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Protein

Oxysterol-binding protein-related protein 3

Gene

OSBPL3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Phosphoinositide-binding protein which associates with both cell and endoplasmic reticulum (ER) membranes (PubMed:16143324). Can bind to the ER membrane protein VAPA and recruit VAPA to plasma membrane sites, thus linking these intracellular compartments (PubMed:25447204). The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface (PubMed:18270267, PubMed:25447204). With VAPA, may regulate ER morphology (PubMed:16143324). Has a role in regulation of the actin cytoskeleton, cell polarity and cell adhesion (PubMed:18270267). Binds to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3 (PubMed:16143324). Also binds 25-hydroxycholesterol and cholesterol (PubMed:17428193).4 Publications

GO - Molecular functioni

  • cholesterol binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Oxysterol-binding protein-related protein 3
Short name:
ORP-3
Short name:
OSBP-related protein 3
Gene namesi
Name:OSBPL3
Synonyms:KIAA0704, ORP3, OSBP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:16370. OSBPL3.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: BHF-UCL
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • filopodium tip Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • nuclear membrane Source: BHF-UCL
  • perinuclear endoplasmic reticulum Source: BHF-UCL
  • plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi60 – 601K → I: Abolishes plasma membrane targeting and nuclear localization. 1 Publication
Mutagenesisi61 – 611K → A: Abolishes plasma membrane targeting and nuclear localization. 1 Publication
Mutagenesisi71 – 711K → A: Abolishes plasma membrane targeting and nuclear localization. 1 Publication
Mutagenesisi72 – 721R → I: Abolishes plasma membrane targeting and nuclear localization. 1 Publication
Mutagenesisi97 – 971G → E: Decreases plasma membrane targeting and nuclear localization. 1 Publication
Mutagenesisi162 – 1676FFSGST → AAAAAA: No effect on interaction with VAPA. 1 Publication
Mutagenesisi451 – 4533FFD → VVV: Reduces VAPA binding. Abolishes association with endoplasmic reticulum. 2 Publications

Organism-specific databases

PharmGKBiPA32828.

Polymorphism and mutation databases

BioMutaiOSBPL3.
DMDMi20139176.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 887887Oxysterol-binding protein-related protein 3PRO_0000100371Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161PhosphoserineCombined sources
Modified residuei34 – 341PhosphoserineCombined sources
Modified residuei200 – 2001PhosphoserineCombined sources
Modified residuei251 – 2511PhosphoserineCombined sources
Modified residuei265 – 2651PhosphoserineCombined sources1 Publication
Modified residuei304 – 3041PhosphoserineCombined sources1 Publication
Modified residuei309 – 3091PhosphoserineCombined sources
Modified residuei320 – 3201PhosphoserineCombined sources1 Publication
Modified residuei323 – 3231Phosphoserine1 Publication
Modified residuei371 – 3711Phosphoserine1 Publication
Modified residuei372 – 3721PhosphoserineCombined sources1 Publication
Modified residuei410 – 4101PhosphoserineCombined sources1 Publication
Modified residuei425 – 4251PhosphoserineCombined sources
Modified residuei437 – 4371PhosphoserineCombined sources1 Publication
Modified residuei440 – 4401PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation is enhanced in vitro by phorbol-12-myristate-13-acetate (PMA), forskolin and calcium ionophore A23187 (PubMed:25447204). Phosphorylation seems to be stimulated in conditions of low cell-cell (or cell-matrix) adhesion (PubMed:18270267).2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9H4L5.
MaxQBiQ9H4L5.
PaxDbiQ9H4L5.
PeptideAtlasiQ9H4L5.
PRIDEiQ9H4L5.

PTM databases

iPTMnetiQ9H4L5.
PhosphoSiteiQ9H4L5.

Expressioni

Tissue specificityi

Expressed in a subset of small lymphocytes (at protein level). Expressed at high concentration in kidney, lymph node and thymus. Expressed at moderate concentration in stomach, jejunum, ileum, appendix, spleen, leukocytes, trachea, lung and thyroid gland. Expressed at low concentration in whole brain, esophagus, duodenum, ileocecum, colon, skeletal muscle, bone marrow, placenta and mammary gland (PubMed:14593528). 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 (PubMed:12590732).2 Publications

Developmental stagei

Expressed in several fetal tissues including kidney, thymus, spleen and lung.1 Publication

Gene expression databases

BgeeiQ9H4L5.
ExpressionAtlasiQ9H4L5. baseline and differential.
GenevisibleiQ9H4L5. HS.

