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Protein

Oxysterol-binding protein 1

Gene

OSBP

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

Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum (PubMed:24209621). Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol (PubMed:15746430, PubMed:17428193). Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly (PubMed:15746430). Regulates cholesterol efflux by decreasing ABCA1 stability (PubMed:18450749).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei314SterolBy similarity1

<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

  • lipid binding Source: GO_Central
  • oxysterol binding Source: ProtInc
  • phosphatidylinositol-4-phosphate binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • sterol binding Source: GO_Central
  • sterol transporter activity Source: UniProtKB

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 processLipid transport, Transport
LigandLipid-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1660661 Sphingolipid de novo biosynthesis
R-HSA-192105 Synthesis of bile acids and bile salts

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P22059

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000490

<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:
Oxysterol-binding protein 1Curated
<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:OSBPImported
Synonyms:OSBP1
<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 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000110048.11

Human Gene Nomenclature Database

More...
HGNCi
HGNC:8503 OSBP

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
167040 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P22059

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, 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

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>Mutagenesisi108R → L: Impaired lipid exchange activity. Induces a shift in subcellular location to the endoplasmic reticulum. 1 Publication1
Mutagenesisi359 – 360FF → AA: Impaired lipid exchange activity. Abolishes interaction with VAPA. 1 Publication2

Organism-specific databases

DisGeNET

More...
DisGeNETi
5007

Open Targets

More...
OpenTargetsi
ENSG00000110048

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA32822

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
OSBP

Domain mapping of disease mutations (DMDM)

More...
DMDMi
129308

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00001003642 – 807Oxysterol-binding protein 1Add BLAST806

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 residuei2N-acetylalanineCombined sources1
Modified residuei190PhosphoserineCombined sources1
Modified residuei193PhosphoserineCombined sources1
Modified residuei198PhosphoserineCombined sources1
Modified residuei238PhosphoserineCombined sources1
Modified residuei240PhosphoserineCombined sources1
Modified residuei338PhosphoserineCombined sources1
Modified residuei345PhosphoserineBy similarity1
Modified residuei351PhosphoserineCombined sources1
Modified residuei377PhosphothreonineCombined sources1
Modified residuei379PhosphoserineCombined sources1
Modified residuei382PhosphoserineCombined sources1
Modified residuei385PhosphoserineCombined sources1
Modified residuei386PhosphoserineCombined sources1
Modified residuei389PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P22059

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P22059

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

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PaxDbi
P22059

PeptideAtlas

More...
PeptideAtlasi
P22059

PRoteomics IDEntifications database

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PRIDEi
P22059

ProteomicsDB human proteome resource

More...
ProteomicsDBi
53954

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P22059

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

More...
PhosphoSitePlusi
P22059

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P22059

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000110048 Expressed in 237 organ(s), highest expression level in oviduct epithelium

CleanEx database of gene expression profiles

More...
CleanExi
HS_OSBP

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P22059 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P22059 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA039227
HPA043625

<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

Homodimer or homotrimer. Interacts (via FFAT motif) with VAPA (PubMed:24209621, PubMed:20178991). Interacts (via C-terminus) with RELCH (via the third HEAT repeat) (By similarity). Found in a complex composed of RELCH, OSBP1 and RAB11A (By similarity).By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
111048, 46 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-489 VAPA-OSBP complex

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P22059

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P22059

Protein interaction database and analysis system

More...
IntActi
P22059, 8 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000263847

<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

1807
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P22059

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

More...
SMRi
P22059

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P22059

<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>Domaini88 – 181PHPROSITE-ProRule annotationAdd BLAST94

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>Regioni117 – 122Phosphatidylinositol 4-phosphate bindingBy similarity6
Regioni406 – 457Sterol bindingBy similarityAdd BLAST52
Regioni493 – 496Phosphatidylinositol 4-phosphate bindingBy similarity4
Regioni522 – 523Phosphatidylinositol 4-phosphate bindingBy similarity2

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili291 – 326Sequence analysisAdd BLAST36
Coiled coili730 – 760Sequence analysisAdd BLAST31

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi358 – 364FFAT1 Publication7

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 biasi1 – 93Ala/Gly-richAdd BLAST93

<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 FFAT motif is required for interaction with VATA and proper localization of the protein.1 Publication
The PH and the Ala/Gly-rich domains control cholesterol binding without affecting 25-hydroxycholesterol binding.By similarity
The second coiled-coil domain is required for interaction with the tyrosine phosphatase.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the OSBP family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1737 Eukaryota
ENOG410XP9E LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156164

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231233

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG053374

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P22059

KEGG Orthology (KO)

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KOi
K20456

Identification of Orthologs from Complete Genome Data

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OMAi
IHCIFHA

Database of Orthologous Groups

More...
OrthoDBi
EOG091G04HK

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P22059

TreeFam database of animal gene trees

More...
TreeFami
TF320922

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.29.30, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR037239 OSBP_sf
IPR000648 Oxysterol-bd
IPR018494 Oxysterol-bd_CS
IPR011993 PH-like_dom_sf
IPR001849 PH_domain

The PANTHER Classification System

More...
PANTHERi
PTHR10972 PTHR10972, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF01237 Oxysterol_BP, 1 hit
PF00169 PH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00233 PH, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF144000 SSF144000, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01013 OSBP, 1 hit
PS50003 PH_DOMAIN, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P22059-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAATELRGVV GPGPAAIAAL GGGGAGPPVV GGGGGRGDAG PGSGAASGTV
60 70 80 90 100
VAAAAGGPGP GAGGVAAAGP APAPPTGGSG GSGAGGSGSA REGWLFKWTN
110 120 130 140 150
YIKGYQRRWF VLSNGLLSYY RSKAEMRHTC RGTINLATAN ITVEDSCNFI
160 170 180 190 200
ISNGGAQTYH LKASSEVERQ RWVTALELAK AKAVKMLAES DESGDEESVS
210 220 230 240 250
QTDKTELQNT LRTLSSKVED LSTCNDLIAK HGTALQRSLS ELESLKLPAE
260 270 280 290 300
SNEKIKQVNE RATLFRITSN AMINACRDFL MLAQTHSKKW QKSLQYERDQ
310 320 330 340 350
RIRLEETLEQ LAKQHNHLER AFRGATVLPA NTPGNVGSGK DQCCSGKGDM
360 370 380 390 400
SDEDDENEFF DAPEIITMPE NLGHKRTGSN ISGASSDISL DEQYKHQLEE
410 420 430 440 450
TKKEKRTRIP YKPNYSLNLW SIMKNCIGKE LSKIPMPVNF NEPLSMLQRL
460 470 480 490 500
TEDLEYHELL DRAAKCENSL EQLCYVAAFT VSSYSTTVFR TSKPFNPLLG
510 520 530 540 550
ETFELDRLEE NGYRSLCEQV SHHPPAAAHH AESKNGWTLR QEIKITSKFR
560 570 580 590 600
GKYLSIMPLG TIHCIFHATG HHYTWKKVTT TVHNIIVGKL WIDQSGEIDI
610 620 630 640 650
VNHKTGDKCN LKFVPYSYFS RDVARKVTGE VTDPSGKVHF ALLGTWDEKM
660 670 680 690 700
ECFKVQPVIG ENGGDARQRG HEAEESRVML WKRNPLPKNA ENMYYFSELA
710 720 730 740 750
LTLNAWESGT APTDSRLRPD QRLMENGRWD EANAEKQRLE EKQRLSRKKR
760 770 780 790 800
EAEAMKATED GTPYDPYKAL WFERKKDPVT KELTHIYRGE YWECKEKQDW

SSCPDIF
Length:807
Mass (Da):89,421
Last modified:August 1, 1991 - v1
<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:i2590A47BCB54FDFB
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YCV6H0YCV6_HUMAN
Oxysterol-binding protein 1
OSBP
171Annotation score:

Annotation score:1 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH63121 differs from that shown. Aberrant splicing.Curated

Natural variant

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_036099278D → A in a colorectal cancer sample; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
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
M86917 mRNA Translation: AAA59973.1
AF185696 mRNA Translation: AAG17011.1
AF185705
, AF185697, AF185698, AF185699, AF185700, AF185701, AF185702, AF185703, AF185704 Genomic DNA Translation: AAG28373.1
BC011581 mRNA Translation: AAH11581.1
BC063121 mRNA Translation: AAH63121.1 Sequence problems.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS7974.1

Protein sequence database of the Protein Information Resource

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PIRi
A34581

NCBI Reference Sequences

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RefSeqi
NP_002547.1, NM_002556.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.597091

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000263847; ENSP00000263847; ENSG00000110048

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5007

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:5007

UCSC genome browser

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UCSCi
uc001noc.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
M86917 mRNA Translation: AAA59973.1
AF185696 mRNA Translation: AAG17011.1
AF185705
, AF185697, AF185698, AF185699, AF185700, AF185701, AF185702, AF185703, AF185704 Genomic DNA Translation: AAG28373.1
BC011581 mRNA Translation: AAH11581.1
BC063121 mRNA Translation: AAH63121.1 Sequence problems.
CCDSiCCDS7974.1
PIRiA34581
RefSeqiNP_002547.1, NM_002556.2
UniGeneiHs.597091

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
2RR3NMR-B346-379[»]
ProteinModelPortaliP22059
SMRiP22059
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111048, 46 interactors
ComplexPortaliCPX-489 VAPA-OSBP complex
CORUMiP22059
ELMiP22059
IntActiP22059, 8 interactors
STRINGi9606.ENSP00000263847

Chemistry databases

SwissLipidsiSLP:000000490

PTM databases

iPTMnetiP22059
PhosphoSitePlusiP22059
SwissPalmiP22059

Polymorphism and mutation databases

BioMutaiOSBP
DMDMi129308

Proteomic databases

EPDiP22059
MaxQBiP22059
PaxDbiP22059
PeptideAtlasiP22059
PRIDEiP22059
ProteomicsDBi53954

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263847; ENSP00000263847; ENSG00000110048
GeneIDi5007
KEGGihsa:5007
UCSCiuc001noc.1 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5007
DisGeNETi5007
EuPathDBiHostDB:ENSG00000110048.11

GeneCards: human genes, protein and diseases

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GeneCardsi
OSBP
HGNCiHGNC:8503 OSBP
HPAiHPA039227
HPA043625
MIMi167040 gene
neXtProtiNX_P22059
OpenTargetsiENSG00000110048
PharmGKBiPA32822

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG1737 Eukaryota
ENOG410XP9E LUCA
GeneTreeiENSGT00940000156164
HOGENOMiHOG000231233
HOVERGENiHBG053374
InParanoidiP22059
KOiK20456
OMAiIHCIFHA
OrthoDBiEOG091G04HK
PhylomeDBiP22059
TreeFamiTF320922

Enzyme and pathway databases

ReactomeiR-HSA-1660661 Sphingolipid de novo biosynthesis
R-HSA-192105 Synthesis of bile acids and bile salts
SIGNORiP22059

Miscellaneous databases

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

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ChiTaRSi
OSBP human
EvolutionaryTraceiP22059

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
OSBP

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

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GenomeRNAii
5007

Protein Ontology

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PROi
PR:P22059

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000110048 Expressed in 237 organ(s), highest expression level in oviduct epithelium
CleanExiHS_OSBP
ExpressionAtlasiP22059 baseline and differential
GenevisibleiP22059 HS

Family and domain databases

Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR037239 OSBP_sf
IPR000648 Oxysterol-bd
IPR018494 Oxysterol-bd_CS
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
PANTHERiPTHR10972 PTHR10972, 1 hit
PfamiView protein in Pfam
PF01237 Oxysterol_BP, 1 hit
PF00169 PH, 1 hit
SMARTiView protein in SMART
SM00233 PH, 1 hit
SUPFAMiSSF144000 SSF144000, 1 hit
PROSITEiView protein in PROSITE
PS01013 OSBP, 1 hit
PS50003 PH_DOMAIN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiOSBP1_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: P22059
Secondary accession number(s): Q6P524
<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: August 1, 1991
Last sequence update: August 1, 1991
Last modified: December 5, 2018
This is version 173 of the entry and version 1 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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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