P22059 (OSBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Oxysterol-binding protein 1

Gene names

Name:	OSBP
Synonyms:	OSBP1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	807 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds cholesterol and a range of oxysterols. Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylate ERK1/2, whereas 25-hydroxycholesterol causes its disassembly. Regulates cholesterol efflux by decreasing ABCA1 stability. Ref.5 Ref.7
Subunit structure	Homodimer or homotrimer.
Subcellular location	Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Note: When bound to oxysterols, translocates to the periphery of Golgi membranes.
Tissue specificity	Widely expressed. Ref.2
Domain	The PH and 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 similarities	Belongs to the OSBP family. Contains 1 PH domain.
Sequence caution	The sequence AAH63121.1 differs from that shown. Reason: Aberrant splicing.

Ontologies

Keywords
Biological process	Lipid transport Transport
Cellular component	Cytoplasm Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Ligand	Lipid-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	lipid transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	oxysterol binding Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 807

807

Oxysterol-binding protein 1

PRO_0000100364

Regions

Domain

88 – 181

94

PH

Region

406 – 457

52

Sterol binding By similarity

Coiled coil

291 – 326

36

Potential

Coiled coil

730 – 760

31

Potential

Compositional bias

1 – 93

93

Ala/Gly-rich

Amino acid modifications

Modified residue

103

1

N6-acetyllysine Ref.13

Modified residue

190

1

Phosphoserine Ref.4 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Modified residue

193

1

Phosphoserine Ref.4 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Modified residue

198

1

Phosphoserine Ref.9

Modified residue

238

1

Phosphoserine By similarity

Modified residue

351

1

Phosphoserine Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Modified residue

377

1

Phosphothreonine Ref.11

Modified residue

379

1

Phosphoserine Ref.8 Ref.9 Ref.11

Modified residue

382

1

Phosphoserine Ref.8 Ref.9 Ref.11 Ref.12

Modified residue

385

1

Phosphoserine Ref.8 Ref.9 Ref.11

Modified residue

386

1

Phosphoserine Ref.8 Ref.11

Modified residue

389

1

Phosphoserine Ref.8 Ref.11

Natural variations

Natural variant

278

1

D → A in a colorectal cancer sample; somatic mutation. Ref.15

VAR_036099

Secondary structure

1

.

.

.

807

Helix Strand Turn

Details...

