PITPNM1
entrez
9600
canonical
uniprot
O00562
canonical
ensembl
ENSG00000110697
resolver
ensp
ENSP00000348772
resolver
ensp
ENSP00000398787
resolver
ensp
ENSP00000437286
resolver
ensp
ENSP00000567647
resolver
ensp
ENSP00000567648
resolver
ensp
ENSP00000567649
resolver
genesymbol
PITPNM1
resolver
genesymbol_syn
DRES9
resolver
genesymbol_syn
NIR2
resolver
genesymbol_syn
PITPNM
resolver
hgnc
HGNC:9003
resolver
uniprot
A6NME4
resolver
uniprot
B2R787
resolver
uniprot
Q6T7X3
resolver
uniprot
Q8TBN3
resolver
uniprot
Q9BZ73
resolver
uniprot_entry
B2R787_HUMAN
resolver
uniprot_entry
PITM1_HUMAN
resolver
uniprot_sec
A6NME4
resolver
uniprot_sec
Q6T7X3
resolver
uniprot_sec
Q8TBN3
resolver
uniprot_sec
Q9BZ73
resolver
amino_acid_sequence
MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGSGQYTHKVYHVGSHIPGWFRALLPKAALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDPRLYHSVKTGRGPLSDDWARTAAQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWTELSMADIRALEEETARMLAQRMAKCNTGSEGSEAQPPGKPSTEARSAASNTGTPDGPEAPPGPDASPDASFGKQWSSSSRSSYSSQHGGAVSPQSLSEWRMQNIARDSENSSEEEFFDAHEGFSDSEEVFPKEMTKWNSNDFIDAFASPVEAEGTPEPGAEAAKGIEDGAQAPRDSEGLDGAGELGAEACAVHALFLILHSGNILDSGPGDANSKQADVQTLSSAFEAVTRIHFPEALGHVALRLVPCPPICAAAYALVSNLSPYSHDGDSLSRSQDHIPLAALPLLATSSSRYQGAVATVIARTNQAYSAFLRSPEGAGFCGQVALIGDGVGGILGFDALCHSANAGTGSRGSSRRGSMNNELLSPEFGPVRDPLADGVEGLGRGSPEPSALPPQRIPSDMASPEPEGSQNSLQAAPATTSSWEPRRASTAFCPPAASSEAPDGPSSTARLDFKVSGFFLFGSPLGLVLALRKTVMPALEAAQMRPACEQIYNLFHAADPCASRLEPLLAPKFQAIAPLTVPRYQKFPLGDGSSLLLADTLQTHSSLFLEELEMLVPSTPTSTSGAFWKGSELATDPPAQPAAPSTTSEVVKILERWWGTKRIDYSLYCPEALTAFPTVTLPHLFHASYWESADVVAFILRQVIEKERPQLAECEEPSIYSPAFPREKWQRKRTQVKIRNVTSNHRASDTVVCEGRPQVLSGRFMYGPLDVVTLTGEKVDVYIMTQPLSGKWIHFGTEVTNSSGRLTFPVPPERALGIGVYPVRMVVRGDHTYAECCLTVVARGTEAVVFSIDGSFTASVSIMGSDPKVRAGAVDVVRHWQDSGYLIVYVTGRPDMQKHRVVAWLSQHNFPHGVVSFCDGLTHDPLRQKAMFLQSLVQEVELNIVAGYGSPKDVAVYAALGLSPSQTYIVGRAVRKLQAQCQFLSDGYVAHLGQLEAGSHSHASSGPPRAALGKSSYGVAAPVDFLRKQSQLLRSRGPSQAEREGPGTPPTTLARGKARSISLKLDSEE
uniprot
proteins
function
FUNCTION: Membrane-associated phosphatidylinositol (PI) transfer protein that shuttles PI between intracellular membranes and thereby maintains plasma-membrane phosphoinositide signaling competence (PubMed:10531358, PubMed:22822086, PubMed:25887399, PubMed:26028218, PubMed:41129229). Transfers phosphatidylinositol from the endoplasmic reticulum to the plasma membrane and mediates counter-transport of phosphatidic acid (PA) from the plasma membrane to the endoplasmic reticulum at endoplasmic reticulum-plasma membrane contact sites, this PI/PA exchange is required for sustained PLC-coupled receptor signaling and for replenishment of plasma membrane phosphoinositide following receptor-induced hydrolysis (PubMed:10531358, PubMed:22822086, PubMed:26028218). Regulates RHOA activity, and plays a role in cytoskeleton remodeling (PubMed:11909959). Necessary for normal completion of cytokinesis (PubMed:15125835). Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus (PubMed:15723057). Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus (PubMed:15545272). Required for protein export from the endoplasmic reticulum and the Golgi (PubMed:11909959, PubMed:15545272, PubMed:15723057). {ECO:0000269|PubMed:10531358, ECO:0000269|PubMed:11909959, ECO:0000269|PubMed:15545272, ECO:0000269|PubMed:15723057, ECO:0000269|PubMed:22822086, ECO:0000269|PubMed:25887399, ECO:0000269|PubMed:26028218, ECO:0000269|PubMed:41129229}.
