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Entry version 136 (11 Dec 2019)
Sequence version 2 (07 Dec 2004)
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Protein

Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1

Gene

GPIHBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).By similarity5 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processTransport
LigandLipid-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-163125 Post-translational modification: synthesis of GPI-anchored proteins
R-HSA-8963889 Assembly of active LPL and LIPC lipase complexes
R-HSA-8963901 Chylomicron remodeling
R-HSA-975634 Retinoid metabolism and transport

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
Short name:
GPI-HBP1
Short name:
GPI-anchored HDL-binding protein 1
Alternative name(s):
High density lipoprotein-binding protein 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GPIHBP1
Synonyms:HBP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000277494.1

Human Gene Nomenclature Database

More...
HGNCi
HGNC:24945 GPIHBP1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
612757 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q8IV16

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Hyperlipoproteinemia 1D (HLPP1D)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by hyperlipoproteinemia, decreased plasma LPL levels in some patients, high plasma triglyceride levels, and refractory fasting chylomicronemia.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_07188165C → S in HLPP1D; does not affect protein expression at the cell surface; does not interact with LPL; promotes formation of dimers and oligomers severely reducing number of monomers. 2 PublicationsCorresponds to variant dbSNP:rs587777638EnsemblClinVar.1
Natural variantiVAR_07763465C → Y in HLPP1D; does not interact with LPL; promotes formation of dimers and oligomers severely reducing number of monomers. 2 PublicationsCorresponds to variant dbSNP:rs587777638EnsemblClinVar.1
Natural variantiVAR_07188268C → G in HLPP1D; does not affect protein expression at the cell surface; does not interact with LPL; promotes formation of dimers and oligomers reducing number of monomers. 2 PublicationsCorresponds to variant dbSNP:rs587777639EnsemblClinVar.1
Natural variantiVAR_07763568C → R in HLPP1D; unknown pathological significance; results in decreased GPIHBP1 expression; promotes formation of dimers and oligomers severely reducing number of monomers; does not affect interaction with LPL when associated in cis with F-14 in one individual. 2 PublicationsCorresponds to variant dbSNP:rs587777639EnsemblClinVar.1
Natural variantiVAR_07763668C → Y in HLPP1D; does not interact with LPL; promotes formation of dimers and oligomers severely reducing number of monomers. 2 Publications1
Natural variantiVAR_07763783C → R in HLPP1D. 1 Publication1
Natural variantiVAR_07188389C → F in HLPP1D; drastically affects interaction with LPL; promotes formation of dimers and oligomers reducing number of monomers. 2 PublicationsCorresponds to variant dbSNP:rs587777640EnsemblClinVar.1
Natural variantiVAR_077638108T → R in HLPP1D; does not interact with LPL; promotes formation of dimers and oligomers reducing number of monomers. 2 Publications1
Natural variantiVAR_058086115Q → P in HLPP1D; a patient with chylomicronemia; no effect on protein expression at the cell surface; loss of interaction with LPL; loss of interaction with chylomicrons; promotes formation of dimers and oligomers reducing number of monomers. 3 PublicationsCorresponds to variant dbSNP:rs587777637EnsemblClinVar.1
Natural variantiVAR_077639144S → F in HLPP1D. 1 PublicationCorresponds to variant dbSNP:rs78367243Ensembl.1
Natural variantiVAR_071884175G → R in HLPP1D; affects protein expression at the cell surface; reduces interaction with LPL. 1 PublicationCorresponds to variant dbSNP:rs145844329EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi38Y → F: Loss of sulfotyrosine formation. 1 Publication1
Mutagenesisi66Y → A: Promotes formation of dimers and oligomers reducing number of monomers. 1 Publication1
Mutagenesisi71L → A: Promotes formation of dimers and oligomers reducing number of monomers. 1 Publication1
Mutagenesisi91T → A: Promotes formation of dimers and oligomers reducing number of monomers. 1 Publication1
Mutagenesisi92L → A: Only slightly increased formation of dimers and oligomers. No effect on number of monomers. Loss of LPL interaction. 1 Publication1
Mutagenesisi93I → A: Promotes formation of dimers and oligomers reducing number of monomers. 1 Publication1
Mutagenesisi101G → S: Promotes formation of dimers and oligomers reducing number of monomers. Retained some interaction with LPL. 1 Publication1
Mutagenesisi104T → A: Promotes formation of dimers and oligomers reducing number of monomers. Retained some interaction with LPL. 1 Publication1
Mutagenesisi105T → A: Promotes formation of dimers and oligomers reducing number of monomers. 1 Publication1
Mutagenesisi106H → L: Promotes formation of dimers and oligomers severely reducing number of monomers. 1 Publication1
Mutagenesisi107S → A: Promotes formation of dimers and oligomers reducing number of monomers. 1 Publication1
Mutagenesisi108T → A: Retained some interaction with LPL. No effect on number of monomers. 1 Publication1
Mutagenesisi109W → C, P or T: Promotes formation of dimers and oligomers reducing number of monomers. Loss of LPL interaction. 1 Publication1
Mutagenesisi109W → S, Y, H, A or F: Loss of interaction with LPL. Only slightly increased formation of dimers and oligomers. No effect on number of monomers. 4 Publications1
Mutagenesisi115Q → K: No effect on number of monomers. 1 Publication1
Mutagenesisi126V → A: Promotes formation of dimers and oligomers reducing number of monomers. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
338328

