| UniProt ID | PFD6_HUMAN | |
|---|---|---|
| UniProt AC | O15212 | |
| Protein Name | Prefoldin subunit 6 | |
| Gene Name | PFDN6 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 129 | |
| 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 | MAELIQKKLQGEVEKYQQLQKDLSKSMSGRQKLEAQLTENNIVKEELALLDGSNVVFKLLGPVLVKQELGEARATVGKRLDYITAEIKRYESQLRDLERQSEQQRETLAQLQQEFQRAQAAKAGAPGKA | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAELIQKKL ------CHHHHHHHH | 21.94 | 22814378 | |
| 7 | Ubiquitination | -MAELIQKKLQGEVE -CHHHHHHHHHHHHH | 48.75 | - | |
| 7 | Acetylation | -MAELIQKKLQGEVE -CHHHHHHHHHHHHH | 48.75 | 25953088 | |
| 8 | Ubiquitination | MAELIQKKLQGEVEK CHHHHHHHHHHHHHH | 29.66 | - | |
| 15 | Acetylation | KLQGEVEKYQQLQKD HHHHHHHHHHHHHHH | 54.24 | 23954790 | |
| 15 | Ubiquitination | KLQGEVEKYQQLQKD HHHHHHHHHHHHHHH | 54.24 | 21890473 | |
| 16 | Phosphorylation | LQGEVEKYQQLQKDL HHHHHHHHHHHHHHH | 6.49 | 27642862 | |
| 21 | Acetylation | EKYQQLQKDLSKSMS HHHHHHHHHHHHHHC | 70.04 | 19608861 | |
| 21 | Ubiquitination | EKYQQLQKDLSKSMS HHHHHHHHHHHHHHC | 70.04 | 19608861 | |
| 25 | Acetylation | QLQKDLSKSMSGRQK HHHHHHHHHHCHHHH | 58.43 | 25953088 | |
| 25 | Ubiquitination | QLQKDLSKSMSGRQK HHHHHHHHHHCHHHH | 58.43 | - | |
| 32 | Ubiquitination | KSMSGRQKLEAQLTE HHHCHHHHHHHHHHH | 47.11 | - | |
| 38 | Phosphorylation | QKLEAQLTENNIVKE HHHHHHHHHCCCHHH | 25.29 | - | |
| 44 | Ubiquitination | LTENNIVKEELALLD HHHCCCHHHHHHHHC | 41.49 | - | |
| 58 | Ubiquitination | DGSNVVFKLLGPVLV CCCCHHHHHHHHHHH | 31.06 | - | |
| 66 | Acetylation | LLGPVLVKQELGEAR HHHHHHHHHHHHHHH | 33.62 | 19608861 | |
| 66 | Ubiquitination | LLGPVLVKQELGEAR HHHHHHHHHHHHHHH | 33.62 | 21890473 | |
| 66 | Sumoylation | LLGPVLVKQELGEAR HHHHHHHHHHHHHHH | 33.62 | 19608861 | |
| 82 | Phosphorylation | TVGKRLDYITAEIKR HHHHHHHHHHHHHHH | 12.55 | 25884760 | |
| 84 | Phosphorylation | GKRLDYITAEIKRYE HHHHHHHHHHHHHHH | 16.41 | 28152594 | |
| 88 | Acetylation | DYITAEIKRYESQLR HHHHHHHHHHHHHHH | 40.19 | 25953088 | |
| 88 | Ubiquitination | DYITAEIKRYESQLR HHHHHHHHHHHHHHH | 40.19 | 21890473 | |
| 90 | Phosphorylation | ITAEIKRYESQLRDL HHHHHHHHHHHHHHH | 18.22 | 22817900 | |
| 92 | Phosphorylation | AEIKRYESQLRDLER HHHHHHHHHHHHHHH | 26.11 | 23898821 | |
| 122 | Ubiquitination | FQRAQAAKAGAPGKA HHHHHHHHCCCCCCC | 50.82 | - | |
| 128 | Acetylation | AKAGAPGKA------ HHCCCCCCC------ | 50.27 | 156419 |
| 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 PFD6_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PFD6_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 PFD6_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CSTF2_HUMAN | CSTF2 | physical | 26344197 | |
| PFD2_HUMAN | PFDN2 | physical | 26344197 | |
| PFD5_HUMAN | PFDN5 | physical | 26344197 | |
| PFD3_HUMAN | VBP1 | physical | 26344197 |
| 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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| 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. | |
| "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-21 AND LYS-66, AND MASSSPECTROMETRY. | |
