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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei314 – 3141SterolBy similarity

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

ReactomeiR-HSA-1660661. Sphingolipid de novo biosynthesis.

Chemistry

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
ProteomesiUP000005640 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1081R → L: Impaired lipid exchange activity. Induces a shift in subcellular location to the endoplasmic reticulum. 1 Publication
Mutagenesisi359 – 3602FF → AA: Impaired lipid exchange activity. Abolishes interaction with VAPA. 1 Publication

Organism-specific databases

PharmGKBiPA32822.

Polymorphism and mutation databases

BioMutaiOSBP.
DMDMi129308.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 807806Oxysterol-binding protein 1PRO_0000100364Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei190 – 1901PhosphoserineCombined sources
Modified residuei193 – 1931PhosphoserineCombined sources
Modified residuei198 – 1981PhosphoserineCombined sources
Modified residuei240 – 2401PhosphoserineBy similarity
Modified residuei345 – 3451PhosphoserineBy similarity
Modified residuei351 – 3511PhosphoserineCombined sources
Modified residuei377 – 3771PhosphothreonineCombined sources
Modified residuei382 – 3821PhosphoserineCombined sources
Modified residuei385 – 3851PhosphoserineCombined sources
Modified residuei386 – 3861PhosphoserineCombined sources
Modified residuei389 – 3891PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP22059.
PaxDbiP22059.
PeptideAtlasiP22059.
PRIDEiP22059.

PTM databases

iPTMnetiP22059.
PhosphoSiteiP22059.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiP22059.
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.

Protein-protein interaction databases

BioGridi111048. 42 interactions.
IntActiP22059. 8 interactions.
MINTiMINT-5005941.
STRINGi9606.ENSP00000263847.

Structurei

Secondary structure

1
807
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi377 – 3793Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2RR3NMR-B346-379[»]
ProteinModelPortaliP22059.
SMRiP22059. Positions 91-180, 346-380, 405-801.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22059.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini88 – 18194PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni117 – 1226Phosphatidylinositol 4-phosphate bindingBy similarity
Regioni406 – 45752Sterol bindingBy similarityAdd
BLAST
Regioni493 – 4964Phosphatidylinositol 4-phosphate bindingBy similarity
Regioni522 – 5232Phosphatidylinositol 4-phosphate bindingBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili291 – 32636Sequence analysisAdd
BLAST
Coiled coili730 – 76031Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi358 – 3647FFAT1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 9393Ala/Gly-richAdd
BLAST

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.
OMAiVGSGKDQ.
OrthoDBiEOG7MPRD7.
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 AAH63121.1 differs from that shown.Aberrant splicing.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti278 – 2781D → A in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036099

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2RR3NMR-B346-379[»]
ProteinModelPortaliP22059.
SMRiP22059. Positions 91-180, 346-380, 405-801.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111048. 42 interactions.
IntActiP22059. 8 interactions.
MINTiMINT-5005941.
STRINGi9606.ENSP00000263847.

Chemistry

SwissLipidsiSLP:000000490.

PTM databases

iPTMnetiP22059.
PhosphoSiteiP22059.

Polymorphism and mutation databases

BioMutaiOSBP.
DMDMi129308.

Proteomic databases

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

Phylogenomic databases

eggNOGiKOG1737. Eukaryota.
ENOG410XP9E. LUCA.
GeneTreeiENSGT00760000119155.
HOGENOMiHOG000231233.
HOVERGENiHBG053374.
InParanoidiP22059.
OMAiVGSGKDQ.
OrthoDBiEOG7MPRD7.
PhylomeDBiP22059.
TreeFamiTF320922.

Enzyme and pathway databases

ReactomeiR-HSA-1660661. Sphingolipid de novo biosynthesis.

Miscellaneous databases

ChiTaRSiOSBP. human.
EvolutionaryTraceiP22059.
GeneWikiiOSBP.
GenomeRNAii5007.
NextBioi19280.
PROiP22059.
SOURCEiSearch...

Gene expression databases

BgeeiP22059.
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...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of human oxysterol-binding protein and localization of the gene to human chromosome 11 and mouse chromosome 19."
    Levanon D., Hsieh C.L., Francke U., Dawson P.A., Ridgway N.D., Brown M.S., Goldstein J.L.
    Genomics 7:65-74(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular and biochemical characterization of a novel oxysterol-binding protein (OSBP2) highly expressed in retina."
    Moreira E.F., Jaworski C., Li A., Rodriguez I.R.
    J. Biol. Chem. 276:18570-18578(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney and Placenta.
  4. "OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation."
    Wang P.-Y., Weng J., Anderson R.G.W.
    Science 307:1472-1476(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351 AND SER-382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "The mammalian oxysterol-binding protein-related proteins (ORPs) bind 25-hydroxycholesterol in an evolutionarily conserved pocket."
    Suchanek M., Hynynen R., Wohlfahrt G., Lehto M., Johansson M., Saarinen H., Radzikowska A., Thiele C., Olkkonen V.M.
    Biochem. J. 405:473-480(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "OSBP negatively regulates ABCA1 protein stability."
    Bowden K., Ridgway N.D.
    J. Biol. Chem. 283:18210-18217(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351; SER-382 AND SER-389, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-198; SER-351 AND SER-382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193 AND SER-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351 AND SER-382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193 AND SER-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP."
    Mesmin B., Bigay J., Moser von Filseck J., Lacas-Gervais S., Drin G., Antonny B.
    Cell 155:830-843(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, FFAT MOTIF, INTERACTION WITH VAPA, MUTAGENESIS OF ARG-108 AND 359-PHE-PHE-360.
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351; THR-377; SER-382; SER-385 AND SER-386, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Electrostatic interaction between oxysterol-binding protein and VAMP-associated protein A revealed by NMR and mutagenesis studies."
    Furuita K., Jee J., Fukada H., Mishima M., Kojima C.
    J. Biol. Chem. 285:12961-12970(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 346-379, INTERACTION WITH VAPA.
  20. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-278.

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: January 20, 2016
This is version 153 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.