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Protein

Oxysterol-binding protein 1

Gene

OSBP

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

Keywordsi

Biological processLipid transport, Transport
LigandLipid-binding

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000110048.11
HGNCiHGNC:8503 OSBP
MIMi167040 gene
neXtProtiNX_P22059

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

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
ProteomicsDBi53954

PTM databases

iPTMnetiP22059
PhosphoSitePlusiP22059
SwissPalmiP22059

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000110048 Expressed in 237 organ(s), highest expression level in oviduct epithelium
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). 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

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

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

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

Sequence (1+)i

Sequence statusi: Complete.

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.iShow 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
Checksum:i2590A47BCB54FDFB
GO

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:

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

Similar proteinsi

Entry informationi

Entry nameiOSBP1_HUMAN
AccessioniPrimary (citable) accession number: P22059
Secondary accession number(s): Q6P524
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: September 12, 2018
This is version 171 of the entry and version 1 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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