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. |
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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. |