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Protein

Oxysterol-binding protein-related protein 8

Gene

OSBPL8

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 endoplasmic reticulum and the plasma membrane: specifically exchanges phosphatidylserine with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the plasma membrane in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum. Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:26206935). Binds oxysterol, 25-hydroxycholesterol and cholesterol (PubMed:17428193, PubMed:17991739, PubMed:21698267).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei485 – 4851PhosphatidylserineBy similarity
Binding sitei540 – 5401PhosphatidylserineBy similarity
Binding sitei706 – 7061Phosphatidylinositol 4-phosphateBy similarity
Binding sitei710 – 7101Phosphatidylinositol 4-phosphateBy similarity
Binding sitei714 – 7141Phosphatidylinositol 4-phosphateBy similarity

GO - Molecular functioni

  • cholesterol binding Source: BHF-UCL
  • phosphatidylinositol-4-phosphate binding Source: UniProtKB
  • phosphatidylserine binding Source: UniProtKB
  • phospholipid transporter activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Protein family/group databases

TCDBi2.D.1.1.2. the pi4p/ps counter transporter (p/p-ct) family.

Chemistry

SwissLipidsiSLP:000001535.

Names & Taxonomyi

Protein namesi
Recommended name:
Oxysterol-binding protein-related protein 8
Short name:
ORP-8
Short name:
OSBP-related protein 8
Gene namesi
Name:OSBPL8
Synonyms:KIAA14511 Publication, ORP8, OSBP10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:16396. OSBPL8.

Subcellular locationi

Isoform 1 :
Isoform 3 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei871 – 88818HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • cortical endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • nuclear membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi514 – 5152HH → AA: Impaired lipid countertransport between the endoplasmic reticulum and the plasma membrane. 1 Publication

Organism-specific databases

PharmGKBiPA32832.

Polymorphism and mutation databases

BioMutaiOSBPL8.
DMDMi39932732.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 889889Oxysterol-binding protein-related protein 8PRO_0000100378Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei14 – 141PhosphoserineCombined sources
Modified residuei65 – 651PhosphoserineCombined sources
Modified residuei68 – 681PhosphoserineCombined sources
Modified residuei314 – 3141PhosphoserineCombined sources
Modified residuei328 – 3281PhosphoserineCombined sources
Modified residuei342 – 3421PhosphoserineCombined sources
Modified residuei807 – 8071PhosphoserineCombined sources
Modified residuei808 – 8081PhosphoserineCombined sources
Modified residuei810 – 8101PhosphoserineCombined sources
Modified residuei814 – 8141PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9BZF1.
MaxQBiQ9BZF1.
PaxDbiQ9BZF1.
PeptideAtlasiQ9BZF1.
PRIDEiQ9BZF1.

PTM databases

iPTMnetiQ9BZF1.
PhosphoSiteiQ9BZF1.
SwissPalmiQ9BZF1.

Miscellaneous databases

PMAP-CutDBQ9BZF1.

Expressioni

Tissue specificityi

Widely expressed (PubMed:11735225). Expressed at higher level in macrophages (PubMed:17991739).2 Publications

Gene expression databases

BgeeiQ9BZF1.
CleanExiHS_OSBPL8.
ExpressionAtlasiQ9BZF1. baseline and differential.
GenevisibleiQ9BZF1. HS.

Organism-specific databases

HPAiHPA001309.

Interactioni

Subunit structurei

Interacts with SPAG5 (PubMed:24424245). Interacts with NUP62 (PubMed:21698267).2 Publications

Protein-protein interaction databases

BioGridi125383. 34 interactions.
DIPiDIP-56130N.
IntActiQ9BZF1. 11 interactions.
MINTiMINT-2816858.
STRINGi9606.ENSP00000261183.

