PLEKHO1
entrez
51177
canonical
uniprot
Q53GL0
canonical
ensembl
ENSG00000023902
resolver
ensp
ENSP00000358120
resolver
ensp
ENSP00000358122
resolver
enst
ENST00000369126
resolver
genesymbol
PLEKHO1
resolver
genesymbol_syn
CKIP1
resolver
genesymbol_syn
OC120
resolver
hgnc
HGNC:24310
resolver
uniprot
Q336K5
resolver
uniprot
Q5T4P9
resolver
uniprot
Q8IZ51
resolver
uniprot
Q9NRV3
resolver
uniprot
Q9UL48
resolver
uniprot_entry
PKHO1_HUMAN
resolver
uniprot_entry
Q5T4P9_HUMAN
resolver
uniprot_sec
Q336K5
resolver
uniprot_sec
Q8IZ51
resolver
uniprot_sec
Q9NRV3
resolver
uniprot_sec
Q9UL48
resolver
amino_acid_sequence
MMKKNNSAKRGPQDGNQQPAPPEKVGWVRKFCGKGIFREIWKNRYVVLKGDQLYISEKEVKDEKNIQEVFDLSDYEKCEELRKSKSRSKKNHSKFTLAHSKQPGNTAPNLIFLAVSPEEKESWINALNSAITRAKNRILDEVTVEEDSYLAHPTRDRAKIQHSRRPPTRGHLMAVASTSTSDGMLTLDLIQEEDPSPEEPTSCAESFRVDLDKSVAQLAGSRRRADSDRIQPSADRASSLSRPWEKTDKGATYTPQAPKKLTPTEKGRCASLEEILSQRDAASARTLQLRAEEPPTPALPNPGQLSRIQDLVARKLEETQELLAEVQGLGDGKRKAKDPPRSPPDSESEQLLLETERLLGEASSNWSQAKRVLQEVRELRDLYRQMDLQTPDSHLRQTTPHSQYRKSLM
uniprot
proteins
function
FUNCTION: Plays a role in the regulation of the actin cytoskeleton through its interactions with actin capping protein (CP). May function to target CK2 to the plasma membrane thereby serving as an adapter to facilitate the phosphorylation of CP by protein kinase 2 (CK2). Appears to target ATM to the plasma membrane. Appears to also inhibit tumor cell growth by inhibiting AKT-mediated cell-survival. Also implicated in PI3K-regulated muscle differentiation, the regulation of AP-1 activity (plasma membrane bound AP-1 regulator that translocates to the nucleus) and the promotion of apoptosis induced by tumor necrosis factor TNF. When bound to PKB, it inhibits it probably by decreasing PKB level of phosphorylation. {ECO:0000269|PubMed:14729969, ECO:0000269|PubMed:15706351, ECO:0000269|PubMed:15831458, ECO:0000269|PubMed:16325375, ECO:0000269|PubMed:16987810, ECO:0000269|PubMed:17197158, ECO:0000269|PubMed:17942896}.
uniprot
proteins
mass_dalton
46237
uniprot
proteins
mutagenesis
MUTAGEN 42; /note="K->C: No effect on subcellular localization. No effect on subcellular localization; when associated with C-44. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with W-123. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with C-44 and W-123."; /evidence="ECO:0000269|PubMed:15254037"; MUTAGEN 44; /note="R->C: No effect on subcellular localization. No effect on subcellular localization; when associated with C-42. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with W-123. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with C-42 and W-123."; /evidence="ECO:0000269|PubMed:15254037"; MUTAGEN 123; /note="W->A: Disruption of membrane localization and impaired interaction with CK2. Loss of phospholipid binding; when associated with C-42. Loss of phospholipid binding; when associated with C-44. Disruption of membrane localization, loss of phospholipid binding and impaired interaction with CK2; when associated with C-42 and C-44."; /evidence="ECO:0000269|PubMed:15254037"; MUTAGEN 133; /note="R->A: No effect on binding to capping proteins and loss of phospholipid binding; when associated with A-135 and A-137."; MUTAGEN 133; /note="R->E: No effect on binding to capping proteins; when associated with E-135."; MUTAGEN 135; /note="K->A: No effect on binding to capping proteins; when associated with A-133 and A-137."; MUTAGEN 135; /note="K->E: No effect on binding to capping proteins; when associated with E-133."; MUTAGEN 137; /note="R->A: No effect on binding to capping proteins; when associated with A-133 and A-135."; MUTAGEN 155; /note="R->A: No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins; when associated with A-157. Great loss of binding to capping proteins; when associated with A-157 and A-159."; /evidence="ECO:0000269|PubMed:16987810"; MUTAGEN 155; /note="R->E: No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins and no change in cell morphology and actin cytoskeleton; when associated with E-157."; /evidence="ECO:0000269|PubMed:16987810"; MUTAGEN 157; /note="R->A: No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins; when associated with A-155. Great loss of binding to capping proteins; when associated with A-155 and A-159."; /evidence="ECO:0000269|PubMed:16987810"; MUTAGEN 157; /note="R->E: No change in cell morphology and actin cytoskeleton. Great loss of binding to capping proteins and no change in cell morphology and actin cytoskeleton; when associated with E-155."; /evidence="ECO:0000269|PubMed:16987810"; MUTAGEN 159; /note="K->A: Great loss of binding to capping proteins; when associated with A-155 and A-157.
uniprot
proteins
post_translational_modification
PTM: C-terminal fragments could be released during apoptosis via caspase-3-dependent cleavage. {ECO:0000269|PubMed:15706351}.
uniprot
proteins
pubmed
10799509
uniprot
proteins
pubmed
11483580
uniprot
proteins
pubmed
11827170
uniprot
proteins
pubmed
14729969
uniprot
proteins
pubmed
15254037
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15706351
uniprot
proteins
pubmed
15831458
uniprot
proteins
pubmed
16325375
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16987810
uniprot
proteins
pubmed
17197158
uniprot
proteins
pubmed
17942896
uniprot
proteins
sequence_length
409
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10799509, ECO:0000269|PubMed:11827170, ECO:0000269|PubMed:14729969, ECO:0000269|PubMed:15254037, ECO:0000269|PubMed:16325375}; Peripheral membrane protein {ECO:0000305|PubMed:14729969}. Nucleus {ECO:0000269|PubMed:10799509, ECO:0000269|PubMed:11827170, ECO:0000269|PubMed:15706351}. Cytoplasm {ECO:0000269|PubMed:15706351}. Note=Predominantly localized to the plasma membrane through the binding to phosphatidylinositol 3-phosphate (PubMed:14729969). In C2C12 cells, with the absence of growth factor, it is found in the nucleus (PubMed:14729969). It rapidly translocates to the plasma membrane after insulin stimulation (PubMed:14729969). In response to TNF, it translocates from the plasma membrane to the cytoplasm and then to the nucleus accompanied by cleavage by caspase-3 (PubMed:15706351). However, the subcellular location is highly dependent of the cell type, and this explains why it is found exclusively at the plasma membrane, in some type of cells (Probable). {ECO:0000269|PubMed:14729969, ECO:0000269|PubMed:15706351, ECO:0000305}.
uniprot
proteins