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Q9H4L5 (OSBL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Oxysterol-binding protein-related protein 3

Short name=ORP-3
Short name=OSBP-related protein 3
Gene names
Name:OSBPL3
Synonyms:KIAA0704, ORP3, OSBP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length887 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Tissue specificity

Isoform 1a, isoform 1b, isoform 1c and isoform 1d are highly expressed in brain, bone marrow, colon, kidney, lung, skeletal muscle, spleen, thymus and thyroid. Not expressed in heart and liver. Isoform 2a, isoform 2b, isoform 2c and isoform 2d are expressed in brain, bone marrow, kidney, skeletal muscle, spleen, thymus and thyroid. Not expressed in heart, liver and lung.

Sequence similarities

Belongs to the OSBP family.

Contains 1 PH domain.

Sequence caution

The sequence BAA31679.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ORFQ9Q2G45EBI-1051317,EBI-6248094From a different organism.

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1a (identifier: Q9H4L5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1b (identifier: Q9H4L5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     259-289: Missing.
Isoform 1c (identifier: Q9H4L5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     387-422: Missing.
Isoform 1d (identifier: Q9H4L5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     259-289: Missing.
     387-422: Missing.
Isoform 2a (identifier: Q9H4L5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     584-631: YVAAFAISAY...FQFFSEQVSH → RSQPSLATVQ...SSAWLFPVTL
     632-887: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 2b (identifier: Q9H4L5-6)

The sequence of this isoform differs from the canonical sequence as follows:
     259-289: Missing.
     584-631: YVAAFAISAY...FQFFSEQVSH → RSQPSLATVQ...SSAWLFPVTL
     632-887: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 2c (identifier: Q9H4L5-7)

The sequence of this isoform differs from the canonical sequence as follows:
     387-422: Missing.
     584-631: YVAAFAISAY...FQFFSEQVSH → RSQPSLATVQ...SSAWLFPVTL
     632-887: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 2d (identifier: Q9H4L5-8)

The sequence of this isoform differs from the canonical sequence as follows:
     259-289: Missing.
     387-422: Missing.
     584-631: YVAAFAISAY...FQFFSEQVSH → RSQPSLATVQ...SSAWLFPVTL
     632-887: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 887887Oxysterol-binding protein-related protein 3
PRO_0000100371

Regions

Domain51 – 14696PH

Amino acid modifications

Modified residue161Phosphoserine Ref.13
Modified residue341Phosphoserine Ref.15
Modified residue2511Phosphoserine Ref.13
Modified residue3041Phosphoserine Ref.13 Ref.16 Ref.17
Modified residue3721Phosphoserine Ref.13 Ref.17
Modified residue4101Phosphoserine Ref.12 Ref.13 Ref.15 Ref.17
Modified residue4371Phosphoserine Ref.11 Ref.12 Ref.15

Natural variations

Alternative sequence259 – 28931Missing in isoform 1b, isoform 1d, isoform 2b and isoform 2d.
VSP_008219
Alternative sequence387 – 42236Missing in isoform 1c, isoform 1d, isoform 2c and isoform 2d.
VSP_008220
Alternative sequence584 – 63148YVAAF…EQVSH → RSQPSLATVQPRSPSHEAIH GAHQRDSPCSLRFHFDCSVN RFITQSCLASSAWLFPVTL in isoform 2a, isoform 2b, isoform 2c and isoform 2d.
VSP_008221
Alternative sequence632 – 887256Missing in isoform 2a, isoform 2b, isoform 2c and isoform 2d.
VSP_008222
Natural variant3541M → V.
Corresponds to variant rs11768296 [ dbSNP | Ensembl ].
VAR_053548

Sequences

Sequence LengthMass (Da)Tools
Isoform 1a [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 12E16912BD3F2E99

FASTA887101,224
        10         20         30         40         50         60 
MMSDEKNLGV SQKLVSPSRS TSSCSSKQGS RQDSWEVVEG LRGEMNYTQE PPVQKGFLLK 

        70         80         90        100        110        120 
KRKWPLKGWH KRFFYLDKGI LKYAKSQTDI EREKLHGCID VGLSVMSVKK SSKCIDLDTE 

       130        140        150        160        170        180 
EHIYHLKVKS EEVFDEWVSK LRHHRMYRQN EIAMFPHEVN HFFSGSTITD SSSGVFDSIS 

       190        200        210        220        230        240 
SRKRSSISKQ NLFQTGSNVS FSCGGETRVP LWLQSSEDME KCSKDLAHCH AYLVEMSQLL 

       250        260        270        280        290        300 
QSMDVLHRTY SAPAINAIQG GSFESPKKEK RSHRRWRSRA IGKDAKGTLQ VPKPFSGPVR 

       310        320        330        340        350        360 
LHSSNPNLST LDFGEEKNYS DGSETSSEFS KMQEDLCHIA HKVYFTLRSA FNIMSAEREK 