Organism-specific databases

HPAiHPA000691.
HPA048401.

Interactioni

Subunit structurei

Homodimer (PubMed:16143324). Interacts with RRAS (PubMed:18270267). Interacts (phosphorylated form) with VAPA (PubMed:16143324, PubMed:25447204).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ORFQ9Q2G45EBI-1051317,EBI-6248094From a different organism.

Protein-protein interaction databases

BioGridi117497. 31 interactions.
IntActiQ9H4L5. 12 interactions.
MINTiMINT-1631853.
STRINGi9606.ENSP00000315410.

Structurei

3D structure databases

ProteinModelPortaliQ9H4L5.
SMRiQ9H4L5. Positions 54-147, 519-887.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 14696PHPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi161 – 1677FFAT 11 Publication
Motifi450 – 4545FFAT 21 Publication

Domaini

The FFAT 2 motif is required for interaction with VAPA and regulation of the endoplasmic reticulum targeting of ORP3. The FFAT 1 motif may contribute to VAPA binding.2 Publications
The PH domain binds phosphoinositides, with a preference for PI(3,4)P2 and PI(3,4,5)P3. The PH domain mediates targeting to the plasma membrane (PubMed:18270267).2 Publications

Sequence similaritiesi

Belongs to the OSBP family.Curated
Contains 1 PH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1737. Eukaryota.
ENOG410XP9E. LUCA.
GeneTreeiENSGT00760000119155.
HOVERGENiHBG058934.
InParanoidiQ9H4L5.
OMAiEIAMFPR.
OrthoDBiEOG780RKR.
PhylomeDBiQ9H4L5.
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.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1a (identifier: Q9H4L5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MMSDEKNLGV SQKLVSPSRS TSSCSSKQGS RQDSWEVVEG LRGEMNYTQE
60 70 80 90 100
PPVQKGFLLK KRKWPLKGWH KRFFYLDKGI LKYAKSQTDI EREKLHGCID
110 120 130 140 150
VGLSVMSVKK SSKCIDLDTE EHIYHLKVKS EEVFDEWVSK LRHHRMYRQN
160 170 180 190 200
EIAMFPHEVN HFFSGSTITD SSSGVFDSIS SRKRSSISKQ NLFQTGSNVS
210 220 230 240 250
FSCGGETRVP LWLQSSEDME KCSKDLAHCH AYLVEMSQLL QSMDVLHRTY
260 270 280 290 300
SAPAINAIQG GSFESPKKEK RSHRRWRSRA IGKDAKGTLQ VPKPFSGPVR
310 320 330 340 350
LHSSNPNLST LDFGEEKNYS DGSETSSEFS KMQEDLCHIA HKVYFTLRSA
360 370 380 390 400
FNIMSAEREK LKQLMEQDAS SSPSAQVIGL KNALSSALAQ NTDLKERLRR
410 420 430 440 450
IHAESLLLDS PAVAKSGDNL AEENSRDENR ALVHQLSNES RLSITDSLSE
460 470 480 490 500
FFDAQEVLLS PSSSENEISD DDSYVSDISD NLSLDNLSND LDNERQTLGP
510 520 530 540 550
VLDSGREAKS RRRTCLPAPC PSSSNISLWN ILRNNIGKDL SKVAMPVELN
560 570 580 590 600
EPLNTLQRLC EELEYSELLD KAAQIPSPLE RMVYVAAFAI SAYASSYYRA
610 620 630 640 650
GSKPFNPVLG ETYECIREDK GFQFFSEQVS HHPPISACHA ESRNFVFWQD
660 670 680 690 700
VRWKNKFWGK SMEIVPIGTT HVTLPVFGDH FEWNKVTSCI HNILSGQRWI
710 720 730 740 750
EHYGEIVIKN LHDDSCYCKV NFIKAKYWST NAHEIEGTVF DRSGKAVHRL
760 770 780 790 800
FGKWHESIYC GGGSSSACVW RANPMPKGYE QYYSFTQFAL ELNEMDPSSK
810 820 830 840 850
SLLPPTDTRF RPDQRFLEEG NLEEAEIQKQ RIEQLQRERR RVLEENHVEH
860 870 880
QPRFFRKSDD DSWVSNGTYL ELRKDLGFSK LDHPVLW
Length:887
Mass (Da):101,224
Last modified:March 1, 2001 - v1
Checksum:i12E16912BD3F2E99
GO
Isoform 1b (identifier: Q9H4L5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     259-289: Missing.

