HUMANPFDN1physical
26344197
PFD2_HUMANPFDN2physical
26344197
PFD5_HUMANPFDN5physical
26344197
PFD6_HUMANPFDN6physical
26344197
PPM1G_HUMANPPM1Gphysical
26344197
TRUA_HUMANPUS1physical
26344197
SIL1_HUMANSIL1physical
26344197
SLMAP_HUMANSLMAPphysical
26344197
PFD3_HUMANVBP1physical
26344197
RUSD2_HUMANRPUSD2physical
28514442
PFD3_HUMANVBP1physical
28514442
PFD2_HUMANPFDN2physical
28514442
KTNB1_HUMANKATNB1physical
28514442
PFD5_HUMANPFDN5physical
28514442
PFD1_HUMANPFDN1physical
28514442
RC3H2_HUMANRC3H2physical
28514442
KTNA1_HUMANKATNA1physical
28514442
PFD6_HUMANPFDN6physical
28514442
SPI2B_HUMANSPIN2Bphysical
28514442
ERCC8_HUMANERCC8physical
28514442
ATF2_HUMANATF2physical
28514442
MFR1L_HUMANMTFR1Lphysical
28514442
MIO_HUMANMIOSphysical
28514442
FBX28_HUMANFBXO28physical
28514442
BANP_HUMANBANPphysical
28514442
SPIN3_HUMANSPIN3physical
28514442
NEDD1_HUMANNEDD1physical
28514442
TRAF7_HUMANTRAF7physical
28514442
ZZZ3_HUMANZZZ3physical
28514442
CTU2_HUMANCTU2physical
28514442
PDRG1_HUMANPDRG1physical
28514442
KAISO_HUMANZBTB33physical
28514442
CREB1_HUMANCREB1physical
28514442
UBB_HUMANUBBphysical
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 PFD4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASSSPECTROMETRY.
"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-125, AND MASSSPECTROMETRY.

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