       370        380        390        400        410        420 
LKQLMEQDAS SSPSAQVIGL KNALSSALAQ NTDLKERLRR IHAESLLLDS PAVAKSGDNL 

       430        440        450        460        470        480 
AEENSRDENR ALVHQLSNES RLSITDSLSE FFDAQEVLLS PSSSENEISD DDSYVSDISD 

       490        500        510        520        530        540 
NLSLDNLSND LDNERQTLGP VLDSGREAKS RRRTCLPAPC PSSSNISLWN ILRNNIGKDL 

       550        560        570        580        590        600 
SKVAMPVELN EPLNTLQRLC EELEYSELLD KAAQIPSPLE RMVYVAAFAI SAYASSYYRA 

       610        620        630        640        650        660 
GSKPFNPVLG ETYECIREDK GFQFFSEQVS HHPPISACHA ESRNFVFWQD VRWKNKFWGK 

       670        680        690        700        710        720 
SMEIVPIGTT HVTLPVFGDH FEWNKVTSCI HNILSGQRWI EHYGEIVIKN LHDDSCYCKV 

       730        740        750        760        770        780 
NFIKAKYWST NAHEIEGTVF DRSGKAVHRL FGKWHESIYC GGGSSSACVW RANPMPKGYE 

       790        800        810        820        830        840 
QYYSFTQFAL ELNEMDPSSK SLLPPTDTRF RPDQRFLEEG NLEEAEIQKQ RIEQLQRERR 

       850        860        870        880 
RVLEENHVEH QPRFFRKSDD DSWVSNGTYL ELRKDLGFSK LDHPVLW 

« Hide

Isoform 1b [UniParc].

Checksum: 1D56185E3FB98744
Show »

FASTA85697,687
Isoform 1c [UniParc].

Checksum: DA08C319F2BAEDCE
Show »

FASTA85197,325
Isoform 1d [UniParc].

Checksum: 3D0A8947F6EE4DC5
Show »

FASTA82093,788
Isoform 2a [UniParc].

Checksum: 7AC19EA7AE07E5E4
Show »

FASTA64272,211
Isoform 2b [UniParc].

Checksum: 1A92347357A219CE
Show »

FASTA61168,674
Isoform 2c [UniParc].

Checksum: EA72B4600CF3C1B8
Show »

FASTA60668,313
Isoform 2d [UniParc].

Checksum: CD8F92033643E963
Show »

FASTA57564,776

References

« Hide 'large scale' references
[1]"ORP-3, a human oxysterol-binding protein gene differentially expressed in hematopoietic cells."
Gregorio-King C.C., Collier G.R., McMillan J.S., Waugh C.M., McLeod J.L., Collier F.M., Kirkland M.A.
Blood 98:2279-2281(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
[2]"A family of 12 human genes containing oxysterol-binding domains."
Jaworski C.J., Moreira E., Li A., Lee R., Rodriguez I.R.
Genomics 78:185-196(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
[3]"ORP3 splice variants and their expression in human tissues and hematopoietic cells."
Collier F.M., Gregorio-King C.C., Apostolopoulos J., Walder K., Kirkland M.A.
DNA Cell Biol. 22:1-9(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B; 1C; 1D; 2A; 2B; 2C AND 2D).
[4]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A).
Tissue: Brain.
[5]Ohara O., Suyama M., Nagase T., Ishikawa K.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[6]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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].
[8]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] (ISOFORM 1A).
Tissue: Uterus.
[10]"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] OF 1-245 (ISOFORM 1A).
[11]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410 AND SER-437, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-251; SER-304; SER-372 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-410 AND SER-437, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"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-304; SER-372 AND SER-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY008372 mRNA. Translation: AAG23400.1.
AF392444 mRNA. Translation: AAL40657.1.
AF491781 mRNA. Translation: AAM27386.1.
AF491782 mRNA. Translation: AAM27387.1.
AF491783 mRNA. Translation: AAM27388.1.
AF491784 mRNA. Translation: AAM27389.1.
AF491785 mRNA. Translation: AAM27390.1.
AF491786 mRNA. Translation: AAM27391.1.
AF515639 mRNA. Translation: AAM74165.1.
AF515640 mRNA. Translation: AAM74166.1.
AB014604 mRNA. Translation: BAA31679.2. Different initiation.
AC003093 Genomic DNA. Translation: AAB83939.1.
AC004008 Genomic DNA. No translation available.
AC004016 Genomic DNA. Translation: AAC26986.2.
AC004239 Genomic DNA. No translation available.
CH236948 Genomic DNA. Translation: EAL24240.1.
CH236948 Genomic DNA. Translation: EAL24241.1.
CH236948 Genomic DNA. Translation: EAL24242.1.
CH236948 Genomic DNA. Translation: EAL24243.1.
CH236948 Genomic DNA. Translation: EAL24244.1.
CH236948 Genomic DNA. Translation: EAL24245.1.
CH471073 Genomic DNA. Translation: EAW93816.1.
CH471073 Genomic DNA. Translation: EAW93817.1.
CH471073 Genomic DNA. Translation: EAW93818.1.
CH471073 Genomic DNA. Translation: EAW93819.1.
CH471073 Genomic DNA. Translation: EAW93820.1.
CH471073 Genomic DNA. Translation: EAW93821.1.
BC017731 mRNA. Translation: AAH17731.1.
AF323727 mRNA. Translation: AAG53408.1.
CCDSCCDS47564.1. [Q9H4L5-4]
CCDS5390.1. [Q9H4L5-1]
CCDS5391.1. [Q9H4L5-2]
CCDS5392.1. [Q9H4L5-3]
RefSeqNP_056365.1. NM_015550.3. [Q9H4L5-1]
NP_663160.1. NM_145320.2. [Q9H4L5-2]
NP_663161.1. NM_145321.2. [Q9H4L5-3]
NP_663162.1. NM_145322.2. [Q9H4L5-4]
XP_005249755.1. XM_005249698.1. [Q9H4L5-1]
XP_006715744.1. XM_006715681.1. [Q9H4L5-2]
XP_006715745.1. XM_006715682.1. [Q9H4L5-3]
XP_006715746.1. XM_006715683.1. [Q9H4L5-4]
UniGeneHs.520259.