Show »
Length:856
Mass (Da):97,687
Checksum:i1D56185E3FB98744
GO
Isoform 1c (identifier: Q9H4L5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     387-422: Missing.

Show »
Length:851
Mass (Da):97,325
Checksum:iDA08C319F2BAEDCE
GO
Isoform 1d (identifier: Q9H4L5-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     259-289: Missing.
     387-422: Missing.

Show »
Length:820
Mass (Da):93,788
Checksum:i3D0A8947F6EE4DC5
GO
Isoform 2a (identifier: Q9H4L5-5) [UniParc]FASTAAdd to basket

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.
Show »
Length:642
Mass (Da):72,211
Checksum:i7AC19EA7AE07E5E4
GO
Isoform 2b (identifier: Q9H4L5-6) [UniParc]FASTAAdd to basket

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.
Show »
Length:611
Mass (Da):68,674
Checksum:i1A92347357A219CE
GO
Isoform 2c (identifier: Q9H4L5-7) [UniParc]FASTAAdd to basket

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.
Show »
Length:606
Mass (Da):68,313
Checksum:iEA72B4600CF3C1B8
GO
Isoform 2d (identifier: Q9H4L5-8) [UniParc]FASTAAdd to basket

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.
Show »
Length:575
Mass (Da):64,776
Checksum:iCD8F92033643E963
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti354 – 3541M → V.
Corresponds to variant rs11768296 [ dbSNP | Ensembl ].
VAR_053548

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei259 – 28931Missing in isoform 1b, isoform 1d, isoform 2b and isoform 2d. 1 PublicationVSP_008219Add
BLAST
Alternative sequencei387 – 42236Missing in isoform 1c, isoform 1d, isoform 2c and isoform 2d. 1 PublicationVSP_008220Add
BLAST
Alternative sequencei584 – 63148YVAAF…EQVSH → RSQPSLATVQPRSPSHEAIH GAHQRDSPCSLRFHFDCSVN RFITQSCLASSAWLFPVTL in isoform 2a, isoform 2b, isoform 2c and isoform 2d. 1 PublicationVSP_008221Add
BLAST
Alternative sequencei632 – 887256Missing in isoform 2a, isoform 2b, isoform 2c and isoform 2d. 1 PublicationVSP_008222Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47564.1. [Q9H4L5-4]
CCDS5390.1. [Q9H4L5-1]
CCDS5391.1. [Q9H4L5-2]
CCDS5392.1. [Q9H4L5-3]
RefSeqiNP_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_005249698.2. [Q9H4L5-1]
XP_006715744.1. XM_006715681.2. [Q9H4L5-2]
XP_006715745.1. XM_006715682.2. [Q9H4L5-3]
XP_006715746.1. XM_006715683.2. [Q9H4L5-4]
XP_011513560.1. XM_011515258.1. [Q9H4L5-1]
UniGeneiHs.520259.

Genome annotation databases

EnsembliENST00000313367; ENSP00000315410; ENSG00000070882. [Q9H4L5-1]
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]
GeneIDi26031.
KEGGihsa:26031.
UCSCiuc003sxf.5. human. [Q9H4L5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47564.1. [Q9H4L5-4]
CCDS5390.1. [Q9H4L5-1]
CCDS5391.1. [Q9H4L5-2]
CCDS5392.1. [Q9H4L5-3]
RefSeqiNP_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_005249698.2. [Q9H4L5-1]
XP_006715744.1. XM_006715681.2. [Q9H4L5-2]
XP_006715745.1. XM_006715682.2. [Q9H4L5-3]
XP_006715746.1. XM_006715683.2. [Q9H4L5-4]
XP_011513560.1. XM_011515258.1. [Q9H4L5-1]
UniGeneiHs.520259.