Structurei

Secondary structure

1
889
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi151 – 1577Combined sources
Beta strandi160 – 1634Combined sources
Beta strandi165 – 1728Combined sources
Beta strandi175 – 1806Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi189 – 1924Combined sources
Turni203 – 2053Combined sources
Beta strandi209 – 2135Combined sources
Beta strandi244 – 2463Combined sources
Helixi250 – 26415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V88NMR-A149-265[»]
ProteinModelPortaliQ9BZF1.
SMRiQ9BZF1. Positions 147-265, 426-733.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BZF1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini148 – 265118PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni420 – 4256Phosphatidylinositol 4-phosphate bindingBy similarity
Regioni420 – 4256Phosphatidylserine bindingBy similarity
Regioni482 – 4854Phosphatidylinositol 4-phosphate bindingBy similarity
Regioni514 – 5152Phosphatidylinositol 4-phosphate bindingBy similarity

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2210. Eukaryota.
ENOG410XRW6. LUCA.
GeneTreeiENSGT00550000074515.
HOGENOMiHOG000233870.
HOVERGENiHBG053375.
InParanoidiQ9BZF1.
OMAiDLYQPSF.
OrthoDBiEOG7D59MQ.
PhylomeDBiQ9BZF1.
TreeFamiTF312807.

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. 1 hit.
PfamiPF01237. Oxysterol_BP. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 2 hits.
PROSITEiPS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BZF1-1) [UniParc]FASTAAdd to basket

Also known as: ORP8L1 Publication

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
MEGGLADGEP DRTSLLGDSK DVLGPSTVVA NSDESQLLTP GKMSQRQGKE
60 70 80 90 100
AYPTPTKDLH QPSLSPASPH SQGFERGKED ISQNKDESSL SMSKSKSESK
110 120 130 140 150
LYNGSEKDSS TSSKLTKKES LKVQKKNYRE EKKRATKELL STITDPSVIV
160 170 180 190 200
MADWLKIRGT LKSWTKLWCV LKPGVLLIYK TQKNGQWVGT VLLNACEIIE
210 220 230 240 250
RPSKKDGFCF KLFHPLEQSI WAVKGPKGEA VGSITQPLPS SYLIIRATSE
260 270 280 290 300
SDGRCWMDAL ELALKCSSLL KRTMIREGKE HDLSVSSDST HVTFYGLLRA
310 320 330 340 350
NNLHSGDNFQ LNDSEIERQH FKDQDMYSDK SDKENDQEHD ESDNEVMGKS
360 370 380 390 400
EESDTDTSER QDDSYIEPEP VEPLKETTYT EQSHEELGEA GEASQTETVS
410 420 430 440 450
EENKSLIWTL LKQVRPGMDL SKVVLPTFIL EPRSFLDKLS DYYYHADFLS
460 470 480 490 500
EAALEENPYF RLKKVVKWYL SGFYKKPKGL KKPYNPILGE TFRCLWIHPR
510 520 530 540 550
TNSKTFYIAE QVSHHPPISA FYVSNRKDGF CLSGSILAKS KFYGNSLSAI
560 570 580 590 600
LEGEARLTFL NRGEDYVMTM PYAHCKGILY GTMTLELGGT VNITCQKTGY
610 620 630 640 650
SAILEFKLKP FLGSSDCVNQ ISGKLKLGKE VLATLEGHWD SEVFITDKKT
660 670 680 690 700
DNSEVFWNPT PDIKQWRLIR HTVKFEEQGD FESEKLWQRV TRAINAKDQT
710 720 730 740 750
EATQEKYVLE EAQRQAARDR KTKNEEWSCK LFELDPLTGE WHYKFADTRP
760 770 780 790 800
WDPLNDMIQF EKDGVIQTKV KHRTPMVSVP KMKHKPTRQQ KKVAKGYSSP
810 820 830 840 850
EPDIQDSSGS EAQSVKPSTR RKKGIELGDI QSSIESIKQT QEEIKRNIMA
860 870 880
LRNHLVSSTP ATDYFLQQKD YFIIFLLILL QVIINFMFK
Length:889
Mass (Da):101,196
Last modified:December 15, 2003 - v3
Checksum:i79DB8055BD15FE95
GO
Isoform 2 (identifier: Q9BZF1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     15-29: Missing.

Note: No experimental confirmation available.
Show »
Length:874
Mass (Da):99,714
Checksum:i309510B3F9E184DB
GO
Isoform 3 (identifier: Q9BZF1-3) [UniParc]FASTAAdd to basket

Also known as: ORP8S1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.