3D structure databases

ProteinModelPortalQ9H4L5.
SMRQ9H4L5. Positions 49-146, 519-887.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117497. 7 interactions.
IntActQ9H4L5. 5 interactions.
MINTMINT-1631853.

PTM databases

PhosphoSiteQ9H4L5.

Polymorphism databases

DMDM20139176.

Proteomic databases

MaxQBQ9H4L5.
PaxDbQ9H4L5.
PRIDEQ9H4L5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313367; ENSP00000315410; ENSG00000070882. [Q9H4L5-1]
ENST00000352860; ENSP00000315331; ENSG00000070882. [Q9H4L5-2]
ENST00000353930; ENSP00000315277; ENSG00000070882. [Q9H4L5-3]
ENST00000396429; ENSP00000379706; ENSG00000070882. [Q9H4L5-3]
ENST00000396431; ENSP00000379708; ENSG00000070882. [Q9H4L5-2]
ENST00000409069; ENSP00000386953; ENSG00000070882. [Q9H4L5-4]
ENST00000409452; ENSP00000386801; ENSG00000070882. [Q9H4L5-5]
ENST00000409555; ENSP00000386990; ENSG00000070882. [Q9H4L5-8]
ENST00000409759; ENSP00000386325; ENSG00000070882. [Q9H4L5-7]
ENST00000409863; ENSP00000386429; ENSG00000070882. [Q9H4L5-6]
ENST00000431825; ENSP00000389779; ENSG00000070882. [Q9H4L5-4]
GeneID26031.
KEGGhsa:26031.
UCSCuc003sxf.3. human. [Q9H4L5-1]
uc003sxg.3. human. [Q9H4L5-3]
uc003sxh.3. human. [Q9H4L5-2]
uc003sxi.3. human. [Q9H4L5-4]
uc003sxj.1. human. [Q9H4L5-7]
uc003sxk.1. human. [Q9H4L5-8]

Organism-specific databases

CTD26031.
GeneCardsGC07M024836.
HGNCHGNC:16370. OSBPL3.
HPAHPA000691.
HPA048401.
MIM606732. gene.
neXtProtNX_Q9H4L5.
PharmGKBPA32828.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG281324.
HOVERGENHBG058934.
InParanoidQ9H4L5.
OMAPLERMVY.
OrthoDBEOG780RKR.
PhylomeDBQ9H4L5.
TreeFamTF320922.

Gene expression databases

ArrayExpressQ9H4L5.
BgeeQ9H4L5.
GenevestigatorQ9H4L5.

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.
[Graphical view]
SMARTSM00233. PH. 1 hit.
[Graphical view]
PROSITEPS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSOSBPL3. human.
GeneWikiOSBPL3.
GenomeRNAi26031.
NextBio47824.
PROQ9H4L5.
SOURCESearch...

Entry information

Entry nameOSBL3_HUMAN
AccessionPrimary (citable) accession number: Q9H4L5
Secondary accession number(s): A4D167 expand/collapse secondary AC list , A4D168, A4D169, A4D170, A4D171, A4D172, B8ZZ79, B8ZZP0, O14591, O43357, O43358, Q8N702, Q8N703, Q8N704, Q8NFH0, Q8NFH1, Q8NI12, Q8NI13, Q9BZF4, Q9UED6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 111 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM