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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-Experimental evidence at protein leveli

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
Binding sitei314SterolBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • positive regulation of growth of symbiont in host Source: AgBase
  • sterol transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000110048-MONOMER.
ReactomeiR-HSA-1660661. Sphingolipid de novo biosynthesis.
R-HSA-192105. Synthesis of bile acids and bile salts.
SIGNORiP22059.

Chemistry databases

SwissLipidsiSLP:000000490.

Names & Taxonomyi

Protein namesi
Recommended name:
Oxysterol-binding protein 1Curated
Gene namesi
Name:OSBPImported
Synonyms:OSBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:8503. OSBP.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: HPA
  • cytoplasm Source: AgBase
  • cytosol Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • Golgi apparatus Source: HPA
  • Golgi membrane Source: UniProtKB
  • membrane Source: AgBase
  • nucleolus Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi5007.
OpenTargetsiENSG00000110048.
PharmGKBiPA32822.

Polymorphism and mutation databases

BioMutaiOSBP.
DMDMi129308.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001003642 – 807Oxysterol-binding protein 1Add BLAST806

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

EPDiP22059.
MaxQBiP22059.
PaxDbiP22059.
PeptideAtlasiP22059.
PRIDEiP22059.

PTM databases

iPTMnetiP22059.
PhosphoSitePlusiP22059.
SwissPalmiP22059.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000110048.
CleanExiHS_OSBP.
ExpressionAtlasiP22059. baseline and differential.
GenevisibleiP22059. HS.

Organism-specific databases

HPAiHPA039227.
HPA043625.

Interactioni

Subunit structurei

Homodimer or homotrimer. Interacts (via FFAT motif) with VAPA (PubMed:24209621, PubMed:20178991).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FKBP6O753442EBI-2681902,EBI-744771
sseLA0A0H3NDL63EBI-2681902,EBI-10726249From a different organism.
sseLQ8ZNG24EBI-2681902,EBI-10690213From a different organism.

GO - Molecular functioni

  • protein domain specific binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111048. 44 interactors.
IntActiP22059. 8 interactors.
MINTiMINT-5005941.
STRINGi9606.ENSP00000263847.

Structurei

Secondary structure

1807
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi377 – 379Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RR3NMR-B346-379[»]
ProteinModelPortaliP22059.
SMRiP22059.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22059.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini88 – 181PHPROSITE-ProRule annotationAdd BLAST94

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Coiled coili291 – 326Sequence analysisAdd BLAST36
Coiled coili730 – 760Sequence analysisAdd BLAST31

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi358 – 364FFAT1 Publication7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 93Ala/Gly-richAdd BLAST93

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

Sequence similaritiesi

Belongs to the OSBP family.Curated
Contains 1 PH domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1737. Eukaryota.
ENOG410XP9E. LUCA.
GeneTreeiENSGT00760000119155.
HOGENOMiHOG000231233.
HOVERGENiHBG053374.
InParanoidiP22059.
KOiK20456.
OMAiVGSGKDQ.
OrthoDBiEOG091G04HK.
PhylomeDBiP22059.
TreeFamiTF320922.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PANTHERiPTHR10972. PTHR10972. 2 hits.
PfamiPF01237. Oxysterol_BP. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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
Checksum:i2590A47BCB54FDFB
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036099278D → A in a colorectal cancer sample; somatic mutation. 1 Publication1

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.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

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:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RR3NMR-B346-379[»]
ProteinModelPortaliP22059.
SMRiP22059.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111048. 44 interactors.
IntActiP22059. 8 interactors.
MINTiMINT-5005941.
STRINGi9606.ENSP00000263847.

Chemistry databases

SwissLipidsiSLP:000000490.

PTM databases

iPTMnetiP22059.
PhosphoSitePlusiP22059.
SwissPalmiP22059.

Polymorphism and mutation databases

BioMutaiOSBP.
DMDMi129308.

Proteomic databases

EPDiP22059.
MaxQBiP22059.
PaxDbiP22059.
PeptideAtlasiP22059.
PRIDEiP22059.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5007.
DisGeNETi5007.
GeneCardsiOSBP.
HGNCiHGNC:8503. OSBP.
HPAiHPA039227.
HPA043625.
MIMi167040. gene.
neXtProtiNX_P22059.
OpenTargetsiENSG00000110048.
PharmGKBiPA32822.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1737. Eukaryota.
ENOG410XP9E. LUCA.
GeneTreeiENSGT00760000119155.
HOGENOMiHOG000231233.
HOVERGENiHBG053374.
InParanoidiP22059.
KOiK20456.
OMAiVGSGKDQ.
OrthoDBiEOG091G04HK.
PhylomeDBiP22059.
TreeFamiTF320922.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000110048-MONOMER.
ReactomeiR-HSA-1660661. Sphingolipid de novo biosynthesis.
R-HSA-192105. Synthesis of bile acids and bile salts.
SIGNORiP22059.

Miscellaneous databases

ChiTaRSiOSBP. human.
EvolutionaryTraceiP22059.
GeneWikiiOSBP.
GenomeRNAii5007.
PROiP22059.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000110048.
CleanExiHS_OSBP.
ExpressionAtlasiP22059. baseline and differential.
GenevisibleiP22059. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PANTHERiPTHR10972. PTHR10972. 2 hits.
PfamiPF01237. Oxysterol_BP. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiOSBP1_HUMAN
AccessioniPrimary (citable) accession number: P22059
Secondary accession number(s): Q6P524
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: November 30, 2016
This is version 161 of the entry and version 1 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.