Show »
Length:847
Mass (Da):96,956
Checksum:i9DD6AB040C2FD20B
GO

Sequence cautioni

The sequence AAG53411.1 differs from that shown. Reason: Frameshift at position 30. Curated
The sequence BAA95975.3 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti347 – 3471M → V in CAH18345 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4242Missing in isoform 3. CuratedVSP_045801Add
BLAST
Alternative sequencei15 – 2915Missing in isoform 2. 1 PublicationVSP_009120Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF392452 mRNA. Translation: AAL40665.1.
AB040884 mRNA. Translation: BAA95975.3. Different initiation.
AK289997 mRNA. Translation: BAF82686.1.
CR749542 mRNA. Translation: CAH18345.1.
AC117491 Genomic DNA. No translation available.
AC122687 Genomic DNA. No translation available.
AC124943 Genomic DNA. No translation available.
BC093834 mRNA. Translation: AAH93834.1.
BC101529 mRNA. Translation: AAI01530.1.
BC111728 mRNA. Translation: AAI11729.1.
AF323730 mRNA. Translation: AAG53411.1. Frameshift.
CCDSiCCDS31862.1. [Q9BZF1-1]
CCDS41814.1. [Q9BZF1-3]
RefSeqiNP_001003712.1. NM_001003712.1. [Q9BZF1-3]
NP_001306581.1. NM_001319652.1. [Q9BZF1-3]
NP_001306584.1. NM_001319655.1.
NP_065892.1. NM_020841.4. [Q9BZF1-1]
XP_005268678.1. XM_005268621.3. [Q9BZF1-1]
XP_006719287.1. XM_006719224.1. [Q9BZF1-3]
UniGeneiHs.430849.

Genome annotation databases

EnsembliENST00000261183; ENSP00000261183; ENSG00000091039. [Q9BZF1-1]
ENST00000393249; ENSP00000376939; ENSG00000091039. [Q9BZF1-3]
ENST00000393250; ENSP00000376940; ENSG00000091039. [Q9BZF1-3]
ENST00000611266; ENSP00000478240; ENSG00000091039. [Q9BZF1-3]
GeneIDi114882.
KEGGihsa:114882.
UCSCiuc001sye.2. human. [Q9BZF1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF392452 mRNA. Translation: AAL40665.1.
AB040884 mRNA. Translation: BAA95975.3. Different initiation.
AK289997 mRNA. Translation: BAF82686.1.
CR749542 mRNA. Translation: CAH18345.1.
AC117491 Genomic DNA. No translation available.
AC122687 Genomic DNA. No translation available.
AC124943 Genomic DNA. No translation available.
BC093834 mRNA. Translation: AAH93834.1.
BC101529 mRNA. Translation: AAI01530.1.
BC111728 mRNA. Translation: AAI11729.1.
AF323730 mRNA. Translation: AAG53411.1. Frameshift.
CCDSiCCDS31862.1. [Q9BZF1-1]
CCDS41814.1. [Q9BZF1-3]
RefSeqiNP_001003712.1. NM_001003712.1. [Q9BZF1-3]
NP_001306581.1. NM_001319652.1. [Q9BZF1-3]
NP_001306584.1. NM_001319655.1.
NP_065892.1. NM_020841.4. [Q9BZF1-1]
XP_005268678.1. XM_005268621.3. [Q9BZF1-1]
XP_006719287.1. XM_006719224.1. [Q9BZF1-3]
UniGeneiHs.430849.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V88NMR-A149-265[»]
ProteinModelPortaliQ9BZF1.
SMRiQ9BZF1. Positions 147-265, 426-733.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125383. 34 interactions.
DIPiDIP-56130N.
IntActiQ9BZF1. 11 interactions.
MINTiMINT-2816858.
STRINGi9606.ENSP00000261183.

Chemistry

SwissLipidsiSLP:000001535.

Protein family/group databases

TCDBi2.D.1.1.2. the pi4p/ps counter transporter (p/p-ct) family.

PTM databases

iPTMnetiQ9BZF1.
PhosphoSiteiQ9BZF1.
SwissPalmiQ9BZF1.

Polymorphism and mutation databases

BioMutaiOSBPL8.
DMDMi39932732.