Beta strand

377 – 379

3

Sequences

	Sequence		Length	Mass (Da)
	P22059 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 2590A47BCB54FDFB	FASTA	807	89,421
	10 20 30 40 50 60 MAATELRGVV GPGPAAIAAL GGGGAGPPVV GGGGGRGDAG PGSGAASGTV VAAAAGGPGP 70 80 90 100 110 120 GAGGVAAAGP APAPPTGGSG GSGAGGSGSA REGWLFKWTN YIKGYQRRWF VLSNGLLSYY 130 140 150 160 170 180 RSKAEMRHTC RGTINLATAN ITVEDSCNFI ISNGGAQTYH LKASSEVERQ RWVTALELAK 190 200 210 220 230 240 AKAVKMLAES DESGDEESVS QTDKTELQNT LRTLSSKVED LSTCNDLIAK HGTALQRSLS 250 260 270 280 290 300 ELESLKLPAE SNEKIKQVNE RATLFRITSN AMINACRDFL MLAQTHSKKW QKSLQYERDQ 310 320 330 340 350 360 RIRLEETLEQ LAKQHNHLER AFRGATVLPA NTPGNVGSGK DQCCSGKGDM SDEDDENEFF 370 380 390 400 410 420 DAPEIITMPE NLGHKRTGSN ISGASSDISL DEQYKHQLEE TKKEKRTRIP YKPNYSLNLW 430 440 450 460 470 480 SIMKNCIGKE LSKIPMPVNF NEPLSMLQRL TEDLEYHELL DRAAKCENSL EQLCYVAAFT 490 500 510 520 530 540 VSSYSTTVFR TSKPFNPLLG ETFELDRLEE NGYRSLCEQV SHHPPAAAHH AESKNGWTLR 550 560 570 580 590 600 QEIKITSKFR GKYLSIMPLG TIHCIFHATG HHYTWKKVTT TVHNIIVGKL WIDQSGEIDI 610 620 630 640 650 660 VNHKTGDKCN LKFVPYSYFS RDVARKVTGE VTDPSGKVHF ALLGTWDEKM ECFKVQPVIG 670 680 690 700 710 720 ENGGDARQRG HEAEESRVML WKRNPLPKNA ENMYYFSELA LTLNAWESGT APTDSRLRPD 730 740 750 760 770 780 QRLMENGRWD EANAEKQRLE EKQRLSRKKR EAEAMKATED GTPYDPYKAL WFERKKDPVT 790 800 KELTHIYRGE YWECKEKQDW SSCPDIF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1970801] [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: 11278871] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney and Placenta.
[4]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190 AND SER-193, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"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: 15746430] [Abstract] Cited for: FUNCTION.
[6]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193 AND SER-351, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"OSBP negatively regulates ABCA1 protein stability." Bowden K., Ridgway N.D. J. Biol. Chem. 283:18210-18217(2008) [PubMed: 18450749] [Abstract] Cited for: FUNCTION.
[8]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351; SER-379; SER-382; SER-385; SER-386 AND SER-389, MASS SPECTROMETRY. Tissue: Platelet.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-198; SER-351; SER-379; SER-382 AND SER-385, MASS SPECTROMETRY. 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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193 AND SER-351, MASS SPECTROMETRY. 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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351; THR-377; SER-379; SER-382; SER-385; SER-386 AND SER-389, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-193; SER-351 AND SER-382, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103, MASS SPECTROMETRY.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-278.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00024971.

PIR

A34581.

RefSeq

NP_002547.1. NM_002556.2.

UniGene

Hs.597091.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2RR3	NMR	-	B	346-379	[»]

ProteinModelPortal

P22059.

SMR

P22059. Positions 89-184, 346-380.

ModBase

Search...

Protein-protein interaction databases

IntAct

P22059. 1 interaction.

STRING

P22059.

PTM databases

PhosphoSite

P22059.

Polymorphism databases

DMDM

129308.

Proteomic databases

PeptideAtlas

P22059.

PRIDE

P22059.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263847; ENSP00000263847; ENSG00000110048.

GeneID

5007.

KEGG

hsa:5007.

UCSC

uc001noc.1. human.

Organism-specific databases

CTD

5007.

GeneCards

GC11M059341.

H-InvDB

HIX0201667.

HGNC

HGNC:8503. OSBP.

MIM

167040. gene.

neXtProt

NX_P22059.

PharmGKB

PA32822.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG04525.

GeneTree

ENSGT00550000074251.

HOGENOM

HBG445378.

HOVERGEN

HBG053374.

InParanoid

P22059.

OMA

WEAGTAP.

OrthoDB

EOG49S65T.

PhylomeDB

P22059.

Gene expression databases

ArrayExpress

P22059.

Bgee

P22059.

CleanEx

HS_OSBP.

Genevestigator

P22059.

GermOnline

ENSG00000110048. Homo sapiens.

Family and domain databases

InterPro

IPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR011993. PH_type.
IPR001849. Pleckstrin_homology.
[Graphical view]

Gene3D

G3DSA:2.30.29.30. PH_type. 1 hit.

PANTHER

PTHR10972. Oxysterol_bd. 1 hit.

Pfam

PF01237. Oxysterol_BP. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]

SMART

SM00233. PH. 1 hit.
[Graphical view]

PROSITE

PS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

19280.

SOURCE

Search...

Entry information

Entry name

OSBP1_HUMAN

Accession

Primary (citable) accession number: P22059
Secondary accession number(s): Q6P524

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	January 25, 2012
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.