uniprot
proteins
mass_dalton
134848
uniprot
proteins
mutagenesis
MUTAGEN 59; /note="T->A,E: Loss of phosphatidic acid transfer form plasma membrane."; /evidence="ECO:0000269|PubMed:26028218"; MUTAGEN 59; /note="T->A: Prevents association with lipid droplets."; /evidence="ECO:0000269|PubMed:12225667"; MUTAGEN 59; /note="T->E: Causes association with lipid droplets."; /evidence="ECO:0000269|PubMed:12225667"; MUTAGEN 287; /note="T->A: Slightly reduced phosphorylation. Strongly reduced phosphorylation; when associated with A-794 or A-389. Loss of threonine phosphorylation; when associated with A-389; A-793 and A-1222."; /evidence="ECO:0000269|PubMed:15125835"; MUTAGEN 300; /note="S->A: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:15125835"; MUTAGEN 326; /note="S->A: No effect on phosphorylation."; /evidence="ECO:0000269|PubMed:15125835"; MUTAGEN 349..353; /note="EFFDA->ALLAG: Loss of interaction with VAPB."; /evidence="ECO:0000269|PubMed:15545272"; MUTAGEN 350..351; /note="FF->AA: Loss of endoplasmic reticulum membrane location but rapidly translocates to plasma membrane upon PLC activation."; /evidence="ECO:0000269|PubMed:26028218"; MUTAGEN 350; /note="F->S: Unable to mediate ER-PM membrane contact sites formation."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 382; /note="S->A: Strongly reduced phosphorylation."; /evidence="ECO:0000269|PubMed:15125835"; MUTAGEN 389; /note="T->A: No detectable effect on phosphorylation; when associated with A-793 and A-1222. Strongly reduced phosphorylation; when associated with A-287. Loss of threonine phosphorylation; when associated with A-287; A-794 and A-1222."; /evidence="ECO:0000269|PubMed:15125835"; MUTAGEN 520; /note="L->D: Loss of oligomerization. Decreased association with plasma membrane."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 794; /note="T->A: No detectable effect on phosphorylation; when associated with A-389 and A-1222. Strongly reduced phosphorylation; when associated with A-287. Loss of threonine phosphorylation; when associated with A-287; A-389 and A-1222."; /evidence="ECO:0000269|PubMed:15125835"; MUTAGEN 896; /note="S->A: Reduced phosphorylation."; /evidence="ECO:0000269|PubMed:15125835"; MUTAGEN 934..935; /note="VL->AA: Decreases translocation to the plasma membrane."; /evidence="ECO:0000269|PubMed:26028218"; MUTAGEN 944..946; /note="LDV->DDD: Strongly decreases association with plasma membrane."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 1027..1030; /note="IDGS->PDGP: Decreases association with phosphatidic acid and plasma membrane; when associated with A-1104 and A-1127."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 1066; /note="T->A: Abolishes association with phosphatidic acid and plasma membrane; when associated with A-1104 and A-1127."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 1104; /note="K->A: Abolishes association with phosphatidic acid and plasma membrane; when associated with A-1066 and A-1127."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 1127; /note="K->A: Abolishes association with phosphatidic acid and plasma membrane; when associated with A-1104 and A-1104."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 1150..1151; /note="RK->DD: Strongly decreases association with plasma membrane."; /evidence="ECO:0000269|PubMed:41129229"; MUTAGEN 1223; /note="T->A: No detectable effect on phosphorylation; when associated with A-389 and A-793. Loss of threonine phosphorylation; when associated with A-287; A-389 and A-794."; /evidence="ECO:0000269|PubMed:15125835
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on multiple sites by CDK1 at the onset of mitosis (PubMed:15125835). Phosphorylation facilitates dissociation from the Golgi complex and is required for interaction with PLK1 (PubMed:15125835). {ECO:0000269|PubMed:15125835}.; PTM: Phosphorylated on threonine residues upon treatment with oleic acid.; PTM: Phosphorylated on tyrosine residues by PTK2B. {ECO:0000269|PubMed:10022914}.
uniprot
proteins
protein_family
PI transfer class IIA subfamily
uniprot
proteins
protein_family
PtdIns transfer protein family
uniprot
proteins
pubmed
10022914
uniprot
proteins
pubmed
10531358
uniprot
proteins
pubmed
11909959
uniprot
proteins
pubmed
12225667
uniprot
proteins
pubmed
15125835
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15545272
uniprot
proteins
pubmed
15627748
uniprot
proteins
pubmed
15723057
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
22822086
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23897088
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25887399
uniprot
proteins
pubmed
26028218
uniprot
proteins
pubmed
41129229
uniprot
proteins
pubmed
9680295
uniprot
proteins
sequence_length
1244
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25887399, ECO:0000269|PubMed:26028218, ECO:0000269|PubMed:41129229}; Peripheral membrane protein {ECO:0000269|PubMed:25887399, ECO:0000269|PubMed:26028218, ECO:0000269|PubMed:41129229}; Cytoplasmic side {ECO:0000269|PubMed:25887399, ECO:0000269|PubMed:26028218, ECO:0000269|PubMed:41129229}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:12225667}; Peripheral membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12225667, ECO:0000269|PubMed:25887399, ECO:0000269|PubMed:26028218}; Peripheral membrane protein {ECO:0000269|PubMed:25887399, ECO:0000269|PubMed:26028218}; Cytoplasmic side {ECO:0000269|PubMed:25887399, ECO:0000269|PubMed:26028218}. Lipid droplet {ECO:0000269|PubMed:12225667}. Cleavage furrow {ECO:0000269|PubMed:15125835}. Midbody {ECO:0000269|PubMed:15125835}. Note=Upon PIP2 hydrolysis, translocates to endoplasmic reticulum-plasma membrane contact sites (PubMed:25887399). Peripheral membrane protein associated with Golgi stacks in interphase cells. Associated with lipid droplets (PubMed:12225667). Dissociates from the Golgi early on in mitosis and localizes to the cleavage furrow and midbody during cytokinesis (PubMed:15125835). {ECO:0000269|PubMed:12225667, ECO:0000269|PubMed:15125835, ECO:0000269|PubMed:25887399}.
uniprot
proteins