PITPNB
entrez
23760
canonical
uniprot
P48739
canonical
ensembl
ENSG00000180957
resolver
ensp
ENSP00000321266
resolver
ensp
ENSP00000334738
resolver
ensp
ENSP00000487693
resolver
genesymbol
PITPNB
resolver
hgnc
HGNC:9002
resolver
uniprot
B3KYB8
resolver
uniprot
B7Z7Q0
resolver
uniprot
Q8N5W1
resolver
uniprot_entry
PIPNB_HUMAN
resolver
uniprot_sec
B3KYB8
resolver
uniprot_sec
B7Z7Q0
resolver
uniprot_sec
Q8N5W1
resolver
activity_regulation
ACTIVITY REGULATION: Phosphatidylinositol transfer activity is inhibited by N-ethylmaleimide. {ECO:0000269|PubMed:18636990}.
uniprot
proteins
amino_acid_sequence
MVLIKEFRVVLPCSVQEYQVGQLYSVAEASKNETGGGEGIEVLKNEPYEKDGEKGQYTHKIYHLKSKVPAFVRMIAPEGSLVFHEKAWNAYPYCRTIVTNEYMKDDFFIKIETWHKPDLGTLENVHGLDPNTWKTVEIVHIDIADRSQVEPADYKADEDPALFQSVKTKRGPLGPNWKKELANSPDCPQMCAYKLVTIKFKWWGLQSKVENFIQKQEKRIFTNFHRQLFCWIDKWIDLTMEDIRRMEDETQKELETMRKRGSVRGTSAADV
uniprot
proteins
function
FUNCTION: Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes (PubMed:10531358, PubMed:18636990, PubMed:20332109). Also catalyzes the transfer of sphingomyelin (By similarity). Required for COPI-mediated retrograde transport from the Golgi to the endoplasmic reticulum; phosphatidylinositol and phosphatidylcholine transfer activity is essential for this function (PubMed:20332109). {ECO:0000250|UniProtKB:Q9TR36, ECO:0000269|PubMed:10531358, ECO:0000269|PubMed:18636990, ECO:0000269|PubMed:20332109}.
uniprot
proteins
mass_dalton
31540
uniprot
proteins
mutagenesis
MUTAGEN 60; /note="K->A: Loss of phosphatidylinositol transfer activity but no effect on phosphatidylcholine transfer activity. Fails to rescue the retrograde transport defect from the Golgi to endoplasmic reticulum in PITPNB-deficient cells."; /evidence="ECO:0000269|PubMed:20332109"; MUTAGEN 89; /note="N->F: Loss of phosphatidylinositol transfer activity but no effect on phosphatidylcholine transfer activity. Fails to rescue the retrograde transport defect from the Golgi to endoplasmic reticulum in PITPNB-deficient cells."; /evidence="ECO:0000269|PubMed:20332109"; MUTAGEN 94; /note="C->T,A: Loss of phosphatidylcholine transfer activity but no effect on phosphatidylinositol transfer activity. Not inhibited by N-ethylmaleimide. Fails to rescue the retrograde transport defect from the Golgi to endoplasmic reticulum in PITPNB-deficient cells."; /evidence="ECO:0000269|PubMed:18636990, ECO:0000269|PubMed:20332109"; MUTAGEN 187; /note="C->A: No effect on phosphatidylinositol transfer activity."; /evidence="ECO:0000269|PubMed:18636990"; MUTAGEN 202..203; /note="WW->AA: Loss of phosphatidylinositol transfer activity. Fails to rescue the retrograde transport defect from the Golgi to endoplasmic reticulum in PITPNB-deficient cells."; /evidence="ECO:0000269|PubMed:18636990, ECO:0000269|PubMed:20332109
uniprot
proteins
post_translational_modification
PTM: Constitutive phosphorylation of Ser-262 has no effect on phospholipid transfer activity but is required for Golgi targeting. {ECO:0000250|UniProtKB:P53811}.
uniprot
proteins
protein_family
PI transfer class I subfamily
uniprot
proteins
protein_family
PtdIns transfer protein family
uniprot
proteins
pubmed
10531358
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18636990
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20332109
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
8541325
uniprot
proteins
sequence_length
271
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P53812}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P53812}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53812}; Cytoplasmic side {ECO:0000250|UniProtKB:P53812}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P53812}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53812}; Cytoplasmic side {ECO:0000250|UniProtKB:P53812}. Golgi apparatus {ECO:0000250|UniProtKB:P53811}. Note=Primarily cytosolic in its closed conformation, it becomes enriched on Golgi and endoplasmic reticulum membranes in its open state, where it mediates lipid transfer. {ECO:0000250|UniProtKB:P53812}.
uniprot
proteins