3D structure databases

ProteinModelPortaliQ9H4L5.
SMRiQ9H4L5. Positions 54-147, 519-887.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117497. 31 interactions.
IntActiQ9H4L5. 12 interactions.
MINTiMINT-1631853.
STRINGi9606.ENSP00000315410.

PTM databases

iPTMnetiQ9H4L5.
PhosphoSiteiQ9H4L5.

Polymorphism and mutation databases

BioMutaiOSBPL3.
DMDMi20139176.

Proteomic databases

EPDiQ9H4L5.
MaxQBiQ9H4L5.
PaxDbiQ9H4L5.
PeptideAtlasiQ9H4L5.
PRIDEiQ9H4L5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313367; ENSP00000315410; ENSG00000070882. [Q9H4L5-1]
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]
GeneIDi26031.
KEGGihsa:26031.
UCSCiuc003sxf.5. human. [Q9H4L5-1]

Organism-specific databases

CTDi26031.
GeneCardsiOSBPL3.
HGNCiHGNC:16370. OSBPL3.
HPAiHPA000691.
HPA048401.
MIMi606732. gene.
neXtProtiNX_Q9H4L5.
PharmGKBiPA32828.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1737. Eukaryota.
ENOG410XP9E. LUCA.
GeneTreeiENSGT00760000119155.
HOVERGENiHBG058934.
InParanoidiQ9H4L5.
OMAiEIAMFPR.
OrthoDBiEOG780RKR.
PhylomeDBiQ9H4L5.
TreeFamiTF320922.

Miscellaneous databases

ChiTaRSiOSBPL3. human.
GeneWikiiOSBPL3.
GenomeRNAii26031.
PROiQ9H4L5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H4L5.
ExpressionAtlasiQ9H4L5. baseline and differential.
GenevisibleiQ9H4L5. 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.
[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. "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), TISSUE SPECIFICITY.
  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.
    , 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. 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.
    , 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. "Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues: the expression and intracellular localization of ORP3, ORP6, and ORP7."
    Lehto M., Tienari J., Lehtonen S., Lehtonen E., Olkkonen V.M.
    Cell Tissue Res. 315:39-57(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  12. "Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and plasma membrane is controlled by multiple determinants."
    Lehto M., Hynynen R., Karjalainen K., Kuismanen E., Hyvaerinen K., Olkkonen V.M.
    Exp. Cell Res. 310:445-462(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, PH DOMAIN, FFAT MOTIF, MUTAGENESIS OF LYS-60; LYS-61; LYS-71; ARG-72; GLY-97 AND 451-PHE--ASP-453.
  13. "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.
  14. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RRAS, DOMAIN PH, AND PHOSPHORYLATION.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  16. "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.
  17. 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.
  18. "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].
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-410 AND SER-437, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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.
  21. "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.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-200; SER-251; SER-265; SER-304; SER-309; SER-320; SER-372; SER-410; SER-425; SER-437 AND SER-440, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  24. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  25. "OSBP-related protein 3 (ORP3) coupling with VAMP-associated protein A regulates R-Ras activity."
    Weber-Boyvat M., Kentala H., Lilja J., Vihervaara T., Hanninen R., Zhou Y., Peranen J., Nyman T.A., Ivaska J., Olkkonen V.M.
    Exp. Cell Res. 331:278-291(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, DOMAIN FFAT MOTIF, PHOSPHORYLATION AT SER-251; SER-265; SER-304; SER-320; SER-323; SER-371; SER-372; SER-410 AND SER-437, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 162-PHE--THR-167 AND 451-PHE--ASP-453.

Entry informationi

Entry nameiOSBL3_HUMAN
AccessioniPrimary (citable) accession number: Q9H4L5
Secondary accession number(s): A4D167
, A4D168, A4D169, A4D170, A4D171, A4D172, B8ZZ79, B8ZZP0, O14591, O43357, O43358, Q8N702, Q8N703, Q8N704, Q8NFH0, Q8NFH1, Q8NI12, Q8NI13, Q9BZF4, Q9UED6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 129 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. 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.