MalaCards human disease database

More...
MalaCardsi
GPIHBP1
MIMi615947 phenotype

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
535458 Familial GPIHBP1 deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA162390135

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q8IV16 Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
GPIHBP1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
74728020

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 20Sequence analysisAdd BLAST20
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000031820821 – 151Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1Add BLAST131
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000429858152 – 184Removed in mature formCuratedAdd BLAST33

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei38Sulfotyrosine1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi65 ↔ 89Combined sources1 Publication
Disulfide bondi68 ↔ 77Combined sources1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi78N-linked (GlcNAc...) asparagineCombined sources2 Publications1
Disulfide bondi83 ↔ 110Combined sources1 Publication
Disulfide bondi114 ↔ 130Combined sources1 Publication
Disulfide bondi131 ↔ 136Combined sources1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi151GPI-anchor amidated glycineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Glycosylation of Asn-78 is critical for cell surface localization.By similarity
Sulfation of a Tyr in the N-terminal acidic region increases the affinity for LPL.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein, Sulfation

Proteomic databases

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q8IV16

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q8IV16

PeptideAtlas

More...
PeptideAtlasi
Q8IV16

PRoteomics IDEntifications database

More...
PRIDEi
Q8IV16

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
70643

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8IV16

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q8IV16

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000277494 Expressed in 143 organ(s), highest expression level in C1 segment of cervical spinal cord

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q8IV16 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA066302

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Mostly monomer, but also homodimer and homooligomer (PubMed:25387803).

Interacts with lipoprotein lipase (LPL) with 1:1 stoichiometry (PubMed:17997385, PubMed:26725083, PubMed:27929370, PubMed:29899144, PubMed:30559189, PubMed:19304573, PubMed:25387803).

Interacts with high affinity with high-density lipoprotein (HDL) (By similarity).

Interacts with chylomicrons.

Interacts with APOA5 (PubMed:17997385).

By similarity7 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
130712, 6 interactors

Protein interaction database and analysis system

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IntActi
Q8IV16, 1 interactor

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000480053

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q8IV16 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1184
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q8IV16

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini63 – 148UPAR/Ly6Add BLAST86

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni21 – 35Intrinsically disordered1 PublicationAdd BLAST15
Regioni27 – 50Important for LPL transport to the lumenal surface of endothelial cellsBy similarityAdd BLAST24
Regioni103 – 109Important for interaction with LPL2 Publications7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi25 – 31Poly-Glu7
Compositional biasi40 – 50Poly-GluAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal acidic region is intrinsically disordered (PubMed:26725083). This region contributes to LPL binding, stabilizes LPL and protects LPL against loss of activity (PubMed:26725083, PubMed:27929370).2 Publications

