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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MAATMKKAA ------CCCHHHHHH | 16.19 | 22814378 | |
4 | Phosphorylation | ----MAATMKKAAAE ----CCCHHHHHHHH | 21.71 | - | |
6 | Ubiquitination | --MAATMKKAAAEDV --CCCHHHHHHHHHC | 34.60 | 22817900 | |
7 | Ubiquitination | -MAATMKKAAAEDVN -CCCHHHHHHHHHCC | 32.22 | 22817900 | |
31 | Phosphorylation | NKFARNTSRITELKE HHHHHCCHHHHHHHH | 25.82 | 25159151 | |
37 | Ubiquitination | TSRITELKEEIEVKK CHHHHHHHHHHHHHH | 47.25 | 33845483 | |
43 | 2-Hydroxyisobutyrylation | LKEEIEVKKKQLQNL HHHHHHHHHHHHCCH | 41.27 | - | |
92 | Ubiquitination | EMLEEAKKNLQEEID HHHHHHHHHHHHHHH | 70.68 | 29967540 | |
103 | Phosphorylation | EEIDALESRVESIQR HHHHHHHHHHHHHHH | 42.34 | 21712546 | |
125 | Phosphorylation | QLYAKFGSNINLEAD HHHHHCCCCCCCCCC | 37.36 | 26846344 | |
134 | Phosphorylation | INLEADES------- CCCCCCCC------- | 46.17 | 23927012 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PFD4_HUMAN !! |
* 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 !! |
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. |
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Phosphorylation | |
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: 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. |