GPIHBP1
entrez
338328
canonical
uniprot
Q8IV16
canonical
ensembl
ENSG00000277494
resolver
ensp
ENSP00000480053
resolver
enst
ENST00000622500
resolver
genesymbol
GPIHBP1
resolver
genesymbol_syn
HBP1
resolver
hgnc
HGNC:24945
resolver
uniprot
Q6P3T2
resolver
uniprot
Q86W15
resolver
uniprot_entry
HDBP1_HUMAN
resolver
uniprot_sec
Q6P3T2
resolver
uniprot_sec
Q86W15
resolver
amino_acid_sequence
MKALGAVLLALLLFGRPGRGQTQQEEEEEDEDHGPDDYDEEDEDEVEEEETNRLPGGRSRVLLRCYTCKSLPRDERCNLTQNCSHGQTCTTLIAHGNTESGLLTTHSTWCTDSCQPITKTVEGTQVTMTCCQSSLCNVPPWQSSRVQDPTGKGAGGPRGSSETVGAALLLNLLAGLGAMGARRP
uniprot
proteins
disease_involvement
DISEASE: Hyperlipoproteinemia 1D (HLPP1D) [MIM:615947]: An autosomal recessive disorder characterized by hyperlipoproteinemia, decreased plasma LPL levels in some patients, high plasma triglyceride levels, and refractory fasting chylomicronemia. {ECO:0000269|PubMed:19304573, ECO:0000269|PubMed:20026666, ECO:0000269|PubMed:21314738, ECO:0000269|PubMed:21816778, ECO:0000269|PubMed:22239554, ECO:0000269|PubMed:23831619, ECO:0000269|PubMed:25387803, ECO:0000269|PubMed:27578123}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Mediates the transport of lipoprotein lipase LPL from the basolateral to the apical surface of endothelial cells in capillaries (By similarity). Anchors LPL on the surface of endothelial cells in the lumen of blood capillaries (By similarity). Protects LPL against loss of activity, and against ANGPTL4-mediated unfolding (PubMed:27929370, PubMed:29899144). Thereby, plays an important role in lipolytic processing of chylomicrons by LPL, triglyceride metabolism and lipid homeostasis (PubMed:19304573, PubMed:21314738). Binds chylomicrons and phospholipid particles that contain APOA5 (PubMed:17997385, PubMed:19304573). Binds high-density lipoprotein (HDL) and plays a role in the uptake of lipids from HDL (By similarity). {ECO:0000250|UniProtKB:Q9D1N2, ECO:0000269|PubMed:17997385, ECO:0000269|PubMed:19304573, ECO:0000269|PubMed:21314738, ECO:0000269|PubMed:27929370, ECO:0000269|PubMed:29899144}.
uniprot
proteins
mass_dalton
19850
uniprot
proteins
mutagenesis
MUTAGEN 38; /note="Y->F: Loss of sulfotyrosine formation."; /evidence="ECO:0000269|PubMed:29899144"; MUTAGEN 66; /note="Y->A: Promotes formation of dimers and oligomers reducing number of monomers."; /evidence="ECO:0000269|PubMed:25387803"; MUTAGEN 71; /note="L->A: Promotes formation of dimers and oligomers reducing number of monomers."; /evidence="ECO:0000269|PubMed:25387803"; MUTAGEN 91; /note="T->A: Promotes formation of dimers and oligomers reducing number of monomers."; /evidence="ECO:0000269|PubMed:25387803"; MUTAGEN 92; /note="L->A: Only slightly increased formation of dimers and oligomers. No effect on number of monomers. Loss of LPL interaction."; /evidence="ECO:0000269|PubMed:25387803"; MUTAGEN 93; /note="I->A: Promotes formation of dimers and oligomers reducing number of monomers."; /evidence="ECO:0000269|PubMed:25387803"; MUTAGEN 101; /note="G->S: Promotes formation of dimers and oligomers reducing number of monomers. Retained some interaction with LPL."; /evidence="ECO:0000269|PubMed:25387803"; MUTAGEN 104; /note="T->A: Promotes formation of dimers and oligomers reducing number of monomers. Retained some interaction with LPL."; /evidence="ECO:0000269|PubMed:25387803"; MUTAGEN 105; /note="T->A: Promotes formation of dimers and oligomers reducing number of monomers."; /evidence="ECO:0000269|PubMed:25387803"; MUTAGEN 106; /note="H->L: Promotes formation of dimers and oligomers severely reducing number of monomers."; /evidence="ECO:0000269|PubMed:25387803"; MUTAGEN 107; /note="S->A: Promotes formation of dimers and oligomers reducing number of monomers."; /evidence="ECO:0000269|PubMed:25387803"; MUTAGEN 108; /note="T->A: Retained some interaction with LPL. No effect on number of monomers."; /evidence="ECO:0000269|PubMed:25387803"; MUTAGEN 109; /note="W->C,P,T: Promotes formation of dimers and oligomers reducing number of monomers. Loss of LPL interaction."; /evidence="ECO:0000269|PubMed:25387803"; MUTAGEN 109; /note="W->S,Y,H,A,F: Loss of interaction with LPL. Only slightly increased formation of dimers and oligomers. No effect on number of monomers."; /evidence="ECO:0000269|PubMed:25387803, ECO:0000269|PubMed:26725083, ECO:0000269|PubMed:27811232, ECO:0000269|PubMed:30559189"; MUTAGEN 115; /note="Q->K: No effect on number of monomers."; /evidence="ECO:0000269|PubMed:25387803"; MUTAGEN 126; /note="V->A: Promotes formation of dimers and oligomers reducing number of monomers."; /evidence="ECO:0000269|PubMed:25387803
uniprot
proteins
post_translational_modification
PTM: Glycosylation of Asn-78 is critical for cell surface localization. {ECO:0000250|UniProtKB:Q9D1N2}.; PTM: Sulfation of a Tyr in the N-terminal acidic region increases the affinity for LPL. {ECO:0000269|PubMed:29899144}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17883852
uniprot
proteins
pubmed
17997385
uniprot
proteins
pubmed
19304573
uniprot
proteins
pubmed
20026666
uniprot
proteins
pubmed
21314738
uniprot
proteins
pubmed
21816778
uniprot
proteins
pubmed
21844202
uniprot
proteins
pubmed
22239554
uniprot
proteins
pubmed
23831619
uniprot
proteins
pubmed
25387803
uniprot
proteins
pubmed
26725083
uniprot
proteins
pubmed
27578123
uniprot
proteins
pubmed
27811232
uniprot
proteins
pubmed
27929370
uniprot
proteins
pubmed
29899144
uniprot
proteins
pubmed
30559189
uniprot
proteins
sequence_length
184
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q9D1N2}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9D1N2}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9D1N2}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9D1N2}. Cell membrane {ECO:0000269|PubMed:19304573}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9D1N2}.
uniprot
proteins