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410J46G Eukaryota
ENOG41116TR LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000112872

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8IV16

KEGG Orthology (KO)

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KOi
K20001

Database of Orthologous Groups

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OrthoDBi
515367at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8IV16

TreeFam database of animal gene trees

More...
TreeFami
TF338440

Family and domain databases

Database of protein disorder

More...
DisProti
DP01327

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016054 LY6_UPA_recep-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00021 UPAR_LY6, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q8IV16-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKALGAVLLA LLLCGRPGRG QTQQEEEEED EDHGPDDYDE EDEDEVEEEE
60 70 80 90 100
TNRLPGGRSR VLLRCYTCKS LPRDERCNLT QNCSHGQTCT TLIAHGNTES
110 120 130 140 150
GLLTTHSTWC TDSCQPITKT VEGTQVTMTC CQSSLCNVPP WQSSRVQDPT
160 170 180
GKGAGGPRGS SETVGAALLL NLLAGLGAMG ARRP
Length:184
Mass (Da):19,806
Last modified:December 7, 2004 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i89FF61B08A008C70
GO

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

The missense variant Arg-56 may be associated with severe hypertriglyceridemia and chylomicronemia.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04450314C → F Polymorphism; it may act as a disease modifier contributing to severe HLPP1D when associated with R-68 or F-89; results in decreased GPIHBP1 expression at the cell surface; does not affect interaction with LPL when associated in cis with R-68 in one individual. 3 PublicationsCorresponds to variant dbSNP:rs11538389Ensembl.1
Natural variantiVAR_04450456G → R Polymorphism; no discernible effect on interaction with LPL, chylomicrons or APOA5. 2 PublicationsCorresponds to variant dbSNP:rs587777636EnsemblClinVar.1
Natural variantiVAR_07188165C → S in HLPP1D; does not affect protein expression at the cell surface; does not interact with LPL; promotes formation of dimers and oligomers severely reducing number of monomers. 2 PublicationsCorresponds to variant dbSNP:rs587777638EnsemblClinVar.1
Natural variantiVAR_07763465C → Y in HLPP1D; does not interact with LPL; promotes formation of dimers and oligomers severely reducing number of monomers. 2 PublicationsCorresponds to variant dbSNP:rs587777638EnsemblClinVar.1
Natural variantiVAR_07188268C → G in HLPP1D; does not affect protein expression at the cell surface; does not interact with LPL; promotes formation of dimers and oligomers reducing number of monomers. 2 PublicationsCorresponds to variant dbSNP:rs587777639EnsemblClinVar.1
Natural variantiVAR_07763568C → R in HLPP1D; unknown pathological significance; results in decreased GPIHBP1 expression; promotes formation of dimers and oligomers severely reducing number of monomers; does not affect interaction with LPL when associated in cis with F-14 in one individual. 2 PublicationsCorresponds to variant dbSNP:rs587777639EnsemblClinVar.1
Natural variantiVAR_07763668C → Y in HLPP1D; does not interact with LPL; promotes formation of dimers and oligomers severely reducing number of monomers. 2 Publications1
Natural variantiVAR_07763783C → R in HLPP1D. 1 Publication1
Natural variantiVAR_07188389C → F in HLPP1D; drastically affects interaction with LPL; promotes formation of dimers and oligomers reducing number of monomers. 2 PublicationsCorresponds to variant dbSNP:rs587777640EnsemblClinVar.1
Natural variantiVAR_077638108T → R in HLPP1D; does not interact with LPL; promotes formation of dimers and oligomers reducing number of monomers. 2 Publications1
Natural variantiVAR_058086115Q → P in HLPP1D; a patient with chylomicronemia; no effect on protein expression at the cell surface; loss of interaction with LPL; loss of interaction with chylomicrons; promotes formation of dimers and oligomers reducing number of monomers. 3 PublicationsCorresponds to variant dbSNP:rs587777637EnsemblClinVar.1
Natural variantiVAR_077639144S → F in HLPP1D. 1 PublicationCorresponds to variant dbSNP:rs78367243Ensembl.1
Natural variantiVAR_071884175G → R in HLPP1D; affects protein expression at the cell surface; reduces interaction with LPL. 1 PublicationCorresponds to variant dbSNP:rs145844329EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AY245915 mRNA Translation: AAO86519.1
CH471162 Genomic DNA Translation: EAW82276.1
BC035810 mRNA Translation: AAH35810.2
BC063857 mRNA Translation: AAH63857.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS34954.1

