| UniProt ID | PKHF1_HUMAN | |
|---|---|---|
| UniProt AC | Q96S99 | |
| Protein Name | Pleckstrin homology domain-containing family F member 1 | |
| Gene Name | PLEKHF1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 279 | |
| Subcellular Localization | Nucleus . Cytoplasm, perinuclear region . Lysosome . Translocates to lysosome during apoptosis. | |
| Protein Description | May induce apoptosis through the lysosomal-mitochondrial pathway. Translocates to the lysosome initiating the permeabilization of lysosomal membrane (LMP) and resulting in the release of CTSD and CTSL to the cytoplasm. Triggers the caspase-independent apoptosis by altering mitochondrial membrane permeabilization (MMP) resulting in the release of PDCD8.. | |
| Protein Sequence | MVDHLANTEINSQRIAAVESCFGASGQPLALPGRVLLGEGVLTKECRKKAKPRIFFLFNDILVYGSIVLNKRKYRSQHIIPLEEVTLELLPETLQAKNRWMIKTAKKSFVVSAASATERQEWISHIEECVRRQLRATGRPPSTEHAAPWIPDKATDICMRCTQTRFSALTRRHHCRKCGFVVCAECSRQRFLLPRLSPKPVRVCSLCYRELAAQQRQEEAEEQGAGSPGQPAHLARPICGASSGDDDDSDEDKEGSRDGDWPSSVEFYASGVAWSAFHS | |
| 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 |
|---|---|---|---|---|---|
| 8 | Phosphorylation | MVDHLANTEINSQRI CCCCCCCCCCHHHHH | 32.41 | 25002506 | |
| 12 | Phosphorylation | LANTEINSQRIAAVE CCCCCCHHHHHHHHH | 26.88 | 25002506 | |
| 44 | Malonylation | LGEGVLTKECRKKAK ECCCCCCHHHHHHCC | 51.13 | 26320211 | |
| 44 | Acetylation | LGEGVLTKECRKKAK ECCCCCCHHHHHHCC | 51.13 | 23749302 | |
| 44 | Ubiquitination | LGEGVLTKECRKKAK ECCCCCCHHHHHHCC | 51.13 | 19608861 | |
| 97 | Ubiquitination | LPETLQAKNRWMIKT CHHHHHHCCCEEEHH | 33.80 | - | |
| 108 | Phosphorylation | MIKTAKKSFVVSAAS EEHHCHHHEEEECCC | 23.67 | 21955146 | |
| 112 | Phosphorylation | AKKSFVVSAASATER CHHHEEEECCCCHHH | 16.89 | 21955146 | |
| 115 | Phosphorylation | SFVVSAASATERQEW HEEEECCCCHHHHHH | 35.13 | 21955146 | |
| 137 | Phosphorylation | VRRQLRATGRPPSTE HHHHHHHHCCCCCCC | 27.56 | 26437602 | |
| 142 | Phosphorylation | RATGRPPSTEHAAPW HHHCCCCCCCCCCCC | 49.46 | 28348404 | |
| 143 | Phosphorylation | ATGRPPSTEHAAPWI HHCCCCCCCCCCCCC | 37.25 | 28348404 | |
| 197 | Phosphorylation | RFLLPRLSPKPVRVC CCCCCCCCCCCEEHH | 31.96 | 26434776 | |
| 205 | Phosphorylation | PKPVRVCSLCYRELA CCCEEHHHHHHHHHH | 20.72 | 22617229 | |
| 227 | Phosphorylation | AEEQGAGSPGQPAHL HHHCCCCCCCCCCCC | 25.89 | 23401153 | |
| 242 | Phosphorylation | ARPICGASSGDDDDS CCCCCCCCCCCCCCC | 21.82 | 23663014 | |
| 243 | Phosphorylation | RPICGASSGDDDDSD CCCCCCCCCCCCCCC | 45.79 | 23663014 | |
| 249 | Phosphorylation | SSGDDDDSDEDKEGS CCCCCCCCCCCCCCC | 50.31 | 23663014 | |
| 256 | Phosphorylation | SDEDKEGSRDGDWPS CCCCCCCCCCCCCCC | 28.43 | 25850435 |
| 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 PKHF1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PKHF1_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 PKHF1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| LMBL3_HUMAN | L3MBTL3 | physical | 25416956 |
| 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. | ||||||
loading...
| Acetylation | |
| Reference | PubMed |
| "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-44, AND MASS SPECTROMETRY. | |