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Q969R2 (OSBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Oxysterol-binding protein 2
Alternative name(s):
Oxysterol-binding protein-related protein 4
Short name=ORP-4
Short name=OSBP-related protein 4
Gene names
Name:OSBP2
Synonyms:KIAA1664, ORP4, OSBPL4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length916 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds 7-ketocholesterol.

Subcellular location

Membrane; Peripheral membrane protein.

Tissue specificity

Expressed mainly in retina, testis, and fetal liver. Ref.1

Sequence similarities

Belongs to the OSBP family.

Contains 1 PH domain.

Sequence caution

The sequence AAK56864.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAK56865.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB33334.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   LigandLipid-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipid transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmembrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncholesterol binding

Inferred from direct assay PubMed 17428193. Source: BHF-UCL

phospholipid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 916916Oxysterol-binding protein 2
PRO_0000100366

Regions

Domain182 – 27493PH

Natural variations

Natural variant7601M → V.
Corresponds to variant rs34240867 [ dbSNP | Ensembl ].
VAR_053546

Experimental info

Sequence conflict341T → A in BAB33334. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q969R2 [UniParc].

Last modified February 21, 2006. Version 2.
Checksum: 3EAC49EB56516F18

FASTA916101,266
        10         20         30         40         50         60 
MGKAAAPSRG GGCGGRSRGL SSLFTVVPCL SCHTAAPGMS ASTSGSGPEP KPQPQPVPEP 

        70         80         90        100        110        120 
ERGPLSEQVS EAVSEAVPRS EPVSETTSEP EPGAGQPSEL LQGSRPGSES SSGVGAGPFT 

       130        140        150        160        170        180 
KAASEPLSRA VGSATFLRPE SGSLPALKPL PLLRPGQAKT PLGVPMSGTG TTSSAPLALL 

       190        200        210        220        230        240 
PLDSFEGWLL KWTNYLKGYQ RRWFVLGNGL LSYYRNQGEM AHTCRGTINL STAHIDTEDS 

       250        260        270        280        290        300 
CGILLTSGAR SYHLKASSEV DRQQWITALE LAKAKAVRVM NTHSDDSGDD DEATTPADKS 

       310        320        330        340        350        360 
ELHHTLKNLS LKLDDLSTCN DLIAKHGAAL QRSLTELDGL KIPSESGEKL KVVNERATLF 

       370        380        390        400        410        420 
RITSNAMINA CRDFLELAEI HSRKWQRALQ YEQEQRVHLE ETIEQLAKQH NSLERAFHSA 

       430        440        450        460        470        480 
PGRPANPSKS FIEGSLLTPK GEDSEEDEDT EYFDAMEDST SFITVITEAK EDSRKAEGST 

       490        500        510        520        530        540 
GTSSVDWSSA DNVLDGASLV PKGSSKVKRR VRIPNKPNYS LNLWSIMKNC IGRELSRIPM 

       550        560        570        580        590        600 
PVNFNEPLSM LQRLTEDLEY HHLLDKAVHC TSSVEQMCLV AAFSVSSYST TVHRIAKPFN 

       610        620        630        640        650        660 
PMLGETFELD RLDDMGLRSL CEQVSHHPPS AAHYVFSKHG WSLWQEITIS SKFRGKYISI 

       670        680        690        700        710        720 
MPLGAIHLEF QASGNHYVWR KSTSTVHNII VGKLWIDQSG DIEIVNHKTN DRCQLKFLPY 

       730        740        750        760        770        780 
SYFSKEAARK VTGVVSDSQG KAHYVLSGSW DEQMECSKVM HSSPSSPSSD GKQKTVYQTL 

       790        800        810        820        830        840 
SAKLLWKKYP LPENAENMYY FSELALTLNE HEEGVAPTDS RLRPDQRLME KGRWDEANTE 

       850        860        870        880        890        900 
KQRLEEKQRL SRRRRLEACG PGSSCSSEEE KEADAYTPLW FEKRLDPLTG EMACVYKGGY 

       910 
WEAKEKQDWH MCPNIF 

« Hide

References

« Hide 'large scale' references
[1]"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], NUCLEOTIDE SEQUENCE [MRNA] OF 2-916, TISSUE SPECIFICITY.
[2]"The OSBP-related protein family in humans."
Lehto M., Laitinen S., Chinetti G., Johansson M., Ehnholm C., Staels B., Ikonen E., Olkkonen V.M.
J. Lipid Res. 42:1203-1213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping."
Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.
DNA Res. 8:1-9(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]Ohara O., Nagase T., Kikuno R.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[5]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF288741 mRNA. Translation: AAK56864.1. Different initiation.
AF288742 Genomic DNA. Translation: AAK56865.1. Different initiation.
AF323731 mRNA. Translation: AAG53406.1.
AB051451 mRNA. Translation: BAB33334.2. Different initiation.
AC004542 Genomic DNA. Translation: AAC12953.1.
AL079299, AC004542, AL022336 Genomic DNA. Translation: CAQ07396.1.
AL022336, AC004542, AL079299 Genomic DNA. Translation: CAQ07892.1.
CH471095 Genomic DNA. Translation: EAW59916.1.
IPIIPI00746936.
PIRT02435.
RefSeqNP_110385.1. NM_030758.3.
UniGeneHs.517546.

3D structure databases

ProteinModelPortalQ969R2.
ModBaseSearch...

Protein-protein interaction databases

STRING9606.ENSP00000332576.

PTM databases

PhosphoSiteQ969R2.

Polymorphism databases

DMDM88984633.

Proteomic databases

PaxDbQ969R2.
PRIDEQ969R2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332585; ENSP00000332576; ENSG00000184792.
GeneID23762.
KEGGhsa:23762.
UCSCuc003aiy.1. human.

Organism-specific databases

CTD23762.
GeneCardsGC22P031089.
H-InvDBHIX0041322.
HGNCHGNC:8504. OSBP2.
HPAHPA021514.
MIM606729. gene.
neXtProtNX_Q969R2.
PharmGKBPA32823.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG281324.
HOGENOMHOG000231233.
HOVERGENHBG053374.
OMADGLKIPS.

Gene expression databases

ArrayExpressQ969R2.
BgeeQ969R2.
CleanExHS_OSBP2.
GenevestigatorQ969R2.
GermOnlineENSG00000184792. Homo sapiens.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PANTHERPTHR10972. PTHR10972. 1 hit.
PfamPF01237. Oxysterol_BP. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
[Graphical view]
PROSITEPS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi23762.
NextBio46715.
SOURCESearch...

Entry information

Entry nameOSBP2_HUMAN
AccessionPrimary (citable) accession number: Q969R2
Secondary accession number(s): B0QYG1 expand/collapse secondary AC list , O60396, Q9BY96, Q9BZF0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: February 21, 2006
Last modified: May 1, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families