NCBI Reference Sequences

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RefSeqi
NP_001288701.1, NM_001301772.1
NP_835466.2, NM_178172.5

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000622500; ENSP00000480053; ENSG00000277494

Database of genes from NCBI RefSeq genomes

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GeneIDi
338328

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:338328

UCSC genome browser

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UCSCi
uc033cbs.1 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY245915 mRNA Translation: AAO86519.1
CH471162 Genomic DNA Translation: EAW82276.1
BC035810 mRNA Translation: AAH35810.2
BC063857 mRNA Translation: AAH63857.1
CCDSiCCDS34954.1
RefSeqiNP_001288701.1, NM_001301772.1
NP_835466.2, NM_178172.5

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6E7KX-ray2.80C/D21-151[»]
6OAUX-ray2.48C/D21-151[»]
6OAZX-ray3.04E/F/G/H21-151[»]
6OB0X-ray2.81E/F/G/H21-151[»]
SMRiQ8IV16
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi130712, 6 interactors
IntActiQ8IV16, 1 interactor
STRINGi9606.ENSP00000480053

PTM databases

iPTMnetiQ8IV16
PhosphoSitePlusiQ8IV16

Polymorphism and mutation databases

BioMutaiGPIHBP1
DMDMi74728020

Proteomic databases

MassIVEiQ8IV16
PaxDbiQ8IV16
PeptideAtlasiQ8IV16
PRIDEiQ8IV16
ProteomicsDBi70643

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
338328

Genome annotation databases

EnsembliENST00000622500; ENSP00000480053; ENSG00000277494
GeneIDi338328
KEGGihsa:338328
UCSCiuc033cbs.1 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
338328
DisGeNETi338328
EuPathDBiHostDB:ENSG00000277494.1

GeneCards: human genes, protein and diseases

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GeneCardsi
GPIHBP1
HGNCiHGNC:24945 GPIHBP1
HPAiHPA066302
MalaCardsiGPIHBP1
MIMi612757 gene
615947 phenotype
neXtProtiNX_Q8IV16
Orphaneti535458 Familial GPIHBP1 deficiency
PharmGKBiPA162390135

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410J46G Eukaryota
ENOG41116TR LUCA
HOGENOMiHOG000112872
InParanoidiQ8IV16
KOiK20001
OrthoDBi515367at2759
PhylomeDBiQ8IV16
TreeFamiTF338440

Enzyme and pathway databases

ReactomeiR-HSA-163125 Post-translational modification: synthesis of GPI-anchored proteins
R-HSA-8963889 Assembly of active LPL and LIPC lipase complexes
R-HSA-8963901 Chylomicron remodeling
R-HSA-975634 Retinoid metabolism and transport

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
GPIHBP1 human

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
338328
PharosiQ8IV16 Tbio

Protein Ontology

More...
PROi
PR:Q8IV16
RNActiQ8IV16 protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000277494 Expressed in 143 organ(s), highest expression level in C1 segment of cervical spinal cord
GenevisibleiQ8IV16 HS

Family and domain databases

DisProtiDP01327
InterProiView protein in InterPro
IPR016054 LY6_UPA_recep-like
PfamiView protein in Pfam
PF00021 UPAR_LY6, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHDBP1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8IV16
Secondary accession number(s): Q6P3T2, Q86W15
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 7, 2004
Last modified: December 11, 2019
This is version 136 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
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