Proteomic databases

EPDiQ9BZF1.
MaxQBiQ9BZF1.
PaxDbiQ9BZF1.
PeptideAtlasiQ9BZF1.
PRIDEiQ9BZF1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261183; ENSP00000261183; ENSG00000091039. [Q9BZF1-1]
ENST00000393249; ENSP00000376939; ENSG00000091039. [Q9BZF1-3]
ENST00000393250; ENSP00000376940; ENSG00000091039. [Q9BZF1-3]
ENST00000611266; ENSP00000478240; ENSG00000091039. [Q9BZF1-3]
GeneIDi114882.
KEGGihsa:114882.
UCSCiuc001sye.2. human. [Q9BZF1-1]

Organism-specific databases

CTDi114882.
GeneCardsiOSBPL8.
HGNCiHGNC:16396. OSBPL8.
HPAiHPA001309.
MIMi606736. gene.
neXtProtiNX_Q9BZF1.
PharmGKBiPA32832.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2210. Eukaryota.
ENOG410XRW6. LUCA.
GeneTreeiENSGT00550000074515.
HOGENOMiHOG000233870.
HOVERGENiHBG053375.
InParanoidiQ9BZF1.
OMAiDLYQPSF.
OrthoDBiEOG7D59MQ.
PhylomeDBiQ9BZF1.
TreeFamiTF312807.

Miscellaneous databases

ChiTaRSiOSBPL8. human.
EvolutionaryTraceiQ9BZF1.
GeneWikiiOSBPL8.
GenomeRNAii114882.
PMAP-CutDBQ9BZF1.
PROiQ9BZF1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BZF1.
CleanExiHS_OSBPL8.
ExpressionAtlasiQ9BZF1. baseline and differential.
GenevisibleiQ9BZF1. 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. 1 hit.
PfamiPF01237. Oxysterol_BP. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 2 hits.
PROSITEiPS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 1), TISSUE SPECIFICITY.
  2. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hippocampus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterine endothelium.
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 1).
  8. "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 1-578 (ISOFORM 2).
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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.
  11. "OSBP-related protein 8 (ORP8) suppresses ABCA1 expression and cholesterol efflux from macrophages."
    Yan D., Mayranpaa M.I., Wong J., Perttila J., Lehto M., Jauhiainen M., Kovanen P.T., Ehnholm C., Brown A.J., Olkkonen V.M.
    J. Biol. Chem. 283:332-340(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  12. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68; SER-314; SER-807; SER-808; SER-810 AND SER-814, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "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-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "OSBP-related protein 8 (ORP8) regulates plasma and liver tissue lipid levels and interacts with the nucleoporin Nup62."
    Zhou T., Li S., Zhong W., Vihervaara T., Beaslas O., Perttila J., Luo W., Jiang Y., Lehto M., Olkkonen V.M., Yan D.
    PLoS ONE 6:E21078-E21078(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NUP62.
  18. "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-68; SER-328; SER-342; SER-807 AND SER-808, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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-14; SER-65 AND SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  21. "OSBP-related protein 8 (ORP8) interacts with Homo sapiens sperm associated antigen 5 (SPAG5) and mediates oxysterol interference of HepG2 cell cycle."
    Zhong W., Zhou Y., Li J., Mysore R., Luo W., Li S., Chang M.S., Olkkonen V.M., Yan D.
    Exp. Cell Res. 322:227-235(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPAG5.
  22. "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-807 AND SER-808, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER-plasma membrane contacts."
    Chung J., Torta F., Masai K., Lucast L., Czapla H., Tanner L.B., Narayanaswamy P., Wenk M.R., Nakatsu F., De Camilli P.
    Science 349:428-432(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), MUTAGENESIS OF 514-HIS-515.
  25. "Solution structure of the pleckstrin homology domain of oxysterol-binding protein-related protein 8 (KIAA1451 protein)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUN-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 147-265.

Entry informationi

Entry nameiOSBL8_HUMAN
AccessioniPrimary (citable) accession number: Q9BZF1
Secondary accession number(s): A8K1T2
, E9PE66, E9PE68, Q52LQ3, Q68D75, Q8WXP8, Q9P277
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: December 15, 2003
Last modified: July 6, 2016
This is version 138 of the entry and version 3 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.